GCSP_HUMAN
ID GCSP_HUMAN Reviewed; 1020 AA.
AC P23378; Q2M2F8;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Glycine dehydrogenase (decarboxylating), mitochondrial {ECO:0000303|PubMed:15489334};
DE EC=1.4.4.2 {ECO:0000269|PubMed:1993704, ECO:0000269|PubMed:1996985, ECO:0000269|PubMed:28244183};
DE AltName: Full=Glycine cleavage system P protein;
DE AltName: Full=Glycine decarboxylase {ECO:0000303|PubMed:1993704, ECO:0000303|PubMed:1996985};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring);
DE Flags: Precursor;
GN Name=GLDC {ECO:0000312|HGNC:HGNC:4313};
GN Synonyms=GCSP {ECO:0000312|HGNC:HGNC:4313};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND VARIANT NKH PHE-756
RP DEL.
RX PubMed=1996985; DOI=10.1016/0006-291x(91)91545-n;
RA Kure S., Narisawa K., Tada K.;
RT "Structural and expression analyses of normal and mutant mRNA encoding
RT glycine decarboxylase: three-base deletion in mRNA causes nonketotic
RT hyperglycinemia.";
RL Biochem. Biophys. Res. Commun. 174:1176-1182(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
RX PubMed=1993704; DOI=10.1016/s0021-9258(18)49991-7;
RA Kume A., Koyata H., Sakakibara T., Ishiguro Y., Kure S., Hiraga K.;
RT "The glycine cleavage system. Molecular cloning of the chicken and human
RT glycine decarboxylase cDNAs and some characteristics involved in the
RT deduced protein structures.";
RL J. Biol. Chem. 266:3323-3329(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, INVOLVEMENT IN NKH,
RP VARIANTS NKH LYS-146; PRO-173; ALA-267; CYS-362; TRP-373; GLU-376; TRP-461;
RP PRO-548; TYR-580; ARG-581; ASP-624; ASP-763; GLU-768; TRP-790; HIS-866;
RP GLY-905; THR-933 AND ARG-994, AND CHARACTERIZATION OF VARIANTS NKH LYS-146;
RP PRO-173; ALA-267; CYS-362; TRP-373; GLU-376; TRP-461; PRO-548; TYR-580;
RP ARG-581; ASP-624; ASP-763; GLU-768; TRP-790; HIS-866; GLY-905; THR-933 AND
RP ARG-994.
RX PubMed=28244183; DOI=10.1002/humu.23208;
RA Bravo-Alonso I., Navarrete R., Arribas-Carreira L., Perona A., Abia D.,
RA Couce M.L., Garcia-Cazorla A., Morais A., Domingo R., Ramos M.A.,
RA Swanson M.A., Van Hove J.L., Ugarte M., Perez B., Perez-Cerda C.,
RA Rodriguez-Pombo P.;
RT "Nonketotic Hyperglycinemia: functional assessment of missense variants in
RT GLDC to understand phenotypes of the disease.";
RL Hum. Mutat. 38:678-691(2017).
RN [11]
RP VARIANT NKH ILE-564.
RX PubMed=1634607; DOI=10.1172/jci115831;
RA Kure S., Takayanagi M., Narisawa K., Tada K., Leisti J.;
RT "Identification of a common mutation in Finnish patients with nonketotic
RT hyperglycinemia.";
RL J. Clin. Invest. 90:160-164(1992).
RN [12]
RP VARIANT NKH SER-515.
RX PubMed=11286506; DOI=10.1006/mgme.2001.3158;
RA Toone J.R., Applegarth D.A., Coulter-Mackie M.B., James E.R.;
RT "Recurrent mutations in P- and T-proteins of the glycine cleavage complex
RT and a novel T-protein mutation (N145I): a strategy for the molecular
RT investigation of patients with nonketotic hyperglycinemia (NKH).";
RL Mol. Genet. Metab. 72:322-325(2001).
RN [13]
RP VARIANT NKH PRO-283, AND VARIANT THR-329.
RX PubMed=11592811; DOI=10.1006/mgme.2001.3224;
RA Applegarth D.A., Toone J.R.;
RT "Nonketotic hyperglycinemia (glycine encephalopathy): laboratory
RT diagnosis.";
RL Mol. Genet. Metab. 74:139-146(2001).
RN [14]
RP VARIANT NKH CYS-839.
RX PubMed=28737873; DOI=10.5546/aap.2017.eng.e225;
RA Liu S., Wang Z., Liang J., Chen N., Ouyang H., Zeng W., Chen L., Xie X.,
RA Jiang J.;
RT "Two novel mutations in the glycine decarboxylase gene in a boy with
RT classic nonketotic hyperglycinemia: case report.";
RL Arch. Argent. Pediatr. 115:E225-E229(2017).
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. The P protein (GLDC) binds the alpha-amino group of glycine
CC through its pyridoxal phosphate cofactor; CO(2) is released and the
CC remaining methylamine moiety is then transferred to the lipoamide
CC cofactor of the H protein (GCSH). {ECO:0000269|PubMed:1993704,
CC ECO:0000269|PubMed:1996985, ECO:0000269|PubMed:28244183}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] +
CC glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-
CC [glycine-cleavage complex H protein] + CO2; Xref=Rhea:RHEA:24304,
CC Rhea:RHEA-COMP:10494, Rhea:RHEA-COMP:10495, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57305, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:83143; EC=1.4.4.2; Evidence={ECO:0000269|PubMed:1993704,
CC ECO:0000269|PubMed:1996985, ECO:0000269|PubMed:28244183};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P15505};
CC -!- ACTIVITY REGULATION: Stimulated by lipoic acid. Inhibited in presence
CC of methylamine (By similarity). {ECO:0000250|UniProtKB:P15505}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with GCSH (By
CC similarity). The glycine cleavage system is composed of four proteins:
CC P (GLDC), T (GCST), L (DLD) and H (GCSH).
CC {ECO:0000250|UniProtKB:P15505}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:28244183}.
CC -!- DISEASE: Non-ketotic hyperglycinemia (NKH) [MIM:605899]: Autosomal
CC recessive disease characterized by accumulation of a large amount of
CC glycine in body fluid and by severe neurological symptoms.
CC {ECO:0000269|PubMed:11286506, ECO:0000269|PubMed:11592811,
CC ECO:0000269|PubMed:1634607, ECO:0000269|PubMed:1996985,
CC ECO:0000269|PubMed:28244183, ECO:0000269|PubMed:28737873}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M63635; AAA36478.1; -; mRNA.
DR EMBL; M64590; AAA36463.1; -; mRNA.
DR EMBL; D90239; BAA14286.1; -; mRNA.
DR EMBL; AK314156; BAG36841.1; -; mRNA.
DR EMBL; AL353718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL162411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58740.1; -; Genomic_DNA.
DR EMBL; BC111993; AAI11994.1; -; mRNA.
DR EMBL; BC111995; AAI11996.1; -; mRNA.
DR CCDS; CCDS34987.1; -.
DR PIR; JN0124; JN0124.
DR RefSeq; NP_000161.2; NM_000170.2.
DR PDB; 6I33; X-ray; 2.30 A; A/B=45-1020.
DR PDB; 6I34; X-ray; 2.10 A; A/B/C/D=45-1020.
DR PDB; 6I35; X-ray; 2.00 A; A/B/C/D=45-1020.
DR PDBsum; 6I33; -.
DR PDBsum; 6I34; -.
DR PDBsum; 6I35; -.
DR AlphaFoldDB; P23378; -.
DR SASBDB; P23378; -.
DR SMR; P23378; -.
DR BioGRID; 108993; 28.
DR IntAct; P23378; 17.
DR MINT; P23378; -.
DR STRING; 9606.ENSP00000370737; -.
DR DrugBank; DB00145; Glycine.
DR DrugBank; DB00114; Pyridoxal phosphate.
DR iPTMnet; P23378; -.
DR PhosphoSitePlus; P23378; -.
DR BioMuta; GLDC; -.
DR DMDM; 229462870; -.
DR EPD; P23378; -.
DR jPOST; P23378; -.
DR MassIVE; P23378; -.
DR MaxQB; P23378; -.
DR PaxDb; P23378; -.
DR PeptideAtlas; P23378; -.
DR PRIDE; P23378; -.
DR ProteomicsDB; 54084; -.
DR Antibodypedia; 9715; 204 antibodies from 31 providers.
DR DNASU; 2731; -.
DR Ensembl; ENST00000321612.8; ENSP00000370737.4; ENSG00000178445.10.
DR GeneID; 2731; -.
DR KEGG; hsa:2731; -.
DR MANE-Select; ENST00000321612.8; ENSP00000370737.4; NM_000170.3; NP_000161.2.
DR UCSC; uc003zkc.4; human.
DR CTD; 2731; -.
DR DisGeNET; 2731; -.
DR GeneCards; GLDC; -.
DR GeneReviews; GLDC; -.
DR HGNC; HGNC:4313; GLDC.
DR HPA; ENSG00000178445; Tissue enriched (liver).
DR MalaCards; GLDC; -.
DR MIM; 238300; gene.
DR MIM; 605899; phenotype.
DR neXtProt; NX_P23378; -.
DR OpenTargets; ENSG00000178445; -.
DR Orphanet; 289863; Atypical glycine encephalopathy.
DR Orphanet; 289860; Infantile glycine encephalopathy.
DR Orphanet; 289857; Neonatal glycine encephalopathy.
DR PharmGKB; PA28716; -.
DR VEuPathDB; HostDB:ENSG00000178445; -.
DR eggNOG; KOG2040; Eukaryota.
DR GeneTree; ENSGT00390000017970; -.
DR HOGENOM; CLU_004620_3_2_1; -.
DR InParanoid; P23378; -.
DR OMA; CVPMSEY; -.
DR OrthoDB; 390348at2759; -.
DR PhylomeDB; P23378; -.
DR TreeFam; TF300678; -.
DR BioCyc; MetaCyc:HS00622-MON; -.
DR BRENDA; 1.4.1.27; 2681.
DR BRENDA; 1.4.4.2; 2681.
DR PathwayCommons; P23378; -.
DR Reactome; R-HSA-6783984; Glycine degradation.
DR SABIO-RK; P23378; -.
DR SignaLink; P23378; -.
DR SIGNOR; P23378; -.
DR BioGRID-ORCS; 2731; 9 hits in 1072 CRISPR screens.
DR ChiTaRS; GLDC; human.
DR GeneWiki; Glycine_dehydrogenase_(decarboxylating); -.
DR GenomeRNAi; 2731; -.
DR Pharos; P23378; Tbio.
DR PRO; PR:P23378; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P23378; protein.
DR Bgee; ENSG00000178445; Expressed in right lobe of liver and 150 other tissues.
DR ExpressionAtlas; P23378; baseline and differential.
DR Genevisible; P23378; HS.
DR GO; GO:0005960; C:glycine cleavage complex; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB.
DR GO; GO:0016594; F:glycine binding; IBA:GO_Central.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IDA:UniProtKB.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0070280; F:pyridoxal binding; ISS:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0006546; P:glycine catabolic process; IDA:UniProtKB.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
DR GO; GO:1903442; P:response to lipoic acid; ISS:UniProtKB.
DR GO; GO:0036255; P:response to methylamine; ISS:UniProtKB.
DR CDD; cd00613; GDC-P; 2.
DR Gene3D; 3.40.640.10; -; 2.
DR Gene3D; 3.90.1150.10; -; 2.
DR HAMAP; MF_00711; GcvP; 1.
DR InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR InterPro; IPR003437; GcvP.
DR InterPro; IPR020581; GDC_P.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11773; PTHR11773; 1.
DR Pfam; PF01212; Beta_elim_lyase; 1.
DR Pfam; PF02347; GDC-P; 1.
DR SUPFAM; SSF53383; SSF53383; 2.
DR TIGRFAMs; TIGR00461; gcvP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Disease variant; Mitochondrion; Oxidoreductase;
KW Pyridoxal phosphate; Reference proteome; Transit peptide.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..1020
FT /note="Glycine dehydrogenase (decarboxylating),
FT mitochondrial"
FT /id="PRO_0000010740"
FT REGION 21..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 447
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91W43"
FT MOD_RES 514
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91W43"
FT MOD_RES 648
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91W43"
FT MOD_RES 664
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91W43"
FT MOD_RES 754
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P15505"
FT VARIANT 146
FT /note="T -> K (in NKH; loss of glycine catabolic process;
FT loss of expression; dbSNP:rs376578742)"
FT /evidence="ECO:0000269|PubMed:28244183"
FT /id="VAR_078776"
FT VARIANT 173
FT /note="L -> P (in NKH; loss of glycine catabolic process;
FT decreased abundance)"
FT /evidence="ECO:0000269|PubMed:28244183"
FT /id="VAR_078777"
FT VARIANT 267
FT /note="P -> A (in NKH; decreased glycine catabolic process;
FT changed localization to the mitochondria; also expressed
FT diffusely throughout the cytosol; decreased abundance;
FT dbSNP:rs1554648117)"
FT /evidence="ECO:0000269|PubMed:28244183"
FT /id="VAR_078778"
FT VARIANT 283
FT /note="A -> P (in NKH; dbSNP:rs386833589)"
FT /evidence="ECO:0000269|PubMed:11592811"
FT /id="VAR_016849"
FT VARIANT 329
FT /note="P -> T (in one non-ketotic hyperglycinemia patient;
FT dbSNP:rs386833593)"
FT /evidence="ECO:0000269|PubMed:11592811"
FT /id="VAR_016850"
FT VARIANT 362
FT /note="R -> C (in NKH; decreased glycine catabolic process;
FT decreased abundance; dbSNP:rs10975674)"
FT /evidence="ECO:0000269|PubMed:28244183"
FT /id="VAR_078779"
FT VARIANT 373
FT /note="R -> W (in NKH; decreased glycine catabolic process;
FT decreased abundance; dbSNP:rs150171524)"
FT /evidence="ECO:0000269|PubMed:28244183"
FT /id="VAR_078780"
FT VARIANT 376
FT /note="K -> E (in NKH; decreased glycine catabolic process;
FT decreased abundance; dbSNP:rs774093619)"
FT /evidence="ECO:0000269|PubMed:28244183"
FT /id="VAR_078781"
FT VARIANT 461
FT /note="R -> W (in NKH; decreased glycine catabolic process;
FT changed localization to the mitochondria; also expressed
FT diffusely throughout the cytosol; decreased abundance;
FT dbSNP:rs761957837)"
FT /evidence="ECO:0000269|PubMed:28244183"
FT /id="VAR_078782"
FT VARIANT 515
FT /note="R -> S (in NKH; dbSNP:rs121964976)"
FT /evidence="ECO:0000269|PubMed:11286506"
FT /id="VAR_016851"
FT VARIANT 548
FT /note="L -> P (in NKH; decreased GCS P-protein glycine
FT exchange activity; no effect on abundance)"
FT /evidence="ECO:0000269|PubMed:28244183"
FT /id="VAR_078783"
FT VARIANT 564
FT /note="S -> I (in NKH; common mutation in Finland;
FT dbSNP:rs121964974)"
FT /evidence="ECO:0000269|PubMed:1634607"
FT /id="VAR_004979"
FT VARIANT 580
FT /note="H -> Y (in NKH; loss of glycine catabolic process;
FT loss of expression)"
FT /evidence="ECO:0000269|PubMed:28244183"
FT /id="VAR_078784"
FT VARIANT 581
FT /note="P -> R (in NKH; loss of glycine catabolic process;
FT decreased abundance; dbSNP:rs772871471)"
FT /evidence="ECO:0000269|PubMed:28244183"
FT /id="VAR_078785"
FT VARIANT 624
FT /note="A -> D (in NKH; loss of GCS P-protein glycine
FT exchange activity; no effect on abundance)"
FT /evidence="ECO:0000269|PubMed:28244183"
FT /id="VAR_078786"
FT VARIANT 756
FT /note="Missing (in NKH)"
FT /evidence="ECO:0000269|PubMed:1996985"
FT /id="VAR_009939"
FT VARIANT 763
FT /note="G -> D (in NKH; loss of GCS P-protein glycine
FT exchange activity; no effect on abundance;
FT dbSNP:rs1374110692)"
FT /evidence="ECO:0000269|PubMed:28244183"
FT /id="VAR_078787"
FT VARIANT 768
FT /note="G -> E (in NKH; loss of GCS P-protein glycine
FT exchange activity; no effect on abundance)"
FT /evidence="ECO:0000269|PubMed:28244183"
FT /id="VAR_078788"
FT VARIANT 790
FT /note="R -> W (in NKH; decreased glycine catabolic process;
FT decreased abundance; dbSNP:rs386833556)"
FT /evidence="ECO:0000269|PubMed:28244183"
FT /id="VAR_078789"
FT VARIANT 839
FT /note="Y -> C (in NKH)"
FT /evidence="ECO:0000269|PubMed:28737873"
FT /id="VAR_079313"
FT VARIANT 866
FT /note="D -> H (in NKH; decreased glycine catabolic process;
FT decreased abundance)"
FT /evidence="ECO:0000269|PubMed:28244183"
FT /id="VAR_078790"
FT VARIANT 905
FT /note="V -> G (in NKH; decreased GCS P-protein glycine
FT exchange activity; no effect on abundance;
FT dbSNP:rs188269735)"
FT /evidence="ECO:0000269|PubMed:28244183"
FT /id="VAR_078791"
FT VARIANT 933
FT /note="I -> T (in NKH; decreased glycine catabolic process;
FT decreased abundance; dbSNP:rs758029533)"
FT /evidence="ECO:0000269|PubMed:28244183"
FT /id="VAR_078792"
FT VARIANT 994
FT /note="G -> R (in NKH; loss of glycine catabolic process;
FT loss of expression; dbSNP:rs1406713104)"
FT /evidence="ECO:0000269|PubMed:28244183"
FT /id="VAR_078793"
FT CONFLICT 396
FT /note="A -> R (in Ref. 2; AAA36463/BAA14286)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="Q -> H (in Ref. 1; AAA36478 and 2; AAA36463/
FT BAA14286)"
FT /evidence="ECO:0000305"
FT CONFLICT 608
FT /note="Y -> H (in Ref. 1; AAA36478)"
FT /evidence="ECO:0000305"
FT CONFLICT 976
FT /note="V -> M (in Ref. 2; AAA36463/BAA14286)"
FT /evidence="ECO:0000305"
FT HELIX 52..56
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 87..94
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 113..124
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 145..150
FT /evidence="ECO:0007829|PDB:6I35"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 170..187
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 199..214
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 227..240
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 259..267
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 277..285
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 305..308
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:6I35"
FT TURN 318..321
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 338..343
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 370..373
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 386..424
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 432..441
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 446..455
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 468..471
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 478..487
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 494..500
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 508..510
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 523..526
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 531..543
FT /evidence="ECO:0007829|PDB:6I35"
FT TURN 548..550
FT /evidence="ECO:0007829|PDB:6I35"
FT TURN 556..558
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 565..568
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 569..572
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 574..577
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 585..587
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 589..606
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 609..612
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 618..635
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 643..647
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 653..660
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 664..668
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 674..676
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 678..688
FT /evidence="ECO:0007829|PDB:6I35"
FT TURN 689..691
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 692..700
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 710..718
FT /evidence="ECO:0007829|PDB:6I35"
FT TURN 719..721
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 723..727
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 728..733
FT /evidence="ECO:0007829|PDB:6I35"
FT TURN 734..737
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 740..742
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 746..749
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 752..755
FT /evidence="ECO:0007829|PDB:6I35"
FT TURN 761..763
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 770..772
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 774..779
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 784..786
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 791..793
FT /evidence="ECO:0007829|PDB:6I34"
FT STRAND 801..803
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 808..810
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 811..844
FT /evidence="ECO:0007829|PDB:6I35"
FT TURN 845..847
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 848..850
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 863..866
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 869..874
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 878..887
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 893..896
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 903..905
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 913..934
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 940..943
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 944..947
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 952..956
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 966..970
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 978..980
FT /evidence="ECO:0007829|PDB:6I35"
FT STRAND 985..987
FT /evidence="ECO:0007829|PDB:6I35"
FT HELIX 991..996
FT /evidence="ECO:0007829|PDB:6I35"
SQ SEQUENCE 1020 AA; 112730 MW; 8FAEA7D56BEB17B2 CRC64;
MQSCARAWGL RLGRGVGGGR RLAGGSGPCW APRSRDSSSG GGDSAAAGAS RLLERLLPRH
DDFARRHIGP GDKDQREMLQ TLGLASIDEL IEKTVPANIR LKRPLKMEDP VCENEILATL
HAISSKNQIW RSYIGMGYYN CSVPQTILRN LLENSGWITQ YTPYQPEVSQ GRLESLLNYQ
TMVCDITGLD MANASLLDEG TAAAEALQLC YRHNKRRKFL VDPRCHPQTI AVVQTRAKYT
GVLTELKLPC EMDFSGKDVS GVLFQYPDTE GKVEDFTELV ERAHQSGSLA CCATDLLALC
ILRPPGEFGV DIALGSSQRF GVPLGYGGPH AAFFAVRESL VRMMPGRMVG VTRDATGKEV
YRLALQTREQ HIRRDKATSN ICTAQALLAN MAAMFAIYHG SHGLEHIARR VHNATLILSE
GLKRAGHQLQ HDLFFDTLKI QCGCSVKEVL GRAAQRQINF RLFEDGTLGI SLDETVNEKD
LDDLLWIFGC ESSAELVAES MGEECRGIPG SVFKRTSPFL THQVFNSYHS ETNIVRYMKK
LENKDISLVH SMIPLGSCTM KLNSSSELAP ITWKEFANIH PFVPLDQAQG YQQLFRELEK
DLCELTGYDQ VCFQPNSGAQ GEYAGLATIR AYLNQKGEGH RTVCLIPKSA HGTNPASAHM
AGMKIQPVEV DKYGNIDAVH LKAMVDKHKE NLAAIMITYP STNGVFEENI SDVCDLIHQH
GGQVYLDGAN MNAQVGICRP GDFGSDVSHL NLHKTFCIPH GGGGPGMGPI GVKKHLAPFL
PNHPVISLKR NEDACPVGTV SAAPWGSSSI LPISWAYIKM MGGKGLKQAT ETAILNANYM
AKRLETHYRI LFRGARGYVG HEFILDTRPF KKSANIEAVD VAKRLQDYGF HAPTMSWPVA
GTLMVEPTES EDKAELDRFC DAMISIRQEI ADIEEGRIDP RVNPLKMSPH SLTCVTSSHW
DRPYSREVAA FPLPFVKPEN KFWPTIARID DIYGDQHLVC TCPPMEVYES PFSEQKRASS
