GCST_HUMAN
ID GCST_HUMAN Reviewed; 403 AA.
AC P48728; A8K3I5; B4DE61; B4DJQ0; E9PBG1; Q96IG6;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Aminomethyltransferase, mitochondrial {ECO:0000305};
DE EC=2.1.2.10 {ECO:0000269|PubMed:16051266};
DE AltName: Full=Glycine cleavage system T protein {ECO:0000303|PubMed:7916605};
DE Short=GCVT;
DE Flags: Precursor;
GN Name=AMT {ECO:0000312|HGNC:HGNC:473};
GN Synonyms=GCST {ECO:0000312|HGNC:HGNC:473};
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] (ISOFORM 1).
RX PubMed=7916605; DOI=10.1006/bbrc.1993.1480;
RA Hayasaka K., Nanao K., Takada G., Okamura-Ikeda K., Motokawa Y.;
RT "Isolation and sequence determination of cDNA encoding human T-protein of
RT the glycine cleavage system.";
RL Biochem. Biophys. Res. Commun. 192:766-771(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8188235; DOI=10.1006/geno.1994.1007;
RA Nanao K., Takada G., Takahashi E., Seki N., Komatsu Y., Okamura-Ikeda K.,
RA Motokawa Y., Hayasaka K.;
RT "Structure and chromosomal localization of the aminomethyltransferase gene
RT (AMT).";
RL Genomics 19:27-30(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Cerebellum, Heart, and Thalamus;
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=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-386 (ISOFORM 4).
RC TISSUE=Colon;
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 INVOLVEMENT IN NKH, AND VARIANTS NKH TRP-94; CYS-222 AND CYS-296.
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 [8]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-403 ALONE AND IN COMPLEX WITH
RP 5-METHYLTETRAHYDROFOLATE, SUBSTRATE-BINDING SITES, CATALYTIC ACTIVITY,
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS NKH
RP ILE-145; ASP-269 AND HIS-320, AND MUTAGENESIS OF ASP-129.
RX PubMed=16051266; DOI=10.1016/j.jmb.2005.06.056;
RA Okamura-Ikeda K., Hosaka H., Yoshimura M., Yamashita E., Toma S.,
RA Nakagawa A., Fujiwara K., Motokawa Y., Taniguchi H.;
RT "Crystal structure of human T-protein of glycine cleavage system at 2.0 A
RT resolution and its implication for understanding non-ketotic
RT hyperglycinemia.";
RL J. Mol. Biol. 351:1146-1159(2005).
RN [9]
RP VARIANTS NKH ARG-47; ASP-269 AND HIS-320, AND INVOLVEMENT IN NKH.
RX PubMed=8005589; DOI=10.1007/bf00201565;
RA Nanao K., Okamura-Ikeda K., Motokawa Y., Danks D.M., Baumgartner E.R.,
RA Takada G., Hayasaka K.;
RT "Identification of the mutations in the T-protein gene causing typical and
RT atypical nonketotic hyperglycinemia.";
RL Hum. Genet. 93:655-658(1994).
RN [10]
RP VARIANT NKH ARG-42.
RX PubMed=9600239; DOI=10.1007/s004390050716;
RA Kure S., Mandel H., Rolland M.-O., Sakata Y., Shinka T., Drugan A.,
RA Boneh A., Tada K., Matsubara Y., Narisawa K.;
RT "A missense mutation (His42Arg) in the T-protein gene from a large Israeli-
RT Arab kindred with nonketotic hyperglycinemia.";
RL Hum. Genet. 102:430-434(1998).
RN [11]
RP VARIANT NKH HIS-276.
RX PubMed=9621520; DOI=10.1007/s100380050055;
RA Kure S., Shinka T., Sakata Y., Osamu N., Takayanagi M., Tada K.,
RA Matsubara Y., Narisawa K.;
RT "A one-base deletion (183delC) and a missense mutation (D276H) in the T-
RT protein gene from a Japanese family with nonketotic hyperglycinemia.";
RL J. Hum. Genet. 43:135-137(1998).
RN [12]
RP VARIANTS NKH LYS-211 AND HIS-320.
RX PubMed=10873393; DOI=10.1006/mgme.2000.3000;
RA Toone J.R., Applegarth D.A., Coulter-Mackie M.B., James E.R.;
RT "Biochemical and molecular investigations of patients with nonketotic
RT hyperglycinemia.";
RL Mol. Genet. Metab. 70:116-121(2000).
RN [13]
RP VARIANTS NKH ILE-145 AND HIS-320.
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 [14]
RP VARIANT NKH CYS-265.
RX PubMed=26371980; DOI=10.1016/j.ejpn.2015.08.008;
RA Belcastro V., Barbarini M., Barca S., Mauro I.;
RT "A novel AMT gene mutation in a newborn with nonketotic hyperglycinemia and
RT early myoclonic encephalopathy.";
RL Eur. J. Paediatr. Neurol. 20:192-195(2016).
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. {ECO:0000269|PubMed:16051266}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-
CC aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-
CC 5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] +
CC NH4(+); Xref=Rhea:RHEA:16945, Rhea:RHEA-COMP:10475, Rhea:RHEA-
CC COMP:10492, ChEBI:CHEBI:15636, ChEBI:CHEBI:28938, ChEBI:CHEBI:57453,
CC ChEBI:CHEBI:83100, ChEBI:CHEBI:83143; EC=2.1.2.10;
CC Evidence={ECO:0000269|PubMed:16051266};
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H. {ECO:0000305|PubMed:16051266}.
CC -!- INTERACTION:
CC P48728-4; P50479: PDLIM4; NbExp=5; IntAct=EBI-14394829, EBI-372861;
CC P48728-4; Q08AM6: VAC14; NbExp=3; IntAct=EBI-14394829, EBI-2107455;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:16051266}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P48728-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P48728-2; Sequence=VSP_042557;
CC Name=3;
CC IsoId=P48728-3; Sequence=VSP_043288;
CC Name=4;
CC IsoId=P48728-4; Sequence=VSP_045418;
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:10873393, ECO:0000269|PubMed:11286506,
CC ECO:0000269|PubMed:16051266, ECO:0000269|PubMed:26371980,
CC ECO:0000269|PubMed:28244183, ECO:0000269|PubMed:8005589,
CC ECO:0000269|PubMed:9600239, ECO:0000269|PubMed:9621520}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000305}.
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DR EMBL; D13811; BAA02967.1; -; mRNA.
DR EMBL; D14686; BAA03512.1; -; Genomic_DNA.
DR EMBL; AK290600; BAF83289.1; -; mRNA.
DR EMBL; AK293481; BAG56972.1; -; mRNA.
DR EMBL; AK296177; BAG58912.1; -; mRNA.
DR EMBL; AC104452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW64984.1; -; Genomic_DNA.
DR EMBL; BC007546; AAH07546.2; -; mRNA.
DR CCDS; CCDS2797.1; -. [P48728-1]
DR CCDS; CCDS54583.1; -. [P48728-2]
DR CCDS; CCDS54584.1; -. [P48728-3]
DR CCDS; CCDS54585.1; -. [P48728-4]
DR PIR; I54192; I54192.
DR RefSeq; NP_000472.2; NM_000481.3. [P48728-1]
DR RefSeq; NP_001158182.1; NM_001164710.1. [P48728-3]
DR RefSeq; NP_001158183.1; NM_001164711.1. [P48728-2]
DR RefSeq; NP_001158184.1; NM_001164712.1. [P48728-4]
DR PDB; 1WSR; X-ray; 2.00 A; A/B=29-403.
DR PDB; 1WSV; X-ray; 2.60 A; A/B=29-403.
DR PDBsum; 1WSR; -.
DR PDBsum; 1WSV; -.
DR AlphaFoldDB; P48728; -.
DR SMR; P48728; -.
DR BioGRID; 106772; 12.
DR IntAct; P48728; 3.
DR STRING; 9606.ENSP00000273588; -.
DR DrugBank; DB04789; 5-methyltetrahydrofolic acid.
DR DrugBank; DB00145; Glycine.
DR DrugBank; DB00157; NADH.
DR DrugBank; DB00116; Tetrahydrofolic acid.
DR iPTMnet; P48728; -.
DR PhosphoSitePlus; P48728; -.
DR BioMuta; AMT; -.
DR DMDM; 1346122; -.
DR EPD; P48728; -.
DR jPOST; P48728; -.
DR MassIVE; P48728; -.
DR MaxQB; P48728; -.
DR PaxDb; P48728; -.
DR PeptideAtlas; P48728; -.
DR PRIDE; P48728; -.
DR ProteomicsDB; 19216; -.
DR ProteomicsDB; 55925; -. [P48728-1]
DR ProteomicsDB; 55926; -. [P48728-2]
DR ProteomicsDB; 55927; -. [P48728-3]
DR Antibodypedia; 1586; 187 antibodies from 27 providers.
DR DNASU; 275; -.
DR Ensembl; ENST00000273588.9; ENSP00000273588.3; ENSG00000145020.16. [P48728-1]
DR Ensembl; ENST00000395338.7; ENSP00000378747.2; ENSG00000145020.16. [P48728-4]
DR Ensembl; ENST00000458307.6; ENSP00000415619.2; ENSG00000145020.16. [P48728-3]
DR Ensembl; ENST00000636522.1; ENSP00000489758.1; ENSG00000145020.16. [P48728-2]
DR GeneID; 275; -.
DR KEGG; hsa:275; -.
DR MANE-Select; ENST00000273588.9; ENSP00000273588.3; NM_000481.4; NP_000472.2.
DR UCSC; uc003cww.4; human. [P48728-1]
DR CTD; 275; -.
DR DisGeNET; 275; -.
DR GeneCards; AMT; -.
DR GeneReviews; AMT; -.
DR HGNC; HGNC:473; AMT.
DR HPA; ENSG00000145020; Tissue enhanced (liver).
DR MalaCards; AMT; -.
DR MIM; 238310; gene.
DR MIM; 605899; phenotype.
DR neXtProt; NX_P48728; -.
DR OpenTargets; ENSG00000145020; -.
DR Orphanet; 289863; Atypical glycine encephalopathy.
DR Orphanet; 289860; Infantile glycine encephalopathy.
DR Orphanet; 289857; Neonatal glycine encephalopathy.
DR PharmGKB; PA24780; -.
DR VEuPathDB; HostDB:ENSG00000145020; -.
DR eggNOG; KOG2770; Eukaryota.
DR GeneTree; ENSGT00940000157524; -.
DR HOGENOM; CLU_007884_10_0_1; -.
DR InParanoid; P48728; -.
DR OMA; MPVQYPA; -.
DR PhylomeDB; P48728; -.
DR TreeFam; TF313026; -.
DR BioCyc; MetaCyc:HS07223-MON; -.
DR BRENDA; 1.4.1.27; 2681.
DR BRENDA; 2.1.2.10; 2681.
DR PathwayCommons; P48728; -.
DR Reactome; R-HSA-6783984; Glycine degradation.
DR SABIO-RK; P48728; -.
DR SignaLink; P48728; -.
DR SIGNOR; P48728; -.
DR BioGRID-ORCS; 275; 9 hits in 1078 CRISPR screens.
DR ChiTaRS; AMT; human.
DR EvolutionaryTrace; P48728; -.
DR GenomeRNAi; 275; -.
DR Pharos; P48728; Tbio.
DR PRO; PR:P48728; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P48728; protein.
DR Bgee; ENSG00000145020; Expressed in right lobe of liver and 96 other tissues.
DR ExpressionAtlas; P48728; baseline and differential.
DR Genevisible; P48728; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0004047; F:aminomethyltransferase activity; IMP:UniProtKB.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0006546; P:glycine catabolic process; TAS:Reactome.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IMP:UniProtKB.
DR Gene3D; 3.30.1360.120; -; 1.
DR InterPro; IPR006223; GCS_T.
DR InterPro; IPR028896; GCST/YgfZ/DmdA.
DR InterPro; IPR013977; GCV_T_C.
DR InterPro; IPR006222; GCV_T_N.
DR InterPro; IPR029043; GcvT/YgfZ_C.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR PANTHER; PTHR43757; PTHR43757; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR SUPFAM; SSF101790; SSF101790; 1.
DR TIGRFAMs; TIGR00528; gcvT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Aminotransferase; Disease variant;
KW Mitochondrion; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P25285"
FT CHAIN 29..403
FT /note="Aminomethyltransferase, mitochondrial"
FT /id="PRO_0000010755"
FT BINDING 232
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16051266"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16051266"
FT BINDING 399
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16051266"
FT VAR_SEQ 30..85
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042557"
FT VAR_SEQ 113..156
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043288"
FT VAR_SEQ 380..403
FT /note="VRRKQQMAVVSKMPFVPTNYYTLK -> LPSGPCF (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045418"
FT VARIANT 42
FT /note="H -> R (in NKH; dbSNP:rs121964983)"
FT /evidence="ECO:0000269|PubMed:9600239"
FT /id="VAR_007951"
FT VARIANT 47
FT /note="G -> R (in NKH; dbSNP:rs121964982)"
FT /evidence="ECO:0000269|PubMed:8005589"
FT /id="VAR_007952"
FT VARIANT 94
FT /note="R -> W (in NKH; dbSNP:rs1126422)"
FT /evidence="ECO:0000269|PubMed:28244183"
FT /id="VAR_078794"
FT VARIANT 145
FT /note="N -> I (in NKH; loss of aminomethyltransferase
FT activity; dbSNP:rs386833682)"
FT /evidence="ECO:0000269|PubMed:11286506,
FT ECO:0000269|PubMed:16051266"
FT /id="VAR_016847"
FT VARIANT 211
FT /note="E -> K (in NKH; dbSNP:rs116192290)"
FT /evidence="ECO:0000269|PubMed:10873393"
FT /id="VAR_016848"
FT VARIANT 222
FT /note="R -> C (in NKH; dbSNP:rs781466698)"
FT /evidence="ECO:0000269|PubMed:28244183"
FT /id="VAR_078795"
FT VARIANT 265
FT /note="R -> C (in NKH; dbSNP:rs779483959)"
FT /evidence="ECO:0000269|PubMed:26371980"
FT /id="VAR_074107"
FT VARIANT 269
FT /note="G -> D (in NKH; decreased aminomethyltransferase
FT activity; dbSNP:rs121964981)"
FT /evidence="ECO:0000269|PubMed:16051266,
FT ECO:0000269|PubMed:8005589"
FT /id="VAR_007953"
FT VARIANT 276
FT /note="D -> H (in NKH; dbSNP:rs121964984)"
FT /evidence="ECO:0000269|PubMed:9621520"
FT /id="VAR_007954"
FT VARIANT 296
FT /note="R -> C (in NKH; dbSNP:rs1056820947)"
FT /evidence="ECO:0000269|PubMed:28244183"
FT /id="VAR_078796"
FT VARIANT 320
FT /note="R -> H (in NKH; loss of aminomethyltransferase
FT activity; dbSNP:rs121964985)"
FT /evidence="ECO:0000269|PubMed:10873393,
FT ECO:0000269|PubMed:11286506, ECO:0000269|PubMed:16051266,
FT ECO:0000269|PubMed:8005589"
FT /id="VAR_007955"
FT MUTAGEN 129
FT /note="D->A,N: Loss of aminomethyltransferase activity."
FT /evidence="ECO:0000269|PubMed:16051266"
FT CONFLICT 95
FT /note="V -> C (in Ref. 2; BAA03512)"
FT /evidence="ECO:0000305"
FT HELIX 39..44
FT /evidence="ECO:0007829|PDB:1WSR"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:1WSR"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:1WSR"
FT HELIX 65..74
FT /evidence="ECO:0007829|PDB:1WSR"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:1WSR"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:1WSR"
FT HELIX 94..101
FT /evidence="ECO:0007829|PDB:1WSR"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1WSR"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:1WSR"
FT STRAND 126..134
FT /evidence="ECO:0007829|PDB:1WSR"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:1WSR"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:1WSR"
FT HELIX 149..165
FT /evidence="ECO:0007829|PDB:1WSR"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:1WSR"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:1WSR"
FT HELIX 187..192
FT /evidence="ECO:0007829|PDB:1WSR"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:1WSR"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:1WSR"
FT STRAND 215..222
FT /evidence="ECO:0007829|PDB:1WSR"
FT STRAND 225..235
FT /evidence="ECO:0007829|PDB:1WSR"
FT HELIX 237..248
FT /evidence="ECO:0007829|PDB:1WSR"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:1WSR"
FT HELIX 258..267
FT /evidence="ECO:0007829|PDB:1WSR"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:1WSR"
FT TURN 283..287
FT /evidence="ECO:0007829|PDB:1WSR"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:1WSR"
FT HELIX 294..299
FT /evidence="ECO:0007829|PDB:1WSR"
FT HELIX 305..312
FT /evidence="ECO:0007829|PDB:1WSR"
FT STRAND 319..328
FT /evidence="ECO:0007829|PDB:1WSR"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:1WSR"
FT STRAND 343..353
FT /evidence="ECO:0007829|PDB:1WSR"
FT TURN 354..357
FT /evidence="ECO:0007829|PDB:1WSR"
FT STRAND 358..365
FT /evidence="ECO:0007829|PDB:1WSR"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:1WSR"
FT STRAND 375..380
FT /evidence="ECO:0007829|PDB:1WSR"
FT STRAND 383..390
FT /evidence="ECO:0007829|PDB:1WSR"
SQ SEQUENCE 403 AA; 43946 MW; 218DC9EEADFA9102 CRC64;
MQRAVSVVAR LGFRLQAFPP ALCRPLSCAQ EVLRRTPLYD FHLAHGGKMV AFAGWSLPVQ
YRDSHTDSHL HTRQHCSLFD VSHMLQTKIL GSDRVKLMES LVVGDIAELR PNQGTLSLFT
NEAGGILDDL IVTNTSEGHL YVVSNAGCWE KDLALMQDKV RELQNQGRDV GLEVLDNALL
ALQGPTAAQV LQAGVADDLR KLPFMTSAVM EVFGVSGCRV TRCGYTGEDG VEISVPVAGA
VHLATAILKN PEVKLAGLAA RDSLRLEAGL CLYGNDIDEH TTPVEGSLSW TLGKRRRAAM
DFPGAKVIVP QLKGRVQRRR VGLMCEGAPM RAHSPILNME GTKIGTVTSG CPSPSLKKNV
AMGYVPCEYS RPGTMLLVEV RRKQQMAVVS KMPFVPTNYY TLK
