GCSH3_ARATH
ID GCSH3_ARATH Reviewed; 166 AA.
AC Q9LQL0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Glycine cleavage system H protein 3, mitochondrial;
DE Flags: Precursor;
GN Name=GDH3; OrderedLocusNames=At1g32470; ORFNames=F5D14.25;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP REVIEW.
RX PubMed=11286922; DOI=10.1016/s1360-1385(01)01892-1;
RA Douce R., Bourguignon J., Neuburger M., Rebeille F.;
RT "The glycine decarboxylase system: a fascinating complex.";
RL Trends Plant Sci. 6:167-176(2001).
RN [5]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=12730263; DOI=10.1093/jxb/erg171;
RA Bauwe H., Kolukisaoglu U.;
RT "Genetic manipulation of glycine decarboxylation.";
RL J. Exp. Bot. 54:1523-1535(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [8]
RP ACTIVITY REGULATION, S-NITROSYLATION, AND GLUTATHIONYLATION.
RX PubMed=20089767; DOI=10.1104/pp.109.152579;
RA Palmieri M.C., Lindermayr C., Bauwe H., Steinhauser C., Durner J.;
RT "Regulation of plant glycine decarboxylase by s-nitrosylation and
RT glutathionylation.";
RL Plant Physiol. 152:1514-1528(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP PHE-35.
RX PubMed=25862457; DOI=10.1104/pp.15.00300;
RA Huang S., Nelson C.J., Li L., Taylor N.L., Stroeher E., Peteriet J.,
RA Millar A.H.;
RT "INTERMEDIATE CLEAVAGE PEPTIDASE55 modifies enzyme amino termini and alters
RT protein stability in Arabidopsis mitochondria.";
RL Plant Physiol. 168:415-427(2015).
CC -!- FUNCTION: The glycine decarboxylase (GDC) or glycine cleavage system
CC catalyzes the degradation of glycine. The H protein shuttles the
CC methylamine group of glycine from the P protein to the T protein (By
CC similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250};
CC Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by harpin, S-nitrosoglutathione (GSNO),
CC nitric oxide, N-ethylmaleimide and 5,5'-dithiobis-(2-nitrobenzoic
CC acid). {ECO:0000269|PubMed:20089767}.
CC -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC T, L and H.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14671022,
CC ECO:0000305|PubMed:25862457}.
CC -!- PTM: S-nitrosylated and/or glutathionylated at unknown positions in
CC response to nitric oxide. {ECO:0000269|PubMed:20089767}.
CC -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000305}.
CC -!- CAUTION: Was wrongly referred as Gly dehydrogenase subunit P2 in
CC PubMed:20089767. {ECO:0000305}.
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DR EMBL; AC007767; AAF81345.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31490.1; -; Genomic_DNA.
DR EMBL; AF332465; AAG48828.1; -; mRNA.
DR EMBL; AF385740; AAK60330.1; -; mRNA.
DR EMBL; AY078028; AAL77729.1; -; mRNA.
DR PIR; A86450; A86450.
DR RefSeq; NP_174525.1; NM_102982.4.
DR AlphaFoldDB; Q9LQL0; -.
DR SMR; Q9LQL0; -.
DR BioGRID; 25375; 1.
DR STRING; 3702.AT1G32470.1; -.
DR iPTMnet; Q9LQL0; -.
DR MetOSite; Q9LQL0; -.
DR PaxDb; Q9LQL0; -.
DR PRIDE; Q9LQL0; -.
DR ProteomicsDB; 222031; -.
DR EnsemblPlants; AT1G32470.1; AT1G32470.1; AT1G32470.
DR GeneID; 840141; -.
DR Gramene; AT1G32470.1; AT1G32470.1; AT1G32470.
DR KEGG; ath:AT1G32470; -.
DR Araport; AT1G32470; -.
DR TAIR; locus:2033802; AT1G32470.
DR eggNOG; KOG3373; Eukaryota.
DR HOGENOM; CLU_097408_1_0_1; -.
DR InParanoid; Q9LQL0; -.
DR OMA; ESHEWIK; -.
DR OrthoDB; 1348095at2759; -.
DR PhylomeDB; Q9LQL0; -.
DR BRENDA; 1.4.1.27; 399.
DR PRO; PR:Q9LQL0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LQL0; baseline and differential.
DR Genevisible; Q9LQL0; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005960; C:glycine cleavage complex; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
DR GO; GO:0009249; P:protein lipoylation; IBA:GO_Central.
DR CDD; cd06848; GCS_H; 1.
DR HAMAP; MF_00272; GcvH; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR002930; GCV_H.
DR InterPro; IPR033753; GCV_H/Fam206.
DR InterPro; IPR017453; GCV_H_sub.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR11715; PTHR11715; 1.
DR Pfam; PF01597; GCV_H; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR TIGRFAMs; TIGR00527; gcvH; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 1: Evidence at protein level;
KW Glutathionylation; Lipoyl; Mitochondrion; Phosphoprotein;
KW Reference proteome; S-nitrosylation; Transit peptide.
FT TRANSIT 1..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25862457"
FT CHAIN 36..166
FT /note="Glycine cleavage system H protein 3, mitochondrial"
FT /id="PRO_0000010730"
FT DOMAIN 57..139
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 98
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25855"
SQ SEQUENCE 166 AA; 17897 MW; C21658C0B9E75ADB CRC64;
MALRMWASST ANALKLSSSA SKSHLLPAFS ISRCFSSVLE GLKYANSHEW VKHEGSVATI
GITDHAQDHL GEVVFVELPE ANSSVSKEKS FGAVESVKAT SEILSPISGE VIEVNTKLTE
SPGLINSSPY EDGWMIKVKP SSPAELEALM GPKEYTKFCE EEDAAH
