ID GCSH1_ARATH Reviewed; 165 AA.
AC P25855; Q0WR60;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 27-MAR-2024, entry version 167.
DE RecName: Full=Glycine cleavage system H protein 1, mitochondrial;
DE Flags: Precursor;
GN Name=GDH1; Synonyms=GCDH, GDCH, GDCSH; OrderedLocusNames=At2g35370;
GN ORFNames=T32F12.25;
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 [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION BY
RP LIGHT.
RX PubMed=7480320; DOI=10.1104/pp.109.1.161;
RA Srinivasan R., Oliver D.J.;
RT "Light-dependent and tissue-specific expression of the H-protein of the
RT glycine decarboxylase complex.";
RL Plant Physiol. 109:161-168(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND CLEAVAGE OF TRANSIT PEPTIDE AFTER
RP PHE-34.
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.
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Note=Binds 1 lipoyl cofactor covalently.;
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:0000305|PubMed:25862457}.
CC -!- TISSUE SPECIFICITY: Highly expressed in leaves, lower expression in
CC green veins, petioles, and stems, and detected in roots.
CC {ECO:0000269|PubMed:7480320}.
CC -!- INDUCTION: Up-regulated by light. {ECO:0000269|PubMed:7480320}.
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}.
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DR EMBL; U27144; AAA87942.1; -; Genomic_DNA.
DR EMBL; M82921; AAA32802.1; -; mRNA.
DR EMBL; AC005314; AAC36184.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09100.1; -; Genomic_DNA.
DR EMBL; AY050446; AAK91461.1; -; mRNA.
DR EMBL; AY058854; AAL24242.1; -; mRNA.
DR EMBL; AY097349; AAM19865.1; -; mRNA.
DR EMBL; AK228462; BAF00389.1; -; mRNA.
DR EMBL; AY086345; AAM64413.1; -; mRNA.
DR PIR; G84767; G84767.
DR RefSeq; NP_181080.1; NM_129089.2.
DR AlphaFoldDB; P25855; -.
DR SMR; P25855; -.
DR BioGRID; 3450; 1.
DR IntAct; P25855; 1.
DR STRING; 3702.P25855; -.
DR iPTMnet; P25855; -.
DR MetOSite; P25855; -.
DR PaxDb; 3702-AT2G35370-1; -.
DR ProteomicsDB; 222029; -.
DR EnsemblPlants; AT2G35370.1; AT2G35370.1; AT2G35370.
DR GeneID; 818104; -.
DR Gramene; AT2G35370.1; AT2G35370.1; AT2G35370.
DR KEGG; ath:AT2G35370; -.
DR Araport; AT2G35370; -.
DR TAIR; AT2G35370; GDCH.
DR eggNOG; KOG3373; Eukaryota.
DR HOGENOM; CLU_097408_1_0_1; -.
DR InParanoid; P25855; -.
DR OMA; PYGKGWM; -.
DR OrthoDB; 52189at2759; -.
DR PhylomeDB; P25855; -.
DR BioCyc; ARA:AT2G35370-MONOMER; -.
DR BioCyc; MetaCyc:AT2G35370-MONOMER; -.
DR BRENDA; 1.4.1.27; 399.
DR BRENDA; 1.4.4.2; 399.
DR PRO; PR:P25855; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P25855; baseline and differential.
DR Genevisible; P25855; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005960; C:glycine cleavage complex; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
DR GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:InterPro.
DR CDD; cd06848; GCS_H; 1.
DR Gene3D; 2.40.50.100; -; 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 NCBIfam; TIGR00527; gcvH; 1.
DR PANTHER; PTHR11715; GLYCINE CLEAVAGE SYSTEM H PROTEIN; 1.
DR PANTHER; PTHR11715:SF27; GLYCINE CLEAVAGE SYSTEM H PROTEIN 1, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF01597; GCV_H; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 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..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:25862457"
FT CHAIN 35..165
FT /note="Glycine cleavage system H protein 1, mitochondrial"
FT /id="PRO_0000010729"
FT DOMAIN 56..138
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT MOD_RES 97
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22092075"
SQ SEQUENCE 165 AA; 17947 MW; 48309650C88F9BE2 CRC64;
MALRMWASST ANALKLSSSV SKSHLSPFSF SRCFSTVLEG LKYANSHEWV KHEGSVATIG
ITAHAQDHLG EVVFVELPED NTSVSKEKSF GAVESVKATS EILSPISGEI IEVNKKLTES
PGLINSSPYE DGWMIKVKPS SPAELESLMG PKEYTKFCEE EDAAH
//
