GCSPA_FLAPR
ID GCSPA_FLAPR Reviewed; 1037 AA.
AC P49361;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Glycine dehydrogenase (decarboxylating) A, mitochondrial;
DE EC=1.4.4.2;
DE AltName: Full=Glycine cleavage system P protein A;
DE AltName: Full=Glycine decarboxylase A;
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) A;
DE Flags: Precursor;
GN Name=GDCSPA;
OS Flaveria pringlei.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Tageteae; Flaveria.
OX NCBI_TaxID=4226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Leaf;
RX PubMed=7724679; DOI=10.1104/pp.107.2.655;
RA Bauwe H., Kopriva S.;
RT "The gdcsPA gene from Flaveria pringlei (Asteraceae).";
RL Plant Physiol. 107:655-655(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX PubMed=8165245; DOI=10.1104/pp.104.3.1077;
RA Kopriva S., Bauwe H.;
RT "P-protein of glycine decarboxylase from Flaveria pringlei.";
RL Plant Physiol. 104:1077-1078(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC TISSUE=Leaf;
RX PubMed=8529630; DOI=10.1111/j.1432-1033.1995.116_c.x;
RA Bauwe H., Chu C.-C., Kopriva S., Nan Q.;
RT "Structure and expression analysis of the gdcsPA and gdcsPB genes encoding
RT two P-isoproteins of the glycine-cleavage system from Flaveria pringlei.";
RL Eur. J. Biochem. 234:116-124(1995).
CC -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC glycine. The P protein binds the alpha-amino group of glycine through
CC its pyridoxal phosphate cofactor; CO(2) is released and the remaining
CC methylamine moiety is then transferred to the lipoamide cofactor of the
CC H protein.
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;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- SUBUNIT: Homodimer (By similarity). The glycine cleavage system is
CC composed of four proteins: P, T, L and H. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and roots.
CC {ECO:0000269|PubMed:8529630}.
CC -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000305}.
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DR EMBL; Z36879; CAA85353.1; -; Genomic_DNA.
DR EMBL; Z25857; CAA81076.1; -; mRNA.
DR PIR; S63535; S63535.
DR AlphaFoldDB; P49361; -.
DR SMR; P49361; -.
DR PRIDE; P49361; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
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; 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; PF02347; GDC-P; 2.
DR SUPFAM; SSF53383; SSF53383; 2.
DR TIGRFAMs; TIGR00461; gcvP; 1.
PE 2: Evidence at transcript level;
KW Mitochondrion; Oxidoreductase; Pyridoxal phosphate; Transit peptide.
FT TRANSIT 1..66
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 67..1037
FT /note="Glycine dehydrogenase (decarboxylating) A,
FT mitochondrial"
FT /id="PRO_0000010746"
FT MOD_RES 773
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 2
FT /note="E -> D (in Ref. 2; CAA81076)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="T -> I (in Ref. 2; CAA81076)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1037 AA; 113032 MW; ED248FA227F9E0F3 CRC64;
MERARRLANK AILGRLVSQT KHNPSISSPA LCSPSRYVSS LSPYVCSGTN VRSDRNLNGF
GSQVRTISVE ALKPSDTFPR RHNSATPEEQ TKMAEFVGFP NLDSLIDATV PKSIRLDSMK
YSKFDEGLTE SQMIAHMQDL ASKNKIFKSF IGMGYYNTSV PTVILRNIME NPGWYTQYTP
YQAEIAQGRL ESLLNFQTMV TDLTGLPMSN ASLLDEGTAA AEAMAMCNNI QKGKKKTFII
ASNCHPQTID ICKTRADGFD LKVVTSDLKD FDYSSGDVCG VLVQYPGTEG ELLDYSEFIK
NAHANGVKVV MASDLLALTI LKPPGELGAD IVVGSAQRFG VPMGYGGPHA AFLATSQEYK
RMMPGRIIGV SVDSSGKPAL RMAMQTREQH IRRDKATSNI CTAQALLANM AAMFGVYHGP
EGLKTIAKRV HGLAGTFAAG LKKLGTVQVQ DLPFFDTVKV TCVDSKAIAE EAYKHKMNLR
IVDKNTITVA FDETTTIEDV DTLFKVFALG KPVTFTAASI APEVQDAIPS GLVRETPYLT
HPIFNMYHTE HELLRYISKL QSKDLSLCHS MIPLGSCTMK LNATTEMMPV TWPAFADIHP
FAPTEQAQGY QEMFKNLGDL LCTITGFDSF SLQPNAGAAG EYAGLMVIRA YHMARGDHHR
NVCIIPVSAH GTNPASAAMC GMKIITVGTD SKGNINIEEL RKAAEANKEN LSALMVTYPS
THGVYEEGID EICKIIHDNG GQVYMDGANM NAQVGLTSPG WIGADVCHLN LHKTFCIPHG
GGGPGMGPIG VKKHLAPYLP SHPVVATGGI PAPEQSQPLG TIAAAPWGSA LILPISYTYI
AMMGSQGITN ASKIAILNAN YMAKRLENHY PILFRGVNGT VAHEFIVDLR PLKTTAGIEP
EDVAKRLIDY GFHGPTMSWP VPGTLMIEPT ESESKAELDR FCDALISIRQ EIAEIEKGNV
DLNNNVIKGA PHPPQLLMAD KWTKPYSREY AAYPAPWLRA AKFWPTTCRV DNVYGDRNLI
CTLQPPQEYE EKAEATA
