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   27-MAR-2024, entry version 101.
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=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage
CC         complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-
CC         L-lysyl-[glycine-cleavage complex H protein]; 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   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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR   HAMAP; MF_00711; GcvP; 1.
DR   InterPro; IPR003437; GcvP.
DR   InterPro; IPR049316; GDC-P_C.
DR   InterPro; IPR049315; GDC-P_N.
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   NCBIfam; TIGR00461; gcvP; 1.
DR   PANTHER; PTHR11773:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF21478; GcvP2_C; 1.
DR   Pfam; PF02347; GDC-P; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 2.
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
//