ID   GCSP_FLATR              Reviewed;        1034 AA.
AC   O49852;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Glycine dehydrogenase (decarboxylating), mitochondrial;
DE            EC=1.4.4.2;
DE   AltName: Full=Glycine cleavage system P protein;
DE   AltName: Full=Glycine decarboxylase;
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring);
DE   Flags: Precursor;
GN   Name=GDCSPA; Synonyms=GDCSP;
OS   Flaveria trinervia (Clustered yellowtops) (Oedera trinervia).
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=4227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Leaf;
RA   Cossu R., Bauwe H.;
RT   "Two genes of the GDCSP gene family from the C4 plant Flaveria trinervia:
RT   GDCSPA encoding P-protein and GDCSPB, a pseudogene.";
RL   (er) Plant Gene Register PGR98-002(1998).
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   -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000305}.
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DR   EMBL; Z99767; CAB16916.1; -; Genomic_DNA.
DR   AlphaFoldDB; O49852; -.
DR   SMR; O49852; -.
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   3: Inferred from homology;
KW   Mitochondrion; Oxidoreductase; Pyridoxal phosphate; Transit peptide.
FT   TRANSIT         1..63
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           64..1034
FT                   /note="Glycine dehydrogenase (decarboxylating),
FT                   mitochondrial"
FT                   /id="PRO_0000010748"
FT   MOD_RES         770
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1034 AA;  112735 MW;  14A71076C05A5062 CRC64;
     MERARRLAML GRLVSQTKHN PSISSSALCS PSRYVSSLSP YVCSGTNVRS DRNLNGFGSQ
     VRTISVEALK PSDTFPRRHN SATPEEQTKM AEFVGFSNLD SLIDATVPKA IRLDSMKYSK
     FDEGLTESQM IAHMQDLASK NKIFKSFIGM GYYNTSVPTV ILRNIMENPG WYTQYTPYQA
     EIAQGRLESL LNFQTMITDL TGLPMSNASL LDEGTAAAEA MAMCNNIQKG KKKTFIIASN
     CHPQTIDICK TRADGFDLKV VTSDLKDFDY SSGDVCGVLV QYPGTEGELL DYSEFIKNAH
     ANGVKVVMAS DLLALTILKP PGELGADIVV GSAQRFGVPM GYGGPHAAFL ATSQEYKRMM
     PGRIIGVSVD SSGKPALRMA MQTREQHIRR DKATSNICTA QALLANMAAM YGVYHGPEGL
     KTIAKRVHGL AGTFAAGLKK LGTVQVQDLP FFDTVKVTCA DSKAIAEEAY KHKMNLRIVD
     KNTITVAFDE TTTIEDVDTL FKVFALGKPV TFTAASIAPE VQDAIPSGLV RETPYLTHPI
     FNMYHTEHEL LRYISKLQSK DLSLCHSMIP LGSCTMKLNA TTEMMPVTWP AFADIHPFAP
     TEQAQGYQEM FKNLGDLLCT ITGFDSFSLQ PNAGAAGEYA GLMVIQAYHM ARGDHHRKVC
     IIPVSAHGTN PASAAMCGMK IITVGTDSKG NINIEELRKA AEANKENLSA LMVTYPSTHG
     VYEEGIDEIC KIIHDNGGQV YMDGANMNAQ VGLTSPGWIG ADVCHLNLHK TFCIPHGGGG
     PGMGPIGVKK HLAPYLPSHP VVPTGGIPAP EQSQPLGTIA AAPWGSALIL PISYTYIAMM
     GSQGITNASK IAILNANYMA KRLENHYPIL FRGVNGTVAH EFIVDLRPLK TTAGIEPEDV
     AKRLIDYGFH GPTMSWPVPG TLMIEPTESE SKAELDRFCD ALISIRQEIA EIEKGTVDFN
     NNVIKGAPHP PQLLMADKWT KPYSREYAAY PAPWLRAAKF WPTTCRVDNV YGDRNLICTL
     QPPQEYEEKA EATA
//