ID   GCSP_FLAAN              Reviewed;        1034 AA.
AC   O49850;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   27-MAR-2024, entry version 99.
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=GDCSP;
OS   Flaveria anomala (Yellowtops).
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=35877;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Leaf;
RA   Nan Q., Bauwe H.;
RT   "The GDCSP gene encoding P-protein of the glycine cleavage system in the
RT   C3-C4 intermediate plant Flaveria anomala.";
RL   (er) Plant Gene Register PGR98-004(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; Z99762; CAB16911.1; -; Genomic_DNA.
DR   AlphaFoldDB; O49850; -.
DR   SMR; O49850; -.
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_0000010745"
FT   MOD_RES         770
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1034 AA;  112695 MW;  C2F424C76EF104BA CRC64;
     MERARRLAML GRLVSQTKHN PSISSPALCS PSRYVSSLSP YVCGGTNVRS DRNLNGFGSQ
     VRTISVEALK PSDTFPRRHN SATPEEQTKM AEFVGFSNLD SLIDATVPKS 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 DSKAIAEEAC KHKMNLRIVD
     KNTITVAFDE TTTIEDVDTL FKVFALGKPV PFTAASIAPE VQDAIPSGLV RETPYLTHPI
     FNMYHTEHEL LRYISKLQSK DLSLCHSMIP LGSCTMKLNA TTEMMPVTWP AFADIHPFAP
     TEQAQGYQEM FKNLGDLLCT ITGFDSFSLQ PNAGAAGEYA GLMVIRAYHM ARGDHHRNVC
     IIPVSAHGTN PASAAMCGMK IITVGTDSKG NINIEELRKA AEANKENLSA LMVTYPSTHG
     VYEEGIDEIC KIIHDNGGQV YMDGANMNAQ VGLTSPGWIG ADVCHLNLHK TFCIPHGGGG
     PGMGPIGVKK HLAPYLPSHP VVPTGGIPAP EESQPLGTIA AAPWGSALIL PISYTYIAMM
     GSQGITNASK IAILNANYMA KRLENHYPIL FRGVNGTVAH EFIVDLRPLK TTAGIEPEDV
     AKRLIDYGFH GPTMSWPVPG TLMIEPTESE SKAELDRFCD ALISIRQEIA EIEKGNVDFN
     NNVIKGAPHP PQLLMADKWT KPYSREYAAY PAPWLRAAKF WPTTCRVDNV YGDRNLICTL
     QPPQEYEEKA EATA
//