ID   GCSPB_FLAPR             Reviewed;        1034 AA.
AC   P49362;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Glycine dehydrogenase (decarboxylating) B, mitochondrial;
DE            EC=1.4.4.2;
DE   AltName: Full=Glycine cleavage system P protein B;
DE   AltName: Full=Glycine decarboxylase B;
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) B;
DE   Flags: Precursor;
GN   Name=GDCSPB;
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=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   -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000305}.
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DR   EMBL; Z54239; CAA91000.1; -; Genomic_DNA.
DR   PIR; S63536; S63536.
DR   AlphaFoldDB; P49362; -.
DR   SMR; P49362; -.
DR   PRIDE; P49362; -.
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   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) B,
FT                   mitochondrial"
FT                   /id="PRO_0000010747"
FT   MOD_RES         770
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1034 AA;  112780 MW;  713D6490B48C2932 CRC64;
     MERARRLAIL GRLVSQTKHN PSISSPALCS PSRYVSSLSP YVCSGTNVRS DRNLNGFGSQ
     VRTISVEALK PSDTFPRRHN SATPEEQTKM AEFVGFPNLD 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 FGVYHGPEGL
     KTIAKRVHGL AGTFASGLKK LGTVQVQDLP FFDTVKVTCA DSKAIAEEAY KHKMNLRIVD
     KNTITVAFDE TTTIEDVDTL FKVFALGKPV TFTAASIAPE 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 EQSQPLGTIA AAPWGSALIL PISYTYIAMM
     GSQGITNASK IAILNANYMA KRLENHYPIL FRGVNGTVAH EFIVDLRPLK TTAGIEPEDV
     AKRLIDYGFH GPTMSWPVPG TLMIEPTESE SKAELDRFCD ALISIRQEIA EIEKGNVDFN
     NNVIKGAPHP PQLLMADKWT KPYSREYAAY PAPWLRAAKF WPTTCRVDNV YGDRNLICTL
     QPPQEYEEKA EATA