ID   GCSPB_BACCN             Reviewed;         491 AA.
AC   A7GSN6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE            EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE   AltName: Full=Glycine cleavage system P-protein subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE   AltName: Full=Glycine decarboxylase subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 2 {ECO:0000255|HAMAP-Rule:MF_00713};
GN   Name=gcvPB {ECO:0000255|HAMAP-Rule:MF_00713};
GN   OrderedLocusNames=Bcer98_2913;
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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. {ECO:0000255|HAMAP-Rule:MF_00713}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00713};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00713};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. In this organism, the P 'protein' is a heterodimer of two
CC       subunits. {ECO:0000255|HAMAP-Rule:MF_00713}.
CC   -!- SIMILARITY: Belongs to the GcvP family. C-terminal subunit subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00713}.
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DR   EMBL; CP000764; ABS23144.1; -; Genomic_DNA.
DR   RefSeq; WP_012095372.1; NC_009674.1.
DR   AlphaFoldDB; A7GSN6; -.
DR   SMR; A7GSN6; -.
DR   STRING; 315749.Bcer98_2913; -.
DR   EnsemblBacteria; ABS23144; ABS23144; Bcer98_2913.
DR   GeneID; 56418457; -.
DR   KEGG; bcy:Bcer98_2913; -.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_5_0_9; -.
DR   OMA; MHINLHK; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000002300; Chromosome.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR   CDD; cd00613; GDC-P; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_00713; GcvPB; 1.
DR   InterPro; IPR023012; GcvPB.
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; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Pyridoxal phosphate.
FT   CHAIN           1..491
FT                   /note="Probable glycine dehydrogenase (decarboxylating)
FT                   subunit 2"
FT                   /id="PRO_1000083227"
FT   MOD_RES         273
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00713"
SQ   SEQUENCE   491 AA;  54867 MW;  6C31F335795C2718 CRC64;
     MKNQDQALIF EMSKEGRVGY SLPQLDVEEV KLEDVFESNY IRAEDAELPE VSELDIMRHY
     TALSNRNHGV DSGFYPLGSC TMKYNPKINE NVARFPGFAN IHPLQDEKTV QGAMELMYDL
     QEHLVEITGM DAVTLQPAAG AHGEWTGLML IRAYHEANGD HNRTKVIVPD SAHGTNPASA
     TVAGFETITV KSNEHGLVDL EDLKRVVNEE TAALMLTNPN TLGLFEENIL EMAEIVHNAG
     GKLYYDGANL NAVLSQARPG DMGFDVVHLN LHKTFTGPHG GGGPGSGPVG VKEDLIPFLP
     KPILEKTENG YHFNYDRPQA IGRVKPFYGN FGINVRAYTY IRSMGPDGLR AVTENAVLNA
     NYMMRRLAPY YDLPFDRHCK HEFVLSGRCQ KKLGVRTLDI AKRLLDFGYH PPTIYFPLNV
     EECIMIEPTE TESKETLDGF IDKMIQIAKE AKENPEIVQE APHTTVITRL DETMAARKPI
     LRYQKPTPVQ V