GCSPB_STAAC
ID GCSPB_STAAC Reviewed; 490 AA.
AC Q5HFM4;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 94.
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}; OrderedLocusNames=SACOL1593;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000046; AAW38209.1; -; Genomic_DNA.
DR RefSeq; WP_000202192.1; NC_002951.2.
DR AlphaFoldDB; Q5HFM4; -.
DR SMR; Q5HFM4; -.
DR EnsemblBacteria; AAW38209; AAW38209; SACOL1593.
DR KEGG; sac:SACOL1593; -.
DR HOGENOM; CLU_004620_5_0_9; -.
DR OMA; MHINLHK; -.
DR Proteomes; UP000000530; 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; IPR000192; Aminotrans_V_dom.
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; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 3: Inferred from homology;
KW Oxidoreductase; Pyridoxal phosphate.
FT CHAIN 1..490
FT /note="Probable glycine dehydrogenase (decarboxylating)
FT subunit 2"
FT /id="PRO_0000167011"
FT MOD_RES 273
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00713"
SQ SEQUENCE 490 AA; 54781 MW; 5D01D5D7A35E07D7 CRC64;
MTSKSSPLIF ERSREGRYAY SLPKSDIKTN SVESLLDDKF IRKNKAEFPE VAELDLVRHY
TELSNKNFGV DNGFYPLGSC TMKYNPKINE KVARIPGFSE SHPLQDEDQV QGSLEIIYSL
QEELKEITGM DEVTLQPAAG AHGEWTALMI FKAYHENNGE GHRDEVIVPD SAHGTNPASA
SFAGFKSVTV KSNERGEVNI DDLKRVVNEN TAAIMLTNPN TLGIFEKNIM EIREIVHNAG
GLLYYDGANL NAIMDKVRPG DMGFDAVHLN LHKTFTGPHG GGGPGSGPVG VVKELASYLP
KPMVIKDGDK FKYDNDIKNS IGRVKPFYGN FGIYLRAYTY IRTMGATGLK EVSEAAVLNA
NYIKARLSKH FEIPYKQYCK HEFVLSGVRQ KEFGVRTLDM AKRLLDFGVH PPTIYFPLNV
EEGMMIEPTE TESKETLDYF IDTLISIAEE AKNDPDKVLE APHTTVIDRL DEATAARKPI
LKFENLKQEK