GCSPB_STAAM
ID GCSPB_STAAM Reviewed; 490 AA.
AC P64219; Q99TV9;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=SAV1535;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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; BA000017; BAB57697.1; -; Genomic_DNA.
DR RefSeq; WP_000202188.1; NC_002758.2.
DR AlphaFoldDB; P64219; -.
DR SMR; P64219; -.
DR World-2DPAGE; 0002:P64219; -.
DR PaxDb; P64219; -.
DR EnsemblBacteria; BAB57697; BAB57697; SAV1535.
DR KEGG; sav:SAV1535; -.
DR HOGENOM; CLU_004620_5_0_9; -.
DR OMA; MHINLHK; -.
DR PhylomeDB; P64219; -.
DR BioCyc; SAUR158878:SAV_RS08270-MON; -.
DR Proteomes; UP000002481; 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_0000167012"
FT MOD_RES 273
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00713"
SQ SEQUENCE 490 AA; 54783 MW; 6EC8CCBA16D35CBF CRC64;
MTSKSSPLIF ERSREGRYAY SLPKSDIKTN SVESLLDDKF IRKNKAEFPE VAELDLVRHY
TELSNKNFGV DNGFYPLGSC TMKYNPKINE KVARIPGFSE SHPLQDEDQV QGSLEIIYSL
QEELKEITGM DEVTLQPAAG AHGEWTALMI FKAYHENNGE GHRDEVIVPD SAHGTNPASA
SFAGFKSVTV KSNERGEVDI DDLKRVVNEN TAAIMLTNPN TLGIFEKNIM EIREIVHNAG
GLLYYDGANL NAIMDKVRPG DMGFDAVHLN LHKTFTGPHG GGGPGSGPVG VVKELASYLP
KPMVIKDGDK FKYDNDIKNS IGRVKPFYGN FGIYLRAYTY IRTMGATGLK EVSEAAVLNA
NYIKARLSEH FEIPYKQYCK HEFVLSGVRQ KEFGVRTLDM AKRLLDFGVH PPTIYFPLNV
EEGMMIEPTE TESKETLDYF IDTLISIAEE AKNDPDKVLE APHTTVIDRL DEATAARKPI
LKFENLKQEK