GCSPA_BACAC
ID GCSPA_BACAC Reviewed; 447 AA.
AC C3LKQ3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
DE EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00712};
DE AltName: Full=Glycine cleavage system P-protein subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
DE AltName: Full=Glycine decarboxylase subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 1 {ECO:0000255|HAMAP-Rule:MF_00712};
GN Name=gcvPA {ECO:0000255|HAMAP-Rule:MF_00712}; OrderedLocusNames=BAMEG_4483;
OS Bacillus anthracis (strain CDC 684 / NRRL 3495).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=568206;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 684 / NRRL 3495;
RA Dodson R.J., Munk A.C., Brettin T., Bruce D., Detter C., Tapia R., Han C.,
RA Sutton G., Sims D.;
RT "Genome sequence of Bacillus anthracis str. CDC 684.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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_00712}.
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_00712};
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_00712}.
CC -!- SIMILARITY: Belongs to the GcvP family. N-terminal subunit subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00712}.
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DR EMBL; CP001215; ACP14616.1; -; Genomic_DNA.
DR RefSeq; WP_000903231.1; NC_012581.1.
DR AlphaFoldDB; C3LKQ3; -.
DR SMR; C3LKQ3; -.
DR GeneID; 64199575; -.
DR KEGG; bah:BAMEG_4483; -.
DR HOGENOM; CLU_004620_0_2_9; -.
DR OMA; MYDGASA; -.
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 GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR CDD; cd00613; GDC-P; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00712; GcvPA; 1.
DR InterPro; IPR023010; GcvPA.
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; PTHR42806; PTHR42806; 1.
DR Pfam; PF02347; GDC-P; 1.
DR PIRSF; PIRSF006815; GcvPA; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 3: Inferred from homology;
KW Oxidoreductase.
FT CHAIN 1..447
FT /note="Probable glycine dehydrogenase (decarboxylating)
FT subunit 1"
FT /id="PRO_1000147976"
SQ SEQUENCE 447 AA; 49421 MW; 93AAE031125E3A64 CRC64;
MLHRYLPMTE EDKKEMLQTI GVQTIDELFS DIPESVRFKG DLKIKEAKSE PELLKELSQM
ASKNANLKEY ASFLGAGVYD HYAPVIVDHV ISRSEFYTAY TPYQPEISQG ELQAIFEFQT
MICELTGMDV ANSSMYDGGT ALAEAAMLAA GHTRKKKILV SSAVHPESRA VLETYAKGQH
LEVVEINHKD GVTDLDVLQS EVDDTVACVI VQYPNFFGQV EKLADIEKIV HQQKSLFIVS
SNPLSLGALT PPGKFGADIV IGDAQPFGIP TQFGGPHCGY FATTKAFMRK IPGRLVGQTV
DSDGKRGFVL TLQAREQHIR RDKATSNICS NQALNALAAS VAMTALGKQG VKEMARQNIS
KAQYAKRQFE AKGFTVTFAG PFFNEFVVDC KRPVKEVNDA LLQKNIIGGY DLGRDYKEHE
NHMLVAVTEL RTKEEIDTLV NEMGAIQ