ID W6SJP6_9CLOT Unreviewed; 436 AA.
AC W6SJP6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Probable glycine dehydrogenase (decarboxylating) subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
DE EC=1.4.4.2 {ECO:0000256|HAMAP-Rule:MF_00712};
DE AltName: Full=Glycine cleavage system P-protein subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
DE AltName: Full=Glycine decarboxylase subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
DE AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) subunit 1 {ECO:0000256|HAMAP-Rule:MF_00712};
GN Name=gcvPA {ECO:0000256|HAMAP-Rule:MF_00712,
GN ECO:0000313|EMBL:CDM69920.1};
GN ORFNames=CM240_2803 {ECO:0000313|EMBL:CDM69920.1};
OS Clostridium bornimense.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1216932 {ECO:0000313|EMBL:CDM69920.1, ECO:0000313|Proteomes:UP000019426};
RN [1] {ECO:0000313|EMBL:CDM69920.1, ECO:0000313|Proteomes:UP000019426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M2/40 {ECO:0000313|Proteomes:UP000019426};
RA Wibberg D., Puehler A., Schlueter A.;
RT "Complete genome sequence of Clostridum sp. M2/40.";
RL Submitted (NOV-2013) 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:0000256|ARBA:ARBA00003788, ECO:0000256|HAMAP-
CC Rule:MF_00712}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage
CC complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-
CC L-lysyl-[glycine-cleavage complex H protein]; 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 Evidence={ECO:0000256|ARBA:ARBA00043839, ECO:0000256|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:0000256|HAMAP-Rule:MF_00712}.
CC -!- SIMILARITY: Belongs to the GcvP family. N-terminal subunit subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00712}.
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DR EMBL; HG917869; CDM69920.1; -; Genomic_DNA.
DR RefSeq; WP_044040106.1; NZ_HG917869.1.
DR AlphaFoldDB; W6SJP6; -.
DR STRING; 1216932.CM240_2803; -.
DR KEGG; clt:CM240_2803; -.
DR PATRIC; fig|1216932.3.peg.2765; -.
DR eggNOG; COG0403; Bacteria.
DR HOGENOM; CLU_004620_0_2_9; -.
DR OrthoDB; 9771867at2; -.
DR Proteomes; UP000019426; Chromosome 2.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_00712; GcvPA; 1.
DR InterPro; IPR023010; GcvPA.
DR InterPro; IPR049315; GDC-P_N.
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; GLYCINE CLEAVAGE SYSTEM P-PROTEIN; 1.
DR PANTHER; PTHR42806:SF1; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 1.
DR Pfam; PF02347; GDC-P; 1.
DR PIRSF; PIRSF006815; GcvPA; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00712}; Reference proteome {ECO:0000313|Proteomes:UP000019426}.
FT DOMAIN 3..433
FT /note="Glycine cleavage system P-protein N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02347"
SQ SEQUENCE 436 AA; 47613 MW; 93D53AEE91AAFA20 CRC64;
MGSYVSTTIK EEKEMLDAIG VNSIDDLFKN VPEEVKIKGE LNLPDGLSEM EVKKLMESIA
NKNKVFCSIF RGAGAYNHYI PSIVNSVTSK EEFVTAYTPY QAEISQGILQ SIFEYQTMIC
NLTGMDVSNA SVYDGATAAA ESLAMCRDRK HNKAYVSATT NPQVIETMKT YCSGSGMELV
IVPEKDGVTD IEFLKNNLEA GAACLYVQQP NFYGNIEDAS ELGECIHSVG GKYVMGVYPI
SLGVIKTPRE YGADIAVGEG QPLGMPLSCG GPYLGFMASI DSMVRKLPGR IVGETTDVEG
KRAFVLTLQA REQHIRREKA SSNICSNEAL CALTASVYLA AMGSKGIKEV ASQSMSKAKY
MSEKLSEVGQ KLKYDKPFFN EFVTISEAPV RSVLKALEDN GILGGYPLSD NEILWCCTEM
NSKEEIDKVV EILKEV
//
