ID   GCSP_YERPG              Reviewed;         959 AA.
AC   A9R4K8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=Glycine dehydrogenase (decarboxylating) {ECO:0000255|HAMAP-Rule:MF_00711};
DE            EC=1.4.4.2 {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine cleavage system P-protein {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine decarboxylase {ECO:0000255|HAMAP-Rule:MF_00711};
DE   AltName: Full=Glycine dehydrogenase (aminomethyl-transferring) {ECO:0000255|HAMAP-Rule:MF_00711};
GN   Name=gcvP {ECO:0000255|HAMAP-Rule:MF_00711};
GN   OrderedLocusNames=YpAngola_A3832;
OS   Yersinia pestis bv. Antiqua (strain Angola).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Angola;
RX   PubMed=20061468; DOI=10.1128/jb.01518-09;
RA   Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA   Achtman M., Lindler L.E., Ravel J.;
RT   "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT   new insights into the evolution and pangenome of the plague bacterium.";
RL   J. Bacteriol. 192:1685-1699(2010).
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_00711}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00711};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00711};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. {ECO:0000255|HAMAP-Rule:MF_00711}.
CC   -!- SIMILARITY: Belongs to the GcvP family. {ECO:0000255|HAMAP-
CC       Rule:MF_00711}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000901; ABX86860.1; -; Genomic_DNA.
DR   RefSeq; WP_002209947.1; NZ_CP009935.1.
DR   AlphaFoldDB; A9R4K8; -.
DR   SMR; A9R4K8; -.
DR   GeneID; 66844389; -.
DR   KEGG; ypg:YpAngola_A3832; -.
DR   PATRIC; fig|349746.12.peg.548; -.
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; 2.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR   HAMAP; MF_00711; GcvP; 1.
DR   InterPro; IPR003437; GcvP.
DR   InterPro; IPR049316; GDC-P_C.
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   NCBIfam; TIGR00461; gcvP; 1.
DR   PANTHER; PTHR11773:SF13; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 1.
DR   PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF21478; GcvP2_C; 1.
DR   Pfam; PF02347; GDC-P; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE   3: Inferred from homology;
KW   Oxidoreductase; Pyridoxal phosphate.
FT   CHAIN           1..959
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000132463"
FT   MOD_RES         708
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   959 AA;  104737 MW;  BDD898DA71EF98A5 CRC64;
     MTQNLSQLEH NDAFIQRHIG SSVEQQQQML AAVGASSLST LIQQIVPADI QLPGPPPVGE
     AATEHQALAE LKGIASQNQC YKSYIGMGYS PVLTPPVILR NMLENPGWYT AYTPYQPEVS
     QGRLEALLNF QQLTQDLTGL DLASASLLDE ATAAAESMAL AKRASKLKDA NRFFVADDVH
     PQTLDVVLTR AETFGFDVIV DRAEKVLELD GIFGVLLQQV GTTGELHDYS ALLAELKKRK
     IITSVAADIM ALVLLTAPGA QGADVVFGSA QRFGVPMGYG GPHAAFFACR DEFKRSMPGR
     IIGVSRDAAG NTALRMAMQT REQHIRREKA NSNICTSQVL LANIASLYAV YHGPQGLQRI
     AGRIHRMTDI LAAGLQHAGL TLRFKHWFDT LTVEVKDKAA VLARALSFGI NLRTDIHGAV
     GITLNETTSR EDIQTLFALF VGDNHGLDID QLDAAVSQHS QSIQDSMLRR DPILTHPVFN
     RYHSETEMMR YMHRLERKDL ALNQAMIPLG SCTMKLNAAA EMIPITWPEF AELHPFCPPE
     QAAGYQQMIG QLSQWLVQLT GYDAVCMQPN SGAQGEYAGL LAIRRYHESR NQANRHICLI
     PSSAHGTNPA SAQMAGMSVV VVACDKQGNI DLHDLRQKAE HAGDELSCIM VTYPSTHGVY
     EETIREVCQI VHQFGGQVYL DGANMNAQVG ITTPGYIGAD VSHLNLHKTF CIPHGGGGPG
     MGPIGVKAHL APFVPGHSVV QIDGMTTQQG AVSAAPFGSA SILPISWMYI RMMGADGLKQ
     ASQVAILNAN YIATRLKNAY PVLYTGHDGR VAHECILDIR PLKEATGISE MDIAKRLIDF
     GFHAPTMSFP VAGTLMVEPT ESESKVELDR FIDAMLAIRA EIEKVAQGEW PLEDNPLVNA
     PHTQAELVGE WTHPYSRELA VFPVAGVLEN KYWPTVKRLD DVYGDRNLFC SCVPISDYE
//