ID   GCSP_YERE8              Reviewed;         959 AA.
AC   A1JPN3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 87.
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}; OrderedLocusNames=YE3391;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
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=(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_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}.
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DR   EMBL; AM286415; CAL13417.1; -; Genomic_DNA.
DR   RefSeq; WP_011817028.1; NC_008800.1.
DR   RefSeq; YP_001007560.1; NC_008800.1.
DR   AlphaFoldDB; A1JPN3; -.
DR   SMR; A1JPN3; -.
DR   STRING; 393305.YE3391; -.
DR   EnsemblBacteria; CAL13417; CAL13417; YE3391.
DR   KEGG; yen:YE3391; -.
DR   PATRIC; fig|393305.7.peg.3601; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_6; -.
DR   OMA; CVPMSEY; -.
DR   Proteomes; UP000000642; 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; 2.
DR   Gene3D; 3.40.640.10; -; 2.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   HAMAP; MF_00711; GcvP; 1.
DR   InterPro; IPR003437; GcvP.
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; PF02347; GDC-P; 2.
DR   SUPFAM; SSF53383; SSF53383; 2.
DR   TIGRFAMs; TIGR00461; gcvP; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Pyridoxal phosphate.
FT   CHAIN           1..959
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000045629"
FT   MOD_RES         708
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   959 AA;  104678 MW;  5B50694291651441 CRC64;
     MTQNLSQLEH NDAFIQRHIG SSAEQQQQML AAVGANSLST LIQQIVPADI QLPSPPPVGE
     AATEHQALAE LKGIASQNQR YKSYIGMGYS PVLTPPVILR NMLENPGWYT AYTPYQPEVS
     QGRLEALLNF QQLTQDLTGL DLASASLLDE ATAAAESMAL AKRASKLKDA NRFFVADDVH
     PQTLDVVLTR AETFGFEVIV DRAEKVLELD GVFGVLLQQV GTTGELHDYS ALLAELKKRK
     IITSVAADIM ALVLLTAPGK QGADVVFGSA QRFGVPMGYG GPHAAFFACR DEFKRSMPGR
     IIGVSRDAAG NTALRMAMQT REQHIRREKA NSNICTSQVL LANIASLYAV YHGPQGLQRI
     AGRIHRMTDI LAAGLQQAGL ALRFTHWFDT LTVEVKDKAA VLARALSFGI NLRTDIHGAV
     GITLDETTSR EDLQILFTLL VGDNHGLDID LLDAKVSQNS QSIQTGMLRQ EPILTHPVFN
     RYHSETEMMR YMHRLERKDL ALNQAMIPLG SCTMKLNAAA EMIPITWPEF AELHPFCPPE
     QAAGYQQMIG QLSQWLVQLT GYDAVCMQPN SGAQGEYAGL LAIRRYHESR NQASRHICLI
     PSSAHGTNPA SAQMAGMSVV VVACDKQGNI DLHDLRQKAG EAGDELSCIM VTYPSTHGVY
     EETIREVCQI VHQFGGQVYL DGANMNAQVG ITTPGYIGAD VSHLNLHKTF CIPHGGGGPG
     MGPIGVKAHL APFVPGHSVV QIDGMTTQQG AVSAAPFGSA SILPISWMYI RMMGADGLKQ
     ASQVAILNAN YIATRLKEAY PVLYTGHDGS VAHECILDIR PLKEATGISE MDIAKRLIDF
     GFHAPTMSFP VAGTLMVEPT ESESKVELDR FIDAMLAIRA EIEKVARGEW PLEDNPLVNA
     PHTQAELVGE WQHPYSRELA VFPVAGVMEN KYWPSVKRLD DVYGDRNLFC SCVPISDYE