ID   GCSP_YERPE              Reviewed;         959 AA.
AC   Q8ZHI8; Q0WID5;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 128.
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=YPO0905, y3292, YP_3602;
OS   Yersinia pestis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO-92 / Biovar Orientalis;
RX   PubMed=11586360; DOI=10.1038/35097083;
RA   Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA   Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA   Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA   Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA   Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA   Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA   Stevens K., Whitehead S., Barrell B.G.;
RT   "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL   Nature 413:523-527(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIM10+ / Biovar Mediaevalis;
RX   PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA   Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA   Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA   Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA   Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT   "Genome sequence of Yersinia pestis KIM.";
RL   J. Bacteriol. 184:4601-4611(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91001 / Biovar Mediaevalis;
RX   PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA   Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA   Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA   Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA   Wang J., Huang P., Yang R.;
RT   "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT   avirulent to humans.";
RL   DNA Res. 11:179-197(2004).
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; AL590842; CAL19572.1; -; Genomic_DNA.
DR   EMBL; AE009952; AAM86842.1; -; Genomic_DNA.
DR   EMBL; AE017042; AAS63752.1; -; Genomic_DNA.
DR   PIR; AB0111; AB0111.
DR   RefSeq; WP_002209947.1; NZ_WUCM01000038.1.
DR   RefSeq; YP_002345953.1; NC_003143.1.
DR   AlphaFoldDB; Q8ZHI8; -.
DR   SMR; Q8ZHI8; -.
DR   IntAct; Q8ZHI8; 7.
DR   STRING; 214092.YPO0905; -.
DR   PaxDb; Q8ZHI8; -.
DR   DNASU; 1148239; -.
DR   EnsemblBacteria; AAM86842; AAM86842; y3292.
DR   EnsemblBacteria; AAS63752; AAS63752; YP_3602.
DR   GeneID; 66844389; -.
DR   KEGG; ype:YPO0905; -.
DR   KEGG; ypk:y3292; -.
DR   KEGG; ypm:YP_3602; -.
DR   PATRIC; fig|214092.21.peg.1179; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_6; -.
DR   OMA; CVPMSEY; -.
DR   Proteomes; UP000000815; Chromosome.
DR   Proteomes; UP000001019; Chromosome.
DR   Proteomes; UP000002490; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005960; C:glycine cleavage complex; IBA:GO_Central.
DR   GO; GO:0016594; F:glycine binding; IBA:GO_Central.
DR   GO; GO:0004375; F:glycine dehydrogenase (decarboxylating) activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IBA:GO_Central.
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; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..959
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000166952"
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