ID   GCSP_PECAS              Reviewed;         957 AA.
AC   Q6D974;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=ECA0745;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(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; BX950851; CAG73659.1; -; Genomic_DNA.
DR   RefSeq; WP_011092352.1; NC_004547.2.
DR   AlphaFoldDB; Q6D974; -.
DR   SMR; Q6D974; -.
DR   STRING; 218491.ECA0745; -.
DR   EnsemblBacteria; CAG73659; CAG73659; ECA0745.
DR   KEGG; eca:ECA0745; -.
DR   PATRIC; fig|218491.5.peg.743; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_3_2_6; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   Proteomes; UP000007966; 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; Reference proteome.
FT   CHAIN           1..957
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000227104"
FT   MOD_RES         708
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   957 AA;  104119 MW;  CF62740108BFA2A0 CRC64;
     MTQTLSQLEH DGAFIERHIG PSVSQQQHML SVVGATSLDA LIRQIVPADI QLPSPPAVGE
     AVTEHEALAE LKAIAGRNQR YKSYIGMGYS AVLMPPVILR NVLENPGWYT AYTPYQPEVS
     QGRLEALLNF QQVTQDLTGL DLASASLLDE ATAAAEAMAM AKRISKLKQA ERFFVADDVH
     PQTLDVVRTR AETFGFEIVV GKAEEALKDD AVFGVLLQQA GTTGELHDYS DLMAALKARK
     VVSCVASDIM ALVLLTAPGK QGADIVFGSA QRFGVPMGYG GPHAAFFACR DEHKRAMPGR
     IIGVSRDAAG NTAFRMAMQT REQHIRREKA NSNICTSQVL LANIAGMYAV FHGPEGLKRI
     AGRIHRLTDI LAAGLTQGGL LLRHRSWFDT LTIEVADKDV VLSRALSFGI NLRSDLASAV
     GITLDEATTR EDVLALFAVL LGDDHGLDIE ALDASIAQEV ATIPAGLLRH DAILSHPVFN
     RYHSETEMMR YLHRLARKDL ALNQAMIPLG SCTMKLNAAA EMLPITWPEF AELHPFCPPE
     QALGYRQMIE QLSGWLVQLT GYDAVCMQPN SGAQGEYAGL LAIRRYHESR NEAGRHLCLI
     PSSAHGTNPA SAQMAGMEVV VVACDKQGNI DLHDLREKAQ AAGEQLSCIM VTYPSTHGVY
     EETIREVCQI VHQYGGQVYL DGANMNAQVG ITTPGYIGAD VSHLNLHKTF CIPHGGGGPG
     MGPIGVKAHL APFVPGHQVV KIDGVLTEQG AVSAAPFGSA SILPISWMYI RMMGAEGLKQ
     ASQMAILNAN YIATRLQQAY PVLYTGRDGR VAHECILDIR PLKESTGISE MDIAKRLIDY
     GFHAPTMSFP VAGTLMVEPT ESESQVEIDR FIDAMLAIRS EINRVAQGEW PLDDNPLVNA
     PHTQAELVAD WAHPYSRELA VFPAGSEHKY WPSVKRLDDV YGDRNLFCSC VPMSDYA