ID   GCSP_EDWI9              Reviewed;         960 AA.
AC   C5BAT0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=NT01EI_3351;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) 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: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}.
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; CP001600; ACR70489.1; -; Genomic_DNA.
DR   RefSeq; WP_015872563.1; NC_012779.2.
DR   AlphaFoldDB; C5BAT0; -.
DR   SMR; C5BAT0; -.
DR   STRING; 67780.B6E78_08440; -.
DR   PRIDE; C5BAT0; -.
DR   EnsemblBacteria; ACR70489; ACR70489; NT01EI_3351.
DR   GeneID; 7959651; -.
DR   KEGG; eic:NT01EI_3351; -.
DR   PATRIC; fig|634503.3.peg.2978; -.
DR   HOGENOM; CLU_004620_1_1_6; -.
DR   OMA; CVPMSEY; -.
DR   OrthoDB; 70707at2; -.
DR   PHI-base; PHI:2961; -.
DR   Proteomes; UP000001485; 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..960
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000212654"
FT   MOD_RES         709
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   960 AA;  104902 MW;  C429F74ED788B891 CRC64;
     MTQTLTQLEN SDAFIARHIG PTPEEQQQML AQIGAADLDT LLARIVPADI QLPAAPPIGA
     ACSEQQALDE LRAIAAQNQC YRSFIGMGYY GVQTPPAIQR NMLENPGWYT AYTPYQPEVS
     QGRLEALLNF QQMTLDLTGL DLASASLLDE ATAAAEAMGL ARRASRLKQA NTFFIAQDVH
     PQTIDVVCTR AQSCGVEVII DDARRAADHR DLFGVLLQQV GTQGDLHDYR ALMDSLRERG
     VITCMAADPL ALVLLEAPGR QGADVVFGSA QRFGVPMGYG GPHAAFFACR EAFKRAMPGR
     IIGVARDAAG EPALRMAMQT REQHIRREKA NSNICTSQVL LANIAGMYAV YHGPQGLRRI
     AERVHRLADI LALGLQQKGV TLRNHCWFDT LTVAVPDKGA VLARALGFGI NLRGDLDGAV
     GISFDECSTR DDLEALFTIL LGDGHALDID TLDTLVQEAC EGSIPAALLR REPILTHPVF
     NRYHSETALM RYMHALERRD LALNQAMIPL GSCTMKLNAA AEMIPITWPE FAALHPFCPP
     EQAQGYRLLL SQLAEWLVQL TGYDAVCLQP NSGAQGEYAG LLAIRRYHES RGEGQRTRCL
     IPASAHGTNP ASAQMAGMEV EVVACDEQGN IDLHDLRERA RQAGERLAAI MVTYPSTHGV
     YEETIREVCQ IVHQYGGQVY LDGANMNAQV GITTPGYIGA DVSHLNLHKT FAIPHGGGGP
     GMGPIGVKAH LAPFVPGHRV VQLAGLTTRQ GAVSAAPFGS ASILPISWMY IRMMGAEGLR
     RASTVAILNA NYIARRLGAV YPVLYRGKEG YVAHECILDL RPLKARSGIS EMDIAKRLID
     YGFHAPTMSF PVAGTLMVEP TESENKAELD RFIAAMLAIH DEITRVETGE WPLQDNPLVN
     APHTQRELVG EWHHPYGREL AVFPTPQTRE NKYWPAVKRL DDVYGDRHLQ CSCPPLSDWA