ID   GCSP_VIBC3              Reviewed;         954 AA.
AC   A5EYY8; C3M807;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=VC0395_0955, VC395_A0313;
OS   Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS   O395).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=345073;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA   Heidelberg J.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
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; CP000626; ABQ18474.1; -; Genomic_DNA.
DR   EMBL; CP001236; ACP11153.1; -; Genomic_DNA.
DR   RefSeq; WP_000137693.1; NZ_JAACZH010000047.1.
DR   AlphaFoldDB; A5EYY8; -.
DR   SMR; A5EYY8; -.
DR   STRING; 345073.VC395_A0313; -.
DR   EnsemblBacteria; ABQ18474; ABQ18474; VC0395_0955.
DR   GeneID; 57741716; -.
DR   KEGG; vco:VC0395_0955; -.
DR   KEGG; vcr:VC395_A0313; -.
DR   PATRIC; fig|345073.21.peg.3072; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_6; -.
DR   OMA; DEHCHPQ; -.
DR   Proteomes; UP000000249; Chromosome 1.
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; 1.
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..954
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_1000072766"
FT   MOD_RES         704
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   954 AA;  103954 MW;  B2336F8CE80C806A CRC64;
     MTELLHSLST QNEFVARHNG PDKQEQATML KTVNAESLDA LIAQTVPAQI RLEAPMQLAP
     AQSEADMLAT MKSFAKLNQL KRTFIGQGYY NTFTPNVILR NVMENPGWYT AYTPYQPEIS
     QGRLESLLNY QQMVMDLTAM EIANASLLDE ATAAAEAMAL CQRAGKSKSN LFFVADDVHP
     QTIEVVKTRA AFLGFEVKVD SIDNITQQEA FGALLQYPGT TGEVRDLTDI IAKAQANKTL
     VTVATDLLAS VLLKPAGEMG ADVVIGSAQR FGVPMGYGGP HAAFMATRDA HKRTMPGRVI
     GVSIDAKGNQ ALRMAMQTRE QHIRREKATS NICTAQALLA NMAAFYAVYH GPQGLRTIAR
     RAHHLTAILA AGLTKAGYEL AHQHFFDTLA INTGAKTDAL YQAAQQANIN LRKLPNQLGV
     SFDETTTVAD VEALFAIFGI KEEVHALSDR IATNELAAIP ESCRRQSAFL THPVFNTHHS
     ETQMLRYMKH LENKDFSLTH GMIPLGSCTM KLNATAEMIP VTWPEFGALH PFVPKAQAAG
     YAALAEDLKQ KLCEITGYDA FSLQPNSGAS GEYAGLVAIQ RYHQSRGEGH RNVCLIPSSA
     HGTNPATAAM VSMKVVVVKC DENGNIDMVD LADKIEKHKD HLSSIMITYP STHGVYEQQV
     REVCEMVHAA GGQVYLDGAN MNAQVGLTSP GFIGSDVSHL NLHKTFCIPH GGGGPGMGPI
     GVKSHLAPFL PGHIEGGVEG SDFAVSAADL GSASILPISW AYIAMMGADG LAEATKLAIL
     NANYVMERLR PHYPILYRGA NGRVAHECII DIRPLKEETG ISEEDIAKRL MDYGFHAPTM
     SFPVAGTLMV EPTESEDLAE LDRFCDALIA IRGEIDKVKN GEWPLESNPL VHAPHTQADL
     REEKWDRPYS REIACFPSAH TKASKYWPTV NRVDNVYGDR NLVCSCPSID SYQD