ID   GCSP_VIBVY              Reviewed;         954 AA.
AC   Q7MEH9;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 118.
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=VVA0691;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage
CC         complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-
CC         L-lysyl-[glycine-cleavage complex H protein]; 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; BA000038; BAC96717.1; -; Genomic_DNA.
DR   RefSeq; WP_011152031.1; NC_005140.1.
DR   AlphaFoldDB; Q7MEH9; -.
DR   SMR; Q7MEH9; -.
DR   STRING; 672.VV93_v1c36900; -.
DR   KEGG; vvy:VVA0691; -.
DR   PATRIC; fig|196600.6.peg.3886; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_6; -.
DR   Proteomes; UP000002675; Chromosome II.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR   HAMAP; MF_00711; GcvP; 1.
DR   InterPro; IPR003437; GcvP.
DR   InterPro; IPR049316; GDC-P_C.
DR   InterPro; IPR049315; GDC-P_N.
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   NCBIfam; TIGR00461; gcvP; 1.
DR   PANTHER; PTHR11773:SF13; GLYCINE DEHYDROGENASE (DECARBOXYLATING); 1.
DR   PANTHER; PTHR11773; GLYCINE DEHYDROGENASE, DECARBOXYLATING; 1.
DR   Pfam; PF21478; GcvP2_C; 1.
DR   Pfam; PF02347; GDC-P; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE   3: Inferred from homology;
KW   Oxidoreductase; Pyridoxal phosphate.
FT   CHAIN           1..954
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000166947"
FT   MOD_RES         704
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   954 AA;  104208 MW;  FC6C3127F6357598 CRC64;
     MTELLQSLNT QHEFVGRHNG PNHADQQKML STINAESLDA LIAQTVPAQI RLEKPMQLAE
     AQSEADMLAS IKKFADLNQV KRTFIGQGYY NTFTPNVILR NVLENPGWYT AYTPYQPEIS
     QGRLESLLNY QQMVMDLTGM DIANASLLDE ATAAAEAMTL CQRAGKSKSK VFFVADDVHP
     QTIEVIKTRA KYFGFDVVIG NVDALPQTEA FGALLQYPST TGEVRDLTDV IAQAQANKTL
     VSVATDLLAS ALVKPAGEMG ADVVIGSAQR FGVPMGYGGP HAAFMATREQ HKRTMPGRVI
     GVSIDAKGNQ ALRMAMQTRE QHIRREKATS NICTAQALLA NMASFFAVYH GEEGIRTIAR
     RTHHMTAILA AGLTKSGYEL AHNAFFDTIT INTGDKTQAL YAKAQAADIN LRLLDGQIGI
     SFDETTTVAD IDALFAIFDV KESVNALSTD IAGNEFAAIP EACRRTSRFL SHPVFNTHHS
     ETQMMRYLKQ LENKDFSLTH GMIPLGSCTM KLNAAAEMIP VTWPEFGALH PFAPIEQAAG
     YTALAEDLKA KLCEITGYDA FSLQPNSGAS GEYAGLIAIQ RYHESRGEGH RNVCLIPSSA
     HGTNPATAAM VSMKVVVVKC DENGNIDLVD LAAKIEKHQE NLSSIMITYP STHGVYEEQV
     KEVCEMVHAA GGQVYLDGAN MNAQVGLTSP GFIGSDVSHL NLHKTFCIPH GGGGPGMGPI
     GVKSHLAPFL PGHIENGVEG KEFAVSAADL GSASILPISW AYIAMMGADG LTEATKVAIL
     NANYVMERLR PHYPVLYRGT NGRVAHECII DIRPLKEETG ISEEDIAKRL MDYGFHAPTM
     SFPVAGTLMV EPTESEDLEE LDRFCDAMIA IREEMTKVKN GEWPLENNPL VNAPHTQVDL
     MEEQWDRPYP REIACFPSAA TKRSKYWPTV NRVDNVYGDR NLVCSCPGIE NYEE
//