ID   GCSP_VIBPA              Reviewed;         954 AA.
AC   Q87I05;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 107.
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=VPA0801;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(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}.
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; BA000032; BAC62144.1; -; Genomic_DNA.
DR   RefSeq; NP_800311.1; NC_004605.1.
DR   RefSeq; WP_005478418.1; NC_004605.1.
DR   AlphaFoldDB; Q87I05; -.
DR   SMR; Q87I05; -.
DR   GeneID; 1191490; -.
DR   KEGG; vpa:VPA0801; -.
DR   PATRIC; fig|223926.6.peg.3732; -.
DR   eggNOG; COG0403; Bacteria.
DR   eggNOG; COG1003; Bacteria.
DR   HOGENOM; CLU_004620_1_1_6; -.
DR   Proteomes; UP000002493; Chromosome 2.
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; Reference proteome.
FT   CHAIN           1..954
FT                   /note="Glycine dehydrogenase (decarboxylating)"
FT                   /id="PRO_0000166945"
FT   MOD_RES         704
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00711"
SQ   SEQUENCE   954 AA;  104123 MW;  06CE72937E173D84 CRC64;
     MTELLQSLST QNEFVGRHNG PKLSDQQKML EAINAVSLDA LISETVPANI RLEQPMTLAE
     AKSEADMLAT MKQFAKQNQV KRTFIGQGYY NTFTPNVILR NVLENPGWYT AYTPYQPEIS
     QGRLESLLNF QQMVIDLTGM EIANASLLDE ATAAAEAMTL CKRAGKSKSN VFFVADDVHP
     QTIEVVKTRA KFIGFEVLVG SLESLPEQDV FGALVQYPST TGEVRDLTDI IAKAQANKTL
     VTVATDLLAC TLLKPAGEMG ADVAIGSAQR FGVPMGYGGP HAAFMATRDK HKRTMPGRVI
     GVSIDAKGNQ ALRMAMQTRE QHIRREKATS NICTAQALLA NMASFYAVYH GAEGLRTIAR
     RTHHMTAILA AGLTKGGFEL AHNSFFDTIT INTGEKTQDL YTKALAADIN LRVLPGKLGI
     SLDETTTVAD VEALFAIFGV KEDVTALSTE VAGNEFAAIP EALRRTSEYL THPVFNTYHS
     ETQMMRYLKQ LENKDFSLTH GMIPLGSCTM KLNAAAEMIP ITWPEFGSIH PFAPAEQAAG
     YAALAKDLKE KLCEITGYDA FSLQPNSGAS GEYAGLIAIQ RYHESRGEGH RNVCLIPSSA
     HGTNPATASM VSMKVVVVKC DDEGNIDIDD LAAKIEKHKD NLSSIMITYP STHGVYEEKV
     KEVCEMVHAA GGQVYLDGAN MNAQVGLTSP GFIGSDVSHL NLHKTFCIPH GGGGPGMGPI
     GVKSHLAPFL PGHIENGVEG EDFAVSAADF GSASILPISW AYIAMMGEAG LSNATKVAIL
     NANYVMERLR PHYPVLYRGK NGRVAHECII DIRPLKEETG ISEEDIAKRL MDYGFHAPTM
     SFPVAGTLMV EPTESEDLAE LNRFCDAMIS IREEMTKVKN GEWPLENNPL VNAPHTQVDL
     SAEEWDRPYS RELGCFPSKA TKSWKYWPTV NRVDNVYGDR NLICSCPSID NYED
//