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}; 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}.
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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
//
