ID   Q87NC6_VIBPA            Unreviewed;       958 AA.
AC   Q87NC6;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   SubName: Full=Diaminobutyrate-pyruvate transaminase & L-2,4-diaminobutyrate decarboxylase {ECO:0000313|EMBL:BAC60205.1};
GN   OrderedLocusNames=VP1942 {ECO:0000313|EMBL:BAC60205.1};
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC60205.1, ECO:0000313|Proteomes:UP000002493};
RN   [1] {ECO:0000313|EMBL:BAC60205.1, ECO:0000313|Proteomes:UP000002493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633 {ECO:0000313|Proteomes:UP000002493};
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).
RN   [2] {ECO:0007829|PDB:2QMA}
RP   X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 465-958.
RA   Osipiuk J., Sather A., Gu M., Joachimiak A.;
RT   "X-ray crystal structure of glutamate decarboxylase domain of
RT   diaminobutyrate-pyruvate transaminase and L-2,4-diaminobutyrate
RT   decarboxylase from Vibrio parahaemolyticus.";
RL   Submitted (JUL-2007) to the PDB data bank.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50};
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DR   EMBL; BA000031; BAC60205.1; -; Genomic_DNA.
DR   RefSeq; NP_798321.1; NC_004603.1.
DR   RefSeq; WP_005490729.1; NC_004603.1.
DR   PDB; 2QMA; X-ray; 1.81 A; A/B=465-958.
DR   PDBsum; 2QMA; -.
DR   AlphaFoldDB; Q87NC6; -.
DR   SMR; Q87NC6; -.
DR   GeneID; 1189449; -.
DR   KEGG; vpa:VP1942; -.
DR   PATRIC; fig|223926.6.peg.1857; -.
DR   eggNOG; COG0076; Bacteria.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_011856_1_1_6; -.
DR   EvolutionaryTrace; Q87NC6; -.
DR   Proteomes; UP000002493; Chromosome 1.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   CDD; cd06450; DOPA_deC_like; 1.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 2.
DR   Gene3D; 1.20.1650.10; PLP-dependent transferases; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 2.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR004637; Dat.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR00709; dat; 1.
DR   PANTHER; PTHR43552; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43552:SF1; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 2.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:2QMA}; Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR602129-50}; Pyruvate {ECO:0000313|EMBL:BAC60205.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002493}.
FT   MOD_RES         786
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   958 AA;  104387 MW;  449253F3231705BD CRC64;
     MSTAFEVDNT IANIFSSQVP LVEGTYDLTP DQVLLEQAEH ESEVRSYPRR LPIAIKQAYG
     CLVEDTRGQV FLDCLAGAGT LALGYNHPEI NQALKEQLDS GLPYQTLDIA TSAKTHFIKS
     VKSFLPQELG DNCVIQFCGP SGADAVEAAI KLAKQTTGRN TMFAFRGAYH GMTNGTMGMM
     GNLGTKARRT GLMSDVHFMP FPYNLRCPFG LGGDEGAKAS IRYIERLLND DEAGIMKPAA
     IIVEPVQGEG GVIPAPAFWL RELRRICDEH GILLIFDEIQ CGVGKSGYNF AFEEAGIVPD
     VLCLSKAIGG GLPMSLLVIN KQHDTWKPGE HTGTFRGNQL AMVSGAKALE IIQRDNLVEH
     ANVAGQYLRF GLENIQKRVN CIAEVRGKGL MLGVEIKNPN GELNKFGEPL ADGQLTLAIQ
     RAALERGLMV EKGGREGSVI RFLPPLIISF EQIDFALRVL EEAIIAAGGS HVEAAPQEEW
     KKHFIHTGEL GSAEFASVMS HTTSAMKSVF EQVNAPYSGM DPKALEDAIN AVDLDNKNAP
     LKSVIDDVAE LVAKNAIFTQ HPDCIAHLHT PPLMPAVAAE AMIAALNQSM DSWDQASSAT
     YVEQKVVNWL CDKYDLSEKA DGIFTSGGTQ SNQMGLMLAR DWIADKLSGH SIQKLGLPDY
     ADKLRIVCSK KSHFTVQKSA SWMGLGEKAV MTVDANADGT MDITKLDEVI AQAKAEGLIP
     FAIVGTAGTT DHGAIDDLDF IADMAVKHDM WMHVDGAYGG ALILSSHKSR LKGVERAHSI
     SVDFHKLFYQ TISCGALLVN DKSNFKFLLH HADYLNREHD ELPNLVDKSI ATTKRFDALK
     VFMTMQNVGP KALGDMYDHL LAQTLEVADM IRTNDQFELL AEPSLSTVLF RATHETADLD
     ELNKALRLEA LTRGIAVLGE TIVDGKTALK FTILNPCLTT SDFESLLSKI NMLAVELV
//