ID   Q9KLY6_VIBCH            Unreviewed;       465 AA.
AC   Q9KLY6;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   SubName: Full=Aminotransferase, class III {ECO:0000313|EMBL:AAF96506.1};
GN   OrderedLocusNames=VC_A0605 {ECO:0000313|EMBL:AAF96506.1};
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277 {ECO:0000313|EMBL:AAF96506.1, ECO:0000313|Proteomes:UP000000584};
RN   [1] {ECO:0000313|EMBL:AAF96506.1, ECO:0000313|Proteomes:UP000000584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961
RC   {ECO:0000313|Proteomes:UP000000584};
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D., Ermolaeva M.D.,
RA   Vamathevan J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.,
RA   Utterback T., Fleishmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; AE003853; AAF96506.1; -; Genomic_DNA.
DR   PIR; A82438; A82438.
DR   RefSeq; NP_232994.1; NC_002506.1.
DR   RefSeq; WP_000846442.1; NZ_LT906615.1.
DR   AlphaFoldDB; Q9KLY6; -.
DR   STRING; 243277.VC_A0605; -.
DR   DNASU; 2612725; -.
DR   EnsemblBacteria; AAF96506; AAF96506; VC_A0605.
DR   KEGG; vch:VC_A0605; -.
DR   PATRIC; fig|243277.26.peg.3232; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_4_0_6; -.
DR   Proteomes; UP000000584; Chromosome 2.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:AAF96506.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000584};
KW   Transferase {ECO:0000313|EMBL:AAF96506.1}.
SQ   SEQUENCE   465 AA;  51491 MW;  CC0B0B297F24E28C CRC64;
     MKTFDPLSSY SPTHWRSEGD INTTAARRDW LTHVNDETTQ NLLQRDANVF LHQAMSTPCL
     APLASAAGCY LYDVSGKSYL DFHGNNVHQL GHGHPQVIEK ITEQMQTLPF APRRFTHETA
     IRCAEKLTEI AGGELNRVLF APGGTSVIGM ALKLARHITQ NFKVVSLWDA FHGASLDAIS
     VGGEACFRQG MGPLMAGVER IPPAITYRGA FPREDGSDVH YADYLEYVIE KEGGIGAFIA
     EAVRNTDVQV PSRAYWQRVR EICDKHNVLL IIDDIPNGMG RSGEWFTHQA FGIEPDILCI
     GKGLGAGLIP IAALLTKEKY NTAAQVSLGH YTHEKSPLGC AAALATIEVI EQHNLLAKVH
     ADSIYMRQRL SQMQQQFSLI GDVRGIGLLW GIELVIDRHT KQRAHDEAEA ILYHCLRHGL
     SFKVSQGNVI QLSPPLIISR QELDQALDIL YSALLAISQQ MNYSY
//