ID   CQSA_VIBC1              Reviewed;         393 AA.
AC   A7N6R9; Q693Z5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=CAI-1 autoinducer synthase;
DE            EC=2.3.-.-;
DE   AltName: Full=Cholerae quorum-sensing autoinducer;
GN   Name=cqsA; OrderedLocusNames=VIBHAR_06088;
OS   Vibrio campbellii (strain ATCC BAA-1116).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=2902295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION AS THE CAI-1 SYNTHASE.
RX   PubMed=15466044; DOI=10.1128/jb.186.20.6902-6914.2004;
RA   Henke J.M., Bassler B.L.;
RT   "Three parallel quorum-sensing systems regulate gene expression in Vibrio
RT   harveyi.";
RL   J. Bacteriol. 186:6902-6914(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1116 / BB120;
RG   The Vibrio harveyi Genome Sequencing Project;
RA   Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA   Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA   Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA   Wilson R.K.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for the synthesis of the quorum-sensing autoinducer
CC       CAI-1 ((S)-3-hydroxytridecan-4-one) which probably functions as an
CC       intragenus signal. {ECO:0000269|PubMed:15466044}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABU73981.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY625893; AAT86008.1; -; Genomic_DNA.
DR   EMBL; CP000790; ABU73981.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041853530.1; NC_022270.1.
DR   AlphaFoldDB; A7N6R9; -.
DR   SMR; A7N6R9; -.
DR   EnsemblBacteria; ABU73981; ABU73981; VIBHAR_06088.
DR   KEGG; vha:VIBHAR_06088; -.
DR   PATRIC; fig|338187.36.peg.4950; -.
DR   OrthoDB; 479874at2; -.
DR   Proteomes; UP000008152; Chromosome II.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Aminotransferase; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..393
FT                   /note="CAI-1 autoinducer synthase"
FT                   /id="PRO_0000316900"
FT   MOD_RES         240
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   393 AA;  44023 MW;  9E73467E14E2C030 CRC64;
     MSDKPKTKPL PSFVEGRLDF YIQDLIEQNE NQKHLVLGKR PQQGAVVMQS NDYLSLSHNL
     QIQQAHRDAI YEHDDNVVMS AIFLQDDDSK PAFETQLAEY VGMGSCLLSQ SGWAANIGLL
     QTICPPETPV YIDFFAHMSL WEGIRAAGAQ AHPFMHNNMN HLRKQIQRNG SGVIVVDSVY
     STIGTIAPLR DIYEMAREFD CALVVDESHS LGTHGPNGSG LVKALELTEQ VDFITVSLAK
     TFAYRAGAIL GPEKLARTLP FVAFPAIFSS TVLPQEIVRL EKTLEVIRSA DDKRTMLFKR
     AKELRTGLKQ IGFHIRSESQ IVALECGSER NTERVRDFLE ERNVFGAVFC RPATGKNKNI
     IRFSINADMT SRDIDHVLTA CQEAYNHPEL EFA