CQSA_VIBCH
ID CQSA_VIBCH Reviewed; 389 AA.
AC Q9KM65;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=CAI-1 autoinducer synthase;
DE EC=2.3.-.-;
DE AltName: Full=Cholerae quorum-sensing autoinducer;
GN Name=cqsA; OrderedLocusNames=VC_A0523;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
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.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann 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).
RN [2]
RP FUNCTION AS THE CAI-1 SYNTHASE.
RX PubMed=12176318; DOI=10.1016/s0092-8674(02)00829-2;
RA Miller M.B., Skorupski K., Lenz D.H., Taylor R.K., Bassler B.L.;
RT "Parallel quorum sensing systems converge to regulate virulence in Vibrio
RT cholerae.";
RL Cell 110:303-314(2002).
RN [3]
RP IDENTIFICATION OF CAI-1.
RX PubMed=18004304; DOI=10.1038/nature06284;
RA Higgins D.A., Pomianek M.E., Kraml C.M., Taylor R.K., Semmelhack M.F.,
RA Bassler B.L.;
RT "The major Vibrio cholerae autoinducer and its role in virulence factor
RT production.";
RL Nature 450:883-886(2007).
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:12176318}.
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}.
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DR EMBL; AE003853; AAF96426.1; -; Genomic_DNA.
DR PIR; H82448; H82448.
DR RefSeq; NP_232914.1; NC_002506.1.
DR RefSeq; WP_001039912.1; NZ_LT906615.1.
DR PDB; 2WK7; X-ray; 2.50 A; A/B=1-389.
DR PDB; 2WK8; X-ray; 2.10 A; A/B=1-389.
DR PDB; 2WK9; X-ray; 1.90 A; A/B=1-389.
DR PDB; 2WKA; X-ray; 1.91 A; A/B=1-389.
DR PDB; 3HQT; X-ray; 2.70 A; A/B=1-389.
DR PDB; 3KKI; X-ray; 1.80 A; A/B=1-389.
DR PDBsum; 2WK7; -.
DR PDBsum; 2WK8; -.
DR PDBsum; 2WK9; -.
DR PDBsum; 2WKA; -.
DR PDBsum; 3HQT; -.
DR PDBsum; 3KKI; -.
DR AlphaFoldDB; Q9KM65; -.
DR SMR; Q9KM65; -.
DR STRING; 243277.VC_A0523; -.
DR DrugBank; DB08364; 1-{[(1E)-(3-HYDROXY-2-METHYL-5-{[(TRIHYDROXY-LAMBDA^5^-PHOSPHANYL)OXY]METHYL}PYRIDIN-4-YL)METHYLIDENE]AMINO}UNDECAN-2-ONE.
DR DNASU; 2612753; -.
DR EnsemblBacteria; AAF96426; AAF96426; VC_A0523.
DR GeneID; 57741927; -.
DR KEGG; vch:VC_A0523; -.
DR PATRIC; fig|243277.26.peg.3149; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_4_6; -.
DR OMA; VMQSNDY; -.
DR BioCyc; MetaCyc:MON-19105; -.
DR BioCyc; VCHO:VCA0523-MON; -.
DR EvolutionaryTrace; Q9KM65; -.
DR Proteomes; UP000000584; Chromosome 2.
DR GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009102; P:biotin biosynthetic process; IBA:GO_Central.
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 3D-structure; Acyltransferase; Aminotransferase; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..389
FT /note="CAI-1 autoinducer synthase"
FT /id="PRO_0000316899"
FT MOD_RES 236
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT HELIX 8..21
FT /evidence="ECO:0007829|PDB:3KKI"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:3KKI"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:3KKI"
FT HELIX 56..67
FT /evidence="ECO:0007829|PDB:3KKI"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:3KKI"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:3KKI"
FT HELIX 88..97
FT /evidence="ECO:0007829|PDB:3KKI"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:3KKI"
FT HELIX 108..119
FT /evidence="ECO:0007829|PDB:3KKI"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:3KKI"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:3KKI"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:3KKI"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:3KKI"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:3KKI"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:3KKI"
FT HELIX 185..195
FT /evidence="ECO:0007829|PDB:3KKI"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:3KKI"
FT TURN 204..209
FT /evidence="ECO:0007829|PDB:3KKI"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:3KKI"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:3KKI"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:3KKI"
FT STRAND 228..236
FT /evidence="ECO:0007829|PDB:3KKI"
FT STRAND 243..250
FT /evidence="ECO:0007829|PDB:3KKI"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:3KKI"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:3KKI"
FT HELIX 260..264
FT /evidence="ECO:0007829|PDB:3KKI"
FT HELIX 270..285
FT /evidence="ECO:0007829|PDB:3KKI"
FT HELIX 287..305
FT /evidence="ECO:0007829|PDB:3KKI"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:3KKI"
FT STRAND 314..324
FT /evidence="ECO:0007829|PDB:3KKI"
FT HELIX 325..337
FT /evidence="ECO:0007829|PDB:3KKI"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:3KKI"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:2WK9"
FT STRAND 355..360
FT /evidence="ECO:0007829|PDB:3KKI"
FT HELIX 367..383
FT /evidence="ECO:0007829|PDB:3KKI"
SQ SEQUENCE 389 AA; 43594 MW; AB37F11195D54C74 CRC64;
MNKPQLPDFI QNKIDHYIEN YFDINKNGKH LVLGKQASPD DIILQSNDYL ALANHPLIKA
RLAKSLLEEQ QSLFMSASFL QNDYDKPMIE KRLAKFTGFD ECLLSQSGWN ANVGLLQTIC
QPNTNVYIDF FAHMSLWEGA RYANAQAHPF MHNNCDHLRM LIQRHGPGII VVDSIYSTLG
TIAPLAELVN ISKEFGCALL VDESHSLGTH GPNGAGLLAE LGLTREVHFM TASLAKTFAY
RAGAIWCNNE VNRCVPFISY PAIFSSTLLP YEAAGLETTL EIIESADNRR QHLDRMARKL
RIGLSQLGLT IRSESQIIGL ETGDERNTEK VRDYLESNGV FGSVFCRPAT SKNKNIIRLS
LNSDVNDEQI AKIIEVCSDA VNYGDFYFR
