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LOCUS WP_000918437 361 aa linear BCT 11-DEC-2019 ACCESSION WP_000918437 VERSION WP_000918437.1 KEYWORDS RefSeq. SOURCE Vibrio ORGANISM Vibrio Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae. REFERENCE 1 (residues 1 to 361) AUTHORS Viola,C.M., Saridakis,V. and Christendat,D. TITLE Crystal structure of chorismate synthase from Aquifex aeolicus reveals a novel beta alpha beta sandwich topology JOURNAL Proteins 54 (1), 166-169 (2004) PUBMED 14705034 REFERENCE 2 (residues 1 to 361) AUTHORS Ahn,H.J., Yang,J.K., Lee,B.I., Yoon,H.J., Kim,H.W. and Suh,S.W. TITLE Crystallization and preliminary X-ray crystallographic studies of chorismate synthase from Helicobacter pylori JOURNAL Acta Crystallogr. D Biol. Crystallogr. 59 (Pt 3), 569-571 (2003) PUBMED 12595729 REFERENCE 3 (residues 1 to 361) AUTHORS Fitzpatrick,T.B., Killer,P., Thomas,R.M., Jelesarov,I., Amrhein,N. and Macheroux,P. TITLE Chorismate synthase from the hyperthermophile Thermotoga maritima combines thermostability and increased rigidity with catalytic and spectral properties similar to mesophilic counterparts JOURNAL J. Biol. Chem. 276 (21), 18052-18059 (2001) PUBMED 11279147 REFERENCE 4 (residues 1 to 361) AUTHORS Horsburgh,M.J., Foster,T.J., Barth,P.T. and Coggins,J.R. TITLE Chorismate synthase from Staphylococcus aureus JOURNAL Microbiology (Reading, Engl.) 142 (Pt 10), 2943-2950 (1996) PUBMED 8885411 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: HMM Evidence Accession :: NF003793.1 Evidence Source :: NCBI Protein Cluster (PRK) Source Identifier :: PRK05382 ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..361 /organism="Vibrio" /db_xref="taxon:662" gene 1..361 /gene="aroC" Protein 1..361 /product="chorismate synthase" /EC_number="4.2.3.5" /GO_function="GO:0004107 - chorismate synthase activity [Evidence IEA]" /GO_process="GO:0009073 - aromatic amino acid family biosynthetic process [Evidence IEA]" /calculated_mol_wt=38974 Region 8..361 /region_name="PRK05382" /note="chorismate synthase; Validated" /db_xref="CDD:235438" Site order(11..17,24,26,28,32..33,66..67,69..70,77..78,80,82, 84,111..115,125..126,134,196,201..206,217,219..221,225, 227..228,231..233,235..236,238,241..245,248..249,251..252, 256..257,273,276..278,280..282,289,291..294,297,335) /site_type="other" /note="Tetramer interface [polypeptide binding]" /db_xref="CDD:143612" Site order(19,48,105..106,126..129,132,238..239,292..293, 295..297,324,328) /site_type="active" /db_xref="CDD:143612" Site order(105..107,125,127,237..239,293,295..297,321,324,327) /site_type="other" /note="FMN-binding site [chemical binding]" /db_xref="CDD:143612" ORIGIN 1 magnsigqhf rvttfgeshg ialgcivdgc ppgltisead lqvdldrrrp gtsryttqrr 61 epdevkilsg vfegkttgts igllientdq rskdysdikd kfrpghadyt yhqkygvrdy 121 rgggrssare tamrvaagai akkylqqefg ievraylsqm gevaidkvdw neienndffc 181 pdvdkvaafd elirelkkeg dsigakiqvv atgvpvglge pvfdrldadi ahalmsinav 241 kgveigdgfd vvrqkgsqhr dpltpqgfrs nhsggilggi ssgqdivani alkptssitv 301 pgetidvnge ptelitkgrh dpcvgiravp iaeamlaivl mdhllrhrgq nqgvvtttpk 361 i