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LOCUS WP_005371538 391 aa linear BCT 26-DEC-2019 ACCESSION WP_005371538 VERSION WP_005371538.1 KEYWORDS RefSeq. SOURCE Photobacterium angustum ORGANISM Photobacterium angustum Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; Photobacterium. REFERENCE 1 (residues 1 to 391) AUTHORS Prakash,P., Pathak,N. and Hasnain,S.E. TITLE pheA (Rv3838c) of Mycobacterium tuberculosis encodes an allosterically regulated monofunctional prephenate dehydratase that requires both catalytic and regulatory domains for optimum activity JOURNAL J. Biol. Chem. 280 (21), 20666-20671 (2005) PUBMED 15753077 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 :: NF008865.0 Evidence Source :: NCBI Protein Cluster (PRK) Source Identifier :: PRK11898 ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..391 /organism="Photobacterium angustum" /db_xref="taxon:661" gene 1..391 /gene="pheA" Protein 1..391 /product="prephenate dehydratase" /EC_number="4.2.1.51" /GO_function="GO:0004664 - prephenate dehydratase activity [Evidence IEA]" /GO_process="GO:0009094 - L-phenylalanine biosynthetic process [Evidence IEA]" /calculated_mol_wt=43534 Region 8..386 /region_name="pheA" /note="bifunctional chorismate mutase/prephenate dehydratase; Provisional; PRK10622" /db_xref="CDD:182594" ORIGIN 1 mtdtrysldd irqnvsridn allellaerr alslevaksk istakpvrdq trehelllkl 61 iesgklhqld aqyvtqifht iiedsvlfqq aylqklanpd sanptarvaf lgakgsysyl 121 asrnyfsrkq tnlvelscst frdifntvet gnadygvlpi entssgsine vydllqhtsl 181 sivgeitqpi ehclltavdt klehidtlys hpqphqqcse flhsmgsikq eycsstaeam 241 eqvaelkqpn vaaignassg elygltsiks dianqqenft rfivvarkpv dvtslipakt 301 tlimstaqka gslvecllvl knlninmskl esrpvignpw eemfyvdvev nlksdvmqqs 361 leeltrltrf ikvlgcypse nvaptevell d