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LOCUS WP_000979579 253 aa linear BCT 17-MAY-2022 ditrans,polycis-undecaprenyl-diphosphate synthase [Enterobacteriaceae]. ACCESSION WP_000979579 VERSION WP_000979579.1 KEYWORDS RefSeq. SOURCE Enterobacteriaceae ORGANISM Enterobacteriaceae Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales. REFERENCE 1 (residues 1 to 253) AUTHORS Chang,S.Y., Ko,T.P., Chen,A.P., Wang,A.H. and Liang,P.H. TITLE Substrate binding mode and reaction mechanism of undecaprenyl pyrophosphate synthase deduced from crystallographic studies JOURNAL Protein Sci 13 (4), 971-978 (2004) PUBMED 15044730 REFERENCE 2 (residues 1 to 253) AUTHORS Chang,S.Y., Ko,T.P., Liang,P.H. and Wang,A.H. TITLE Catalytic mechanism revealed by the crystal structure of undecaprenyl pyrophosphate synthase in complex with sulfate, magnesium, and triton JOURNAL J Biol Chem 278 (31), 29298-29307 (2003) PUBMED 12756244 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 :: NF007596.1 Evidence Source :: NCBI Protein Cluster (PRK) Source Identifier :: PRK10240 ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..253 /organism="Enterobacteriaceae" /db_xref="taxon:543" gene 1..253 /gene="ispU" /gene_synonym="uppS" Protein 1..253 /product="(2E,6E)-farnesyl-diphosphate-specific ditrans,polycis-undecaprenyl-diphosphate synthase" /GO_function="GO:0002094 - polyprenyltransferase activity [Evidence IEA]" /GO_function="GO:0008834 - di-trans,poly-cis-decaprenylcistransferase activity [Evidence IEA]" /GO_process="GO:0043164 - Gram-negative-bacterium-type cell wall biogenesis [Evidence IEA]" /calculated_mol_wt=28313 Region 25..253 /region_name="PRK10240" /note="(2E,6E)-farnesyl-diphosphate-specific ditrans,polycis-undecaprenyl-diphosphate synthase" /db_xref="CDD:182326" Site order(25..30,39,43,47,50,69,77,81,88..89,92,141,194,200, 202) /site_type="active" /db_xref="CDD:259850" Site order(148..149,151..152,155..156,172..174,177,188, 199..203,206..208,210..214,216) /site_type="other" /note="dimer interface [polypeptide binding]" /db_xref="CDD:259850" ORIGIN 1 mmlsatqpls eklpahgcrh vaiimdgngr wakkqgkira fghkagaksv rravsfaann 61 giealtlyaf ssenwnrpaq evsalmelfv waldsevksl hrhnvrlrii gdtsrfnsrl 121 qerirkseal tagntgltln iaanyggrwd ivqgvrqlae kvqqgnlqpd qideemlnqh 181 vcmhelapvd lvirtggehr isnfllwqia yaelyftdvl wpdfdeqdfe galnafanre 241 rrfggtepgd eta