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LOCUS WP_004198770 434 aa linear BCT 13-MAY-2021 ACCESSION WP_004198770 VERSION WP_004198770.1 KEYWORDS RefSeq. SOURCE Klebsiella ORGANISM Klebsiella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group. REFERENCE 1 (residues 1 to 434) AUTHORS Suksomtip,M., Liu,P., Anderson,T., Tungpradabkul,S., Wood,D.W. and Nester,E.W. TITLE Citrate synthase mutants of Agrobacterium are attenuated in virulence and display reduced vir gene induction JOURNAL J. Bacteriol. 187 (14), 4844-4852 (2005) PUBMED 15995199 REFERENCE 2 (residues 1 to 434) AUTHORS Stokell,D.J., Donald,L.J., Maurus,R., Nguyen,N.T., Sadler,G., Choudhary,K., Hultin,P.G., Brayer,G.D. and Duckworth,H.W. TITLE Probing the roles of key residues in the unique regulatory NADH binding site of type II citrate synthase of Escherichia coli JOURNAL J. Biol. Chem. 278 (37), 35435-35443 (2003) PUBMED 12824188 REFERENCE 3 (residues 1 to 434) AUTHORS Maurus,R., Nguyen,N.T., Stokell,D.J., Ayed,A., Hultin,P.G., Duckworth,H.W. and Brayer,G.D. TITLE Insights into the evolution of allosteric properties. The NADH binding site of hexameric type II citrate synthases JOURNAL Biochemistry 42 (19), 5555-5565 (2003) PUBMED 12741811 REFERENCE 4 (residues 1 to 434) AUTHORS Nguyen,N.T., Maurus,R., Stokell,D.J., Ayed,A., Duckworth,H.W. and Brayer,G.D. TITLE Comparative analysis of folding and substrate binding sites between regulated hexameric type II citrate synthases and unregulated dimeric type I enzymes JOURNAL Biochemistry 40 (44), 13177-13187 (2001) PUBMED 11683626 REFERENCE 5 (residues 1 to 434) AUTHORS Viollier,P.H., Minas,W., Dale,G.E., Folcher,M. and Thompson,C.J. TITLE Role of acid metabolism in Streptomyces coelicolor morphological differentiation and antibiotic biosynthesis JOURNAL J. Bacteriol. 183 (10), 3184-3192 (2001) PUBMED 11325948 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 :: NF004126.0 Evidence Source :: NCBI Protein Cluster (PRK) Source Identifier :: PRK05614 ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..434 /organism="Klebsiella" /db_xref="taxon:570" Protein 1..434 /product="citrate synthase" /EC_number="2.3.3.16" /GO_function="GO:0046912 - acyltransferase, acyl groups converted into alkyl on transfer [Evidence IEA]" /calculated_mol_wt=47807 Region 19..416 /region_name="EcCS_like" /note="Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). The overall CS...; cd06114" /db_xref="CDD:99867" Site order(41..57,59,71..74,77,81,86,94..97,99,102..103, 106..107,118,121..122,124..126,130,134,138,141,144..146, 231..235,238..239,243,246..249,252,259..260,262..267, 269..270,308..309,406,408..416) /site_type="other" /note="dimer interface [polypeptide binding]" /db_xref="CDD:99867" Site order(49,231,234,265..267,269,272,301..308,311,316,357, 359,362,364,385,389,406,409) /site_type="active" /db_xref="CDD:99867" Site order(49,231,234,265..266,301..302,304..308,316,362,389) /site_type="other" /note="citrylCoA binding site [chemical binding]" /db_xref="CDD:99867" Site order(108,110..116,147,165,169,191) /site_type="other" /note="NADH binding [chemical binding]" /db_xref="CDD:99867" Site order(113..121,124..129,180..192,206..207) /site_type="active" /note="cationic pore residues [active]" /db_xref="CDD:99867" Site order(231,234,266..267,307,316,364,385,389,409) /site_type="other" /note="oxalacetate/citrate binding site [chemical binding]" /db_xref="CDD:99867" Site order(265..266,269,272,301..306,308,311,357,359,362,364, 406) /site_type="other" /note="coenzyme A binding site [chemical binding]" /db_xref="CDD:99867" Site order(266,307,364) /site_type="active" /note="catalytic triad [active]" /db_xref="CDD:99867" ORIGIN 1 msttpltlsf agqqpplalp qvpgtrgpvg vdmrgldqsg fcsydpgfan tagcqsaisw 61 idtensvllh rgypvdqlar qcdflevayi mlngdapdea syqtfretit rhtlvheqia 121 rmcsgfrrds hpmalmcalv galaafyhdv ldvenpqhra laatrllskm ptiaamsyky 181 tieqpaaypr ndlsyagnfl qmlfaipaek yvlnpvieqa mnqilvlhad hgqcastttv 241 raagssganl facvaaglas lwgpmhggan essmrmleei esvdqvpafl rqakrdpqaf 301 rrlgfgnsry rhrdpradil retshrvlae vgmsdrllqv amaledvalt dpyfvdngls 361 psvdfytavi lkamnlpssm favvtavgrt vgwvahwnem hqapltiyrp rqiyvgegyr 421 dyvsrrgers aelr