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LOCUS WP_004151782 669 aa linear BCT 23-DEC-2024 [Klebsiella]. ACCESSION WP_004151782 VERSION WP_004151782.1 KEYWORDS RefSeq. SOURCE Klebsiella ORGANISM Klebsiella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group. REFERENCE 1 (residues 1 to 669) AUTHORS Sousa,S.F., Neves,R.P.P., Waheed,S.O., Fernandes,P.A. and Ramos,M.J. TITLE Structural and mechanistic aspects of S-S bonds in the thioredoxin-like family of proteins JOURNAL Biol Chem 400 (5), 575-587 (2019) PUBMED 30367780 REFERENCE 2 (residues 1 to 669) AUTHORS Qi,Y. and Grishin,N.V. TITLE Structural classification of thioredoxin-like fold proteins JOURNAL Proteins 58 (2), 376-388 (2005) PUBMED 15558583 REFERENCE 3 (residues 1 to 669) AUTHORS Porat,A., Cho,S.H. and Beckwith,J. TITLE The unusual transmembrane electron transporter DsbD and its homologues: a bacterial family of disulfide reductases JOURNAL Res Microbiol 155 (8), 617-622 (2004) PUBMED 15380548 REFERENCE 4 (residues 1 to 669) AUTHORS Kimball,R.A., Martin,L. and Saier,M.H. Jr. TITLE Reversing transmembrane electron flow: the DsbD and DsbB protein families JOURNAL J Mol Microbiol Biotechnol 5 (3), 133-149 (2003) PUBMED 12766342 REFERENCE 5 (residues 1 to 669) AUTHORS Kadokura,H., Katzen,F. and Beckwith,J. TITLE Protein disulfide bond formation in prokaryotes JOURNAL Annu Rev Biochem 72, 111-135 (2003) PUBMED 12524212 REFERENCE 6 (residues 1 to 669) AUTHORS Hirota,K., Nakamura,H., Masutani,H. and Yodoi,J. TITLE Thioredoxin superfamily and thioredoxin-inducing agents JOURNAL Ann N Y Acad Sci 957, 189-199 (2002) PUBMED 12074972 REFERENCE 7 (residues 1 to 669) AUTHORS Powis,G. and Montfort,W.R. TITLE Properties and biological activities of thioredoxins JOURNAL Annu Rev Biophys Biomol Struct 30, 421-455 (2001) PUBMED 11441809 REFERENCE 8 (residues 1 to 669) AUTHORS Aslund,F. and Beckwith,J. TITLE The thioredoxin superfamily: redundancy, specificity, and gray-area genomics JOURNAL J Bacteriol 181 (5), 1375-1379 (1999) PUBMED 10049365 REFERENCE 9 (residues 1 to 669) AUTHORS Chivers,P.T., Prehoda,K.E. and Raines,R.T. TITLE The CXXC motif: a rheostat in the active site JOURNAL Biochemistry 36 (14), 4061-4066 (1997) PUBMED 9099998 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 :: Conserved Domain (CDD) Evidence Accession :: Domain architecture ID 12109673 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..669 /organism="Klebsiella" /db_xref="taxon:570" Protein 1..669 /product="protein-disulfide reductase DsbD family protein" /EC_number="1.8.-.-" /EC_number="1.8.1.8" /GO_function="GO:0009055 - electron transfer activity [Evidence IEA]" /GO_function="GO:0015036 - disulfide oxidoreductase activity [Evidence IEA]" /calculated_mol_wt=72069 Region 46..146 /region_name="DsbC" /note="Disulphide bond corrector protein DsbC; pfam11412" /db_xref="CDD:463273" Region 275..668 /region_name="DsbD" /note="Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, chaperones]; COG4232" /db_xref="CDD:443376" ORIGIN 1 mymvfrrllv cllwlwlpvs qaadsgwlra adnqhasvrl raqtesngdt rllldvalek 61 gwktywrspg eggiapaiaw htplevnwrw ptpqrfdvag istqgyhgdv sfpmtlrgki 121 pptlsgvltl stcsnvcilt dypfsldmtt pagerfnydf tramgtlplr dgltsqltas 181 yvsgkltvta rrdagwqqpa lfidsmedvd fgkpsftsrg atltatvpvt dswgeaapdl 241 sgktlslvla dsgqaqesqi avaagsaapg lalgwvllma lagglilnvm pcvlpvlamk 301 lgslvqtegr ergavrrqfl asvcgivvsf lalalmmtal rlgnqalgwg iqfqnpwfig 361 amalvmvlfg asllglfeir lsssastfla trggnglmgh fwqgafatll atpctapflg 421 tavsvalvap lpllwgiffa mgigmslpwl livawpglaq rlprpgrwmn hlrvvlglmm 481 lgsalwlvsl ltihigrtpv ltllvilaia llvatawryr wrtalragal aivvagavaf 541 vaqqdgqgpr rdrvnwqpls eqaiasalae hkrvfidvta dwcvtckank ynvllrddvq 601 qallapdvva lrgdwsrpsa disqfltarg saavpfnqiy gpelpqgqil palldrehll 661 atlsaakgk