MULTISPECIES: SDR family oxidoreductase [Klebsiella].

LOCUS       WP_002896401             480 aa            linear   BCT 21-JUL-2024
ACCESSION   WP_002896401
VERSION     WP_002896401.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
REFERENCE   1  (residues 1 to 480)
  AUTHORS   Persson,B., Kallberg,Y., Bray,J.E., Bruford,E., Dellaporta,S.L.,
            Favia,A.D., Duarte,R.G., Jornvall,H., Kavanagh,K.L., Kedishvili,N.,
            Kisiela,M., Maser,E., Mindnich,R., Orchard,S., Penning,T.M.,
            Thornton,J.M., Adamski,J. and Oppermann,U.
  TITLE     The SDR (short-chain dehydrogenase/reductase and related enzymes)
            nomenclature initiative
  JOURNAL   Chem Biol Interact 178 (1-3), 94-98 (2009)
   PUBMED   19027726
REFERENCE   2  (residues 1 to 480)
  AUTHORS   Kavanagh,K.L., Jornvall,H., Persson,B. and Oppermann,U.
  TITLE     Medium- and short-chain dehydrogenase/reductase gene and protein
            families : the SDR superfamily: functional and structural diversity
            within a family of metabolic and regulatory enzymes
  JOURNAL   Cell Mol Life Sci 65 (24), 3895-3906 (2008)
   PUBMED   19011750
REFERENCE   3  (residues 1 to 480)
  AUTHORS   Oppermann,U., Filling,C., Hult,M., Shafqat,N., Wu,X., Lindh,M.,
            Shafqat,J., Nordling,E., Kallberg,Y., Persson,B. and Jornvall,H.
  TITLE     Short-chain dehydrogenases/reductases (SDR): the 2002 update
  JOURNAL   Chem Biol Interact 143-144, 247-253 (2003)
   PUBMED   12604210
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 10142831
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..480
                     /organism="Klebsiella"
                     /db_xref="taxon:570"
     Protein         1..480
                     /product="SDR family oxidoreductase"
                     /EC_number="1.1.1.-"
                     /GO_function="GO:0016491 - oxidoreductase activity
                     [Evidence IEA]"
                     /GO_function="GO:0070403 - NAD+ binding [Evidence IEA]"
                     /calculated_mol_wt=53601
     Region          5..296
                     /region_name="SDR_a2"
                     /note="atypical (a) SDRs, subgroup 2; cd05245"
                     /db_xref="CDD:187556"
     Site            order(9,11..12,14,33..35,73..75,109..111,122,126,145..148)
                     /site_type="other"
                     /note="putative NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:187556"
     Site            order(122,126)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:187556"
     Region          333..463
                     /region_name="DUF2867"
                     /note="Protein of unknown function (DUF2867); pfam11066"
                     /db_xref="CDD:431633"
ORIGIN      
        1 msqsvlvlga sgyigqhlvr alsargypvl aaarhidrlq klalpgvtcr svdlnqpqdl
       61 palltgidtl yylvhgmgeg gdfiaherrv atyvrdalrq ssvrqvifls slqapaqeqs
      121 dhlrarqitg dllresgvpv telragiivg agsaafevmr dmvynlpvlt pprwvrsrtt
      181 pvalenllvd lvellnhpsd ahrvfeaagp evlsyqqqfi rfmavsgkhr plipiplptr
      241 wisvwflnvi tsvpptiaka liqglkhdli addralrali pqtlipfdqa vrrtlkeeeq
      301 lvnssdwgyd aqafarwrpe ygyypkqagc tvatqasrqa lwqvvnqigg eegyffgnll
      361 wktrgamdll vghrlakgrp qraylqtgdt vdswkviive eekqltllfg mkapglgrls
      421 ftindkgdrr eldvrawwhp hgmpgliywl lmipahlfif rgmaqriarl aeqisgrveg