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formate dehydrogenase-N subunit alpha [Klebsiella pneumoniae].


LOCUS       WP_004184181             803 aa            linear   BCT 10-JUN-2024
ACCESSION   WP_004184181
VERSION     WP_004184181.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella pneumoniae
  ORGANISM  Klebsiella pneumoniae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group;
            Klebsiella; Klebsiella pneumoniae complex.
REFERENCE   1  (residues 1 to 803)
  AUTHORS   Berg,B.L., Li,J., Heider,J. and Stewart,V.
  TITLE     Nitrate-inducible formate dehydrogenase in Escherichia coli K-12.
            I. Nucleotide sequence of the fdnGHI operon and evidence that opal
            (UGA) encodes selenocysteine
  JOURNAL   J Biol Chem 266 (33), 22380-22385 (1991)
   PUBMED   1834669
REFERENCE   2  (residues 1 to 803)
  AUTHORS   Stewart,V.
  TITLE     Nitrate respiration in relation to facultative metabolism in
            enterobacteria
  JOURNAL   Microbiol Rev 52 (2), 190-232 (1988)
   PUBMED   3045516
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 :: TIGR01553.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..803
                     /organism="Klebsiella pneumoniae"
                     /db_xref="taxon:573"
     gene            1..803
                     /gene="fdnG"
     Protein         1..803
                     /product="formate dehydrogenase-N subunit alpha"
                     /EC_number="1.17.5.3"
                     /GO_component="GO:0009326 - formate dehydrogenase complex
                     [Evidence IEA]"
                     /GO_function="GO:0008863 - formate dehydrogenase (NAD+)
                     activity [Evidence IEA]"
                     /GO_function="GO:0009055 - electron transfer activity
                     [Evidence IEA]"
                     /GO_function="GO:0043546 - molybdopterin cofactor binding
                     [Evidence IEA]"
                     /GO_function="GO:0047111 - formate dehydrogenase
                     (cytochrome-c-553) activity [Evidence IEA]"
                     /GO_process="GO:0015942 - formate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=89774
     Region          <1..802
                     /region_name="Molybdopterin-Binding"
                     /note="Molybdopterin-Binding (MopB) domain of the MopB
                     superfamily of proteins, a large, diverse, heterogeneous
                     superfamily of enzymes that, in general, bind
                     molybdopterin as a cofactor. The MopB domain is found in a
                     wide variety of molybdenum- and...; cl09928"
                     /db_xref="CDD:447860"
     Site            order(17..18,20,23..24,46..48,68,197,344..346,370..372,
                     375,404..405,410)
                     /site_type="other"
                     /note="molybdopterin cofactor binding site"
                     /db_xref="CDD:238218"
ORIGIN      
        1 mtnhwvdikn anvvvvmggn aaeahpvgfr wameaknnnd atlivvdprf trtasvadiy
       61 apirsgtdit flsgvllyli ennkinaeyv khytnasllv rddfafeegl fsgydaekrq
      121 ydksswnyqf dengyakrde tlthprcvwn llkqhvsryt pevvenicgt pkadflkvcd
      181 vlastsaadr tttflyalgw tqhtvgaqni rtmamiqlll gnmgmagggv nalrghsniq
      241 gltdlgllst slpgyltlps dkqtdlqsyl santpkatlp eqvnywsnyp kffvslmksf
      301 ygeaaqkend wgfewlpkwd qaydvikyfn mmdngnvtgy icqgfnpvas fpdknkvvrs
      361 lsklkymvvi dplvtetstf wqnhgesndv dpsaiqtevf rlpstcfaee dgsiansgrw
      421 lqwhwkgqda pgearndgei lagiyhrlre lyrteggkga epllkmswry kqpdhpesee
      481 vakenngyal adlydqngtl lakkgqllns fallrddgst asscwiytgs wteqgnqman
      541 rdnadpsglg ntlgwawawp lnrrvlynra sadingkpwd akrmliqwng skwvgndipd
      601 fntappgsnt gpfimqqegl grlfaldkla egpfpehyep metplgtnpl hpkvvsspvv
      661 rlyeedairl gkkdkfpyvg ttyrltehfh twtkhallns iaqpeqfvei seglakskgi
      721 angdwvkvss krgfiravav vtrrlrtlnv ngqqvetvgi plhwgfegva rkgyiantlt
      781 pnvgdsnsqt peykaflvni eka