MULTISPECIES: formate dehydrogenase-N subunit alpha [Pseudomonas].

LOCUS       WP_010895684            1026 aa            linear   BCT 10-JUN-2024
ACCESSION   WP_010895684
VERSION     WP_010895684.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 1026)
  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 1026)
  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..1026
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     gene            1..1026
                     /gene="fdnG"
     Protein         1..1026
                     /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=114031
     Region          2..1025
                     /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(51,53..54,58,93,239..240)
                     /site_type="other"
                     /note="[4Fe-4S] binding site [ion binding]"
                     /db_xref="CDD:239153"
     Site            order(95,193,197,231,233,236..237,260..262,279,281,
                     411..413,416..417,449..450,561..563,567,587..589,592,622,
                     654)
                     /site_type="other"
                     /note="molybdopterin cofactor binding site"
                     /db_xref="CDD:239153"
ORIGIN      
        1 mdmnrrqffk vcgiglggss laalgmapte afadqvrhfk lahtvetrnt ctycsvgcgl
       61 imysqgdgak nvaqniihie gdadhpvnrg tlcpkgagll dyihspnrlk ypevreagss
      121 ewkriewdea leriaklmke drdanfvekn eqgqtvnrwl ttgflaasas sneagyithk
      181 vmrslgilgf dnqarvuhgp tvaslaptfg rgamtnhwtd iknadlvlim ggnaaeahpc
      241 gfkwvteaka hnkarllvvd prftrsasva dyyapirtgt diaflgglin yllendkiqh
      301 eyvrnytdvs fivkegfsfe dglfngydae krtypdkssw gyeigedgya kvdptlthpr
      361 cvfnllkqhy srytpdvvsn icgtpkdmml kvwaeiaets kpgkvmtimy algwtqhsvg
      421 aqmirtgamv qlllgnigmp gggmnalrgh sniqgltdlg llsnslpgyl tlamdaeqdy
      481 dayiakrtak plrpgqlsyw qnygkfhvsl mkawfgksat kennwcydwl pkldmpgagy
      541 dvlryfdmmy qgkvngyfcq gfnpiasfpn kakvgaalar lkwmvvmdpl vtetsefwrn
      601 vgeyndvdta sikttvfrlp tscfaeedgs ivnsgrwlqw hwkgaeppgq arpdiaimag
      661 lfhrlremyr kdggafpdpi lgldwsylkp depgpdelar efngkalsdl vdpangmila
      721 kageqlpgfa llrddgstas gcwifagswt qqgnqmgrrd nsdpygmgqt lgwawawpan
      781 rrilynrasa dvsgkpwdpe kkrlvwwngk swggtdvpdy kadvppeagm npfimnpegv
      841 arlfavdkma egpfpehyep fetpigvnpl hrdnrkaisn paarvfkndm elfgtadefp
      901 yaattyrlte hfhywtkhcr lnaitqpeqf veigealake lginagdkvk vssnrgyika
      961 vavvtkrirp lqvdgktvhh vgipihwgfa gmarngflan tltpfvgdgn tqtpefksfl
     1021 vnveka