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LOCUS WP_011069394 1015 aa linear BCT 10-JUN-2024 ACCESSION WP_011069394 VERSION WP_011069394.1 KEYWORDS RefSeq. SOURCE Shigella ORGANISM Shigella Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae. REFERENCE 1 (residues 1 to 1015) 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 1015) 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..1015 /organism="Shigella" /db_xref="taxon:620" gene 1..1015 /gene="fdnG" Protein 1..1015 /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=112821 Region 2..1014 /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(50,52..53,57,92,238..239) /site_type="other" /note="[4Fe-4S] binding site [ion binding]" /db_xref="CDD:239153" Site order(94,192,196,230,232,235..236,259..261,278,280, 409..411,414..415,447..448,556..558,562,582..584,587,617, 649) /site_type="other" /note="molybdopterin cofactor binding site" /db_xref="CDD:239153" ORIGIN 1 mdvsrrqffk icaggmagtt vaalgfapkq alaqarnykl lrakeirntc tycsvgcgll 61 myslgdgakn areaiyhieg dpdhpvsrga lcpkgaglld yvnsenrlry pkyrapgsdk 121 wqrisweeaf sriaklmkad rdanfiekne qgvtvnrwls tgmlcasgas netgmltqkf 181 arslgmlavd nqarvuhgpt vaslaptfgr gamtnhwvdi knanvvmvmg gnaaeahpvg 241 frwameaknn ndatlivvdp rftrtasvad iyapirsgtd itflsgilry liennkinae 301 yvkhytnasl lvrddfafed glfsgydaek rqydksswny qfdengyakr detlthprcv 361 wnllkahvsr ytpdvvenic gtpkadflkv cevlastsap drtttflyal gwtqhtvgaq 421 nirtmamiql llgnmgmagg gvnalrghsn iqgltdlgll stslpgyltl psekqvdlqs 481 yleantpkat ladqvnywsn ypkffvslmk sfygdaaqke nnwgydwlpk wdqtydviky 541 fnmmdegkvt gyfcqgfnpv asfpdknkvv sclsklkymv vidplvtets tfwqnhgesn 601 dvdpasiqte vfrlpstcfa eedgsiansg rwlqwhwkgq dapgearndg eilagiyhhl 661 relyqaeggk gveplmkmsw nykqphepqs devakenngy aledlydang vliakkgqll 721 ssfahlrddg ttasscwiyt gswteqgnqm anrdnsdpsg lgntlgwawa wplnrrvlyn 781 rasadingkp wdpkrmliqw ngskwtgndi pdfgnaapgt ptgpfimqpe gmgrlfaink 841 maegpfpehy epietplgtn plhpnvvsnp vvrlyeqdal rmgkkeqfpy vgttyrlteh 901 fhtwtkhall naiaqpeqfv eisetqaaak ginngdrvtv sskrgfirav avvtrrlkpl 961 nvngqqvetv gipihwgfeg varkgyiant ltpnvgdans qtpeykaflv nieka