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LOCUS WP_010917870 1016 aa linear BCT 10-JUN-2024 ACCESSION WP_010917870 VERSION WP_010917870.1 KEYWORDS RefSeq. SOURCE Escherichia coli ORGANISM Escherichia coli Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia. REFERENCE 1 (residues 1 to 1016) 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 1016) 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..1016 /organism="Escherichia coli" /db_xref="taxon:562" gene 1..1016 /gene="fdnG" Protein 1..1016 /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=112520 Region 2..1015 /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 mqvsrrqffk icaggmagtt aaalgfapsv alaetrqykl lrtretrntc tycsvgcgll 61 myslgdgakn akasifhieg dpdhpvnrga lcpkgaglvd fihsesrlkf peyrapgsdk 121 wqqisweeaf driaklmked rdanyiaqna egvtvnrwls tgmlcasass netgyltqkf 181 sralgmlavd nqarvuhgpt vaslaptfgr gamtnhwvdi knanlvvvmg gnaaeahpvg 241 frwameakih ngaklividp rftrtaavad yyapirsgtd iaflsgvlly llnnekfnre 301 yteaytnasl ivredygfed glftgydaek rkydksswty eldengfakr dttlqhprcv 361 wnllkqhvsr ytpdvvenic gtpkdaflkv ceyiaetsah dktasflyal gwtqhsvgaq 421 nirtmamiql llgnmgmagg gvnalrghsn iqgltdlgll sqslpgymtl psekqtdlqt 481 yltantpkpl legqenywgn ypkffvsmmk affgdkatae nswgfdwlpk wdkgydvlqy 541 femmkegkvn gyicqgfnpv asfpnknkvi sclsklkflv tidplntets nfwqnhgeln 601 evdsskiqte vfrlpstcfa eengsivnsg rwlqwhwkga dapgialtdg eilsgiflrl 661 rkmyaeqgga npdqvlnmtw nyaiphepks eevamesngk aladitdpat gavivkkgqq 721 lssfaqlrdd gttscgcwif agswtpegnq marrdnadps glgntlgwaw awplnrrily 781 nrasadpqgn pwdpkrqllk wdgtkwtgwd ipdysaappg sgvgpfimqq egmgrlfald 841 kmaegpfpeh yepfetplgt nplhpnvisn paarifkdda ealgkadkfp yvgttyrlte 901 hfhywtkhal lnailqpeqf veigeslank lgiaqgdtvk vssnrgyika kavvtkrirt 961 lkangkdidt igipihwgye gvakkgfian tltpfvgdan tqtpefksfl vnvekv