ID FDNG_ECOLI Reviewed; 1015 AA. AC P24183; P78261; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 3. DT 05-OCT-2010, entry version 112. DE RecName: Full=Formate dehydrogenase, nitrate-inducible, major subunit; DE EC=1.2.1.2; DE AltName: Full=Anaerobic formate dehydrogenase major subunit; DE AltName: Full=Formate dehydrogenase-N subunit alpha; DE Short=FDH-N subunit alpha; DE Flags: Precursor; GN Name=fdnG; OrderedLocusNames=b1474, JW1470; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SELENOCYSTEINE AT SEC-196. RC STRAIN=K12; RX MEDLINE=92042178; PubMed=1834669; RA Berg B.L., Li J., Heider J., Stewart V.; RT "Nitrate-inducible formate dehydrogenase in Escherichia coli K-12. I. RT Nucleotide sequence of the fdnGHI operon and evidence that opal (UGA) RT encodes selenocysteine."; RL J. Biol. Chem. 266:22380-22385(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX MEDLINE=97251357; PubMed=9097039; DOI=10.1093/dnares/3.6.363; RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., RA Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., RA Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., RA Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., RA Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.; RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome RT corresponding to the 28.0-40.1 min region on the linkage map."; RL DNA Res. 3:363-377(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [5] RP EXPORT VIA THE TAT-SYSTEM. RX PubMed=17218314; DOI=10.1074/jbc.M610507200; RA Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P., RA Ribnicky B., Palmer T., Georgiou G.; RT "Export pathway selectivity of Escherichia coli twin arginine RT translocation signal peptides."; RL J. Biol. Chem. 282:8309-8316(2007). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). RX MEDLINE=21882259; PubMed=11884747; DOI=10.1126/science.1068186; RA Jormakka M., Tornroth S., Byrne B., Iwata S.; RT "Molecular basis of proton motive force generation: structure of RT formate dehydrogenase-N."; RL Science 295:1863-1868(2002). CC -!- FUNCTION: Formate dehydrogenase allows E.coli to use formate as CC major electron donor during anaerobic respiration, when nitrate is CC used as electron acceptor. The alpha subunit forms the active CC site. CC -!- CATALYTIC ACTIVITY: Formate + NAD(+) = CO(2) + NADH. CC -!- COFACTOR: Binds 1 molybdenum ion per subunit. CC -!- COFACTOR: Binds 2 molybdopterin guanine dinucleotide (MGD) groups CC per subunit. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. CC -!- SUBUNIT: Trimer of heterotrimers, consisting of subunits alpha, CC beta and gamma. CC -!- SUBCELLULAR LOCATION: Periplasm. CC -!- INDUCTION: By nitrate under anaerobic conditions. CC -!- PTM: Exported by the Tat system. The position of the signal CC peptide cleavage has not been experimentally proven. CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing CC oxidoreductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M75029; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; U00096; AAD13438.1; -; Genomic_DNA. DR EMBL; AP009048; BAA15123.1; -; Genomic_DNA. DR PIR; E64900; JS0628. DR RefSeq; AP_002097.1; -. DR RefSeq; NP_415991.1; -. DR PDB; 1KQF; X-ray; 1.60 A; A=1-1015. DR PDB; 1KQG; X-ray; 2.80 A; A=1-1015. DR PDBsum; 1KQF; -. DR PDBsum; 1KQG; -. DR ProteinModelPortal; P24183; -. DR DIP; DIP-9573N; -. DR IntAct; P24183; 17. DR MINT; MINT-1236143; -. DR STRING; P24183; -. DR TCDB; 5.A.3.2.1; prokaryotic molybdopterin-containing oxidoreductase (PMO) family. DR PRIDE; P24183; -. DR EnsemblBacteria; EBESCT00000001288; EBESCP00000001288; EBESCG00000001068. DR EnsemblBacteria; EBESCT00000016701; EBESCP00000015992; EBESCG00000015760. DR GeneID; 946035; -. DR GenomeReviews; AP009048_GR; JW1470. DR GenomeReviews; U00096_GR; b1474. DR KEGG; ecj:JW1470; -. DR KEGG; eco:b1474; -. DR EchoBASE; EB1209; -. DR EcoGene; EG11227; fdnG. DR eggNOG; COG0243; -. DR HOGENOM; HBG436656; -. DR OMA; QNIRSMA; -. DR ProtClustDB; CLSK880048; -. DR BioCyc; EcoCyc:FDNG-MONOMER; -. DR BioCyc; MetaCyc:FDNG-MONOMER; -. DR Genevestigator; P24183; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0009326; C:formate dehydrogenase complex; IDA:EcoCyc. DR GO; GO:0009326; C:formate dehydrogenase complex; IDA:EcoliWiki. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IDA:EcoCyc. DR GO; GO:0009055; F:electron carrier activity; IDA:EcoliWiki. DR GO; GO:0008863; F:formate dehydrogenase activity; IDA:EcoCyc. DR GO; GO:0030151; F:molybdenum ion binding; IDA:EcoCyc. DR GO; GO:0030151; F:molybdenum ion binding; IDA:EcoliWiki. DR GO; GO:0008430; F:selenium binding; IEP:EcoCyc. DR GO; GO:0008430; F:selenium binding; IEP:EcoliWiki. DR GO; GO:0009061; P:anaerobic respiration; IDA:EcoCyc. DR GO; GO:0009061; P:anaerobic respiration; IDA:EcoliWiki. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR009010; Asp_de-COase-like_fold. DR InterPro; IPR006443; Formate_DH_asu_anaerob. DR InterPro; IPR006657; MoPterin_dinucl-bd_dom. DR InterPro; IPR006656; Mopterin_OxRdtase. DR InterPro; IPR006963; Mopterin_OxRdtase_Fe4S4_dom. DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS. DR InterPro; IPR006311; TAT_signal. DR Gene3D; G3DSA:2.40.40.20; Asp_decarboxylase-like_fold; 1. DR Pfam; PF04879; Molybdop_Fe4S4; 1. DR Pfam; PF00384; Molybdopterin; 1. DR Pfam; PF01568; Molydop_binding; 1. DR SUPFAM; SSF50692; Asp_decarb_fold; 1. DR TIGRFAMs; TIGR01553; formate-DH-alph; 1. DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1. DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1. DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; FALSE_NEG. DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1. DR PROSITE; PS51318; TAT; 1. PE 1: Evidence at protein level; KW 3D-structure; 4Fe-4S; Complete proteome; Iron; Iron-sulfur; KW Metal-binding; Molybdenum; NAD; Oxidoreductase; Periplasm; KW Selenocysteine; Signal. FT SIGNAL 1 33 Tat-type signal (Potential). FT CHAIN 34 1015 Formate dehydrogenase, nitrate-inducible, FT major subunit. FT /FTId=PRO_0000063222. FT METAL 50 50 Iron-sulfur (4Fe-4S). FT METAL 53 53 Iron-sulfur (4Fe-4S). FT METAL 57 57 Iron-sulfur (4Fe-4S). FT METAL 92 92 Iron-sulfur (4Fe-4S). FT METAL 196 196 Molybdenum. FT NON_STD 196 196 Selenocysteine. FT CONFLICT 96 96 A -> P (in Ref. 1). FT CONFLICT 484 491 ANTPKATL -> GEHAERRRW (in Ref. 1). FT CONFLICT 941 941 S -> A (in Ref. 1). FT TURN 39 42 FT STRAND 43 49 FT STRAND 51 53 FT TURN 54 55 FT STRAND 58 65 FT TURN 69 70 FT STRAND 74 80 FT TURN 85 89 FT HELIX 93 96 FT TURN 97 98 FT HELIX 99 102 FT TURN 103 103 FT TURN 105 106 FT STRAND 112 114 FT TURN 116 117 FT HELIX 126 144 FT STRAND 146 148 FT TURN 150 151 FT STRAND 154 158 FT STRAND 160 164 FT TURN 167 168 FT HELIX 171 183 FT TURN 184 185 FT HELIX 192 195 FT TURN 196 197 FT HELIX 198 208 FT TURN 217 217 FT HELIX 218 222 FT STRAND 224 230 FT HELIX 233 236 FT TURN 238 241 FT HELIX 242 250 FT STRAND 254 258 FT HELIX 264 267 FT TURN 268 268 FT STRAND 270 273 FT TURN 277 278 FT HELIX 280 293 FT TURN 294 295 FT HELIX 299 305 FT TURN 308 309 FT STRAND 310 312 FT TURN 314 315 FT TURN 320 321 FT TURN 324 325 FT TURN 328 331 FT TURN 336 337 FT STRAND 338 340 FT TURN 344 345 FT STRAND 346 348 FT TURN 352 353 FT TURN 357 358 FT HELIX 360 368 FT TURN 369 370 FT HELIX 373 380 FT HELIX 384 398 FT TURN 400 401 FT STRAND 404 409 FT HELIX 410 413 FT TURN 416 417 FT HELIX 418 431 FT TURN 432 433 FT TURN 435 436 FT TURN 438 439 FT STRAND 441 444 FT TURN 449 450 FT HELIX 451 456 FT TURN 457 458 FT TURN 461 462 FT HELIX 465 467 FT TURN 473 474 FT HELIX 478 485 FT STRAND 490 493 FT HELIX 497 516 FT HELIX 519 527 FT STRAND 531 533 FT HELIX 537 545 FT TURN 546 547 FT STRAND 551 556 FT HELIX 559 562 FT STRAND 563 565 FT HELIX 566 573 FT TURN 574 575 FT STRAND 577 585 FT TURN 588 593 FT HELIX 597 600 FT HELIX 604 606 FT STRAND 610 616 FT HELIX 619 621 FT STRAND 624 627 FT TURN 629 630 FT STRAND 632 636 FT TURN 644 645 FT HELIX 649 667 FT HELIX 672 677 FT TURN 685 686 FT HELIX 690 698 FT STRAND 700 703 FT TURN 708 709 FT STRAND 712 714 FT TURN 716 717 FT HELIX 723 725 FT STRAND 728 733 FT HELIX 737 739 FT TURN 740 741 FT STRAND 742 744 FT TURN 745 746 FT HELIX 749 751 FT TURN 758 759 FT STRAND 760 762 FT TURN 765 766 FT TURN 771 774 FT TURN 778 779 FT HELIX 780 783 FT TURN 786 787 FT STRAND 790 792 FT TURN 793 794 FT STRAND 798 800 FT STRAND 802 809 FT TURN 818 819 FT TURN 826 827 FT TURN 829 830 FT STRAND 831 833 FT TURN 838 839 FT TURN 842 843 FT STRAND 856 859 FT TURN 861 862 FT TURN 864 865 FT TURN 870 871 FT HELIX 876 879 FT TURN 880 881 FT TURN 885 887 FT STRAND 890 895 FT TURN 898 899 FT TURN 902 904 FT HELIX 905 907 FT HELIX 909 914 FT STRAND 919 922 FT HELIX 924 930 FT TURN 931 931 FT TURN 934 935 FT STRAND 937 941 FT STRAND 946 953 FT TURN 955 956 FT STRAND 960 962 FT TURN 963 964 FT STRAND 965 967 FT STRAND 969 973 FT STRAND 978 982 FT HELIX 988 990 FT TURN 998 1000 FT TURN 1005 1006 FT STRAND 1007 1014 SQ SEQUENCE 1015 AA; 112963 MW; E4B9449D6B2407DA CRC64; MDVSRRQFFK ICAGGMAGTT VAALGFAPKQ ALAQARNYKL LRAKEIRNTC TYCSVGCGLL MYSLGDGAKN AREAIYHIEG DPDHPVSRGA LCPKGAGLLD YVNSENRLRY PEYRAPGSDK WQRISWEEAF SRIAKLMKAD RDANFIEKNE QGVTVNRWLS TGMLCASGAS NETGMLTQKF ARSLGMLAVD NQARVUHGPT VASLAPTFGR GAMTNHWVDI KNANVVMVMG GNAAEAHPVG FRWAMEAKNN NDATLIVVDP RFTRTASVAD IYAPIRSGTD ITFLSGVLRY LIENNKINAE YVKHYTNASL LVRDDFAFED GLFSGYDAEK RQYDKSSWNY QLDENGYAKR DETLTHPRCV WNLLKEHVSR YTPDVVENIC GTPKADFLKV CEVLASTSAP DRTTTFLYAL GWTQHTVGAQ NIRTMAMIQL LLGNMGMAGG GVNALRGHSN IQGLTDLGLL STSLPGYLTL PSEKQVDLQS YLEANTPKAT LADQVNYWSN YPKFFVSLMK SFYGDAAQKE NNWGYDWLPK WDQTYDVIKY FNMMDEGKVT GYFCQGFNPV ASFPDKNKVV SCLSKLKYMV VIDPLVTETS TFWQNHGESN DVDPASIQTE VFRLPSTCFA EEDGSIANSG RWLQWHWKGQ DAPGEARNDG EILAGIYHHL RELYQSEGGK GVEPLMKMSW NYKQPHEPQS DEVAKENNGY ALEDLYDANG VLIAKKGQLL SSFAHLRDDG TTASSCWIYT GSWTEQGNQM ANRDNSDPSG LGNTLGWAWA WPLNRRVLYN RASADINGKP WDPKRMLIQW NGSKWTGNDI PDFGNAAPGT PTGPFIMQPE GMGRLFAINK MAEGPFPEHY EPIETPLGTN PLHPNVVSNP VVRLYEQDAL RMGKKEQFPY VGTTYRLTEH FHTWTKHALL NAIAQPEQFV EISETLAAAK GINNGDRVTV SSKRGFIRAV AVVTRRLKPL NVNGQQVETV GIPIHWGFEG VARKGYIANT LTPNVGDANS QTPEYKAFLV NIEKA //