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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.
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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
//