ID   FDOG_ECOLI     STANDARD;      PRT;  1016 AA.
AC   P32176; P78131;
DT   01-OCT-1993 (Rel. 27, Created)
DT   15-JUL-1998 (Rel. 36, Last sequence update)
DT   15-JUN-2002 (Rel. 41, Last annotation update)
DE   Formate dehydrogenase-O, major subunit (EC 1.2.1.2) (Formate
DE   dehydrogenase-O alpha subunit) (FDH-Z alpha subunit) (Aerobic formate
DE   dehydrogenase major subunit).
GN   FDOG OR B3894.
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriaceae;
OC   Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12 / MG1655;
RX   MEDLINE=93347969; PubMed=8346018;
RA   Plunkett G. III, Burland V.D., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome. III. DNA sequence of the
RT   region from 87.2 to 89.2 minutes.";
RL   Nucleic Acids Res. 21:3391-3398(1993).
RN   [2]
RP   REVISIONS TO 252-261; 344-348 AND 822.
RC   STRAIN=K12 / MG1655;
RX   MEDLINE=97426617; PubMed=9278503;
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   [3]
RP   SEQUENCE OF 1-190 FROM N.A., AND CHARACTERIZATION.
RC   STRAIN=K12;
RX   MEDLINE=96099298; PubMed=8522521;
RA   Abaibou H., Pommier J., Giordano G., Mandrand-Berthelot M.-A.;
RT   "Expression and characterization of the Escherichia coli fdo locus
RT   and a possible physiological role for aerobic formate
RT   dehydrogenase.";
RL   J. Bacteriol. 177:7141-7149(1995).
CC   -!- FUNCTION: ALLOWS TO USE FORMATE AS MAJOR ELECTRON DONOR DURING
CC       AEROBIC RESPIRATION. SUBUNIT ALPHA POSSIBLY FORMS THE ACTIVE
CC       SITE.
CC   -!- CATALYTIC ACTIVITY: Formate + NAD(+) = CO(2) + NADH.
CC   -!- COFACTOR: MOLYBDENUM (MOLYBDOPTERIN) AND SELENOCYSTEINE. THE
CC       ACTIVE-SITE SELENOCYSTEINE IS ENCODED BY THE OPAL CODON, UGA.
CC       MAY BIND A 4FE-4S CLUSTER.
CC   -!- SUBUNIT: FORMATE DEHYDROGENASE IS A MEMBRANE-BOUND COMPLEX, FORMED
CC       BY SUBUNITS ALPHA, BETA AND GAMMA.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic (Potential).
CC   -!- SIMILARITY: BELONGS TO THE PROKARYOTIC MOLYBDOPTERIN-CONTAINING
CC       OXIDOREDUCTASE FAMILY.
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DR   EMBL; L19201; AAB03027.2; -.
DR   EMBL; AE000464; AAD13456.1; ALT_SEQ.
DR   EMBL; X87583; CAA60887.1; -.
DR   HSSP; P07658; 1FDO.
DR   EcoGene; EG11858; fdoG.
DR   InterPro; IPR001467; Prok_Mboxred.
DR   Pfam; PF00384; molybdopterin; 3.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; FALSE_NEG.
DR   PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
KW   Oxidoreductase; Molybdenum; Selenocysteine; Selenium; NAD;
KW   Iron-sulfur; 4Fe-4S; Complete proteome.
FT   METAL        50     50       IRON-SULFUR (4FE-4S) (BY SIMILARITY).
FT   METAL        53     53       IRON-SULFUR (4FE-4S) (BY SIMILARITY).
FT   METAL        57     57       IRON-SULFUR (4FE-4S) (BY SIMILARITY).
FT   METAL        92     92       IRON-SULFUR (4FE-4S) (BY SIMILARITY).
FT   SE_CYS      196    196
FT   CONFLICT    252    261       GAKLIVIDPR -> RREADCDRSC (IN REF. 1).
FT   CONFLICT    344    348       ENGFA -> GKRLR (IN REF. 1).
SQ   SEQUENCE   1016 AA;  112502 MW;  95C06BD9633C0A7C CRC64;
     MQVSRRQFFK ICAGGMAGTT AAALGFAPSV ALAETRQYKL LRTRETRNTC TYCSVGCGLL
     MYSLGDGAKN AKASIFHIEG DPDHPVNRGA LCPKGAGLVD FIHSESRLKF PEYRAPGSDK
     WQQISWEEAF DRIAKLMKED RDANYIAQNA EGVTVNRWLS TGMLCASASS NETGYLTQKF
     SRALGMLAVD NQARVCHGPT VASLAPTFGR GAMTNHWVDI KNANLVVVMG GNAAEAHPVG
     FRWAMEAKIH NGAKLIVIDP RFTRTAAVAD YYAPIRSGTD IAFLSGVLLY LLNNEKFNRE
     YTEAYTNASL IVREDYGFED GLFTGYDAEK RKYDKSSWTY ELDENGFAKR DTTLQHPRCV
     WNLLKQHVSR YTPDVVENIC GTPKDAFLKV CEYIAETSAH DKTASFLYAL GWTQHSVGAQ
     NIRTMAMIQL LLGNMGMAGG GVNALRGHSN IQGLTDLGLL SQSLPGYMTL PSEKQTDLQT
     YLTANTPKPL LEGQVNYWGN YPKFFVSMMK AFFGDKATAE NSWGFDWLPK WDKGYDVLQY
     FEMMKEGKVN GYICQGFNPV ASFPNKNKVI GCLSKLKFLV TIDPLNTETS NFWQNHGELN
     EVDSSKIQTE VFRLPSTCFA EENGSIVNSG RWLQWHWKGA DAPGIALTDG EILSGIFLRL
     RKMYAEQGGA NPDQVLNMTW NYAIPHEPSS EEVAMESNGK ALADITDPAT GAVIVKKGQQ
     LSSFAQLRDD GTTSCGCWIF AGSWTPEGNQ MARRDNADPS GLGNTLGWAW AWPLNRRILY
     NRASADPQGN PWDPKRQLLK WDGTKWTGWD IPDYSAAPPG SGVGPFIMQQ EGMGRLFALD
     KMAEGPFPEH YEPFETPLGT NPLHPNVISN PAARIFKDDA EALGKADKFP YVGTTYRLTE
     HFHYWTKHAL LNAILQPEQF VEIGESLANK LGIAQGDTVK VSSNRGYIKA KAVVTKRIRT
     LKANGKDIDT IGIPIHWGYE GVAKKGFIAN TLTPFVGDAN TQTPEFKSFL VNVEKV
//