ID Q8E8Y7_SHEON Unreviewed; 950 AA.
AC Q8E8Y7;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 133.
DE SubName: Full=Fnr-inducilble formate dehydrogenase molybdopterin-binding subunit FdhA {ECO:0000313|EMBL:AAN57477.1};
DE EC=1.1.5.6 {ECO:0000313|EMBL:AAN57477.1};
GN Name=fdhA {ECO:0000313|EMBL:AAN57477.1};
GN OrderedLocusNames=SO_4513 {ECO:0000313|EMBL:AAN57477.1};
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586 {ECO:0000313|EMBL:AAN57477.1, ECO:0000313|Proteomes:UP000008186};
RN [1] {ECO:0000313|EMBL:AAN57477.1, ECO:0000313|Proteomes:UP000008186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1 {ECO:0000313|EMBL:AAN57477.1,
RC ECO:0000313|Proteomes:UP000008186};
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N., Methe B., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M., Brinkac L., Daugherty S.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J., Weidman J.,
RA Impraim M., Lee K., Berry K., Lee C., Mueller J., Khouri H., Gill J.,
RA Utterback T.R., McDonald L.A., Feldblyum T.V., Smith H.O., Venter J.C.,
RA Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; AE014299; AAN57477.1; -; Genomic_DNA.
DR RefSeq; NP_720033.1; NC_004347.2.
DR RefSeq; WP_011074132.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8E8Y7; -.
DR SMR; Q8E8Y7; -.
DR STRING; 211586.SO_4513; -.
DR PaxDb; 211586-SO_4513; -.
DR KEGG; son:SO_4513; -.
DR PATRIC; fig|211586.12.peg.4374; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_1_1_6; -.
DR OrthoDB; 9810782at2; -.
DR PhylomeDB; Q8E8Y7; -.
DR BioCyc; SONE211586:G1GMP-4174-MONOMER; -.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0030151; F:molybdenum ion binding; IBA:GO_Central.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
DR CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 1.
DR CDD; cd02752; MopB_Formate-Dh-Na-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR PIRSF; PIRSF036643; FDH_alpha; 4.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AAN57477.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008186};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 61..117
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 950 AA; 105444 MW; AC4A986A13664F4A CRC64;
MKLTRKSDVA QVANKPTLGI SRRQFMKQAG IATGGIAAAS LMGTGMMRRA EAKDVPYDAP
IEIKRTICSA CAVGCGLYAE VQNGVWTGQE PAFDHPFNAG GHCAKGAALR EHGHGEKRLK
YPMKLVDGKW KKISWEDAIN EVGDQMLNIR KESGPDSVYF MGSAKFSNEG CYAYRKLAAM
WGTNNVDHSA RICHSTTVAG VANTWGYGAQ TNSFNDIQNA NAIFLIGANP AEAHPVSMQH
ILIAKEKNNA KIIVVDPRFS RTAAHSDLHC AIRPGTDIPF IYGMLWHIFE NGWEDKTFIQ
HRVFEMETIR AEVKKFPPKE VANITGVSEE VVYQAAKLMA ENRPGTVIWC MGGTQHHVGN
ANTRAYCILQ LALGNMGVSG GGTNIFRGHD NVQAATDLGL LFDNLPGYYG LTTAAWEHWT
NVWELDMEWM KSRFDHGTYL GREPMTTPGM PCSRWFDGVL LEKDKLAQKD NIRMAFFWGQ
SVNTGTRQRD VRDALDKLDT VVVVDPFPTI AGIMHSRKNG VYLLPACTQF EASGAVSNSG
RSIQWREQVI QPLFESKNDI EIMYMLAKKV GISEQWAKRW NIAGNMPVVE DISREINRGM
WTIGYTGQSP ERIKQHTQNW GTFSNKTLEA AGGPCKGETY GLPWPCWGTP EAKHPGTQIL
YNQDKHVKDG GGNFRARYGV EYNGKNLLAE GTFSKGAEIQ DGYPEFSDKL LKQLGWWDDL
TAEEKAAAEG KNWKTDLSGG IVRVAIKHGC IPFGNAKARC IVWTFPDQAP VHREPIYTAR
RDLVAKYPTY DDMQVHRLPT LYKTLQENDL SGKYPLVMTS GRLVEYEGGG EESRCNPWLA
ELQQEMFIEI SPADAADRAI RNGEFVWVEG AEGGRIKVQA MVTPRVAPGV TFMPYHFAGV
MHGESLAANY PEGTVPYVIG ESCNTALTYG YDPVTQMQET KASLCQIVKA
//
