ID D3P8N0_DEFDS Unreviewed; 745 AA.
AC D3P8N0;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Molybdopterin oxidoreductase, molybdopterin-binding subunit {ECO:0000313|EMBL:BAI81070.1};
GN OrderedLocusNames=DEFDS_1612 {ECO:0000313|EMBL:BAI81070.1};
OS Deferribacter desulfuricans (strain DSM 14783 / JCM 11476 / NBRC 101012 /
OS SSM1).
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Deferribacteraceae; Deferribacter.
OX NCBI_TaxID=639282 {ECO:0000313|EMBL:BAI81070.1, ECO:0000313|Proteomes:UP000001520};
RN [1] {ECO:0000313|EMBL:BAI81070.1, ECO:0000313|Proteomes:UP000001520}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14783 / JCM 11476 / NBRC 101012 / SSM1
RC {ECO:0000313|Proteomes:UP000001520};
RX PubMed=20189949; DOI=10.1093/dnares/dsq005;
RA Takaki Y., Shimamura S., Nakagawa S., Fukuhara Y., Horikawa H., Ankai A.,
RA Harada T., Hosoyama A., Oguchi A., Fukui S., Fujita N., Takami H.,
RA Takai K.;
RT "Bacterial lifestyle in a deep-sea hydrothermal vent chimney revealed by
RT the genome sequence of the thermophilic bacterium Deferribacter
RT desulfuricans SSM1.";
RL DNA Res. 17:123-137(2010).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; AP011529; BAI81070.1; -; Genomic_DNA.
DR RefSeq; WP_013008316.1; NC_013939.1.
DR AlphaFoldDB; D3P8N0; -.
DR STRING; 639282.DEFDS_1612; -.
DR KEGG; ddf:DEFDS_1612; -.
DR eggNOG; COG1034; Bacteria.
DR HOGENOM; CLU_000422_4_0_0; -.
DR Proteomes; UP000001520; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR CDD; cd00368; Molybdopterin-Binding; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
DR PROSITE; PS00641; COMPLEX1_75K_1; 1.
PE 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000001520}.
FT DOMAIN 8..84
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 84..123
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 141..175
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 180..211
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 745 AA; 85533 MW; 27EDD04202A4E448 CRC64;
MSRSTGMGKI FINDKPYDFK EGETVLDVAR RNDIYIPVMC YLKDITPTGA CRLCLVEVEG
LEKPVASCVT YAIDGMKVYT DTETVWKQRK RNLEFILIKH PLDCPVCDKA GECMLQDTTY
EFGINEESVK STKPNKPKFD WDMIIHDANL CVLCERCVKV CHEIAGCSAL KIEERGFNNL
ITTVNESGLD CDFCGLCVDF CPVGALLDKP YKHSVRNWDL EYVETSCNYC PVGCSVKYGK
HENVIYKSEK GENSYICSLA RYAYKYTEHS DRVKTPLVKE NGEFKSIEWN AAIDVVKSKL
DEVLDRYGKD SVAFVLGSRL SNEALYNYKK LAESIGCEKI VTDVAFYNQK FFNDYYEKFE
TYDVVGKLED IKRSDLIFVI GADLQRESLG YKWFLTNGVV HNDSKLVTIG LKRYEYDYYT
DVSIVADYGN FANEFEKIKN DDDQIYKDIR EYISKAKNVT FIVGNEFLEA EANYKSVFAF
VDYIGHDNLN GFFYTFDKPN INAMFNLNLF NRYDVDKLTN EIEDGKIKFL FVADFYPFDT
KGYYKKLRNA INKVDYFISA DLFLNDFNKN AFAILPVLAH LESEGTYITV DGRVIKYVKV
IEPEVDAKSD VEIAYLLGFS KGINLESYSK AVWDNCIKGK FGYPDINYDE VNGLVYKNKT
YKVNNTDYKY IEEPKGTKEV FVNAKYHNNH LSTKAAIEKK SDETYRKYYF DVDRSVLVGE
NAKCDRNLCS LSKGIAKGIV LVPKN
//
