ID B1I1F3_DESAP Unreviewed; 998 AA.
AC B1I1F3;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:ACA58678.1};
GN OrderedLocusNames=Daud_0110 {ECO:0000313|EMBL:ACA58678.1};
OS Desulforudis audaxviator (strain MP104C).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforudis.
OX NCBI_TaxID=477974 {ECO:0000313|EMBL:ACA58678.1, ECO:0000313|Proteomes:UP000008544};
RN [1] {ECO:0000313|Proteomes:UP000008544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP104C {ECO:0000313|Proteomes:UP000008544};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Pitluck S., Lowry S.R., Larimer F., Land M.L.,
RA Hauser L., Kyrpides N., Ivanova N.N., Richardson P.;
RT "Complete sequence of chromosome of Desulforudis audaxviator MP104C.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACA58678.1, ECO:0000313|Proteomes:UP000008544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP104C {ECO:0000313|EMBL:ACA58678.1,
RC ECO:0000313|Proteomes:UP000008544};
RX PubMed=18845759; DOI=10.1126/science.1155495;
RA Chivian D., Brodie E.L., Alm E.J., Culley D.E., Dehal P.S., Desantis T.Z.,
RA Gihring T.M., Lapidus A., Lin L.H., Lowry S.R., Moser D.P.,
RA Richardson P.M., Southam G., Wanger G., Pratt L.M., Andersen G.L.,
RA Hazen T.C., Brockman F.J., Arkin A.P., Onstott T.C.;
RT "Environmental genomics reveals a single-species ecosystem deep within
RT Earth.";
RL Science 322:275-278(2008).
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; CP000860; ACA58678.1; -; Genomic_DNA.
DR AlphaFoldDB; B1I1F3; -.
DR STRING; 477974.Daud_0110; -.
DR KEGG; dau:Daud_0110; -.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_4_0_9; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000008544; Chromosome.
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:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00207; fer2; 2.
DR Gene3D; 3.10.20.740; -; 2.
DR Gene3D; 3.30.70.20; -; 2.
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; 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; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
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; 2.
DR Pfam; PF12838; Fer4_7; 2.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 2.
DR PIRSF; PIRSF036643; FDH_alpha; 2.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 2.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 2.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 2.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 2.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 4.
DR PROSITE; PS51839; 4FE4S_HC3; 2.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 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:UP000008544}.
FT DOMAIN 4..81
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 81..120
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 142..173
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 186..215
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 254..330
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 330..369
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 389..420
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 432..461
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 465..521
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 998 AA; 107878 MW; 4C18385D56EAD164 CRC64;
MEMEAVEFTI NGLPVRVPGK GATILEAALR NGIYIPHLCH HPDLKPAGLC RVCMVEADGK
MVAACRTPVA DGMKVATGSP NLDQYRRYIV GVILAEHESD CLTCGKNLNC KLQEVARYAN
LEPTKFKELR PVKPGKPLDD THPWIVRNHN KCILCGICVR TCREIAQVNA IDFAFRGRAT
TISTFGNKPL HESNCVSCGE CVARCPVGAL LPKVSAEPAR EAALIPPQVV RECERRPETP
PSLFMLKEKG AVAEKITLTI DGLEASVEKG ATVLEAAQKA GIYIPFLCFH PELTGSGGCR
VCAVEIDGKV VPSCTTRARE GMVVRTSSPQ AREAQAAAVK RILAGHNGDC LNCAKNGRCK
LQEVVGYTGV YQEMAGTPAP FAEVDESNPY FVLDRSRCVA CGICLRTCRQ VNGADALEFK
RVDNHRVVVP RQGGSLAESA CESCGECVAR CPVGALLPKE LQQPGREVET VCTECGIGCG
VYFGARGGRL VSARQNLSHK TSKGRLCGKG RFGWGVLNHP DRLKTPLIKK DGQFVEAGWE
EALGLAAGGF SRYKGGGAVV LYSPRVTNEE IYLALKFARA VLGTSNIADA ESFASRAGLL
DGLGTTVGSN AMTIPVRQIE RAAGHFVISS SPTESHPIIG FEIRKSVNKG AKLIIADSRE
IPLSRLPHIR LALRPSTELA LLLGMARAIL DEKLHDEGFI RERTTNFDAF QKSLADFTVE
KAAEITGVPG AQIREAARVY ATSKPALLFW SEEIAQHPTG QDSVRVLAQL ALMTGNYGKP
GAGFVPLIGR SNFQGALDLD VTHPWSLVSK EKVADAWGCA VPEPAGSAEN KAKAWYIIGA
DPVTKAADAD SVRKALSEAP FVVVQDTFLT ETAKLAQVVL PTAGFAEKEG TFTAVDRLVQ
RVRQVAEPPG AAKPDWWIIC EIAHRMEAEG FAYNHPSQIM EEISSNYPAY AGISYDRLDP
EGLRWPCPDK EHPGTDVLHE SEFFGLGKAQ FRPLQYKP
//
