ID E1QE75_DESB2 Unreviewed; 778 AA.
AC E1QE75;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:ADK83861.1};
GN OrderedLocusNames=Deba_0488 {ECO:0000313|EMBL:ADK83861.1};
OS Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802
OS / 2st14).
OC Bacteria; Thermodesulfobacteriota; Desulfarculia; Desulfarculales;
OC Desulfarculaceae; Desulfarculus.
OX NCBI_TaxID=644282 {ECO:0000313|EMBL:ADK83861.1, ECO:0000313|Proteomes:UP000009047};
RN [1] {ECO:0000313|EMBL:ADK83861.1, ECO:0000313|Proteomes:UP000009047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802 / 2st14
RC {ECO:0000313|Proteomes:UP000009047};
RX PubMed=21304732; DOI=10.4056/sigs.1243258;
RA Sun H., Spring S., Lapidus A., Davenport K., Del Rio T.G., Tice H.,
RA Nolan M., Copeland A., Cheng J.F., Lucas S., Tapia R., Goodwin L.,
RA Pitluck S., Ivanova N., Pagani I., Mavromatis K., Ovchinnikova G., Pati A.,
RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Han C., Rohde M., Brambilla E., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Land M.;
RT "Complete genome sequence of Desulfarculus baarsii type strain (2st14).";
RL Stand. Genomic Sci. 3:276-284(2010).
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; CP002085; ADK83861.1; -; Genomic_DNA.
DR RefSeq; WP_013257317.1; NC_014365.1.
DR AlphaFoldDB; E1QE75; -.
DR STRING; 644282.Deba_0488; -.
DR KEGG; dbr:Deba_0488; -.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_4_0_7; -.
DR OrthoDB; 9757870at2; -.
DR Proteomes; UP000009047; 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; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 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; 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; 1.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 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; 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:UP000009047}.
FT DOMAIN 1..78
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 78..117
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 137..166
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 181..210
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 219..275
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 778 AA; 83069 MW; 6113200CA3E480C7 CRC64;
MPTLTLNGNN ISFEPGWTIL EAAKANGVEI PTLCHLQAAD HKGVCRICVV EARGSDRLLP
ACATPAVEGM ELRTDSPAVI EERKLIVELL LAEGDHNCLC CEANGDCVLQ RLAYAHGVKN
APVANPLATR LVDDSQAFIV RDFKKCVMCG RCVAACNEIQ VNMAIPLPFG RREDRPLPAG
WLPLVDHDRC TQCGECVQAC PVGALTEKKA KGRGRSWELT KVRTTCPHCG VGCQQWLHVK
DDQIVKVTAV EDARPNLGML CVKGRFGHDF VGAAERLTTP LIKENGGFRQ ADWDEALDLV
AGRLAAIKAA HGPEAFCGVA DVGGVNEDAY NMQKFFRAVL GVNNIDHRGR ACLAPQATGP
AAACGSGAMT NSFAELEKAK LILVIGADVT EDNPVAGAYI KRAARRGARL IVADPRRTGL
VEHASLHAPV KAGAEVAFVN GLMRVLMEEG LYDKDQALKR AADFEKLRRT VERYNPEMVA
AVAGVGPELL VELAHALATT KPAMLVHALG PDEGARGLDK ALAYADLQLL LGNVGRECGG
VNLLRGRGNA QGLADMGALP GFYPGYQSVG DATARAKFER AWGVELNPKA GLALPAMFEA
MARGAVKAMW ICGEDVLAAA PDGQHAARCL GALDFLVCGD ILPTATTSLA DVVFPLAAWG
ESDGVFTNSE RRVSRARKAV NPPGQAKPGW WIFREVARRM GHDWPSQSSR EIWDNELSVL
APALAGVTYD RLEGDGLQWP CPGLAHPGSA YLPADACPGP DAFHAVEWAP PADEPDGR
//
