ID W0EC05_9FIRM Unreviewed; 695 AA.
AC W0EC05;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:AHF06714.1};
GN ORFNames=DESME_06315 {ECO:0000313|EMBL:AHF06714.1};
OS Desulfitobacterium metallireducens DSM 15288.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=871968 {ECO:0000313|EMBL:AHF06714.1, ECO:0000313|Proteomes:UP000010847};
RN [1] {ECO:0000313|EMBL:AHF06714.1, ECO:0000313|Proteomes:UP000010847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15288 {ECO:0000313|Proteomes:UP000010847};
RG DOE Joint Genome Institute;
RA Smidt H., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP007032; AHF06714.1; -; Genomic_DNA.
DR AlphaFoldDB; W0EC05; -.
DR STRING; 871968.DESME_06315; -.
DR KEGG; dmt:DESME_06315; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_9; -.
DR OrthoDB; 219031at2; -.
DR Proteomes; UP000010847; Chromosome.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02766; MopB_3; 1.
DR CDD; cd02786; MopB_CT_3; 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 Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 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; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR037920; YoaE_C.
DR PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
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; PS00490; MOLYBDOPTERIN_PROK_2; 1.
PE 3: Inferred from homology;
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:UP000010847}.
FT DOMAIN 17..74
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 695 AA; 78293 MW; FE0871B98C9FFAF9 CRC64;
MHCVDAVHFF KERVDPVEFK YSVCPHDCPD TCAWKIELSQ GRIQRIMGDP LHPVTQGVIC
EKAKYYVERI YGSDRVLFPM RRSGPKGSGQ FERISWEEAM NEITQRWQTL IDKHGAECIL
PYSYAGTEGI INKASMDRRF FNRLASTQLE RTICSAAGSA GYQMAYGASR GVNPLETVKA
RFLLFWGINV LETNLHQAML ANRARQNGAK IVVIDIHLNK TAKWADEFYQ ILPGSDGALA
LGLAHVIVRD GVHDLAWIEK YIQGFKEFNE EIKNYPPERV AKITGLTEVE VVKLAHEYGE
AHPSFIRIGN GFQHHENGGM STWAIACLPA LTGAWKDQGG GLLKFNSGYF PLNKDAVERP
DLLKSSPRVV NMNQLGRALT NLKPSIYALY VYNSNPAAVA PEQKLVLEGL AREDLFTVVH
EQVWTDTARW ADLVLPATTH VEHADLYVSY WHGILQWADP IIPRQGESKP NIEVFQELAQ
RMGFQEACFQ ETTEDIARSA LMTSALQKQG IDLERLKAER YIPLEMEELP FIDHKPGTPS
GKIELYSERA QVLGLSPVPT YIPLVEGLET EDLEHPLMLI SPPHHLILNS TFAQIESVQS
RWRGPELEIH PEDALVRGIH EGDEVEVYND RGSCQLKAVV RKSVLRGVVV TLGVWWPRDY
EKGIGINALT PSRLADMGNG ATFFSNRVEV RKVYE
//
