ID A0A1A0P623_9MYCO Unreviewed; 661 AA.
AC A0A1A0P623;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:OBB05400.1};
GN ORFNames=A5662_00855 {ECO:0000313|EMBL:OBB05400.1};
OS Mycobacteriaceae bacterium 1482268.1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae.
OX NCBI_TaxID=1834080 {ECO:0000313|EMBL:OBB05400.1, ECO:0000313|Proteomes:UP000091934};
RN [1] {ECO:0000313|EMBL:OBB05400.1, ECO:0000313|Proteomes:UP000091934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1482268.1 {ECO:0000313|EMBL:OBB05400.1,
RC ECO:0000313|Proteomes:UP000091934};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBB05400.1}.
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DR EMBL; LZSH01000146; OBB05400.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A0P623; -.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000091934; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
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 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 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; PS00551; MOLYBDOPTERIN_PROK_1; 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}.
FT DOMAIN 1..57
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 661 AA; 71364 MW; FC0614E49C2F336D CRC64;
MQTVRSFCRV CTSVCGILVD VDGDQVIRVR GDQDHPFSRG YTCAKGRALP LLHHHPDRLE
RPQMRVDGRL EDTTWDACLD DLSTRLKDII DRHGPESVGF YFSTMESAGF RMAEALHAAI
GTPAKFSPLT IDGTAKPLVS DLVGGFMGLS GRTDFDNADF LLLVGVNPIV SHGHAISMPN
PTGTVRDIAK RGQVWVIDPR RTETARLATG HVAPRPSTDH AVLAYLVREI LCDGMKSDIP
VQGVDALAAA VEPFTLEQTA TLADVAESEL TALCAAVRSA TCVAVETGTG VTMTADRANV
TQWLAWVLMI LTGAMNRPGG TWFHPGFAYQ LEAFGDLLPI TPIEGSFGPG PRSRPEAQAF
INEWPCAVLP DEVAAGNIRA LINVGGSIVT SFPETGKLIP ALQNLEVFAT TEIIDNETTQ
LATHVLPTKD PLERPDITIH DILSSRVSVQ YSPAVVAPVG QRRSMWWVFA EIGRRLGYQM
GNLGDPSTST DDDVLRVLLA GARSSYDEVA TTGWAEAPRE LPAKWVDDHI ERMGGWRLAP
PLLVDQLAAL QPPAPLVMVP RRQRKKLNAQ LDILGEAAEI LIHPDDGAAA GIVSGRPVIV
RSANGELTGI AKVDDSIRRG AVSIPHGHHE ANVNRLTNKD DIDVVTGMVR YSGIPVTLHP
A
//
