ID A0A0F2P562_9GAMM Unreviewed; 718 AA.
AC A0A0F2P562;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=4Fe-4S Mo/W bis-MGD-type domain-containing protein {ECO:0000259|PROSITE:PS51669};
GN ORFNames=VR73_05350 {ECO:0000313|EMBL:KJS08496.1};
OS Gammaproteobacteria bacterium BRH_c0.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1629722 {ECO:0000313|EMBL:KJS08496.1, ECO:0000313|Proteomes:UP000033581};
RN [1] {ECO:0000313|EMBL:KJS08496.1, ECO:0000313|Proteomes:UP000033581}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c0 {ECO:0000313|EMBL:KJS08496.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-2015) 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 -!- 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:KJS08496.1}.
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DR EMBL; LADM01000045; KJS08496.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2P562; -.
DR STRING; 1629722.VR73_05350; -.
DR PATRIC; fig|1629722.3.peg.3368; -.
DR Proteomes; UP000033581; 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 CDD; cd02775; MopB_CT; 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 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 3..60
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 718 AA; 78182 MW; A923256919D3852C CRC64;
MALSKHKSFC RICTGHCGVV ATVDENRKLV AIQGDREDTQ TLGFICSKGT DAVDSHNSDR
RILQPLKRMD DGSFAPIPLE QALSEIASKL GVIIGRDGPA AVAAYRGSGG FFASASIQVV
NAFLDAIGSH QMYSNLTIDQ SAKWVAIGRV GWWPPGPQPF QTNDVAMMVG CNPLVSIAGS
GFDTRHPLKR IRDAKARGMK IIVIDPRRSE TAEYADLFIQ PLPGNDAGIL AAIIRIILAE
GWHDAEFCAR HVADLDLLQQ ALEPFDPERV AAVADVPVDS LRQAARIFAH DCKRGTVSTG
TGPSMSPFSN LMEHMVTCLN VVCGRFVREG ERIGNPGLVL GWGPKRAQVM DVGRSWDTGP
KSRIGGFGTV GGEMLTGLLA DEILTPGPGQ IKCLFSVGGN PAAAVPDHNK MAKALESLEL
LVSLEPFMTP TAMLADYILP PRMPYERADL HLALFETAIY PDAYARHTQP VATPPEGAEL
CDEWFAFWSL ASRLGRQLVC NGVELDMQTP PGDDALLAIM ARNAPVPWET IRDAPAGYLH
EEAVFALPPD PASTSRFTTL PADVQDEITE LRDYCLQPSA DRATGKFPYR LTSRRSRHRF
NTVGHFSPYL KRLMPYNPAY LNPADMAREG IENGDWVEIS SDHGLIRARA EADDSVRTGV
VSISHCFGFL PGESDFDTYG VSTNLLISTD RDLQTINAMP RMSGIPVAIR PMAERRLG
//