ID A0A0A2TUW1_9BACL Unreviewed; 687 AA.
AC A0A0A2TUW1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:KGP79469.1};
GN ORFNames=P364_0124175 {ECO:0000313|EMBL:KGP79469.1};
OS Paenibacillus sp. MAEPY2.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1395587 {ECO:0000313|EMBL:KGP79469.1, ECO:0000313|Proteomes:UP000030061};
RN [1] {ECO:0000313|EMBL:KGP79469.1, ECO:0000313|Proteomes:UP000030061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAEPY2 {ECO:0000313|EMBL:KGP79469.1,
RC ECO:0000313|Proteomes:UP000030061};
RX PubMed=24526641;
RA Chua P., Yoo H.S., Gan H.M., Lee S.M.;
RT "Draft Genome Sequences of Two Cellulolytic Paenibacillus sp. Strains,
RT MAEPY1 and MAEPY2, from Malaysian Landfill Leachate.";
RL Genome Announc. 2:0-0(2014).
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}.
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:KGP79469.1}.
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DR EMBL; AWUK01000034; KGP79469.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2TUW1; -.
DR eggNOG; COG0243; Bacteria.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000030061; Unassembled WGS sequence.
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}.
FT DOMAIN 6..63
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 687 AA; 76174 MW; 705F3029D51F228B CRC64;
MIDQENGVFP AVCPLDCPDT CGLLLHKENG KIVKVAGNPD HPITKGAICN KVRNMTERVY
HPERLQYPMR RIGAKGEGQF ERISWDEAIR EITAKFSSLS DTYGPESILP YSFYGNMGIL
GVDGMDRRFF NALGASKLEQ TICNAAGNTG WKYTMGANRG TLPEDTEHAD VILVWGGNIV
STNMHQVVLA EKARKKGAQI VVIDVHRNRT AQWGDWFIPL YPGTDSALAL GLMHVLFEQG
LTDEDFMQKY TVGHVALRDH VRSYTPERVA RITGVPEADI VKLAELYGNA QAAHIHIGNG
LQHHDNGGMN VRSVACLPAI TGQWLKRGGG AIRTNSYAST NSDALERPEL RQNPEPRVVN
MNRIGEALLE AEQPIRALMV YCSNPLVVAP DTERVERGFA REDLFTVVHD LFLTDTAKYA
DIVLPATSSF ETTDLYTSYW HQYVHLQEPV IAPLGESKSN VELFSLLGQA MGYDPEIFGE
TPEQMIEEAL QGTGNPYMNG VTLEGLKQHH FVKLDMSPHD SYLDQLPTPS GKIELYSETM
AQRGLPPLPT YSALVEGYDG EKPAGPADVY PLMFLSPPNH NFLNSTFANS AKHQRLEKMP
LLQMHPEDAA RRQVEDGDTV VVWNDRGRIE LTAKVSESML PGTVISQGLW WDGNGKKQRA
NSLTSNRLSD MGNGATFFSA TVEVKRQ
//
