ID A0A231RPD2_9BACL Unreviewed; 678 AA.
AC A0A231RPD2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:OXS60505.1};
GN ORFNames=B1A99_08795 {ECO:0000313|EMBL:OXS60505.1};
OS Cohnella sp. CIP 111063.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=1955714 {ECO:0000313|EMBL:OXS60505.1, ECO:0000313|Proteomes:UP000215193};
RN [1] {ECO:0000313|EMBL:OXS60505.1, ECO:0000313|Proteomes:UP000215193}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 111063 {ECO:0000313|EMBL:OXS60505.1,
RC ECO:0000313|Proteomes:UP000215193};
RA Dastager S.G., Neurgaonkar P.S., Dharne M.S.;
RT "Cohnella sp SGD-V74 (T) CIP 111063, whole genome shotgun sequencing
RT project.";
RL Submitted (MAR-2017) 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}.
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:OXS60505.1}.
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DR EMBL; MWSG01000004; OXS60505.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A231RPD2; -.
DR Proteomes; UP000215193; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000215193}.
FT DOMAIN 6..63
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 678 AA; 75378 MW; 7F11C4530E55EE80 CRC64;
MTVTESKVVR SVCPFDCPDT CSLHVTLENN AIVSIDGNPD HPVTQGAICN KVRHLRERVY
HPDRVLHPLR RIGPKGTLEF ERIAWDEAYD EIVSRLKSAI AAKGAESILP YSFYGNMGIL
NAEGMDRRFF HRIGASQLER TICNAAGSAG YGYTMGASAG TDPETTVHTK YALIWGCNLV
STNMHQVMYL TEARKRGAKI VHIDVHRNRT SAWADEFVGI LPGTDTALAL GMMHVLIKEK
LTDERFIAEY TKGFEELAVQ AEKYPPERVA EITGVPADTI VRLAREYAGT TPSFIRIGNG
LQHHDNGGMA IRTIACLPAL VGQWGIPGGG AIKGNSHYSS VNALQLERPD LLPDRNVRSI
SMNRLGEALL ASEPSVDVLF VYNSNPAVVA PDQNRVRQGL MRDDLFTVTH DLFLTDTCKY
ADIVLPATSH FENLDLFASY WHLYLQLHEP ILEPMGECKS NFTLFKELGL RMGFEPEVFD
VTEEQMIREA LDYKSPFLDG LTYEELRREG SVRMKLDRPS LVPQRIPTPS GKIEFYSERM
LRAGLPPVPE YSPLREPEEY PFLLVTGPNH SFINSTFGNQ ERLKKLEKGP VVDMNAEDAA
ARGIAHGDSV RMWNGRGEVR LTAKVADNVL PGVLVTQGLW WEHGNDGVQA VNSLTSQRLA
DMGGGATFFS TRVEVVKL
//
