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Database: UniProt
Entry: U5BXI0_9BACT
LinkDB: U5BXI0_9BACT
Original site: U5BXI0_9BACT 
ID   U5BXI0_9BACT            Unreviewed;       757 AA.
AC   U5BXI0;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Molybdopterin oxidoreductase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=P872_04530 {ECO:0000313|EMBL:ERM82583.1};
OS   Rhodonellum psychrophilum GCM71 = DSM 17998.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC   Rhodonellum.
OX   NCBI_TaxID=1123057 {ECO:0000313|EMBL:ERM82583.1, ECO:0000313|Proteomes:UP000016843};
RN   [1] {ECO:0000313|EMBL:ERM82583.1, ECO:0000313|Proteomes:UP000016843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GCM71 {ECO:0000313|EMBL:ERM82583.1,
RC   ECO:0000313|Proteomes:UP000016843};
RX   PubMed=24309741;
RA   Hauptmann A.L., Glaring M.A., Hallin P.F., Prieme A., Stougaard P.;
RT   "Draft Genome Sequence of the Psychrophilic and Alkaliphilic Rhodonellum
RT   psychrophilum Strain GCM71T.";
RL   Genome Announc. 1:e01014-13(2013).
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:ERM82583.1}.
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DR   EMBL; AWXR01000024; ERM82583.1; -; Genomic_DNA.
DR   RefSeq; WP_019600255.1; NZ_KB906695.1.
DR   AlphaFoldDB; U5BXI0; -.
DR   PATRIC; fig|1123057.7.peg.2484; -.
DR   eggNOG; COG0243; Bacteria.
DR   OrthoDB; 9792592at2; -.
DR   Proteomes; UP000016843; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   CDD; cd02787; MopB_CT_ydeP; 1.
DR   CDD; cd02767; MopB_ydeP; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR037951; MopB_CT_YdeP.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR010046; Mopterin_OxRdtse_a_bac.
DR   InterPro; IPR041953; YdeP_MopB.
DR   NCBIfam; TIGR01701; Fdhalpha-like; 1.
DR   PANTHER; PTHR43105:SF4; PROTEIN YDEP; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   PIRSF; PIRSF000144; CbbBc; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016843}.
FT   DOMAIN          113..491
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          638..722
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   757 AA;  83992 MW;  D426964C78DCE257 CRC64;
     MTENKDLRIE SPPKSVAGIK AVFIAMKNIF QVMPKSKAIK VLYKLNQKEG VDCPGCAWPD
     PKNRSKLGEY CENGVKAIAE EAMEQVAGPS FFATHSIDDL RAKSDYWLGQ QGRLTHPMVL
     RPGESHYLPI SWNEANACIG EELKGLSHPN EAAFYTSGRT SNEAAFLYQL FARMFGTNNL
     PDCSNMCHES SGVALSRTLG STKGSVTLED FEKAELILVF GQNPATNHPR MLTSLEKAKK
     KGAKIVSINP MKEVGLVHFK NPQTVQGMLG GGVEISDFYL QVRINEDVAL LKAVMFKLLK
     IAEKEPSILD NRFISEKTAG FEAFKNMLLS QDLSVLMKRT GLEEAEIDAL TDLIAKRTKI
     IACWGMGLTQ HVNGVDNIQE LVNLLLMKGS IGKEGAGTCP VRGHSNVQGD RTMGIAERPS
     KELLDKISEN FGFSPPREDG YSVVDTIKAM HEEKVKVFVG MGGNFSAAAP DTHFTAEALR
     KCNLTVHIST KLNRSHLTHG KTALILPSMG RTDKYIKNGK SQFVTVENSM GIVHSTQGIF
     PAPSEFVESE PVIVANIAKA TLDQDKVDWD FLIEDYGNIR DLIEKTIDGF ENFNERIKKP
     LGFELPNASR IGEFNTSNKK ANFTINQMMD NPLEAEEFIM MTTRSHDQFN TTIYGLDDRY
     RGVFNGRMVV FMNGEDAARN NLKKGDKITL FNNYENQERI VEGFSVVPYD LPKGCLATYF
     PEANPLVPIG LMAHSSHTPS SKSVRVKIRL MNPNLKL
//
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