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Database: UniProt
Entry: B2UCZ4_RALPJ
LinkDB: B2UCZ4_RALPJ
Original site: B2UCZ4_RALPJ 
ID   B2UCZ4_RALPJ            Unreviewed;       698 AA.
AC   B2UCZ4;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:ACD28229.1};
GN   OrderedLocusNames=Rpic_3106 {ECO:0000313|EMBL:ACD28229.1};
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD28229.1};
RN   [1] {ECO:0000313|EMBL:ACD28229.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=12J {ECO:0000313|EMBL:ACD28229.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome1 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) 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}.
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DR   EMBL; CP001068; ACD28229.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2UCZ4; -.
DR   STRING; 402626.Rpic_3106; -.
DR   KEGG; rpi:Rpic_3106; -.
DR   PATRIC; fig|402626.5.peg.4245; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_3_4; -.
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          3..60
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   698 AA;  75959 MW;  984283A80B68F0A8 CRC64;
     MSTQVIRAAC PHDCPDTCAL LVTVEDGRAT RVQGDPDHPT TAGVLCTKVN RYAERTYHPN
     RLLTPMKRVG AKGEGKFEPI SWGEAIDTIA TRLGDIAARN PEAILPYSYA GTMGLVQGES
     MAARFFHKLG ASLLDRTICA SAGATALRYT YGASLGMDIE HVQDAKLILI WGANPIASNL
     HFWTRAQEAK RRGATLVAID PYRSLTAEKC HRHLAVRPGT DAALALAMIH VLIRDDLLDH
     DYIANHTLGF EALRERAQQY TPEYAATLCG VDAADVEWLA KLYGTTVVRD KQPAAIRLNY
     GMQRAHGGGQ GVRAVACLPS LVGAWRDAAG GLQLSTSGFF PIDNAKLQRP DLLPSWPALP
     RTINMSTIGD ALLHPGDASF GPKVEAVVVY NSNPVAVAPD SRKVAAGFAR EDLFTVVLEH
     FQTDTADYAD ILLPATTQLE HVDVHKAYGH TYVLANNAAI APMGQSLPNT EIFRRIARRM
     GFDDACFADS DDDIASQAVR RDDPAAAHID WATLKREGWQ KLAHPAAPLA RGGYRTPSGR
     CEFYSEQMAK DGLDPLPGYV PPHESAISTP ELAKRYPLSM ISPPARNFLN STFVNVDSLR
     STEGEPHLDI HPDDANARGV VDGELVRIFN DRGTMQARAR VTDRARRGVV VGLSIWWKKL
     APDGTNANEL TSQRLTDMGR APTFYDCLVE VAPLAQAA
//
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