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
//