ID R0E301_RALPI Unreviewed; 698 AA.
AC R0E301;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Anaerobic dehydrogenase, typically selenocysteine-containing {ECO:0000313|EMBL:ENZ76514.1};
GN ORFNames=OR214_03681 {ECO:0000313|EMBL:ENZ76514.1};
OS Ralstonia pickettii OR214.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=1264675 {ECO:0000313|EMBL:ENZ76514.1, ECO:0000313|Proteomes:UP000013280};
RN [1] {ECO:0000313|EMBL:ENZ76514.1, ECO:0000313|Proteomes:UP000013280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR214 {ECO:0000313|EMBL:ENZ76514.1,
RC ECO:0000313|Proteomes:UP000013280};
RX PubMed=23792748;
RA Utturkar S.M., Bollmann A., Brzoska R.M., Klingeman D.M., Epstein S.E.,
RA Palumbo A.V., Brown S.D.;
RT "Draft Genome Sequence for Ralstonia sp. Strain OR214, a Bacterium with
RT Potential for Bioremediation.";
RL Genome Announc. 1:0-0(2013).
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:ENZ76514.1}.
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DR EMBL; APMQ01000010; ENZ76514.1; -; Genomic_DNA.
DR RefSeq; WP_004633102.1; NZ_APMQ01000010.1.
DR AlphaFoldDB; R0E301; -.
DR PATRIC; fig|1264675.3.peg.3617; -.
DR Proteomes; UP000013280; 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 3..60
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 698 AA; 75993 MW; F24296AD343FED2C CRC64;
MSTQVIRAAC PHDCPDTCAL LVTVEDGRAT RVQGDPDHPT TAGVLCTKVN RYAERTYHPN
RLLTPMKRVG AKGEGKFEPI SWDEAIDTIA TRLGDIAARN PEAILPYSYA GTMGLVQGES
MAARFFHKLG ASLLDRTICA SAGATALRYT YGASLGMDIE HVQDAKLILI WGANPIASNL
HFWTRAQEAK RRGATLVAID PYRSLTAEKC HRHLAVRPGT DAALALAMIH VLIRDDLLDH
DYIANHTLGF EALRERAQQY TPEYAATLCG LDAADVEWLA KLYGTTVVRD KQPAAIRLNY
GMQRAHGGGQ GVRAVACLPS LVGAWRDAAG GLQLSTSGFF PIDNAKLQRP DLLPSWPALP
RTINMSTIGD ALLHPGDASF GPKVEAVVVY NSNPVAVAPD SRKVAAGFAR EDLFTVVLEH
FQTDTADYAD ILLPATTQLE HVDVHKAYGH TYVLANNAAI ASMGQSLPNT EIFRRIARRM
GFDDACFADS DDDIASQAVR RDDPAAAHID WATLKRDGWQ KLAHPAAPLA RGGYRTPSGR
CEFYSEQMAK DGLDPLPGYV PPHESAVSTP ELAKRYPLSM ISPPARNFLN STFVNVDSLR
STEGEPHLDI HPDDANARGV VDGELVRIFN DRGTMQARAR VTDRARRGVV VGLSIWWKKL
APDGTNANEL TSQRLTDMGR APTFYDCLVE VAPLAQAA
//
