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Database: UniProt
Entry: A0A1I5E3I3_9BURK
LinkDB: A0A1I5E3I3_9BURK
Original site: A0A1I5E3I3_9BURK 
ID   A0A1I5E3I3_9BURK        Unreviewed;       979 AA.
AC   A0A1I5E3I3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Molydopterin dinucleotide binding domain-containing protein {ECO:0000313|EMBL:SFO06104.1};
GN   ORFNames=SAMN05443579_101513 {ECO:0000313|EMBL:SFO06104.1};
OS   Variovorax sp. PDC80.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1882827 {ECO:0000313|EMBL:SFO06104.1, ECO:0000313|Proteomes:UP000199369};
RN   [1] {ECO:0000313|Proteomes:UP000199369}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PDC80 {ECO:0000313|Proteomes:UP000199369};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; FOWG01000001; SFO06104.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5E3I3; -.
DR   OrthoDB; 9815647at2; -.
DR   Proteomes; UP000199369; 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:UniProtKB-KW.
DR   CDD; cd02783; MopB_CT_2; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 2.
DR   Gene3D; 2.20.25.90; ADC-like domains; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 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   PANTHER; PTHR43598:SF5; DMSO REDUCTASE CHAIN A; 1.
DR   PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 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.
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:UP000199369}.
FT   DOMAIN          22..83
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   979 AA;  108794 MW;  F8D87060B84424A6 CRC64;
     MFSFLSREPV HDPLAAPTPT DQTEVKTTTC YMCACRCGIR VHLREGEHGP EVRYIDGNPD
     HPLNKGVICA KGSSGIMKQV SPARLTQPLL RRPGSERGAG EFEPIGWDRA FEILTERLAK
     IRATDPKKFA LFTGRDQMQA LTGLFARQFG TPNYAAHGGF CSVNMAAGMI YTIGGSFWEF
     GGPDLERAKL FVMIGTAEDH HSNPMKIAIS KFKRDGGRFI SINPVRTGYS AIADEWIPIK
     PGTDGALLMA LLHELIASEL IDHAFLKRFT NAPQLVVLDD CEREGLFAFD PERGPPGDGR
     HPHNKLVWDK ASGTVKPAYP EGIAEGCDPA LEGHYTLADG TRVAPSFQLL RERVASCTPE
     WAQAITGIDA ARIRKLAREM GETALRQAFE LPIAWTDAWG KRHETTQARP VAFHAMRGLA
     AHSNGFQTVR ALAILMSVLG TIDAPGGFRH KAPYPRHIVP NYRAFNDPGM IQPNTPLNAA
     PLGFPASPDE LAINPDGSPI RIDHAFSWEH PLSAHGLMHN VITNAVKGDP YRIDTLLIFM
     ANMAWNSSMN TMGVREMLNR KDEQGEYMIP FLVVCDAFQS ETVAFADLVL PDTTYLERHD
     VMSMLDRPIS EFDGPVDSVR IPVVPPTGQC KPFQEVLIEL ASRLKFPAFT TAEGGRKYAD
     YPDFVVNFQP QPGIGFLMGW RGKDGTEHLR GEPNPKQWEA YAQNNCVFQY HMPETMHYMR
     NWNREYLDFA KDKGWRQRND PVQLALYSDT LQSFRLAAQG KSQGRQPPEG LRERIATYFD
     PLPFWYAPLE EAATDTAAYP LNALTQRPMA MYHSWDSQNA WLRQIHSHNY LHVNPVTAEA
     AGIADGGWCW VESQWGKVRC MLRYSEAVEP GTVWTWNAIG KADGAWQLAP GADEARKGFL
     LNHLISEELP CAGTASGRIS NSDPITGQAG WYDVRVRIRP AEPGEPEESY PQFASMPSAP
     GVLGKAAQVL TYFAGRGRK
//
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