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
//