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Database: UniProt
Entry: I5CCI4_9BURK
LinkDB: I5CCI4_9BURK
Original site: I5CCI4_9BURK 
ID   I5CCI4_9BURK            Unreviewed;       983 AA.
AC   I5CCI4;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:EIM93602.1};
GN   ORFNames=WQE_48398 {ECO:0000313|EMBL:EIM93602.1};
OS   Paraburkholderia hospita BS001.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1171375 {ECO:0000313|EMBL:EIM93602.1};
RN   [1] {ECO:0000313|EMBL:EIM93602.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BS001 {ECO:0000313|EMBL:EIM93602.1};
RX   PubMed=22843604; DOI=10.1128/JB.00725-12;
RA   Nazir R., Hansen M.A., Sorensen S., van Elsas J.D.;
RT   "Draft Genome Sequence of the Soil Bacterium Burkholderia terrae Strain
RT   BS001, Which Interacts with Fungal Surface Structures.";
RL   J. Bacteriol. 194:4480-4481(2012).
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}.
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:EIM93602.1}.
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DR   EMBL; AKAU01000302; EIM93602.1; -; Genomic_DNA.
DR   AlphaFoldDB; I5CCI4; -.
DR   PATRIC; fig|1171375.3.peg.9982; -.
DR   Proteomes; UP000004980; 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; 3.30.200.210; -; 1.
DR   Gene3D; 3.40.50.740; -; 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}.
FT   DOMAIN          12..68
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
FT   REGION          430..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..452
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   983 AA;  110076 MW;  E9FA1064C346290B CRC64;
     MEHKARTQNE KLEVKTTTCY MCACRCGIRV HLRDGEVRYI DGNPDHPLNQ GVICAKGSSG
     IMKQYSPARL TQPLMRKPDA LRGTAQFEPV SWELAFDVLE KRLAHIRATD PKKFALFTGR
     DQMQALTGLF ARQFGTPNYA AHGGFCSVNM AAGMIYTMGG SFWEFGGPDL DRAKLFFMIG
     TAEDHHSNPL KIAISKFKRA GGRFIAINPV RTGYAAIADE WVPIRPGTDG ALFMALMREL
     IESNAYDREF VERYTNAGEL LDIREDSDTQ GLFVCDEDAQ ACNAMFPQNH LWWDPVSQRE
     VLHHTPGVRP ALEGRYALAD GTPVAPSFVL LREQLADCTP DWASGITGIP VDTIRRLARE
     MADVSRDQKI TLPIQWTDAW GETHETVTGA PIAFHAMRGL AGHSNGFQTI RALAVLMSLL
     GTIDRPGGFR HKSPYPRAVP PSAKPPNSPD DVKPNTPLAN GPLGWPAGPE DLFIHDSGEP
     VRIDKAFSWE YPLAVHGLMH SVITNAWRGD PYPIDTLLIF MANLAWNSSM NTVEVRKMLV
     DRNEDGEYKI PFIVVCDAFQ SEMTAFADLI LPDTTYLERY DAMSMLDRPI SEFDGPVDSV
     RVPVVPATGE CKPFQEVLVE LASRLKFPAF TTPDGKRKYR DYPEFIVNHQ TAPGSGVGFL
     IGWRGKDGKD VLVGEPNPKQ WEEYAKHNCV YHYTLPETLQ YMRNCNGPYL DFAVEKGFRK
     FNTPIVIALY SDVMQKFRLA AQGKTKGRQP PEHLRARIAR YFDPLPSWYP PLEHGTTDHA
     RFPLAAITQR PMAMYHSWDS QNAWLRQIHG ENYLYMNPRT AAAQGIEDGG WIYVESQWGK
     VRCIARYSEA VEPGTVWTWN AIGKSAGAWN LGPDANESQR GFLLNHLITD EIPVDDLRHV
     RTSNSDPVTG QAAWYDVRVR IYPAEADADH TLPQFAPMPA SMPGMVGTES GGMIHRIVQT
     YFAGRGEFAA RLKAVQRKTT QRN
//
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