ID   A0A518N4V1_9GAMM        Unreviewed;       962 AA.
AC   A0A518N4V1;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Molybdopterin-dependent oxidoreductase {ECO:0000313|EMBL:QDW66946.1};
GN   ORFNames=FPZ22_08605 {ECO:0000313|EMBL:QDW66946.1};
OS   Luteimonas granuli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Luteimonas.
OX   NCBI_TaxID=1176533 {ECO:0000313|EMBL:QDW66946.1, ECO:0000313|Proteomes:UP000316584};
RN   [1] {ECO:0000313|EMBL:QDW66946.1, ECO:0000313|Proteomes:UP000316584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gr-4 {ECO:0000313|EMBL:QDW66946.1,
RC   ECO:0000313|Proteomes:UP000316584};
RA   Im W.-T.;
RT   "Full genome sequence of Luteimonas sp. Gr-4.";
RL   Submitted (JUL-2019) 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; CP042218; QDW66946.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A518N4V1; -.
DR   KEGG; lug:FPZ22_08605; -.
DR   OrthoDB; 9810782at2; -.
DR   Proteomes; UP000316584; Chromosome.
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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000316584}.
FT   DOMAIN          22..78
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          430..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          924..962
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   962 AA;  106199 MW;  026C7780824E0C37 CRC64;
     MAPMRAHRPD EPVLDTSPSP GDAVKTTTCY MCACRCGIKV WLRDGSIRYI QGNPAHPVNQ
     GVICAKGAAG IMQHHSPARL TKPLLRVGER GSGEFREIEW DEAMEIATSW LAPVRERNPD
     EFAFFTGRDQ SQALTGWWAQ QFGTVNYAAH GGFCSVNMAA GGLYTLGGSF WEFGEPDWEH
     TRYLMLWGVA EDHDSNPIKL GLGRLKARGA KIVAVNPVRT GYGAIADEWI GIRPGTDGLF
     AFALIHELLR SDRIDLDYLV RYADAHWLVV RDPGGAEDGL FARDAEGRPQ CWVDGRPHPA
     DAPGIAPAVV GEYTLPDGRH AVPAFHLVAE RYLDPEFAPD AVAGRCGIPA DTIRRIAREL
     AEAAFDSNLR LPIAWTDAWG REHAEMVGRP VSLHAMRGIS AHSNGFHTCR ALHLLQLLLG
     AVDAPGSFRY QPPYPKPIPP PNRPGRARRE DGTLDAGPLG FVHGPEDLLV DAEGRPRRID
     HAYSWAYPLS AHGMMHTLLR NAHAGDPYRI DTLMMFMANM AWNSAMNTRE TIAWLTDREE
     DGGYRIPRII YADAYASEMV AYADLVLPDT TYLERFDAIS LLDRPISDAD GAADAIRQPL
     FDPTTQPDRD GRPRDVRGFQ SVLLELGARL GLPGMVHADG SPKYRDYADY IVRHERMPGV
     GLLAGWRGED GSRSGKGAPN PEQLQRYIDN GGFWREEVPE SARWFKMANR AYLDWAHGLG
     FIGSAAPITL HLYAEPLQKF RLAAQGHGAH QPPEEHRERV ATYFDPLPIW YAPFEQAQVD
     GEAFPLHAIT QRPMFMYHAW GSQNAWLRQI AARNWLYMHP DTGARFGVAD EGWVVVASHL
     GEITVQAKFA ANVQPDTLWT WNAIGKRRGA WRLDPDAPEG RQGFLLNHLI SDITPRGDYA
     NADPVTGQAA WFDLRVGLRP AATGAGAEKG AAGADGPAAQ PQFEPLDLGS APAGPLRYGA
     RR
//