ID   A0A410K0Q5_9BACT        Unreviewed;       734 AA.
AC   A0A410K0Q5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:QAR33972.1};
GN   ORFNames=EP073_11320 {ECO:0000313|EMBL:QAR33972.1};
OS   Geovibrio thiophilus.
OC   Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC   Geovibrionaceae; Geovibrio.
OX   NCBI_TaxID=139438 {ECO:0000313|EMBL:QAR33972.1, ECO:0000313|Proteomes:UP000287502};
RN   [1] {ECO:0000313|EMBL:QAR33972.1, ECO:0000313|Proteomes:UP000287502}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11263 {ECO:0000313|EMBL:QAR33972.1,
RC   ECO:0000313|Proteomes:UP000287502};
RA   Spring S., Bunk B., Sproer C.;
RT   "Geovibrio thiophilus DSM 11263, complete genome.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP035108; QAR33972.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A410K0Q5; -.
DR   KEGG; gtl:EP073_11320; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000287502; 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; 3.40.50.740; -; 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; IPR006311; TAT_signal.
DR   PANTHER; PTHR43742:SF9; TETRATHIONATE REDUCTASE SUBUNIT A; 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.
DR   PROSITE; PS51318; TAT; 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};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287502};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           40..734
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019479378"
FT   DOMAIN          45..101
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   734 AA;  82084 MW;  5F639121F6A38C3C CRC64;
     MTKCRISRRR FIQGTASVGA ALASMSSFRL LTGSSPASAE PQQGVTYAQN WCEMCFWKCG
     LTAKVVDGKV KKLEGQPDCP SNYGKLCAKG NAGVFQLYDP DRLKTPLIRD GERGSGKFRK
     ATWEEALTYV AQKTNELKEK YGPETFSIFA HGSGEHSFVE LVEIIGSPNY CIPSYAQCTG
     SRDIGWALSY GKAVGGKEPV DSQNSKCIML LGRNIVEALH VGEMQDFVEG VAKGAHVIYV
     DPRFTKTAAK ANQYMMIKPG TDSALLLGMI NYIIEKEIYN KNFVDGYTHG FDLFKEHVAE
     YTVEWASQIT EIPQTEIIKA AEKLCEAAPH CYIHPGRRLT RYGNDTQFTR IVACLNMLMG
     NWEVRGGIYR TVGFKYDAPH MVHFDKPYAD RADGAGSEEF PLGPKNLGFA NKLMEHIANQ
     DVYPLKGMFV YGCNPLHHHG STEMVKKALE NTELLVTCEI YMTDTAWLSD VILPESTYLE
     RYDPVISTGR RKGYIQFREP AVNPVFDTKG GWEIAAQLSA AMGHENEFLD VREYNRLAFE
     ALGITEEYMK KHGVWVANES TPYPVEDGEE EPSFRTPSGK AEFYSNLCEH FSYPPMPSYE
     ENPVPAEDEF RFLFGRLSFH THARTQNNAW LLALHKSEVP LWIHTDRAKA LGIKDGMQVR
     LVKEGFKSNP CTARVVDYIH PQAVFLPYGF GHETKGLTRI TGKGARTSDF TSNLTDPISG
     AAGFHNGFVK LEIA
//