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Database: UniProt
Entry: D4H658_DENA2
LinkDB: D4H658_DENA2
Original site: D4H658_DENA2 
ID   D4H658_DENA2            Unreviewed;      1036 AA.
AC   D4H658;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:ADD67704.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Dacet_0926 {ECO:0000313|EMBL:ADD67704.1};
OS   Denitrovibrio acetiphilus (strain DSM 12809 / NBRC 114555 / N2460).
OC   Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC   Geovibrionaceae; Denitrovibrio.
OX   NCBI_TaxID=522772 {ECO:0000313|EMBL:ADD67704.1, ECO:0000313|Proteomes:UP000002012};
RN   [1] {ECO:0000313|EMBL:ADD67704.1, ECO:0000313|Proteomes:UP000002012}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12809 / NBRC 114555 / N2460
RC   {ECO:0000313|Proteomes:UP000002012};
RX   PubMed=21304711; DOI=10.4056/sigs.892105;
RA   Kiss H., Lang E., Lapidus A., Copeland A., Nolan M., Glavina Del Rio T.,
RA   Chen F., Lucas S., Tice H., Cheng J.F., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Brettin T.,
RA   Spring S., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Denitrovibrio acetiphilus type strain
RT   (N2460).";
RL   Stand. Genomic Sci. 2:270-279(2010).
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR   EMBL; CP001968; ADD67704.1; -; Genomic_DNA.
DR   RefSeq; WP_013010235.1; NC_013943.1.
DR   AlphaFoldDB; D4H658; -.
DR   STRING; 522772.Dacet_0926; -.
DR   PaxDb; 522772-Dacet_0926; -.
DR   KEGG; dap:Dacet_0926; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_008235_0_0_0; -.
DR   InParanoid; D4H658; -.
DR   OMA; ERYSGCP; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000002012; 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   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR43742:SF9; TETRATHIONATE REDUCTASE SUBUNIT A; 1.
DR   PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 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; 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:UP000002012};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          60..133
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   1036 AA;  114322 MW;  D9F05E06827BEB68 CRC64;
     MSQNKKILNK LELSRRGFMK TSALLGGSAM LISNLGCANS AMKKMTDNSI NSKYDLASPE
     HVIYSICLQC HTACAIKGKV AEGVLLKIDG NPYAAQNLYP NLDLDEPLER SARIDAKICP
     KGQAGIQSLY DPYRVTKVLK RAGKRGENKW VSIDFQQAID EIVDGGNLFS NVPGEENRFV
     EGLKDIYRVR DAKTMKQMAE DAKAVADKKM SMTDFKAKYA GKMDLFANPD HPDAGPANAQ
     FVFMGGRIEH GRKEFMKRFM NDCFGSPNFF EHTTICEQSH HIGYGEMFEG KHHLKPDLMN
     SKCVLYFGTG GFEANFGPPP LSEKITQGLT ERGMKVFVVD PRFSKTAAKA TRWIPIKAGT
     DAAYALGMGR YMIEKRLFDS KYLAAANFRA GNSINETNFT NSTWLVKIEA DGPADILKPS
     EIGLEGDFVV MKDGKPFAGT EKGDSVFGEL EVDTVINGIK VKSGFTIYKE SAFSKSLSDW
     ADECGVPVRD ITDVADEFAK AGKQGTIDFY RGPVQHTNGY YNATAIIALN VMLGNTDWEG
     GMMLGGSHWH EYGGKKGNPY NMSKLVKNKL GKFGYPVTRE KTHYEKTSFF SGYPAKRPFY
     PFTGNVYQEI IPSGHEKFPY GIKCLFTHMG TAAYASPAGN VFIDMLCNTE ALPLFIASDI
     VVGETSMYAD YIFPDKAIWE RWGTSHTTPD VASKSSKIRQ PMVEPQTETT TIYNQKVHLS
     MEAVAYAIAE KLGLAGFGKD GFGEGMDNLR EDDFFMKLIE NIAMEGDGVP AASEDELQVF
     AAARKHLSPT AFDIERAKSS TKNWANIVYV LNRGGRFAQL TKAYKGDKVA AQYKNKISLY
     VPRVATTKDS MTGKRFLGFP VYTQAADMFD RPFDFKGADL HLITYKEITG GQSRTIGNYW
     QNELHQAENF ILMNSVDADR LGFSDGDKGK LVSAFNPEGV WDLKHGKKVP MIGNVKVSEA
     IRPGTVAVSW HYGHWAYGAS DIILDGEVIK GESKRAAGLC SNAVNAVDPV LGDMCPTDKI
     GGSASFYDTK IQVVKA
//
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