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Database: UniProt
Entry: G9Z7A5_9ENTR
LinkDB: G9Z7A5_9ENTR
Original site: G9Z7A5_9ENTR 
ID   G9Z7A5_9ENTR            Unreviewed;      1023 AA.
AC   G9Z7A5;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:EHM47590.1};
GN   ORFNames=HMPREF0880_03339 {ECO:0000313|EMBL:EHM47590.1};
OS   Yokenella regensburgei ATCC 43003.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Yokenella.
OX   NCBI_TaxID=1002368 {ECO:0000313|EMBL:EHM47590.1, ECO:0000313|Proteomes:UP000003044};
RN   [1] {ECO:0000313|EMBL:EHM47590.1, ECO:0000313|Proteomes:UP000003044}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43003 {ECO:0000313|EMBL:EHM47590.1,
RC   ECO:0000313|Proteomes:UP000003044};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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:EHM47590.1}.
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DR   EMBL; AGCL01000039; EHM47590.1; -; Genomic_DNA.
DR   RefSeq; WP_006819797.1; NZ_JH417874.1.
DR   AlphaFoldDB; G9Z7A5; -.
DR   STRING; 1002368.HMPREF0880_03339; -.
DR   PATRIC; fig|1002368.3.peg.3044; -.
DR   HOGENOM; CLU_008235_0_0_6; -.
DR   Proteomes; UP000003044; 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:InterPro.
DR   CDD; cd02780; MopB_CT_Tetrathionate_Arsenate-R; 1.
DR   CDD; cd02758; MopB_Tetrathionate-Ra; 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; IPR037946; MopB_CT_Tetrathionate.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR041929; Tetrathionate-R_A_N.
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.
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}.
FT   DOMAIN          71..155
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   1023 AA;  110798 MW;  FF8EC07DC08AE62C CRC64;
     MAKFTRRQWI KAGLVLGGVS AFGLSYREVA KRALDGMVNG TSGKVTLNRI NGNSLVPEGN
     ARDGWHSNPQ QVVSMTQCFG CWTQCGIRVR VDKAQDKIVR IAGNPWHPLS QEHPFPPSMT
     YSEALEKMAG ESGLDSRSTA CARGATLLEG LYSPLRILLP MKRAGKRGEG KWQRISFEQL
     IHEVVEGGDL FGEGHVDGLR TIRDVKTPLD PARPGLGPKA NQLLVTNTSD DGRDSFLRRF
     AQNSFGSKNF GAHGSFCGLA YRAGSGALMG DLQKNPHVKP DWEHVEFALF MGTSPAQSGN
     PFKRQARQLA SARLRDDFRY VVVAPALPLT TVQADDRGHW LPVTPGTDSA LAMAMIRWII
     DNQRFNAGYL SRPGEAAMQQ AGEKSWTNAS WLVVVSDSHP LYGQHLTANA VYGDAQPDAG
     ALVVSSAGVL MAANLCPEAD LLVEREVTLH DGSQVLVRSS FQCLKQAAQA QTMAEYSQHC
     GVSPQSIARL ADEFTRHGRK AAVITHGGMM SGNGFYSSWA VMMLNVLIGN MSLEGGVFVG
     GGKFNGVADG PRYNMQDFPG KLKPKGLNIA RSNAAYEESD EYKAKTAAGA SPFPARAPWY
     PFVAGQLTEL LSCALEGYPY PLKAWISHMS NPLYGIPGIR AVAEKHLKDP TRLPLFIAID
     AFMNETSALA DYLLPDTHNF ESWGFSAPWA GVASKTTTAR WPVVTPAVAK TAEGQPIAME
     SFCIAVAKKL ALPGFGEAAI VDNDGQTYPL NSAEDYYLRV GANIAFAGQT PVPAASEEDV
     TLSGVKRVLP LLEKTLKAEE AGRVAYIFSR GGRFAPESAG RKEGVVGNRW ETPLQLWNAD
     VARHRHAITG ERYSGCPTFY PPRFANGQSV DEVFPLSRWP LKLMSFKSNL MSSSTTVIPR
     LHHVKPLNLV AMHPDEGARF GVQHGDQVKI STPGGSAIAQ ISLLPGVMPG VIAIEHGYGH
     KEMGARQHWL DGEPLASEAQ IASGINLNDL GFGDPTREVP GIWMDWVTGA AVRQGLPARI
     ERV
//
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