ID B0TM88_SHEHH Unreviewed; 949 AA.
AC B0TM88;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:ABZ74681.1};
GN OrderedLocusNames=Shal_0105 {ECO:0000313|EMBL:ABZ74681.1};
OS Shewanella halifaxensis (strain HAW-EB4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=458817 {ECO:0000313|EMBL:ABZ74681.1, ECO:0000313|Proteomes:UP000001317};
RN [1] {ECO:0000313|EMBL:ABZ74681.1, ECO:0000313|Proteomes:UP000001317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB4 {ECO:0000313|EMBL:ABZ74681.1,
RC ECO:0000313|Proteomes:UP000001317};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella halifaxensis HAW-EB4.";
RL Submitted (JAN-2008) 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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP000931; ABZ74681.1; -; Genomic_DNA.
DR RefSeq; WP_012275238.1; NC_010334.1.
DR AlphaFoldDB; B0TM88; -.
DR STRING; 458817.Shal_0105; -.
DR KEGG; shl:Shal_0105; -.
DR eggNOG; COG0243; Bacteria.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_1_1_6; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000001317; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
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; cd02792; MopB_CT_Formate-Dh-Na-like; 1.
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 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; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 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 PIRSF; PIRSF036643; FDH_alpha; 3.
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; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS51318; TAT; 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 Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 61..117
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 949 AA; 106264 MW; 03046A0582FBEFCE CRC64;
MRLNRKTDQA VTSDKAALGL NRRQFLKSAS LATGGIAAAS MLGAGMMRKA EAKDIPHDVP
TETKRTICSH CSVGCGVYAG VQNGVWTTQE PAFDHPFNAG GHCAKGAALR EHGHGEKRLK
YPMKLEGGKW KRLSWDQAIE EVGQQALDIR KESGPDSVFF MGSAKFSNEQ AYMYRKFAAM
WGTNNVDHSA RICHSTTVAG VANTWGYGAQ TNSFNDIRNA KAMMFIGSNP CEAHPVAMQH
ILIGKERGAK IIVVDPRFTR TAAKSDEFVH IRPGTDIPFI YGLLWHIFEN GWEDQTFIDQ
RVYGMERIRE EVKKYHPAEV ANIVGATEEQ MRRVAKLLAE TKPGTIVWCM GGTQHHVGNA
NTRAYCILQL ALGNMGVSGG GTNIFRGHDN VQGATDFGLL FDTLPGYYGL KTGSWKHWCN
VWDLDYEWVK GRFDQEPRLG QDPMTSTGIP CSRWHDGVLE DKSKIAQKDN IHMAFFWGQS
VNTETRGREV REALNKMKTV VVVDPFPTMA GVMHERTDGV YLLPACTQFE TYGSVSASNR
SLQWRTKVIE PLFESKPDHV IMYKLAKKWG IDKEFFKNIK INGEEPLIED MTREFNRGMW
TIGYTGQSPE RLKMHQENWG TFDIKSLEAP GGPAKGETYG LPWPCWGTPE FKHPGTQILY
RTGREVMNGG GNFRARYGVE HDGVNILAEG SYSKGSEIKD GYPEFTDKML KQLGWWDDLT
AEEKVAAEGK NWKTDISGGI QRVAIKHGCI PYGNAKARCI VWNFPDDIPL HREPLYTPRR
DLVAKYPTYE DRMVARLPTL YKTIQEKDFA KDFPLIITTG RLVEYEGGGE ETRSNPWLAE
LQQEMFIEIN PADAADRGIR DGDNVFVHSP EGAKITVKAM VIPRVVPGEC FMPYHFAGVF
EGESLAKNYP EGTVPYVIGE AANTVMTYGY DVVTQMQETK ASLCQVSKA
//
