ID A8FQ49_SHESH Unreviewed; 816 AA.
AC A8FQ49;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family protein {ECO:0000313|EMBL:ABV34972.1};
DE Flags: Precursor;
GN OrderedLocusNames=Ssed_0359 {ECO:0000313|EMBL:ABV34972.1};
OS Shewanella sediminis (strain HAW-EB3).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34972.1, ECO:0000313|Proteomes:UP000002015};
RN [1] {ECO:0000313|EMBL:ABV34972.1, ECO:0000313|Proteomes:UP000002015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34972.1,
RC ECO:0000313|Proteomes:UP000002015};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella sediminis HAW-EB3.";
RL Submitted (AUG-2007) 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; CP000821; ABV34972.1; -; Genomic_DNA.
DR RefSeq; WP_012140710.1; NC_009831.1.
DR AlphaFoldDB; A8FQ49; -.
DR STRING; 425104.Ssed_0359; -.
DR KEGG; sse:Ssed_0359; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_6; -.
DR OrthoDB; 9815647at2; -.
DR Proteomes; UP000002015; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0009389; F:dimethyl sulfoxide reductase activity; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
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; IPR011888; Anaer_DMSO_reductase.
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 InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR02166; dmsA_ynfE; 1.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR43742:SF3; DIMETHYL SULFOXIDE REDUCTASE DMSA; 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; PS51257; PROKAR_LIPOPROTEIN; 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 Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002015};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 44..107
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 816 AA; 89589 MW; BC3E3B17D9052E6E CRC64;
MERRTFLKFS AAAAAVATVT GCESSSASNP LPAPSEPVLP PVGEGITWGS CATNCWQACP
LKVHSKDGVI TRIETEGKAT DDWDNFDHEI RPCPRGRSMR QKVYNHDRLK YPMKRVGRRG
SDEFVRISWE EAVSSVASAM EQTYSQYGKN AIFMPLGGGS HDLNTGVTQS SVRLLNMAGG
CLFFHNDYSA AQYREGSAGM YGYLASNAGD TVGFWNTGSS LRSLEDSDLM VCFGYNPMEA
RLGGAGSGYE YLNVKKKNNF KTYYIDPRFT DTAVTANDEW IPIRPGTDAA LCEAIAYVLI
EDGYADIPFL EQYTHGYDKY QDYITGVTDG TTKTPERAEG ICGIPAEKIR EIAQAIGAAS
APFVTQGFGP QRQGNGENNA RAVMMLPLLV GKISGDGTNH GGTPGNDGLS HYAMMPADTL
QDLMNMKIMD VTIPAASHLD AIEFGMQMKP STHDVRYSNP DLMAADTPLE TNVRFLWLAS
SNMLANQNGD INRADRLLND ESLVDFVVVV EQHMTASAKY ADIILPEVSW LEMYDVIQSY
NKMDCGSLMY AYGITPAVDP MFECKPAYDI CHMIANQLGI GSKFTNGGMT YLDQVRKVFA
EFKKSNPWIQ GDTFEEFVSF GPQRRPAGEH PNVGKIRDFI TDPIASPLGT PSGKVEIYSQ
YFEGKQTQAE GTDEINPLPV YFACDESYED ATASEFPLQC INYHGKHSAH SIHASTPWLN
EVLEHHLWLN PIDAGAAGVI NGQKVIVESR RGKLEITARV TPRIVPGVVA MPQGQWRRMK
GDIDVGGCAN TLTDSKPSPV AKSFRSNTNR VRVYSA
//
