ID I2B617_SHIBC Unreviewed; 808 AA.
AC I2B617; K6UTQ0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Anaerobic dimethyl sulfoxide reductase chain A {ECO:0000313|EMBL:AFJ45971.1};
GN Name=dmsA1 {ECO:0000313|EMBL:AFJ45971.1};
GN OrderedLocusNames=EBL_c08510 {ECO:0000313|EMBL:AFJ45971.1};
OS Shimwellia blattae (strain ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 /
OS CDC 9005-74) (Escherichia blattae).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shimwellia.
OX NCBI_TaxID=630626 {ECO:0000313|EMBL:AFJ45971.1, ECO:0000313|Proteomes:UP000001955};
RN [1] {ECO:0000313|EMBL:AFJ45971.1, ECO:0000313|Proteomes:UP000001955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 / CDC 9005-74
RC {ECO:0000313|Proteomes:UP000001955};
RX PubMed=22843577; DOI=10.1128/JB.00829-12;
RA Brzuszkiewicz E., Waschkowitz T., Wiezer A., Daniel R.;
RT "Complete genome sequence of the B12-producing Shimwellia blattae strain
RT DSM 4481, isolated from a cockroach.";
RL J. Bacteriol. 194:4436-4436(2012).
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; CP001560; AFJ45971.1; -; Genomic_DNA.
DR RefSeq; WP_002442428.1; NZ_BAHA01000016.1.
DR AlphaFoldDB; I2B617; -.
DR STRING; 630626.EBL_c08510; -.
DR KEGG; ebt:EBL_c08510; -.
DR PATRIC; fig|630626.3.peg.830; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_6; -.
DR OrthoDB; 9815647at2; -.
DR Proteomes; UP000001955; 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 CDD; cd02794; MopB_CT_DmsA-EC; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.12440; -; 2.
DR Gene3D; 3.40.50.740; -; 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 NCBIfam; TIGR02166; dmsA_ynfE; 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 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 Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001955};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 54..114
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 808 AA; 90639 MW; D00ED777426E70E7 CRC64;
MSDKNNSLTV ASSIGLSRRR FLQLSSYLGV GAFLATHSLN SIAASVISEH VGEITKWHNC
WAHCHSSCLL KIVTENGQIK RIETDDQGDD VFGRHQVRAC LRGRSLHKRA FSPDRLKYPM
KRIGKRGEGK FKRISWDEAL DEVYLQMSKI ISKYGNQAIF NRIGFGKPDG PYHFVPRFLN
LIGGFLSAEG NYSSHQIDTA SKYTYGESKY TFGSAPSEMA HSDLIVYFGN NPANTRMSGA
NDTYHYQHYK KQSSAKTVII DPQYTDTACG REDLWLAIRP GSDAALVEAI AWVLITEKFV
DEEFLHKYCY GYDGEPGDSE KGIPSLEPSL GYKAYILGDG PDKLEKKPEY AESICGIPSE
QIYQLARALG NAKAPFIAQG WGPQRHAAGE QTARAIFMLP ILLGKIGLPG TNNGGSDFMF
SGSDITPMPI GKNGVQAKVP CFKWLEAVER GHEMTALSDG ITGAERLTSD VKCIFMYQGN
WLLNQHSDCN ATAKILADES KLEFIFVMDN HMTASAKFAD ILLPDITWLE NSRVVRFATH
LTLTEHVLDP MYECRHPYQV FSDLAERFGV REAFCEGRSW DEWQQYLYEE SRKKHPEFPP
FDVLQKKKTI RLPFDPEAPG YVMREFREDP IIHALKTESG KIQIYSHTLA QYAANWQLPD
GDKITPLPQY IPTWESYADT ETREKYPLQL IGFKSKGRPH STFHNVPWLR EVIQDALMIN
PLDARARNLH QGQQVHVYND RGVISVPIRI TPRIMPGVVG LGEGAWYSPD SHGVDVGGCI
NTLTRLKPTA LAKANPQGTN LVEVSPAP
//
