GenomeNet

Database: UniProt
Entry: A0A083ZYT8_9GAMM
LinkDB: A0A083ZYT8_9GAMM
Original site: A0A083ZYT8_9GAMM 
ID   A0A083ZYT8_9GAMM        Unreviewed;       819 AA.
AC   A0A083ZYT8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Dimethyl sulfoxide reductase DmsA {ECO:0000313|EMBL:KEY58217.1};
DE            EC=1.8.5.3 {ECO:0000313|EMBL:KEY58217.1};
GN   Name=dmsA {ECO:0000313|EMBL:KEY58217.1};
GN   ORFNames=SRDD_28640 {ECO:0000313|EMBL:KEY58217.1};
OS   Serratia sp. DD3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=1410619 {ECO:0000313|EMBL:KEY58217.1, ECO:0000313|Proteomes:UP000017810};
RN   [1] {ECO:0000313|EMBL:KEY58217.1, ECO:0000313|Proteomes:UP000017810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD3 {ECO:0000313|EMBL:KEY58217.1,
RC   ECO:0000313|Proteomes:UP000017810};
RX   PubMed=25212623;
RA   Poehlein A., Freese H.M., Daniel R., Simeonova D.D.;
RT   "Draft Genome Sequence of Serratia sp. Strain DD3, Isolated from the Guts
RT   of Daphnia magna.";
RL   Genome Announc. 2:e00903-14(2014).
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   -!- 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:KEY58217.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AYKS02000072; KEY58217.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A083ZYT8; -.
DR   STRING; 1410619.SRDD_28640; -.
DR   eggNOG; COG0243; Bacteria.
DR   Proteomes; UP000017810; Unassembled WGS sequence.
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   CDD; cd02770; MopB_DmsA-EC; 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; 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; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
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; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR   PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 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   ECO:0000313|EMBL:KEY58217.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017810};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          61..123
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   819 AA;  90239 MW;  25BC4EE27CDE36C6 CRC64;
     MMNESEKKPL SGLQCSRRKL VKNSAIGGLA LAVGGVTLPF SRQVKAENGV TPGAAVPKPE
     EKVVWSACTV NCGSRCPLRM HIVDGAIKYV ETDNTGDDAY QGLHQVRACL RGRSMRRRVY
     NPDRLQYPML RVGKRGEGKF KRISWDEAFT LISDNLKRII KDYGNEAIYL NYGTGTLGGT
     MTRSWPPGAT LIARLMNCCG GYLNHYGDYS TAQIAMGLNY TYGGWADGNS PTDIENSKLV
     VMFGNNPGET RMSGGGVTYL LEQARERSNA RMIVIDPRYT DTAAGREDEW IPIRPGTDAA
     LVAGLAHVLI TENLVDQPFL DKYCIGYDEK TLPAGAPANS HYKAYILGQG EDGIAKTPAW
     AAQITGIPAD RIIKLAREIG SIKPAYICQG WGPQRQANGE LTSRAIAMLP ILTGNVGING
     GNSGAREGSY SLPFVRMPTL TNPVKTSISM FLWTDAILRG PEMTAKRDGV RGKDKLDVPI
     KFVWNYAGNC LINQHSQINR THDILQDEKK CEMIVVIDNH MTSSAKYADL VLPDCTASEQ
     QDFCLDASSG NMGYVIFADQ AIKPIGECKN IYEMTSEIAR RMGVEQLFTE GRTQEEWLRY
     LYQQSRQAIP ALPEFEQFLE QGIFKQRDPE GHHVAYKAFR ADPQANPLTT PSGKIEIYSA
     QLAEVAATWE LEKGDVIHPL PIYTAGFESP SDPLSSQYPL QMTGFHYKAR THSTYGNVDV
     LKASCRQEMW INPIDAESRG IANGDLIRIY NDRGEVRINA KVTPRMRPGV VALGEGAWYA
     PDGNKIDHAG SINVLTTQRP SPLAKGNPSH TNLVQVAKL
//
DBGET integrated database retrieval system