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}.
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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
//