ID W8UMN4_KLEPN Unreviewed; 824 AA.
AC W8UMN4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Anaerobic dimethyl sulfoxide reductase chain A {ECO:0000313|EMBL:AHM80365.1};
DE EC=1.8.5.3 {ECO:0000313|EMBL:AHM80365.1};
DE EC=1.97.1.9 {ECO:0000313|EMBL:AHM80365.1};
GN ORFNames=KPNJ2_03585 {ECO:0000313|EMBL:AHM80365.1};
OS Klebsiella pneumoniae 30684/NJST258_2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1420013 {ECO:0000313|EMBL:AHM80365.1, ECO:0000313|Proteomes:UP000019586};
RN [1] {ECO:0000313|EMBL:AHM80365.1, ECO:0000313|Proteomes:UP000019586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=30684/NJST258_2 {ECO:0000313|EMBL:AHM80365.1};
RX PubMed=24639510; DOI=10.1073/pnas.1321364111;
RA Deleo F.R., Chen L., Porcella S.F., Martens C.A., Kobayashi S.D.,
RA Porter A.R., Chavda K.D., Jacobs M.R., Mathema B., Olsen R.J., Bonomo R.A.,
RA Musser J.M., Kreiswirth B.N.;
RT "Molecular dissection of the evolution of carbapenem-resistant multilocus
RT sequence type 258 Klebsiella pneumoniae.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:4988-4993(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}.
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DR EMBL; CP006918; AHM80365.1; -; Genomic_DNA.
DR AlphaFoldDB; W8UMN4; -.
DR KEGG; kps:KPNJ2_03585; -.
DR PATRIC; fig|1420013.3.peg.3372; -.
DR HOGENOM; CLU_000422_13_3_6; -.
DR Proteomes; UP000019586; 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 GO; GO:0033797; F:selenate reductase activity; IEA:UniProtKB-EC.
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 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 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:AHM80365.1}; Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 66..128
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 805..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 824 AA; 91394 MW; 1F0B810454CEE1E3 CRC64;
MSVYCEQPKR VSMKIKAPDA LLAAEVSRRG LMKTTAIGGL ALASNALTLP FTRLSHAADT
PAPASEKVVW SACTVNCGSR CPLRMHVVDG AIKYVETDNT GDDNYDGLHQ VRACLRGRSM
RRRVYNPDRL KYPMKRVGKR GEGKFEQISW EEALDTIASN MQRLIKEYGN ESIYLNYGTG
TLGGTLTRSW PPGKTLIARL MNCCGGYLNH YGDYSSAQIA AGLNYTYGGW ADGNSPSDIE
NSQLVVLFGN NPGETRMSGG GVTYYLEQAR QKSNARMIII DPRYTDTGAG REDEWIPIRP
GTDAALVSGL AWVMITENLV DQPFLDKYCV GYDEKTLPAG APANGHYKAY ILGQGIDGIA
KTPEWASTIT GIPRERIVKL AREIATAKPA YISQGWGPQR HANGEIATRA ISMLAILTGN
VGINGGNSGA REGSYSLPFE RMPTLENPVE TSISMFMWTD AIERGPEMTA LRDGVRGKDK
LDVPIKMIWN YAGNCLINQH SEINRTHEIL QDDKKCEMIV VIDCHMTSSA KYADILLPDC
TASEQMDFAL DASCGNMSYV IFADQAIKPR FECKTIYEMT SELAKRLGVE EQFTEGRTQE
GWMRYLYEQS RKAIPDLPDF DTFRQQGIYK QRDPQGHHVA YKAFREDPQA NPLTTPSGKI
EIYSQDLAKI AATWELPEGD VIDPLPIYTP GFENYNDPLT AKYPLQLTGF HYKSRVHSTY
GNVDVLKAAC RQEMWINPID ARKRGIANGD RIRIFNDRGE VHIEAKVTPR MMPGVVALGE
GAWYNPDASR VDQAGSINVL TTQRPSPLAK GNPSHTNLVQ VEKL
//
