ID A0A0H3GMZ1_KLEPH Unreviewed; 811 AA.
AC A0A0H3GMZ1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Dimethyl sulfoxide reductase, major subunit {ECO:0000313|EMBL:AEW61190.1};
GN OrderedLocusNames=KPHS_24920 {ECO:0000313|EMBL:AEW61190.1};
OS Klebsiella pneumoniae subsp. pneumoniae (strain HS11286).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1125630 {ECO:0000313|EMBL:AEW61190.1, ECO:0000313|Proteomes:UP000007841};
RN [1] {ECO:0000313|EMBL:AEW61190.1, ECO:0000313|Proteomes:UP000007841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS11286 {ECO:0000313|EMBL:AEW61190.1,
RC ECO:0000313|Proteomes:UP000007841};
RX PubMed=22408243; DOI=10.1128/JB.00043-12;
RA Liu P., Li P., Jiang X., Bi D., Xie Y., Tai C., Deng Z., Rajakumar K.,
RA Ou H.Y.;
RT "Complete genome sequence of Klebsiella pneumoniae subsp. pneumoniae
RT HS11286, a multidrug-resistant strain isolated from human sputum.";
RL J. Bacteriol. 194:1841-1842(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; CP003200; AEW61190.1; -; Genomic_DNA.
DR RefSeq; WP_014343046.1; NC_016845.1.
DR RefSeq; YP_005226792.1; NC_016845.1.
DR AlphaFoldDB; A0A0H3GMZ1; -.
DR STRING; 1125630.KPHS_24920; -.
DR GeneID; 11847510; -.
DR KEGG; kpm:KPHS_24920; -.
DR PATRIC; fig|1125630.4.peg.2423; -.
DR HOGENOM; CLU_000422_13_3_6; -.
DR Proteomes; UP000007841; 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 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; IPR006311; TAT_signal.
DR InterPro; IPR049754; YnfE.
DR NCBIfam; TIGR02166; dmsA_ynfE; 1.
DR NCBIfam; NF041885; selenate_YnfE; 1.
DR PANTHER; PTHR43742:SF7; DIMETHYL SULFOXIDE REDUCTASE CHAIN YNFE-RELATED; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000007841};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 52..113
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 789..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 811 AA; 89921 MW; 538DCFD82C070C6A CRC64;
MSNQESPGGV SRRALLKSTA LGSLALAAGG LTLPFTLRRA AAAVQQATGD TTRIVWGACS
VNCGSRCALR LHVRDDEVVY VETDNTGDDR YGDHQVRACL RGRSIRRRIN HPDRLNYPMK
RVGKRGEGKF VRISWQEALD TLADRLKSVV AQYGNEAVYI NYSSGIVGGN ITRSSPSASP
VARLMNCYGG SLNQYGTYST AQIACAMPYT YGSNDGNSTS DIENSKLVVM FGNNPAETRM
SGGGITWYLE QARERSNARM IVIDPRYTDT AAGREDEWIP IRPGTDAALV AGIAWVLINE
DLVDQPFLDK YCVGYDEKTL PAGAPANGHY KAYILGEGDD GIAKTPQWAS RITGIPTERI
IKLAREIGMS KPAYICQGWG PQRQANGELT ARAIAMLPIL TGNVGINGGN SGARESTYTI
TIERLPVLEN PVKTAISCFT WTDAIARGPE MTASRDGVRG KEKLDVPIKF LWNYAGNTLI
NQHSDINKTH EILQDESKCE TIVVIDNFMT SSAKYADLLL PDLMTVEQED IIPNDYAGNM
GYLIFIQPAT SAKFERKPIY WILSEVAKRP GDDVHQRFTE GRTQEQWLQY LYAKMVAKDP
ALPAYEDLKR MGIYKRKDPN GHFVAYRDFR RDPEAHPLKT PSGKIEIYSS RLAEIAARWQ
LEKDEVISPL PVYASTFEGW DDPLRSQYPL QLFGFHYKAR THSSYGNVDV LQAACRQEVW
INPLDAEKRG IKNGDMVRVF NQRGEVRLPA KVTPRIMPGV SAMGQGAWHD ANMTGDRIDH
GACMNTLTTH RPSPLAKGNP QHTNLVDIEK V
//
