ID B1VG96_CORU7 Unreviewed; 819 AA.
AC B1VG96;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Dimethyl sulfoxide reductase chain A {ECO:0000313|EMBL:CAQ04785.1};
DE EC=1.8.99.- {ECO:0000313|EMBL:CAQ04785.1};
GN Name=dmsA {ECO:0000313|EMBL:CAQ04785.1};
GN OrderedLocusNames=cu0825 {ECO:0000313|EMBL:CAQ04785.1};
OS Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=504474 {ECO:0000313|EMBL:CAQ04785.1, ECO:0000313|Proteomes:UP000001727};
RN [1] {ECO:0000313|EMBL:CAQ04785.1, ECO:0000313|Proteomes:UP000001727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43042 / DSM 7109 {ECO:0000313|Proteomes:UP000001727};
RX PubMed=18367281; DOI=10.1016/j.jbiotec.2008.02.009;
RA Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A.,
RA Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., Kalinowski J.,
RA Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., Soriano F., Droege M.,
RA Puehler A.;
RT "The lifestyle of Corynebacterium urealyticum derived from its complete
RT genome sequence established by pyrosequencing.";
RL J. Biotechnol. 136:11-21(2008).
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; AM942444; CAQ04785.1; -; Genomic_DNA.
DR RefSeq; WP_012360074.1; NC_010545.1.
DR AlphaFoldDB; B1VG96; -.
DR STRING; 504474.cu0825; -.
DR GeneID; 60603602; -.
DR KEGG; cur:cu0825; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_11; -.
DR Proteomes; UP000001727; 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; 3.40.50.12440; -; 1.
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; 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; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CAQ04785.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001727};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 51..112
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 819 AA; 89986 MW; 38199350099FD23E CRC64;
MANLNKVTRR RFLGWSAAAG GAGALVASGA GDILSKQFLG IPAMGQEEAN EKIVWSACTV
NCGSRCPLRL KVRDGQIVQV MADNTGDAEL GTQQIRACVR GRSIRHRIYN PDRLKTPLKR
KPDTKRGDGE WIEISWEQAL DEIAEKMKDI KSNYGNEAFY LQYGTGVIGA TIARSWPPVE
TPFARLMNLW GGYLNHYSDY STAQITSAYP YHYGEWIGSN SFDDVANSKL QVMFGNNPLE
TRMSGGGETF VTQKIKQEHG VKTIVIDPRQ SETSVALADE WVALRPGTDA ALVAGLIHVM
LTENLQDQKF LDKYTVGFDE HTLPDSAPKN SSYRAYVMGK GPDGIEKTPQ WAAKVTGVPA
DRITQLAREI AQAKPCAITQ GWGPQRHANG ENQARAIFLL AAVIGQIGIK GGGTGARESS
ANLGMASPFN TQHENPIETA IPVFGWTEAV ERGEEMTATR DGVQGKDKLD VPIKMIWSYG
GNANTNQHGD LNRTIELLRR EDKAELIVVS DIQMSVSARY ADYVLPDAST AEQEDVIQQG
SAGNMEYTIL ASKAIEPIHN TKPIYEVCAE LAERLGVGKK FTEGRTQEQW VKHTIAESAR
EIPELPSYEK LKEMGVWKRA GESVIPLKEF REDPVANPLE TPSGLIEIYS EELAKLRKEW
EFPNAAPGDE ITALPEHVDT WEGPAEAHKA YTSGGKYPLQ CIGHHTKGRT HSSYANVDWL
RDDAHPQVLW INPLDARKRG IKNDDEVYAF NDRGRIKSVA RVSPRIAPGV ISVPQGSWFA
PDGKGVDAGA SVNTLTSWHP SPLGKGNAQH TTLVEVEKA
//
