ID G5LKN1_SALET Unreviewed; 392 AA.
AC G5LKN1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Anaerobic dimethyl sulfoxide reductase chain A {ECO:0000313|EMBL:EHC43714.1};
GN ORFNames=LTSEALA_0947 {ECO:0000313|EMBL:EHC43714.1};
OS Salmonella enterica subsp. enterica serovar Alachua str. R6-377.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=913241 {ECO:0000313|EMBL:EHC43714.1, ECO:0000313|Proteomes:UP000004642};
RN [1] {ECO:0000313|EMBL:EHC43714.1, ECO:0000313|Proteomes:UP000004642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R6-377 {ECO:0000313|EMBL:EHC43714.1,
RC ECO:0000313|Proteomes:UP000004642};
RX PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA Furtado M.R., Wiedmann M.;
RT "Genome sequencing reveals diversification of virulence factor content and
RT possible host adaptation in distinct subpopulations of Salmonella
RT enterica.";
RL BMC Genomics 12:425-425(2011).
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}.
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:EHC43714.1}.
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DR EMBL; AFCJ01000396; EHC43714.1; -; Genomic_DNA.
DR PATRIC; fig|913241.3.peg.745; -.
DR Proteomes; UP000004642; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02775; MopB_CT; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 46..168
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 266..356
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 392 AA; 43855 MW; FF645CCFD9D90B63 CRC64;
MXEGGGARYG HLHTWGFNYN AMLQKPPVGA IGIPGAAGTT SEFGAAAGSD AVQYSDRSLN
INQTAQGILE ANDPPVRMLW VACKNPFAQD FDRSKMKKAF EKLEMVVCAD QFFNETVQHA
DIVLPVTTAF EEWNVDASYW HYWLSINQPA IKPMYEAKCD LEIATMLSRT INKMAPGSCT
FPQEFDHKRW LDQEFNDGMA KMFGISSWDD LLDGPKKAIL PSSAAWYDRK FKTPSGKYEF
KSELAEKNGH TALPEYKPEA ESKLPFHLFT PHVQFGLHSQ FINLDWMQVF YPEPFVYIHP
SSAKKKGISE NDLVKVFNGT GEVELRAKVT TNVPEDFLVM YEAWFPKRQY NVQNVVADTP
ADMGLMKTGA PGAAIHSQFA DVVLIGKGES VA
//
