ID Q24Y63_DESHY Unreviewed; 880 AA.
AC Q24Y63;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Putative anaerobic DMSO reductase chain A {ECO:0000313|EMBL:BAE83029.1};
DE EC=1.7.99.4 {ECO:0000313|EMBL:BAE83029.1};
GN Name=dmsA {ECO:0000313|EMBL:BAE83029.1};
GN OrderedLocusNames=DSY1240 {ECO:0000313|EMBL:BAE83029.1};
OS Desulfitobacterium hafniense (strain Y51).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=138119 {ECO:0000313|EMBL:BAE83029.1, ECO:0000313|Proteomes:UP000001946};
RN [1] {ECO:0000313|EMBL:BAE83029.1, ECO:0000313|Proteomes:UP000001946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y51 {ECO:0000313|EMBL:BAE83029.1,
RC ECO:0000313|Proteomes:UP000001946};
RX PubMed=16513756; DOI=10.1128/JB.188.6.2262-2274.2006;
RA Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT "Complete genome sequence of the dehalorespiring bacterium
RT Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT ethenogenes 195.";
RL J. Bacteriol. 188:2262-2274(2006).
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; AP008230; BAE83029.1; -; Genomic_DNA.
DR RefSeq; WP_005814558.1; NC_007907.1.
DR AlphaFoldDB; Q24Y63; -.
DR STRING; 138119.DSY1240; -.
DR KEGG; dsy:DSY1240; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_9; -.
DR Proteomes; UP000001946; Chromosome.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0008940; F:nitrate reductase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 2.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
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; IPR019546; TAT_signal_bac_arc.
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; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF10518; TAT_signal; 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; PS51257; PROKAR_LIPOPROTEIN; 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:BAE83029.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001946};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 53..114
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 880 AA; 97203 MW; 03163BC92B5CA663 CRC64;
MSRLLDKIND QKISRRNFLK ATAAGTASLA LAGCGSGLTS AGEKVNALGE EQGEWIPAAC
WHNCGGRCLN KALVVDGVVV RQKTDDTHED SPDYPQQRGC LRGRSQRQQV FGADRLKYPM
KRKHWQPGGG DKSLRGKDEW ERISWDEALT YIADELQRVK KDYGNRSILH IGGWSSRITD
ISRTLGLFGG YCEYWNTNSF GSWAMTPKTV GFLQLGVWDQ TVNDRFDLRN CETIIMLSMN
PAWSAMGSSS WHYLQAKKAG AKFIGIDPFY NESYSMLGAE WVPVRPSTDS ALLLAIAYVL
ITKDHPAMNP LIDWEFLNKY CLGFDAEHMP EGEDPQGNFK DYVLGTYDGV PKTPAWASEI
CGVDKIQIEK LAMEFRKDKK VAFLCGMASA RTTNSDNLPQ LIMTIGAMTG HMGKSGHMTG
STMHATSGNG GPALVCAGSN GLPGIANPVD DSINAGQVWD AILNGKYNFT GSGDFVSPDQ
FKPGQERDID IHIIYHSGGA TLQTSDGMTK GIEAHRKVDL VVSHSQFVTT NSKYADIVLP
VTTEWEKFGG FSGGTLVHSG NREMLIMYSQ ITEPLYEARS DQWIAIELAK KLGIDEKEAF
PFDEKQQFFN ALASATVVNE DGKTYGPLVT ITQKDIDEMG VAGKPQTGKI TYRELKEKGV
YQVKRSPGDN YGYIAYEDFV KDPGKNPLTS ESGKLEIYSR QLAKTVNDMG FSRIHPIPSY
IPPVNGYEDT FQDWESKAKG EYPYQVINPH YLRRSHTVFD NVKWLQEAWS NPVFLNTKDA
QAKGISNGDT VLITSPYGQI LRNACLTERV RPGVVALPHG AWVDIDEQTG IDRGGADNIL
SGQVPTGQGV SGFNTGVARI EKYTPSKLIP DVEKPARIVF
//
