ID Q1Z511_9GAMM Unreviewed; 813 AA.
AC Q1Z511;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Putative dimethyl sulfoxide reductase chain A protein {ECO:0000313|EMBL:EAS43755.1};
GN ORFNames=P3TCK_18287 {ECO:0000313|EMBL:EAS43755.1};
OS Photobacterium profundum 3TCK.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=314280 {ECO:0000313|EMBL:EAS43755.1, ECO:0000313|Proteomes:UP000003789};
RN [1] {ECO:0000313|EMBL:EAS43755.1, ECO:0000313|Proteomes:UP000003789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3TCK {ECO:0000313|EMBL:EAS43755.1,
RC ECO:0000313|Proteomes:UP000003789};
RA Bartlett D.H., Valle G., Lauro F.M., Vezzi A., Simonato F., Eloe E.,
RA Vitulo N., Stratton T.K., D'angelo M., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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:EAS43755.1}.
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DR EMBL; AAPH01000009; EAS43755.1; -; Genomic_DNA.
DR RefSeq; WP_006231567.1; NZ_CH724135.1.
DR AlphaFoldDB; Q1Z511; -.
DR HOGENOM; CLU_000422_13_3_6; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000003789; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-KW.
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; -; 2.
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; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR02166; dmsA_ynfE; 1.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR43742:SF8; ANAEROBIC DIMETHYL SULFOXIDE REDUCTASE, SUBUNIT A-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; PS00551; MOLYBDOPTERIN_PROK_1; 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 Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 52..114
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 813 AA; 90101 MW; DCD6AFEB9CA76510 CRC64;
MTISNKIKSH LLSRRKFIHT SAAVTGAVAA ASSMALPFKA QAISPTVDLA EETIKYSACL
VNCGSRCPFK VHVKEGVAVK ISPEDGVDEA IFGQHQIRPC LRGRSARWRT YNPDRLKYPM
LRVGKRGEGK FKRISWDEAT TIVAKELRRV IDTHGNEAIY YQYGSGLTGA NLQGRNTCKR
LLNIAGGFLD MHNTYSEAQL NCIQPYVFGQ AGNIYGTEQQ TLFSEIKNSD LVVMFGQNLA
ETRMSGGGQI AEIYHALEQS KAKVIIIDPR RTDSVTAFDS EWLPIRPGTD AALVAAMGYV
LIKEDLINEE MLKQYTVGWS DDTLPATASS NASYKSYILG LGEDKTPKTP EWASELTGIP
ADRIKQLARE IANAKAAWVS QGWGVQRTQT GEHAARAIMM LPIMTGQFGR PGTNIGTWGG
SVGYTLSGLA LPNPVKVSIP CFLWTDAIVR GTEMTAAKDY IKGKDRLSTN VKFLWNYASN
ISGNQHSDLN RTHEILTDES LCEFNLVWDN HMTASAKYAD LLLPDVSTLE SDDLINNSYQ
SGSYHYLVRL QQAVEPMWEN RATYDVLAEI AEKMGFKDKF TEGRTYQEWI EHAYNEVRKK
ETHLPTFAET DGMGIIDRRI ADSSKHIALK DFRDNPQAHP LKTPSGKIEI YSEALAQVAK
EREILPGDRI TAIPEYQPAV EGCEDHEMLK KYPLQLTGFH TKGHCHSTYS SVAQLKEVAP
DAVWMNTLDA QSRQIKNGDI VEIFNDRGRI HLPAKVTARI MPGTAAVPEG AWAKTNKKGV
DVGGCINRLT TQRATALAKG NPQHTNLVEI QSV
//