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Database: UniProt
Entry: A0A1A6C537_9GAMM
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ID   A0A1A6C537_9GAMM        Unreviewed;       966 AA.
AC   A0A1A6C537;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Anaerobic dimethyl sulfoxide reductase chain A {ECO:0000313|EMBL:OBS09664.1};
GN   ORFNames=Thpro_021992 {ECO:0000313|EMBL:OBS09664.1};
OS   Acidihalobacter prosperus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Acidihalobacter.
OX   NCBI_TaxID=160660 {ECO:0000313|EMBL:OBS09664.1, ECO:0000313|Proteomes:UP000029273};
RN   [1] {ECO:0000313|EMBL:OBS09664.1, ECO:0000313|Proteomes:UP000029273}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5130 {ECO:0000313|EMBL:OBS09664.1,
RC   ECO:0000313|Proteomes:UP000029273};
RX   PubMed=25342676;
RA   Ossandon F.J., Cardenas J.P., Corbett M., Quatrini R., Holmes D.S.,
RA   Watkin E.;
RT   "Draft Genome Sequence of the Iron-Oxidizing, Acidophilic, and Halotolerant
RT   'Thiobacillus prosperus' Type Strain DSM 5130.";
RL   Genome Announc. 2:0-0(2014).
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:OBS09664.1}.
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DR   EMBL; JQSG02000003; OBS09664.1; -; Genomic_DNA.
DR   RefSeq; WP_038092449.1; NZ_JQSG02000003.1.
DR   AlphaFoldDB; A0A1A6C537; -.
DR   STRING; 160660.BJI67_02840; -.
DR   OrthoDB; 9815647at2; -.
DR   Proteomes; UP000029273; Unassembled WGS sequence.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd02783; MopB_CT_2; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.30.200.210; -; 1.
DR   Gene3D; 3.40.50.740; -; 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   PANTHER; PTHR43598:SF5; DMSO REDUCTASE CHAIN A; 1.
DR   PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 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.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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   Reference proteome {ECO:0000313|Proteomes:UP000029273}.
FT   DOMAIN          13..69
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   966 AA;  109447 MW;  9D144EBC6EF2E017 CRC64;
     MSAIPEFENH AKQEVKYTTC YMCACRCGIK VTVEDNQVRF IQGNRNHPIN KGVLCAKGNA
     GIMKQNSPAK LRSALLRKQG AERGSGEFEE IPMARALDIL TERLKKIRET DPKKLAYFTG
     RDQMQALTGL WATQFGTINW AAHGGFCSVN MAAGGLYTMG HAFWEFGDPD WDRTKYFMMW
     GVAEDHASNP IKIGIEKLKR RGAKFVGVNP VRTGYQAVAD EWIPIRPGTD AMFALSMAHV
     LLKHEQFDWE FMIRYTNSPW LVVSTPGEQG DGLFVRDADG KPLAWDMASE SFVDATRADI
     QPALFWEGQG PDGRPVKSAM MLLAEKYLDE QYAPENAEKV TGVPAETIER LALEMAHVAF
     KETIEVDVEW TDWAGRKHDK FVGRPVSMHA MRGISAHSNG FQACRAIHLV QALLGSIDCP
     GGHVAKPPYP KHVPPSIKPA KEMAPNTPLK SPPLGFPKAP EDLVIDADGN PLRIDKAFSW
     DAPISNHGLM HMVITNAVKG DPYPIDTLMF FMANMSWNST MNTKDVQDML RAKDDNGEYK
     IPFLVVSDAY HSEMVNFADL VIPDTTYLER YDTISMLDRP ISEADLAADS IRQPVIEPKR
     DVMAWQEVQV ELASRLKFPA FTNADGSRKF KDYKDFIVNY EKEPGIGFLS GWRLDENGNE
     VHLRGKPNPK QWDRYIENQS FFAYHLPENT RYYRFANKDY LELAKHAGWV GSTDPIIIEL
     YSETLQKFRL AGQGLYDGPQ PTRPEHKERL VKYFSPLPEH YKPLEQCRID EDEYPFHAVN
     QRPMFMYHSW DSQNAWLRQI VAQNYLFMSR QQATEMGIED LSWVWVESHN GKIRVQVKLM
     EGVERNTVWT WNAIGKQSGA WGLKPDANEA TKGFLMNHLI RELLPSKGDA VDNITNSDPV
     TGQAAWYDLR VKITPAAPGE VGSWPTFDTI KRLPNVAESP DVLRYHTHAP VRMQRDLGDV
     LTRGQK
//
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