ID A0A085GGR5_9ENTR Unreviewed; 814 AA.
AC A0A085GGR5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Anaerobic dimethyl sulfoxide reductase chain A {ECO:0000313|EMBL:KFC82910.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:KFC82910.1};
DE EC=1.8.99.- {ECO:0000313|EMBL:KFC82910.1};
GN Name=dmsA {ECO:0000313|EMBL:KFC82910.1};
GN ORFNames=GBAG_1283 {ECO:0000313|EMBL:KFC82910.1};
OS Buttiauxella agrestis ATCC 33320.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Buttiauxella.
OX NCBI_TaxID=1006004 {ECO:0000313|EMBL:KFC82910.1, ECO:0000313|Proteomes:UP000028653};
RN [1] {ECO:0000313|EMBL:KFC82910.1, ECO:0000313|Proteomes:UP000028653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33320 {ECO:0000313|EMBL:KFC82910.1,
RC ECO:0000313|Proteomes:UP000028653};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (MAY-2014) 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:KFC82910.1}.
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DR EMBL; JMPI01000022; KFC82910.1; -; Genomic_DNA.
DR RefSeq; WP_034494311.1; NZ_JMPI01000022.1.
DR AlphaFoldDB; A0A085GGR5; -.
DR STRING; 1006004.GBAG_1283; -.
DR eggNOG; COG0243; Bacteria.
DR OrthoDB; 9815647at2; -.
DR Proteomes; UP000028653; Unassembled WGS sequence.
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; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 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; PS00932; MOLYBDOPTERIN_PROK_3; 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 ECO:0000313|EMBL:KFC82910.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028653};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 56..118
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 794..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 814 AA; 89754 MW; 28F2C30D70910B48 CRC64;
MKEKTSNAVL SAQVSRRKLV KTTAIGGLAA ASGALTLPFS RMAFAQTAAD TVSTAENVVW
SACTVNCGSR CPLRMHVVDG EIKYVETDNT GIDDYEGLHQ VRACLRGRSM RRRVYNADRL
KYPMKRVGAR GEGKFERISW DEAFDTIANS MKGIIKEHGN EAIYLNYGTG TLGGTMTRSW
PPGSTLIARL MNCCGGYLNH YGDYSTAQIA AGLNYTYGGW ADGNSPSDIE NSKLVVLFGN
NPGETRMSGG GVTYYLEQAR EKSNARMIII DPRYTDTGAG REDEWIPIRP GTDTALISAL
AWVMIAENLV DQPFLDKYCV GYDEKTLPKT APANGHYKAY ILGEGADGVA KTPQWAAKIT
GIPAERIVQL AREIATAKPA FISQGWGPQR HSNGELVSRA IAMLSILTGN VGVNGGNSGA
REGSYSLPFV RMPTLENPVQ TSISMFLWTD AIERGPEMTA TRDGVRGKDK LDVPIKMVWN
YASNCLINQH SEINRTHDIL QDDKKCEMIV VIDNHMTSSA KYADILLPDC TASEQMDFCL
DASCGNMAYV IFAGQAIKPR FECKTIYEMT SEIAKRMGVE QQFTEGRNQE EWMRHLYKQS
QEAIPELPSF EEFSKQGIFK KRDPEGHHVA YKAFREDPAA NPLTTPSGKI EIYSEQLAEI
AATWQLNEGD VIDPLPVYSA GFENYGDPLA EKWPLQMTGF HYKARTHSTY GNVEVLKAAC
RQEMWINPID AQQRGIKNGD MIRIFNGRGE VHINAKVTPR IIPGVVAMGE GAWYSPDANK
VDHAGCINVL TTQRPSPLAK GNPSHSNLVQ VEKA
//
