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Database: UniProt
Entry: G4A5E9_AGGAC
LinkDB: G4A5E9_AGGAC
Original site: G4A5E9_AGGAC 
ID   G4A5E9_AGGAC            Unreviewed;       601 AA.
AC   G4A5E9;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Anaerobic dimethyl sulfoxide reductase chain A {ECO:0000313|EMBL:EGY35339.1};
GN   ORFNames=SC1083_0034 {ECO:0000313|EMBL:EGY35339.1};
OS   Aggregatibacter actinomycetemcomitans serotype e str. SC1083.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Aggregatibacter.
OX   NCBI_TaxID=907488 {ECO:0000313|EMBL:EGY35339.1, ECO:0000313|Proteomes:UP000005508};
RN   [1] {ECO:0000313|EMBL:EGY35339.1, ECO:0000313|Proteomes:UP000005508}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC1083 {ECO:0000313|EMBL:EGY35339.1,
RC   ECO:0000313|Proteomes:UP000005508};
RA   Chen C., Kittichotirat W., Asikainen S., Bumgarner R.;
RL   Submitted (OCT-2010) 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   -!- 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:EGY35339.1}.
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DR   EMBL; AEJM01000001; EGY35339.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4A5E9; -.
DR   SMR; G4A5E9; -.
DR   PATRIC; fig|907488.3.peg.33; -.
DR   Proteomes; UP000005508; 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   CDD; cd02770; MopB_DmsA-EC; 1.
DR   Gene3D; 3.40.50.12440; -; 2.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   InterPro; IPR011888; Anaer_DMSO_reductase.
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   SMART; SM00926; Molybdop_Fe4S4; 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; PS51318; TAT; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00023014};
KW   Molybdenum {ECO:0000256|ARBA:ARBA00022505}.
FT   DOMAIN          47..109
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   601 AA;  66644 MW;  00081B5CEF267E09 CRC64;
     MNNFNQLSRR DFIKSSLAGA AIIAADIVLP FNVMATDTLK KEQESAEKVV WSACTVNCGS
     RCPLRMHVRD NRITYVETDN TDTETYNVDH QVRACLRGRS MRRRVYNPDR LKYPMKRVGK
     RGEGKFKRIS WDEALTEIAN ALKRNIAKYG NESIYLNYGT GTLGGTMTKS WPPASTMVAR
     FMNCIGGYLN HYGDYSTAQI AVGLDYTYGG GWALGNGMAD IENTKLIVLF GNNPAETRMS
     GGGLTYCIEQ AKQRSNAKMI LIDPRYTDTG VGREDEWIPI RPGTDAALVS ALAYVMITED
     LVDQPFLDKY CVGYDETTLP EGAPQNGHYK AYILGQGDDG IAKTPEWASK ITGIPVDRII
     KLAREIGSTK PAFISQGWGP QRRSNGELIS RAIAMLPILT GNVGIHGGNT GARESAYSIP
     FVRMPTLKNP VKASIPMFMW TDTIIRGPEM TALTDGIRGV DKLSAPIKVI WNYSSNCLIN
     QHAQINRTHD ILQDDSQCEM IITIDNHMTS TAKYSDILLP DCTTSEQMDF ALDAFVSNMA
     YVIFADQVVK PSFECRTIYD MLSDLADKMG VKDTFTRSHA GRMATLYLCT IPRKTAGITN
     L
//
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