ID A4MVW3_HAEIF Unreviewed; 211 AA.
AC A4MVW3;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Anaerobic dimethyl sulfoxide reductase chain A {ECO:0000313|EMBL:EDJ89432.1};
GN ORFNames=CGSHi22121_03135 {ECO:0000313|EMBL:EDJ89432.1};
OS Haemophilus influenzae 22.1-21.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=374927 {ECO:0000313|EMBL:EDJ89432.1, ECO:0000313|Proteomes:UP000004131};
RN [1] {ECO:0000313|EMBL:EDJ89432.1, ECO:0000313|Proteomes:UP000004131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22.1-21 {ECO:0000313|EMBL:EDJ89432.1,
RC ECO:0000313|Proteomes:UP000004131};
RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA Ehrlich G.D.;
RT "Characterization and modeling of the Haemophilus influenzae core and
RT supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT nontypeable strains.";
RL Genome Biol. 8:R103.1-R103.18(2007).
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};
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DR EMBL; AAZD01000001; EDJ89432.1; -; Genomic_DNA.
DR AlphaFoldDB; A4MVW3; -.
DR Proteomes; UP000004131; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
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; TIGR01409; TAT_signal_seq; 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; 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};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 47..109
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 211 AA; 23804 MW; EED8AFBDE302B895 CRC64;
MSNFNQISRR DFVKASSAGA ALAVSNLTLP FNVMAKETQR LNENNQERIV WSACTVNCGS
RCPLRMHVKD NRITYVETDN TGTETYNLDH QVRACLRGRS MRRRVYNPDR LKYPMKRIGK
RGEGKFKRIS WDEALTEIAD ALKRNIKKYG NESIYLNYGT GTLGGTMAKS WPPASTMIAR
FMNCIGGYLN HYGDYSTAQI AVGLDYTYGG G
//
