ID K2KQG4_HELPX Unreviewed; 796 AA.
AC K2KQG4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Dimethyl sulfoxide/trimethylamine N-oxide reductase {ECO:0000313|EMBL:EKE84679.1};
DE EC=1.7.2.3 {ECO:0000313|EMBL:EKE84679.1};
GN Name=dorA {ECO:0000313|EMBL:EKE84679.1};
GN ORFNames=OUG_1175 {ECO:0000313|EMBL:EKE84679.1};
OS Helicobacter pylori R32b.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1145112 {ECO:0000313|EMBL:EKE84679.1, ECO:0000313|Proteomes:UP000006767};
RN [1] {ECO:0000313|EMBL:EKE84679.1, ECO:0000313|Proteomes:UP000006767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R32b {ECO:0000313|EMBL:EKE84679.1,
RC ECO:0000313|Proteomes:UP000006767};
RX PubMed=23661595; DOI=10.1111/2049-632X.12045;
RA Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M.,
RA Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K.,
RA Daugherty S., Song Y., Fraser C.M., Fricke W.F.;
RT "Genome sequences of 65 Helicobacter pylori strains isolated from
RT asymptomatic individuals and patients with gastric cancer, peptic ulcer
RT disease, or gastritis.";
RL Pathog. Dis. 68:39-43(2013).
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
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:EKE84679.1}.
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DR EMBL; AMOS01000003; EKE84679.1; -; Genomic_DNA.
DR RefSeq; WP_000028267.1; NZ_AMOS01000003.1.
DR AlphaFoldDB; K2KQG4; -.
DR PATRIC; fig|1145112.3.peg.1156; -.
DR Proteomes; UP000006767; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 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:0050626; F:trimethylamine-N-oxide reductase (cytochrome c) activity; IEA:UniProtKB-EC.
DR GO; GO:0009033; F:trimethylamine-N-oxide reductase activity; IEA:UniProtKB-EC.
DR CDD; cd02793; MopB_CT_DMSOR-BSOR-TMAOR; 1.
DR CDD; cd02769; MopB_DMSOR-BSOR-TMAOR; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR Gene3D; 3.90.55.10; Dimethylsulfoxide Reductase, domain 3; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006658; BisC.
DR InterPro; IPR041954; CT_DMSOR/BSOR/TMAOR.
DR InterPro; IPR041460; Molybdopterin_N.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR NCBIfam; TIGR00509; bisC_fam; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR PANTHER; PTHR43742:SF10; TRIMETHYLAMINE-N-OXIDE REDUCTASE 2; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF18364; Molybdopterin_N; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:EKE84679.1}.
FT DOMAIN 36..76
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 80..532
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 649..768
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 796 AA; 90103 MW; 47AE95DA389C51AB CRC64;
MSISRRSILT KIPIALASAN CLKATGVFEK VESIPHATHF GPFIAKVQNG VIKDIVPQKS
DYNPTMMLKA MVDRVYSDSR VKYPCVRKSF LENKKNHKEL RGREEFVRVS WDVALDLAAK
KLKEIPKENI YNASYGGWGH AGSLHRCHHL AWRFFNTTLG GAIGTDGEYS NGAAARINPM
IVGDMEVYSQ QTTHEEMIKN CKVYVMWGAD LFKCNRIDYF VPNHVNDSYY PKYKRAGIKF
ISIDPIYTET AQAFSAEWIP IRPNTDVALM LGMMHYLYTS NQYDKAFIAK YTDGFDKFLP
YLLGESDNAP KTLEWASQIT GVSAEKIKEL ADLFVSKRTF LAGNWAMQRA QHGEQPDWAL
IVLASMIGQV GLSGGGFGFS MHYGGNAQAS SGARIVPMIS QGHNSVKSVI PASRVSEAVL
NPDKEIDFMG KKLKLPKIKM IYNCGADLLG HEADTNELIR ALRTLDCVIV HEPWWTPTAK
FADIVFASTS TMERDDITFG GSYSKNVVYA MRKVVEPVYE SKDDYEIFRQ LALRIGGNET
EQKFTESKSY MEWIKSLYEK SDGPTLKSFD QFWRDGFVEF EIPENARKFV RHAKFRQDPI
NNKLDTESGK IQIFSQKCAD FKLADFKGHP AWFEPAEWLG SKMAEIYPFH LISPHPKYRV
NSQLDNTWVR NVYKIQGREP VMINELDANK LGIRHGEIVE VFNARGRLLA GAFVTKNIRQ
GVLSIQKGAW YDPEDERVRN PRCNAGHVNT LTSLRPTSSM TQAISANTAL VNIRRLRRYE
LVKPYHSIST PSIIGA
//