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Database: UniProt
Entry: K2KQG4_HELPX
LinkDB: K2KQG4_HELPX
Original site: K2KQG4_HELPX 
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
//
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