ID D3UIN0_HELM1 Unreviewed; 797 AA.
AC D3UIN0;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Putative biotin sulfoxide reductase {ECO:0000313|EMBL:CBG40355.1};
GN OrderedLocusNames=HMU11000 {ECO:0000313|EMBL:CBG40355.1};
OS Helicobacter mustelae (strain ATCC 43772 / LMG 18044 / NCTC 12198 / 12198)
OS (Campylobacter mustelae).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=679897 {ECO:0000313|EMBL:CBG40355.1, ECO:0000313|Proteomes:UP000001522};
RN [1] {ECO:0000313|EMBL:CBG40355.1, ECO:0000313|Proteomes:UP000001522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43772 / LMG 18044 / NCTC 12198 / 12198
RC {ECO:0000313|Proteomes:UP000001522};
RX PubMed=20219135; DOI=10.1186/1471-2164-11-164;
RA O'Toole P.W., Snelling W.J., Canchaya C., Forde B.M., Hardie K.R.,
RA Josenhans C., Graham R.L.J., McMullan G., Parkhill J., Belda E.,
RA Bentley S.D.;
RT "Comparative genomics and proteomics of Helicobacter mustelae, an
RT ulcerogenic and carcinogenic gastric pathogen.";
RL BMC Genomics 11:164-164(2010).
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}.
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DR EMBL; FN555004; CBG40355.1; -; Genomic_DNA.
DR RefSeq; WP_013023425.1; NC_013949.1.
DR AlphaFoldDB; D3UIN0; -.
DR STRING; 679897.HMU11000; -.
DR KEGG; hms:HMU11000; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_7; -.
DR Proteomes; UP000001522; Chromosome.
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:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02793; MopB_CT_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; IPR041954; CT_DMSOR/BSOR/TMAOR.
DR InterPro; IPR041460; Molybdopterin_N.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001522}.
FT DOMAIN 38..78
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 82..535
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 651..770
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 797 AA; 90256 MW; AE8299968B9608E7 CRC64;
MAVSRRDALK AAMGGMTLLQ TQPLQAVGIF TKNEKIPHAT RFGPFYGHVQ DGVLKEIESQ
KNDFNPSVMT KGLIDRAYSK SRVRYPCVRK SYLEKKENHK ELRGREEFVR VSWDMALDLV
AKKLQEIPKE KIYHGGDKGL EQAGRLHNAS IIAGRFFNTV LGGVVQASGG YRNGAAVSVN
PAIIGDMEVY SLQTTHEEMI ANCKVYVMWG ADLFKSNRTD FVVPNHLNDV YYTRYKRSGM
KFICIDPIYT ETAQMFDAEW IKIRPNTDVA LMLGMMHYLF GSKKYDKRFI SKYTDGFEKF
LPYLLGKTDK TPKNAKWAEK ITGIPARKIK ELAELFTTNR TFFAGNWAMQ RAQHGEQVDW
ALITLASMIG QIGLPGGGVG FCMHYAGGGQ ASSGYRIPPG ISQGSSTIKQ SIPTSRLADA
ILNPGKEIPY RGKKITYPKI DMLYLCGTPL LEYEPNTNEL IQALRTLDTI IIHKPWWTPD
AKMADIVLPS TTSLERDDIT FGGFHSKNVI YAMRKVIEPL YESKNDFDIF AMLANKIGGE
TMERKYTENK SSIDWIQEFY KKSDGPSFKD FDQFWKEGFV EFEIPKKAYG FVRHADFRKD
PVHNKLATKS GKIQIFSEVF ASYKLPDFKG HVMWFEPAEW LGGKTAKKYP FHLLSPHPRY
RLHSQLENTW IANFYKIQGR EPMMINTNDA QRLGVKHGEI VEVYNDRGRI LVGAFVSDFI
REGVIAIQVG AWYDPEDPKE ENPRCNSGLV NILTSSRPTS QMAQATSANT ALVNIRKIEN
EVIKPCKSTL PPSILGV
//
