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Database: UniProt
Entry: E6TET1_MYCSR
LinkDB: E6TET1_MYCSR
Original site: E6TET1_MYCSR 
ID   E6TET1_MYCSR            Unreviewed;       762 AA.
AC   E6TET1;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Molybdopterin guanine dinucleotide-containing S/N-oxide reductase family enzyme {ECO:0000313|EMBL:ADT99914.1};
GN   OrderedLocusNames=Mspyr1_33030 {ECO:0000313|EMBL:ADT99914.1};
OS   Mycolicibacterium gilvum (strain DSM 45189 / LMG 24558 / Spyr1)
OS   (Mycobacterium gilvum).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=278137 {ECO:0000313|EMBL:ADT99914.1, ECO:0000313|Proteomes:UP000008916};
RN   [1] {ECO:0000313|Proteomes:UP000008916}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45189 / LMG 24558 / Spyr1
RC   {ECO:0000313|Proteomes:UP000008916};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., LaButti K., Ivanova N.M., Mikhailova N.M., Land M., Hauser L.,
RA   Koukkou A.I., Drainas C., Kyrpides N., Woyke T.;
RT   "Complete sequence of chromosome of Mycobacterium sp. Spyr1.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADT99914.1, ECO:0000313|Proteomes:UP000008916}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45189 / LMG 24558 / Spyr1
RC   {ECO:0000313|Proteomes:UP000008916};
RX   PubMed=22180818;
RA   Kallimanis A., Karabika E., Mavromatis K., Lapidus A., Labutti K.M.,
RA   Liolios K., Ivanova N., Goodwin L., Woyke T., Velentzas A.D.,
RA   Perisynakis A., Ouzounis C.C., Kyrpides N.C., Koukkou A.I., Drainas C.;
RT   "Complete genome sequence of Mycobacterium sp. strain (Spyr1) and
RT   reclassification to Mycobacterium gilvum Spyr1.";
RL   Stand. Genomic Sci. 5:144-153(2011).
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; CP002385; ADT99914.1; -; Genomic_DNA.
DR   RefSeq; WP_013472001.1; NC_014814.1.
DR   AlphaFoldDB; E6TET1; -.
DR   KEGG; msp:Mspyr1_33030; -.
DR   HOGENOM; CLU_000422_13_3_11; -.
DR   Proteomes; UP000008916; Chromosome.
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}.
FT   DOMAIN          7..47
FT                   /note="Molybdopterin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18364"
FT   DOMAIN          51..503
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          617..731
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
FT   REGION          27..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   762 AA;  82564 MW;  E7CCD8887C626C13 CRC64;
     MARTRTSLTH WGAFSATVES GDIASVRPWS GDADPSPALG NLPGSVRHRS RVTAPAVRRG
     WLENGPGPDT LRGADEFVAV TWDDLVELLG GELRRVIDTH GNEAIYGGSY GWSSAGRFHH
     AQSQVHRFLN CLGGYTYSRH SYSLGATGVI MPRVVGTHDD LFTRSTQWQV IVENTDTMVC
     FGGLALKNTA VNDGGTTAHP ARDALNRLRA RGGRIVSFSP LRDDVDGPCD WHAPVPGTDV
     AIMLALAHVL ATESLADREF LASHCTGYDR FERYLLGADD GIPKSPQWAS SLCGLSADDL
     TALARRMAAG RTLVTVSWSL QRTRHGEQAP WMGLTLAAML GQIGLPGGGF GHGYGSMNEA
     GLAPIRCGLP RLPLGVNPVT TFIPVAAVSD MLLQPGEPFD YNGLRLTYPD IRLVYWAGGN
     PFHHHQNLPR LRRALSRPDT VVVHDPYWTA MAKHADIVVP STTFAERDDL SGSRNDPMLM
     AMPRLTETYA QARDDYDTYA ALAGHLGVRE AFTEGRSSRQ WLRHIYETWS RTLDFDVPAF
     DGFWAAGALR LPTDDGLTLL ADFRADPSAH PLATPSGRIE IFSADIDSFG YDDCRGHPAW
     FEPTEWLGGP RAADYPLHLV ANQPAGRLHG QLDAGAASQA TKVAGREPIR MHPADARARD
     LSGGDVVRVF NDRGACLAGV VLDDRVRPQV VQLSTGAWFD PADPADPNSM CVHGNPNVLT
     DDVGTSKLAH GCTGAHVLVQ IEKYAGTPPP VRAHQPPVFT PR
//
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