ID A0A1Y4G2U2_9ACTN Unreviewed; 787 AA.
AC A0A1Y4G2U2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=DMSO reductase {ECO:0000313|EMBL:OUO89675.1};
GN ORFNames=B5F40_09800 {ECO:0000313|EMBL:OUO89675.1};
OS Gordonibacter sp. An230.
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Gordonibacter.
OX NCBI_TaxID=1965592 {ECO:0000313|EMBL:OUO89675.1, ECO:0000313|Proteomes:UP000196177};
RN [1] {ECO:0000313|Proteomes:UP000196177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An230 {ECO:0000313|Proteomes:UP000196177};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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:OUO89675.1}.
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DR EMBL; NFJP01000017; OUO89675.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4G2U2; -.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000196177; Unassembled WGS sequence.
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:UniProtKB-KW.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 2.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
DR Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF00384; Molybdopterin; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 114..577
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 675..778
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 787 AA; 84925 MW; C4A6E9C4C6392F65 CRC64;
MRKSADQGLP SLSRRTFVTA AATTGAAAVL GLSGCSPKAE TDAGAGDGAE GAATDPYADA
QVFYSTCPPE CQHHNLKGYV VDGKLVKVES SELNDCAACA RGISRSQMVN DPDRLTMPLL
LDGEKGSGKF KEISWDEAYQ LIEQKLNDAI ASDGNKSICY VTGSGNFGAM HGPVADAFFA
HLGGASTTVG SLCCAGTTAA IVPIYGKRFL DCRNQIENST YVVVWGNNPA ISKQGYFQRF
ERVVENGGKL VVIDPIYTES AAKATDWLQP WPGTDAALGL AMLKVIVDER LYDEEFLLAH
TCAPCLVDRA TGEPVLKDVD DPASFVVFDK KSGEVVPHDQ GGIEAALALD GTDAADAYRT
EFELIYAEAE PWTLEAAEEE CGVPAADIER IAKEYAGAEH AMIVQNMGGF MRTENGTYAT
AVGAYLVAFC GQVGHVGDGV SDAGGMNEVA TGNLIEVPKV AEEMAAIPRF RFGEAVLNED
PVKVNVLWSM TGSPMTQWPN TGMVKKALEK IPFVVTVDQY LTPTALYSDL VLPCTGIFET
EGVLANARSH WIQLMEKAVD GPGESKSDLE IFAELARRFG FGDAFDVPMK DLISNVLAPT
GVTYDELVEK KAVDVVGKDY IPYKDGVFFT ASKKAEFWVG AWKKEGFNPI CSYTRAEEDA
RNGDELAAKY PLFSVQRKTY RSVHSTFNNL EWMDEVCDRQ PVVLLNKADA EARGIADGDA
VVVFNDRGEH RGVAEVNDRI KAGVVGLQNG WWEQQGGSSS YVTNDKWKTL GGTHCCNQTL
VDVKKEA
//
