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Database: UniProt
Entry: A0A423ULY8_9ACTN
LinkDB: A0A423ULY8_9ACTN
Original site: A0A423ULY8_9ACTN 
ID   A0A423ULY8_9ACTN        Unreviewed;       770 AA.
AC   A0A423ULY8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Dehydrogenase {ECO:0000313|EMBL:ROT90869.1};
GN   ORFNames=DMP12_05150 {ECO:0000313|EMBL:ROT90869.1};
OS   Gordonibacter urolithinfaciens.
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Gordonibacter.
OX   NCBI_TaxID=1335613 {ECO:0000313|EMBL:ROT90869.1, ECO:0000313|Proteomes:UP000285258};
RN   [1] {ECO:0000313|Proteomes:UP000285258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27213 {ECO:0000313|Proteomes:UP000285258};
RA   Danylec N., Stoll D.A., Doetsch A., Huch M.;
RT   "Genome Sequencing of selected type strains of the family
RT   Eggerthellaceae.";
RL   Submitted (MAY-2018) 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:ROT90869.1}.
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DR   EMBL; QIBW01000004; ROT90869.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A423ULY8; -.
DR   Proteomes; UP000285258; Unassembled WGS sequence.
DR   GO; GO:0018818; F:acetylene hydratase activity; IEA:InterPro.
DR   GO; GO:0051536; F:iron-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; cd02781; MopB_CT_Acetylene-hydratase; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 2.20.25.90; ADC-like domains; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR037949; MopB_CT_Acetylene-hydratase.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
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; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          19..75
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   770 AA;  86562 MW;  4A3CB005B5CA17D3 CRC64;
     MAYGKQWQTV MEDGTVVTRS NTWSPPGSHP VGYGVKVVTK DGELVRIEGD DDNPITTGRV
     NAMNLALREY TYAPSRIIHP MKRNPEDRGK DKWVQTTWDE ALDTICDKVR YFQNTYGPES
     IVVFGGTGRE ACIFYYALTF SVLQSPNCCY TQSGWSCYGP RCSISDYVLG AGYPELDYAG
     HLPGSYQDPR YTVPKWIVVW GKEPLPSNGD GFFGHCLVDL MKLGTKIISI DPRITWVGAH
     DGNINLQVRP QTDTALALAI MNLMFENGEY DQEFAEKWIY GLDDMKARAA EYPVDKVAEI
     TGVDAEDIKR VAHIIGTERP IGWAWGLAFD QNKNGVQLSQ AFIVLAALAG SIDRPGGLTL
     GPPSALLGKW RMEQRGAMAD EVWSKRIGAA AWPGLSTGMA TTQPDETLNT METDQPYALK
     MGWFNSSNFL TPTCSAQPKR WHKALQKLEF VVVQDLTMTP TAMAVGDYFL PMATWAEHNG
     IVLTHYGRNT VFMGPMNKAL QVGECKSDVE ICLMFGQRLN PSWWPWYKPA DGKSLDLDAL
     AVAVEDFYSD QLKELGMDWN QFREEGLYQP GAHGFEYEKY EKGLLRFDGE PGFNTITGQI
     EAYSILYESW GEDPLPYYEE PNYSPISKPD FAGQYPLITT SGSRRYSSFH SEHRHVPSLR
     QIDPWPWVQI NPETAAEYGI TDGDWCEVYN MFGEARFKAE VTPVMKPGIL NCAHGWWFPE
     QDGEEPNLFG VWKSNFNSLV PHFNVGKLGF GAPYKGVMCN VRRVRSLDQD
//
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