ID A0A423UH34_9ACTN Unreviewed; 831 AA.
AC A0A423UH34;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:ROT88047.1};
GN ORFNames=DMP12_13565 {ECO:0000313|EMBL:ROT88047.1};
OS Gordonibacter urolithinfaciens.
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Gordonibacter.
OX NCBI_TaxID=1335613 {ECO:0000313|EMBL:ROT88047.1, 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 -!- 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:ROT88047.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QIBW01000025; ROT88047.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423UH34; -.
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; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 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 38..94
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 831 AA; 93614 MW; FE83340F56BBB197 CRC64;
MDSGRKSVRR PELPTIARGE EETVTERKRE EGEETIFRTC AWSPPGCHPV GCGLQVHVKD
GVVVEVEGDP EHPITKGALC PRCLALTEYV YHEDRIVHPM KRAREDRGLD KWESCSWEEA
TDLVADAARE IIEQYGAETI CVFGGTGREA NYWYTQWANL VFGTPNAVYA QAGWSCYGPR
ISNTAFMLGG GYPEIDYAQK FADRYEHEGW VAPEVVVCWG KEPLRSNPDG MYGHALIEMM
RQFGTKVICV DPRIHWLGSR SEIVLQVNPG TDTAMAMAWI YVMDKEGLVD REWIDAWTYG
YDELVERCQT MPPSKAAEIC GVPEDLIWKA ARMYGSARPS ALAWGLAVDE NPNGTQLGQC
LIALMTITGF IDAPGGTTLG MGDDGGNRVH DGGGIDASQR IEDENDSTLM LALKNGIMTQ
EMWDTKRIGV DKYPAVGSIM WTAHPDEFLK ALETEQPYKV HMAGFVSSNP VGTAISAEPQ
RWYKALKQLD FNYACDCFMN PTIMSCCDVV FPVASTIEHD GMVVTHYASN ASFYGAQNKC
VQVGECKSDI EIMMMVGKKL HPGFWNRFET QEDYDNFHVM RSWLPFRELR DKVVVMSEEP
YYKYKIGKLR PDGQPGFPTT TGRVELYSLM YQNWGEDPLP YYEPPVYSPG ALPELGREYP
LMMITGARQQ EFFHSEHKQV PSLRQLTPWP MVDINVYDAE TYGIEEGDWV EISSPYGSIR
QLARVVPTMK KGVVHCMHGF WYPEENGEVP NLYGNWKSNV NMLMPNSVNG KLGFGNTFKQ
MMVSIKRVDG RGGPNDPDAN GIVLEPSRQE EFTVQQTWRP ADESTAVYLQ K
//