ID   D6EA43_9ACTN            Unreviewed;       800 AA.
AC   D6EA43;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Anaerobic dehydrogenases, typically selenocysteine-containing {ECO:0000313|EMBL:CBL04590.1};
GN   ORFNames=GPA_24240 {ECO:0000313|EMBL:CBL04590.1};
OS   Gordonibacter pamelaeae 7-10-1-b.
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Gordonibacter.
OX   NCBI_TaxID=657308 {ECO:0000313|EMBL:CBL04590.1, ECO:0000313|Proteomes:UP000008805};
RN   [1] {ECO:0000313|EMBL:CBL04590.1, ECO:0000313|Proteomes:UP000008805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7-10-1-b {ECO:0000313|Proteomes:UP000008805};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Timmis K., Oxley A., Wurdemann D.;
RT   "The genome sequence of Gordonibacter pamelaeae 7-10-1-bT.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL04590.1, ECO:0000313|Proteomes:UP000008805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7-10-1-b {ECO:0000313|Proteomes:UP000008805};
RA   Pajon A.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR   EMBL; FP929047; CBL04590.1; -; Genomic_DNA.
DR   AlphaFoldDB; D6EA43; -.
DR   KEGG; gpa:GPA_24240; -.
DR   PATRIC; fig|657308.3.peg.1921; -.
DR   HOGENOM; CLU_000422_13_3_11; -.
DR   BioCyc; GPAM657308:GPA_RS11295-MONOMER; -.
DR   Proteomes; UP000008805; Chromosome.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008805}.
FT   DOMAIN          54..113
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   800 AA;  90400 MW;  32D0C285BB7E42A9 CRC64;
     MADSAQAPVQ EHWSETNGKK YRRGSRLPKK TDTRPPVPAA ETPKVPWTWE EDGMTVIRGT
     ARSAPGCHNV CGILSYVKDG KLVKVEGDPE DPYNQGRLCS RCLCIPNYVY HEDRLVKPMK
     RDRADRGKDK FVECSWDEAY DIIVREFKRV VDTYGADKIA MCQGTGRDIH QVTRLNACVG
     SPNEGVPYFA GNSCYLPRIA SMACMLGGAC VMDCSQFLPQ RYDDPRYTVP KYCIVWGHQP
     FYSNADGFYG HWITDLMKRG MKVAVIDPQL TWLAARAGED WLRVRPGGDG ALAMAMLKVV
     CDEKLYDQEF CDKWVYGLEA VCERVAEMDL DDLCEKSWVA KEDVQRVART YAASKPAAIQ
     WGVALDQQTG GQQAAHAITA LWCITGNLDV PGGNVMGDAC WGIEQPNWTG TWGWDELMTE
     EEQSKRIGVE RYPMFAVGFK NLSSNATIEA WQRGEVPIRA AYIVTNNFLA TMGAQAEQQL
     EWYKQIDFIV VSDLFMTPTM MALADVVLPA ATYEERDGFG GLNAYRISCI NKAIEPVGDS
     KPDNTIFLEL GKRLTAAIKP ENQDIAWPWD DVQEMWDYAL EDGGFTWDEL RESTWKYPEF
     KYRKYETGDL RPDGQPGFRT ETGRAEIYSM VFHHTSWSGL DPLPSYVEPV ESPYSAPEDV
     EEYPYIVTSG ARVPHFFHSE QRQIAKLRAL HPDPLVYLHP DTAAANGIEE GDWVWLENKH
     GKCKYKAAFN DTYDPRVLQA EHGWWFPERK DAAEENVENE QEGLFGVLES NINNLVPFDA
     GVSGFGSNYK AMMCKIRKAD
//