ID D6E7S9_9ACTN Unreviewed; 717 AA.
AC D6E7S9;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Anaerobic dehydrogenases, typically selenocysteine-containing {ECO:0000313|EMBL:CBL03776.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:CBL03776.1};
GN ORFNames=GPA_10610 {ECO:0000313|EMBL:CBL03776.1};
OS Gordonibacter pamelaeae 7-10-1-b.
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Gordonibacter.
OX NCBI_TaxID=657308 {ECO:0000313|EMBL:CBL03776.1, ECO:0000313|Proteomes:UP000008805};
RN [1] {ECO:0000313|EMBL:CBL03776.1, 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:CBL03776.1, 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; CBL03776.1; -; Genomic_DNA.
DR RefSeq; WP_015539126.1; NC_021021.1.
DR AlphaFoldDB; D6E7S9; -.
DR GeneID; 78358300; -.
DR KEGG; gpa:GPA_10610; -.
DR PATRIC; fig|657308.3.peg.646; -.
DR HOGENOM; CLU_000422_13_3_11; -.
DR BioCyc; GPAM657308:GPA_RS04880-MONOMER; -.
DR Proteomes; UP000008805; 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:UniProtKB-KW.
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; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:CBL03776.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008805}.
FT DOMAIN 54..494
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 591..670
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 717 AA; 78249 MW; 33EAF25081034C64 CRC64;
METKYTTCVF CDGGCRVKAE VDGDRLRVLP ADPAFPAICP KAGMVDAYRL HPDRVTVPLK
NVGERGEPQW QEMSWDQALD EIAARLRAVA DAYGPEAVAF AEMPLNMGFG GITRRLMNCL
GTPNYTAPVA LCMGNTAQVH RAVYGWFAGA DWERTDCIVY FGQDRDRERW PGEYLALNAA
LERGAVLIEV DPRETATAKR AHYHLRIRYG TDAALALGWI NVVIGEGLYD RAFVEGSCTG
FDELAARAAE YPPERVAALC GIDAELVRET ARVYARAQAA IIPWGVVGDM QRNSTSLLQA
QCILRALCGF VNKSESVCGP ALGGVGNAEL AAFELLPSEK RALQLGRGAH PLLTFAASDL
YRQANEREGV PYEPDLLAES CACDPASLFA AMRGEGPYPV KAFFSVANNT VMSYANQQGI
VDALMNQDLV VAFEHWLTPT AQLADYVLPD DMWAERDVLG SPFDVGPAFS TGQAFRRPAG
QCKSWYYVVK GLADRLGFAE RFPWANEHEL YDWRLAPLGL TWEDACARAP EPLLRELAAP
GRFVTPSGKV ELASSVLAEL GFDPLPSYEE PSDPGCEAAP EGAYPYVAFA GFRERKSYNT
NLHQMPELRA QEPEPRFFVN PADAAAEGIG EGAWCVVETA YGQVELLSHL DEAQPEGTLR
VPHGWWKPET APGVAAGLSG ACLHNDGMLF PDADWNLDPA QGVPNLRGGI HARVRAK
//
