ID A0A0Q8PR80_9ACTN Unreviewed; 737 AA.
AC A0A0Q8PR80;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:KRB72692.1};
GN ORFNames=ASE01_21790 {ECO:0000313|EMBL:KRB72692.1};
OS Nocardioides sp. Root190.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736488 {ECO:0000313|EMBL:KRB72692.1, ECO:0000313|Proteomes:UP000050886};
RN [1] {ECO:0000313|EMBL:KRB72692.1, ECO:0000313|Proteomes:UP000050886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root190 {ECO:0000313|EMBL:KRB72692.1,
RC ECO:0000313|Proteomes:UP000050886};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB72692.1, ECO:0000313|Proteomes:UP000050886}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root190 {ECO:0000313|EMBL:KRB72692.1,
RC ECO:0000313|Proteomes:UP000050886};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRB72692.1}.
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DR EMBL; LMIA01000014; KRB72692.1; -; Genomic_DNA.
DR RefSeq; WP_056758333.1; NZ_LMIA01000014.1.
DR AlphaFoldDB; A0A0Q8PR80; -.
DR STRING; 1736488.ASE01_21790; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000050886; Unassembled WGS sequence.
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 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 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:UP000050886}.
FT DOMAIN 1..56
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 737 AA; 83380 MW; FFD56BAF7CAC44A1 CRC64;
MERKRAVCTV CDIACQLQVE VEDDKVLRVL PPENPVTAGN YCLKGLSAHR LYALEERLRQ
PLRRVGERGE GRFEPVSWDE AMGEIAERLE VLIEKYGPET FAVSTSNWNT SVENGLGRRV
MNLLGSPNWT SGVAMCMGNT AAVNKLTYGW FPWPDLINTD LVVLFGHNPR KHSWTPIYNL
VRQAQAKGAK LIVLDPRVSG QAARADVHLQ LRSGTDAAMC LGWLNVIIEE ELYDKQFVRD
WCVGFDDLKE RAAEYPLSRV RELTGVAEEE IRLAARMYAT ARSATIPWSP TVDQQVSSTS
IIRLQSILRA ICGHLDVPGG ELIYGFNEEM LSETFIELHE ALSPQQRAKQ LGYDEYPAYT
HRAGELLAPH TKRVFGHEYA NIVMGSYMAN PTSLFRAMAT DEPYPVRAFF SLGNNTLMSY
PNQQQVKAAL LRQELLVVHE LFMTPTARLA DFILPGDTWL ERPHVHDSFG WRSWLIASEK
AVDPPAGCRG VFDFWRDLGH RMGLGDHLPW ASVEEMLDFR LQPLGISYRE FCATHDMKIA
AKEYRSYRRT GFGTPSGKVE LRSSILEDLG FDPLPYHREL PEDPDHPFRV FVGVREDPYF
QTGQRQLPSA RRLSPLPAFF LHPEDADELG LAQGDWAEVS TRHGCIQGVI ERRGDMSRRH
VRVPHGWWFP ELIDSDTDGA ADRHNDGILV PDDRESLDYE QGTPQLKGFP GAVRRLERPP
AHIARTGLRS SEEVTAQ
//
