ID A0A0N0MR69_9ACTN Unreviewed; 337 AA.
AC A0A0N0MR69;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Aryl-alcohol dehydrogenase {ECO:0000313|EMBL:KPI04018.1};
DE EC=1.1.1.90 {ECO:0000313|EMBL:KPI04018.1};
GN ORFNames=OK074_4797 {ECO:0000313|EMBL:KPI04018.1};
OS Actinobacteria bacterium OK074.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI04018.1, ECO:0000313|Proteomes:UP000037991};
RN [1] {ECO:0000313|EMBL:KPI04018.1, ECO:0000313|Proteomes:UP000037991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK074 {ECO:0000313|EMBL:KPI04018.1,
RC ECO:0000313|Proteomes:UP000037991};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
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:KPI04018.1}.
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DR EMBL; LJCV01000270; KPI04018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0MR69; -.
DR PATRIC; fig|1592327.3.peg.7309; -.
DR Proteomes; UP000037991; Unassembled WGS sequence.
DR GO; GO:0018456; F:aryl-alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08278; benzyl_alcohol_DH; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43350:SF2; PKS_ER DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KPI04018.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037991};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 2..79
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 168..285
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 337 AA; 34712 MW; 66AE6787F5513EE9 CRC64;
MQVRLVATGV CHTDAIVRDQ WYPTPLPAVL GHEGAGIVEK VGSAVTGITP GDRVVLSFAS
CGACAGCNAG HPAYCTDFAM RNFGGARPDR STAFRAEDGS AVSSHFFGQS SFAGVTNVAE
RSVVKVSETV PLDILGPLGC GVLTGAGAVL DVLKPKPGSN FVLFGTGAVG LSGLLAAVAA
GATTVIAVDI VDSRLEFAKS LGATHTINSR NEDPVARIKE ITGGGADYAL DATGNKVVFR
QMIDSMGLLG HAAIVGLAKP GTESPVDIGS SMLTGVGVTF VLEGDAVPQV LIPQLIALYE
AGRFPFDRLI KQYGFEDINQ AFEDSESGVT LKPVVTF
//
