ADH2_GEOTN
ID ADH2_GEOTN Reviewed; 387 AA.
AC A4ISB9;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Long-chain-alcohol dehydrogenase 2;
DE EC=1.1.1.192;
DE AltName: Full=Alcohol dehydrogenase 2;
DE Short=ADH2;
DE AltName: Full=Fatty alcohol oxidoreductase 2;
GN Name=adh2; OrderedLocusNames=GTNG_2878;
OS Geobacillus thermodenitrificans (strain NG80-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=420246;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NG80-2;
RX PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA Han W., Peng X., Liu R., Wang L.;
RT "Genome and proteome of long-chain alkane degrading Geobacillus
RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=NG80-2;
RX PubMed=19383697; DOI=10.1099/mic.0.027201-0;
RA Liu X., Dong Y., Zhang J., Zhang A., Wang L., Feng L.;
RT "Two novel metal-independent long-chain alkyl alcohol dehydrogenases from
RT Geobacillus thermodenitrificans NG80-2.";
RL Microbiology 155:2078-2085(2009).
CC -!- FUNCTION: Long-chain alkyl alcohol dehydrogenase that can oxidize a
CC broad range of alkyl alcohols from methanol to 1-triacontanol (C1 to
CC C30) as well as 1,3-propanediol and acetaldehyde. Oxidizes isopropyl
CC alcohol, isoamylol, acetone, octanal and decanal. The best substrate is
CC 1-octanol. {ECO:0000269|PubMed:19383697}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain primary fatty alcohol + H2O + 2 NAD(+) = a long-
CC chain fatty acid + 3 H(+) + 2 NADH; Xref=Rhea:RHEA:17977,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57560, ChEBI:CHEBI:57945, ChEBI:CHEBI:77396;
CC EC=1.1.1.192; Evidence={ECO:0000269|PubMed:19383697};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=37.63 mM for ethanol {ECO:0000269|PubMed:19383697};
CC KM=2.25 mM for acetaldehyde {ECO:0000269|PubMed:19383697};
CC KM=3.88 mM for 1-octanol {ECO:0000269|PubMed:19383697};
CC KM=1.15 mM for octanal {ECO:0000269|PubMed:19383697};
CC KM=2.4 mM for NAD {ECO:0000269|PubMed:19383697};
CC KM=0.84 mM for NADH {ECO:0000269|PubMed:19383697};
CC KM=1.44 mM for NADP {ECO:0000269|PubMed:19383697};
CC Note=kcat is 136.24 sec(-1) for ethanol. kcat is 138.05 sec(-1) for
CC acetaldehyde. kcat is 260.71 sec(-1) for 1-octanol. kcat is 518.42
CC sec(-1) for octanal. kcat is 283.08 sec(-1) for NAD. kcat is 4808.18
CC sec(-1) for NADH. kcat is 38.50 sec(-1) for NADP.;
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:19383697};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:19383697};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19383697}.
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC -!- CAUTION: In contrast to other members of the family, it apparently does
CC not use iron or other metals as cofactor.
CC {ECO:0000305|PubMed:19383697}.
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DR EMBL; CP000557; ABO68223.1; -; Genomic_DNA.
DR RefSeq; WP_008881794.1; NC_009328.1.
DR AlphaFoldDB; A4ISB9; -.
DR SMR; A4ISB9; -.
DR STRING; 420246.GTNG_2878; -.
DR EnsemblBacteria; ABO68223; ABO68223; GTNG_2878.
DR KEGG; gtn:GTNG_2878; -.
DR eggNOG; COG1979; Bacteria.
DR HOGENOM; CLU_007207_0_4_9; -.
DR OMA; CTMALNG; -.
DR OrthoDB; 717704at2; -.
DR BRENDA; 1.1.1.1; 705.
DR BRENDA; 1.1.1.192; 705.
DR Proteomes; UP000001578; Chromosome.
DR GO; GO:1990362; F:butanol dehydrogenase activity; IEA:InterPro.
DR GO; GO:0050060; F:long-chain-alcohol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd08187; BDH; 1.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR044731; BDH-like.
DR PANTHER; PTHR43633; PTHR43633; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
DR PROSITE; PS00060; ADH_IRON_2; 1.
PE 1: Evidence at protein level;
KW NAD; Oxidoreductase.
FT CHAIN 1..387
FT /note="Long-chain-alcohol dehydrogenase 2"
FT /id="PRO_0000430262"
FT BINDING 98..102
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 138..141
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 387 AA; 42804 MW; CD20507DB32C969C CRC64;
MQNFTFRNPT KLIFGRGQIE QLKEEVPKYG KKVLLVYGGG SIKRNGLYDE VMSLLTDIGA
EVVELPGVEP NPRLSTVKKG VDICRREGIE FLLAVGGGSV IDCTKAIAAG AKFDGDPWEF
ITKKATVTEA LPFGTVLTLA ATGSEMNAGS VITNWETKEK YGWGSPVTFP QFSILDPTYT
MTVPKDHTVY GIVDMMSHVF EQYFHHTPNT PLQDRMCEAV LKTVIEAAPK LVDDLENYEL
RETIMYSGTI ALNGFLQMGV RGDWATHDIE HAVSAVYDIP HAGGLAILFP NWMKHVLDEN
VSRFAQLAVR VFDVDPTGKT ERDVALEGIE RLRAFWSSLG APSRLADYGI GEENLELMAD
KAMAFGEFGR FKTLNRDDVL AILRASL
