ADH1_GEOTN
ID ADH1_GEOTN Reviewed; 395 AA.
AC A4IP64;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Long-chain-alcohol dehydrogenase 1;
DE EC=1.1.1.192;
DE AltName: Full=Alcohol dehydrogenase 1;
DE Short=ADH1;
DE AltName: Full=Fatty alcohol oxidoreductase 1;
DE AltName: Full=Glycerol dehydrogenase;
DE EC=1.1.1.6;
GN Name=adh1; OrderedLocusNames=GTNG_1754;
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).
RN [3]
RP IDENTIFICATION.
RX PubMed=24826896; DOI=10.1371/journal.pone.0097250;
RA Shearer A.G., Altman T., Rhee C.D.;
RT "Finding sequences for over 270 orphan enzymes.";
RL PLoS ONE 9:E97250-E97250(2014).
CC -!- FUNCTION: Long-chain alkyl alcohol dehydrogenase that can oxidize a
CC broad range of alkyl alcohols from ethanol to 1-triacontanol (C2 to
CC C30) as well as 1,3-propanediol and acetaldehyde. The best substrate is
CC ethanol. Also oxidizes glycerol. {ECO:0000269|PubMed:19383697}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycerol + NAD(+) = dihydroxyacetone + H(+) + NADH;
CC Xref=Rhea:RHEA:13769, ChEBI:CHEBI:15378, ChEBI:CHEBI:16016,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.6;
CC Evidence={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=7.55 mM for ethanol {ECO:0000269|PubMed:19383697};
CC KM=4.71 mM for acetaldehyde {ECO:0000269|PubMed:19383697};
CC KM=1.51 mM for NAD {ECO:0000269|PubMed:19383697};
CC KM=1.40 mM for NADH {ECO:0000269|PubMed:19383697};
CC KM=0.28 mM for NADP {ECO:0000269|PubMed:19383697};
CC Note=kcat is 638.69 sec(-1) for ethanol. kcat is 404.77 sec(-1) for
CC acetaldehyde. kcat is 443.05 sec(-1) for NAD. kcat is 1645.74 sec(-1)
CC for NADH. kcat is 43.90 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: Homooctamer. {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; ABO67118.1; -; Genomic_DNA.
DR RefSeq; WP_008880085.1; NC_009328.1.
DR AlphaFoldDB; A4IP64; -.
DR SMR; A4IP64; -.
DR STRING; 420246.GTNG_1754; -.
DR EnsemblBacteria; ABO67118; ABO67118; GTNG_1754.
DR KEGG; gtn:GTNG_1754; -.
DR eggNOG; COG1454; Bacteria.
DR HOGENOM; CLU_007207_0_0_9; -.
DR OMA; GDCLATR; -.
DR OrthoDB; 1456634at2; -.
DR BRENDA; 1.1.1.1; 705.
DR BRENDA; 1.1.1.192; 705.
DR Proteomes; UP000001578; Chromosome.
DR GO; GO:0008888; F:glycerol dehydrogenase [NAD+] activity; IEA:UniProtKB-EC.
DR GO; GO:0050060; F:long-chain-alcohol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR PANTHER; PTHR11496; PTHR11496; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
PE 1: Evidence at protein level;
KW NAD; Oxidoreductase.
FT CHAIN 1..395
FT /note="Long-chain-alcohol dehydrogenase 1"
FT /id="PRO_0000430261"
FT BINDING 98..102
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 141..144
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 395 AA; 41664 MW; D25DD113FC09D6CD CRC64;
MSVARIVFPP LSHVGWGALD QLVPEVKRLG AKHILVITDP MLVKIGLVDQ VTSPLRQEGY
SVHVYTDVVP EPPLETGEKA VAFARDGKFD LVIGVGGGSA LDLAKLAAVL AVHDGSVADY
LNLTGTRTLE KKGLPKILIP TTSGTGSEVT NISVLSLETT KDVVTHDYLL ADVAIVDPQL
TVSVPPRVTA ATGIDALTHA VEAYVSVNAS PTSDGLAVAA IRLISRSLRK AVANGSDKQA
RIDMANGSYL AGLAFFNAGV AGVHALAYPL GGQFHIAHGE SNAVLLPYVM GYIRQSCTKR
MADIFNALGG NSSFLSEVEA SYRCVEELER FVADVGIPKT LGGFGIPESA LESLTKDAVQ
QKRLLARSPL PLLEADIRAI YEAAFAGTIV EPHKA
