ID   ADHA_THEET              Reviewed;         399 AA.
AC   Q9F282;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Long-chain primary alcohol dehydrogenase AdhA;
DE            EC=1.1.1.2;
GN   Name=adhA;
OS   Thermoanaerobacter ethanolicus (Clostridium thermohydrosulfuricum).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=1757;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-15 AND 171-179,
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, TEMPERATURE
RP   DEPENDENCE, INDUCTION, AND SUBUNIT.
RC   STRAIN=ATCC 31550 / DSM 2246 / JW 200;
RX   PubMed=10981690; DOI=10.1111/j.1574-6968.2000.tb09262.x;
RA   Holt P.J., Williams R.E., Jordan K.N., Lowe C.R., Bruce N.C.;
RT   "Cloning, sequencing and expression in Escherichia coli of the primary
RT   alcohol dehydrogenase gene from Thermoanaerobacter ethanolicus JW200.";
RL   FEMS Microbiol. Lett. 190:57-62(2000).
CC   -!- FUNCTION: Alcohol dehydrogenase active against primary long-chain
CC       alcohols. Pentan-1-ol is the optimum substrate in vitro, but also shows
CC       efficient dehydrogenase activity on propanol, hexanol, and ethanol.
CC       {ECO:0000269|PubMed:10981690}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a primary alcohol + NADP(+) = an aldehyde + H(+) + NADPH;
CC         Xref=Rhea:RHEA:15937, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.2;
CC         Evidence={ECO:0000269|PubMed:10981690};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:10981690};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermostable. Heating at 70 degrees Celsius for 180 minutes gives no
CC         observable loss of enzymatic activity. {ECO:0000269|PubMed:10981690};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10981690}.
CC   -!- INDUCTION: Seems to be constitutively expressed.
CC       {ECO:0000269|PubMed:10981690}.
CC   -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; AF178965; AAG01186.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9F282; -.
DR   SMR; Q9F282; -.
DR   GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   CDD; cd08186; Fe-ADH-like; 1.
DR   InterPro; IPR001670; ADH_Fe/GldA.
DR   InterPro; IPR045910; AdhA-like.
DR   InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR   PANTHER; PTHR11496; PTHR11496; 1.
DR   Pfam; PF00465; Fe-ADH; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NADP; Oxidoreductase; Zinc.
FT   CHAIN           1..399
FT                   /note="Long-chain primary alcohol dehydrogenase AdhA"
FT                   /id="PRO_0000424547"
SQ   SEQUENCE   399 AA;  43241 MW;  C9F4F7B14177EA87 CRC64;
     MWETKINPNK VFELRCKNTT YFGIGSIKKI KDILEVLKNK GINNVILVTG KGSYKASGAW
     DVVKPALETL GFKYSLYDKV GPNPTVDMID EAAKIGRETG AKAVIGIGGG SPIDTAKSVA
     VLLEYTDKNA RELYEQKFIP EKAAPIIAIN LTHGTGTEVD RFAVATIPEK NYKPAIAYDC
     LYPMYAIDDP SLMTKLDKKQ TIAVTIDALN HVTEAATTLV ASPYSVLMAK ETVRLIVRYL
     PAAVNDPENL VARYYLLYAS ALAGISFDNG LLHLTHALEH PLSAVKPEIA HGLGLGAILP
     AVVKAIYPSV AEVLAEVYSP IVPGLKGLPA EAEYVAKKVE EWLFKVGCTQ KLSDFGFTKE
     DIPTLVRLAK TTPSLDGLLS NAPVEATEAV IAKIYEESF