ADHA_SYNY3
ID ADHA_SYNY3 Reviewed; 336 AA.
AC P74721;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Aldehyde reductase AdhA {ECO:0000305};
DE EC=1.1.1.2 {ECO:0000269|PubMed:19411329};
DE AltName: Full=Alcohol dehydrogenase AdhA {ECO:0000303|PubMed:19411329};
GN Name=adhA {ECO:0000303|PubMed:19411329};
GN OrderedLocusNames=slr1192 {ECO:0000312|EMBL:BAA18840.1};
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [2]
RP INDUCTION.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=15805106; DOI=10.1074/jbc.m412174200;
RA Shoumskaya M.A., Paithoonrangsarid K., Kanesaki Y., Los D.A.,
RA Zinchenko V.V., Tanticharoen M., Suzuki I., Murata N.;
RT "Identical Hik-Rre systems are involved in perception and transduction of
RT salt signals and hyperosmotic signals but regulate the expression of
RT individual genes to different extents in synechocystis.";
RL J. Biol. Chem. 280:21531-21538(2005).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, AND INDUCTION
RP BY STRESS.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=19411329; DOI=10.1128/jb.00183-09;
RA Vidal R., Lopez-Maury L., Guerrero M.G., Florencio F.J.;
RT "Characterization of an alcohol dehydrogenase from the Cyanobacterium
RT Synechocystis sp. strain PCC 6803 that responds to environmental stress
RT conditions via the Hik34-Rre1 two-component system.";
RL J. Bacteriol. 191:4383-4391(2009).
RN [4]
RP BIOTECHNOLOGY.
RX DOI=10.1039/C2EE22675H;
RA Gao Z., Zhao H., Li Z., Tan X., Lu X.;
RT "Photosynthetic production of ethanol from carbon dioxide in genetically
RT engineered cyanobacteria.";
RL Energy Environ. Sci. 5:9857-9865(2012).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=28160048; DOI=10.1007/s00253-017-8138-3;
RA Vidal R.;
RT "Alcohol dehydrogenase AdhA plays a role in ethanol tolerance in model
RT cyanobacterium Synechocystis sp. PCC 6803.";
RL Appl. Microbiol. Biotechnol. 101:3473-3482(2017).
CC -!- FUNCTION: Active on a wide variety of primary alcohols and their
CC corresponding aldehydes, but not against ketones nor secondary
CC alcohols. Active on aliphatic compounds up to 5 carbons in length and
CC aromatic alcohols, less effective on branched-chain primary alcohols.
CC Prefers NADPH to NADH. Its catalytic efficiency is greatest for
CC aldehydes, suggesting the reduction of aromatic and medium-chain
CC aliphatic aldehydes is its in vivo activity (PubMed:19411329). Plays a
CC role in tolerance to internally produced ethanol (PubMed:28160048).
CC {ECO:0000269|PubMed:19411329, ECO:0000269|PubMed:28160048}.
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:19411329};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15938;
CC Evidence={ECO:0000269|PubMed:19411329};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15939;
CC Evidence={ECO:0000269|PubMed:19411329};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:19411329};
CC Note=Zn(2+) and Co(2+) are equally efficient in vitro, Fe(2+) is less
CC efficient. {ECO:0000269|PubMed:19411329};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.510 mM for acetaldehyde {ECO:0000269|PubMed:19411329};
CC KM=0.110 mM for butanal {ECO:0000269|PubMed:19411329};
CC KM=0.075 mM for pentanal {ECO:0000269|PubMed:19411329};
CC KM=0.017 mM for cinnamaldehyde {ECO:0000269|PubMed:19411329};
CC KM=18.800 mM for ethanol {ECO:0000269|PubMed:19411329};
CC KM=3.280 mM for butanol {ECO:0000269|PubMed:19411329};
CC KM=1.540 mM for pentanol {ECO:0000269|PubMed:19411329};
CC KM=0.270 mM for cinnamyl alcohol {ECO:0000269|PubMed:19411329};
CC KM=0.025 mM for NADPH {ECO:0000269|PubMed:19411329};
CC KM=0.050 mM for NADP(+) {ECO:0000269|PubMed:19411329};
CC KM=1.310 mM for NADH {ECO:0000269|PubMed:19411329};
CC KM=9.700 mM for NAD(+) {ECO:0000269|PubMed:19411329};
CC Note=kcat is 9458 min(-1) for aceteldehyde. kcat is 9398 min(-1) for
CC butanal. kcat is 9547 min(-1) for pentanal. kcat is 6475 min(-1) for
CC cinnamaldehyde. kcat is 1641 min(-1) for ethanol. kcat is 1023 min(-
CC 1) for butanol. kcat is 789 min(-1) for pentanol. kcat is 3647 min(-
CC 1) for cinnamyl alcohol. {ECO:0000269|PubMed:19411329};
CC -!- SUBUNIT: Homotetramer. {ECO:0000305|PubMed:19411329}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:19411329}.
CC -!- INDUCTION: Induced by salt stress (0.5 M NaCl) under control of rre1
CC and hik34 (PubMed:15805106). Transcription induced by 0.5 M NaCl, 0.5 M
CC sorbitol, heat shock (45 degrees Celsius) and benzyl alcohol (a
CC membrane fluidifier) but not H(2)O(2) or high-light treatment; the
CC induction kinetics are not all the same. Response to all stresses is
CC mediated (in part) by two-component system rre1 and hik34. Expressed at
CC a low constitutive level, protein levels increase 2 hours after
CC sorbitol exposure and 8 hours after NaCl exposure (at protein level).
CC Protein levels do not change upon heat shock (followed for 24 hours)
CC (PubMed:19411329). {ECO:0000269|PubMed:15805106,
CC ECO:0000269|PubMed:19411329}.
CC -!- DISRUPTION PHENOTYPE: Unable to grow heterotrophically on glucose in
CC the dark. Cells photobleach and have significantly reduced survival in
CC 4% ethanol, reduced tolerance to internally produced ethanol.
CC {ECO:0000269|PubMed:28160048}.
CC -!- BIOTECHNOLOGY: Can be used to make bioethanol by insertion of a
CC cassette with Z.mobilis pyruvate decarboxylase and endogenous adhA
CC (this gene) into 2 loci (slr0168 and phaAB). Up to 5.5 g/L, 212
CC mg/L/day, of ethanol can be produced. {ECO:0000269|Ref.4}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; BA000022; BAA18840.1; -; Genomic_DNA.
DR PIR; S76928; S76928.
DR AlphaFoldDB; P74721; -.
DR SMR; P74721; -.
DR IntAct; P74721; 3.
DR STRING; 1148.1653930; -.
DR PaxDb; P74721; -.
DR EnsemblBacteria; BAA18840; BAA18840; BAA18840.
DR KEGG; syn:slr1192; -.
DR eggNOG; COG1064; Bacteria.
DR InParanoid; P74721; -.
DR OMA; YRFSIDM; -.
DR PhylomeDB; P74721; -.
DR BRENDA; 1.1.1.1; 6192.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; NADP; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..336
FT /note="Aldehyde reductase AdhA"
FT /id="PRO_0000453144"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P75691"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P75691"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P75691"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P75691"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P75691"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P75691"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P75691"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P75691"
SQ SEQUENCE 336 AA; 35868 MW; DE216F096C8D8199 CRC64;
MIKAYAALEA NGKLQPFEYD PGALGANEVE IEVQYCGVCH SDLSMINNEW GISNYPLVPG
HEVVGTVAAM GEGVNHVEVG DLVGLGWHSG YCMTCHSCLS GYHNLCATAE STIVGHYGGF
GDRVRAKGVS VVKLPKGIDL ASAGPLFCGG ITVFSPMVEL SLKPTAKVAV IGIGGLGHLA
VQFLRAWGCE VTAFTSSARK QTEVLELGAH HILDSTNPEA IASAEGKFDY IISTVNLKLD
WNLYISTLAP QGHFHFVGVV LEPLDLNLFP LLMGQRSVSA SPVGSPATIA TMLDFAVRHD
IKPVVEQFSF DQINEAIAHL ESGKAHYRVV LSHSKN
