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Magnesium-activated aldehyde dehydrogenase, cytosolic (EC 1.2.1.4) (Mg(2 )-activated acetaldehyde dehydrogenase) (Mg(2 )-ACDH)

 ALDH6_YEAST             Reviewed;         500 AA.
P54115; D6W3V3; Q02782;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
28-MAR-2018, entry version 169.
RecName: Full=Magnesium-activated aldehyde dehydrogenase, cytosolic;
EC=1.2.1.4;
AltName: Full=Mg(2+)-activated acetaldehyde dehydrogenase;
Short=Mg(2+)-ACDH;
Name=ALD6; Synonyms=ALDH1; OrderedLocusNames=YPL061W; ORFNames=LPE9;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=DBY939;
PubMed=9473035;
Wang X., Mann C.J., Bai Y., Ni L., Weiner H.;
"Molecular cloning, characterization, and potential roles of cytosolic
and mitochondrial aldehyde dehydrogenases in ethanol metabolism in
Saccharomyces cerevisiae.";
J. Bacteriol. 180:822-830(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169875;
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
Zollner A., Vo D.H., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
PROTEIN SEQUENCE OF 76-79 AND 482-488.
STRAIN=ATCC 44827 / SKQ2N;
PubMed=9038161; DOI=10.1074/jbc.272.9.5544;
Norbeck J., Blomberg A.;
"Metabolic and regulatory changes associated with growth of
Saccharomyces cerevisiae in 1.4 M NaCl. Evidence for osmotic induction
of glycerol dissimilation via the dihydroxyacetone pathway.";
J. Biol. Chem. 272:5544-5554(1997).
[5]
PROTEIN SEQUENCE OF 2-16, AND CHARACTERIZATION.
PubMed=9392076;
DOI=10.1002/(SICI)1097-0061(199711)13:14<1319::AID-YEA183>3.0.CO;2-T;
Meaden P.G., Dickinson F.M., Mifsud A., Tessier W., Westwater J.,
Bussey H., Midgley M.;
"The ALD6 gene of Saccharomyces cerevisiae encodes a cytosolic,
Mg(2+)-activated acetaldehyde dehydrogenase.";
Yeast 13:1319-1327(1997).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-3, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=SUB592;
PubMed=12872131; DOI=10.1038/nbt849;
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,
Marsischky G., Roelofs J., Finley D., Gygi S.P.;
"A proteomics approach to understanding protein ubiquitination.";
Nat. Biotechnol. 21:921-926(2003).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[12]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-142 AND LYS-196, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
-!- FUNCTION: Cytosolic aldehyde dehydrogenase which utilizes NADP+ as
the preferred coenzyme. Performs the conversion of acetaldehyde to
acetate. {ECO:0000269|PubMed:9473035}.
-!- CATALYTIC ACTIVITY: An aldehyde + NADP(+) + H(2)O = a carboxylate
+ NADPH. {ECO:0000269|PubMed:9473035}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=40 uM for NADP (with acetaldehyde as cosubstrate)
{ECO:0000269|PubMed:9473035};
KM=99 uM for NADP (with propionaldehyde as cosubstrate)
{ECO:0000269|PubMed:9473035};
KM=17.4 mM for NAD (with propionaldehyde as cosubstrate)
{ECO:0000269|PubMed:9473035};
KM=24 uM for acetaldehyde (with NADP as cosubstrate)
{ECO:0000269|PubMed:9473035};
KM=30 uM for propionaldehyde (with NADP as cosubstrate)
{ECO:0000269|PubMed:9473035};
KM=0.7 mM for propionaldehyde (with NAD as cosubstrate)
{ECO:0000269|PubMed:9473035};
Vmax=24 umol/min/mg enzyme with acetaldehyde and NADP as
substrates {ECO:0000269|PubMed:9473035};
Vmax=14 umol/min/mg enzyme with propionaldehyde and NADP as
substrates {ECO:0000269|PubMed:9473035};
Vmax=8.3 umol/min/mg enzyme with propionaldehyde and NAD as
substrates {ECO:0000269|PubMed:9473035};
-!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from
ethanol: step 2/2.
-!- INTERACTION:
P32582:CYS4; NbExp=29; IntAct=EBI-5798, EBI-4167;
P40492:FYV10; NbExp=2; IntAct=EBI-5798, EBI-25137;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- MISCELLANEOUS: Present with 135000 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U56604; AAB01219.1; -; Genomic_DNA.
EMBL; U39205; AAB68304.1; -; Genomic_DNA.
EMBL; BK006949; DAA11369.1; -; Genomic_DNA.
PIR; S60929; S60929.
RefSeq; NP_015264.1; NM_001183875.1.
ProteinModelPortal; P54115; -.
SMR; P54115; -.
BioGrid; 36117; 211.
DIP; DIP-8324N; -.
IntAct; P54115; 85.
MINT; P54115; -.
STRING; 4932.YPL061W; -.
iPTMnet; P54115; -.
MaxQB; P54115; -.
PaxDb; P54115; -.
PRIDE; P54115; -.
TopDownProteomics; P54115; -.
EnsemblFungi; YPL061W; YPL061W; YPL061W.
GeneID; 856044; -.
KEGG; sce:YPL061W; -.
EuPathDB; FungiDB:YPL061W; -.
SGD; S000005982; ALD6.
GeneTree; ENSGT00760000118999; -.
HOGENOM; HOG000271505; -.
InParanoid; P54115; -.
KO; K00128; -.
OMA; PMNQVTL; -.
OrthoDB; EOG092C1LLH; -.
BioCyc; MetaCyc:MONOMER-13664; -.
BioCyc; YEAST:MONOMER-13664; -.
Reactome; R-SCE-196757; Metabolism of folate and pterines.
UniPathway; UPA00780; UER00768.
PRO; PR:P54115; -.
Proteomes; UP000002311; Chromosome XVI.
GO; GO:0005829; C:cytosol; IDA:SGD.
GO; GO:0005739; C:mitochondrion; IDA:SGD.
GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IBA:GO_Central.
GO; GO:0033721; F:aldehyde dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IDA:SGD.
GO; GO:0019413; P:acetate biosynthetic process; IMP:SGD.
GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0006740; P:NADPH regeneration; IGI:SGD.
GO; GO:0009651; P:response to salt stress; IMP:SGD.
Gene3D; 3.40.309.10; -; 1.
Gene3D; 3.40.605.10; -; 2.
InterPro; IPR016161; Ald_DH/histidinol_DH.
InterPro; IPR016163; Ald_DH_C.
InterPro; IPR029510; Ald_DH_CS_GLU.
InterPro; IPR016162; Ald_DH_N.
InterPro; IPR015590; Aldehyde_DH_dom.
Pfam; PF00171; Aldedh; 1.
SUPFAM; SSF53720; SSF53720; 1.
PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Direct protein sequencing;
Isopeptide bond; Magnesium; NADP; Oxidoreductase; Reference proteome;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9392076}.
CHAIN 2 500 Magnesium-activated aldehyde
dehydrogenase, cytosolic.
/FTId=PRO_0000056441.
NP_BIND 249 254 NAD. {ECO:0000250}.
ACT_SITE 272 272 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10007}.
ACT_SITE 306 306 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU10007}.
SITE 173 173 Transition state stabilizer.
{ECO:0000250}.
CROSSLNK 3 3 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:12872131}.
CROSSLNK 142 142 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 196 196 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CONFLICT 121 121 L -> FK (in Ref. 1; AAB01219).
{ECO:0000305}.
SEQUENCE 500 AA; 54414 MW; 542AA956EFA0E676 CRC64;
MTKLHFDTAE PVKITLPNGL TYEQPTGLFI NNKFMKAQDG KTYPVEDPST ENTVCEVSSA
TTEDVEYAIE CADRAFHDTE WATQDPRERG RLLSKLADEL ESQIDLVSSI EALDNGKTLA
LARGDVTIAI NCLRDAAAYA DKVNGRTINT GDGYMNFTTL EPIGVCGQII PWNFPIMMLA
WKIAPALAMG NVCILKPAAV TPLNALYFAS LCKKVGIPAG VVNIVPGPGR TVGAALTNDP
RIRKLAFTGS TEVGKSVAVD SSESNLKKIT LELGGKSAHL VFDDANIKKT LPNLVNGIFK
NAGQICSSGS RIYVQEGIYD ELLAAFKAYL ETEIKVGNPF DKANFQGAIT NRQQFDTIMN
YIDIGKKEGA KILTGGEKVG DKGYFIRPTV FYDVNEDMRI VKEEIFGPVV TVAKFKTLEE
GVEMANSSEF GLGSGIETES LSTGLKVAKM LKAGTVWINT YNDFDSRVPF GGVKQSGYGR
EMGEEVYHAY TEVKAVRIKL


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