ID   ALDH6_YEAST             Reviewed;         500 AA.
AC   P54115; Q02782;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   16-DEC-2008, entry version 79.
DE   RecName: Full=Magnesium-activated aldehyde dehydrogenase, cytosolic;
DE            EC=1.2.1.3;
DE   AltName: Full=Mg(2+)-activated acetaldehyde dehydrogenase;
DE            Short=Mg(2+)-ACDH;
GN   Name=ALD6; Synonyms=ALDH1; OrderedLocusNames=YPL061W; ORFNames=LPE9;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=DBY939;
RX   MEDLINE=98132377; PubMed=9473035;
RA   Wang X., Mann C.J., Bai Y., Ni L., Weiner H.;
RT   "Molecular cloning, characterization, and potential roles of cytosolic
RT   and mitochondrial aldehyde dehydrogenases in ethanol metabolism in
RT   Saccharomyces cerevisiae.";
RL   J. Bacteriol. 180:822-830(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313271; PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
RA   Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
RA   Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
RA   Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
RA   Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
RA   Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
RA   Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
RA   Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
RA   Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
RA   Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
RA   Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
RA   Zollner A., Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 76-79 AND 482-488.
RC   STRAIN=ATCC 44827 / SKQ2N;
RX   MEDLINE=97190279; PubMed=9038161; DOI=10.1074/jbc.272.9.5544;
RA   Norbeck J., Blomberg A.;
RT   "Metabolic and regulatory changes associated with growth of
RT   Saccharomyces cerevisiae in 1.4 M NaCl. Evidence for osmotic induction
RT   of glycerol dissimilation via the dihydroxyacetone pathway.";
RL   J. Biol. Chem. 272:5544-5554(1997).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-16, AND CHARACTERIZATION.
RX   MEDLINE=98053564; PubMed=9392076;
RX   DOI=10.1002/(SICI)1097-0061(199711)13:14<1319::AID-YEA183>3.0.CO;2-T;
RA   Meaden P.G., Dickinson F.M., Mifsud A., Tessier W., Westwater J.,
RA   Bussey H., Midgley M.;
RT   "The ALD6 gene of Saccharomyces cerevisiae encodes a cytosolic,
RT   Mg(2+)-activated acetaldehyde dehydrogenase.";
RL   Yeast 13:1319-1327(1997).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-3, AND MASS SPECTROMETRY.
RX   PubMed=12872131; DOI=10.1038/nbt849;
RA   Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,
RA   Marsischky G., Roelofs J., Finley D., Gygi S.P.;
RT   "A proteomics approach to understanding protein ubiquitination.";
RL   Nat. Biotechnol. 21:921-926(2003).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-491, AND MASS
RP   SPECTROMETRY.
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass
RT   spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250; THR-251 AND
RP   SER-262, AND MASS SPECTROMETRY.
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- CATALYTIC ACTIVITY: An aldehyde + NAD(+) + H(2)O = an acid + NADH.
CC   -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from
CC       ethanol: step 2/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: Present with 135000 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
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DR   EMBL; U56604; AAB01219.1; -; Genomic_DNA.
DR   EMBL; U39205; AAB68304.1; -; Genomic_DNA.
DR   PIR; S60929; S60929.
DR   RefSeq; NP_015264.1; -.
DR   HSSP; Q28399; 1O9J.
DR   IntAct; P54115; 32.
DR   PeptideAtlas; P54115; -.
DR   PRIDE; P54115; -.
DR   Ensembl; YPL061W; Saccharomyces cerevisiae.
DR   GeneID; 856044; -.
DR   KEGG; sce:YPL061W; -.
DR   NMPDR; fig|4932.3.peg.6397; -.
DR   CYGD; YPL061w; -.
DR   SGD; S000005982; ALD6.
DR   HOGENOM; P54115; -.
DR   BioCyc; MetaCyc:MON-13664; -.
DR   LinkHub; P54115; -.
DR   NextBio; 980989; -.
DR   GermOnline; YPL061W; Saccharomyces cerevisiae.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IEA:EC.
DR   GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IDA:SGD.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019413; P:acetate biosynthetic process; IMP:SGD.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR016160; Ald_DHase_CS.
DR   InterPro; IPR016162; Ald_DHase_N.
DR   InterPro; IPR015590; Aldehyde_DHase.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR   PANTHER; PTHR11699; Aldehyde_dehyd; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; FALSE_NEG.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Direct protein sequencing; Magnesium;
KW   NAD; Oxidoreductase; Phosphoprotein; Ubl conjugation.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    500       Magnesium-activated aldehyde
FT                                dehydrogenase, cytosolic.
FT                                /FTId=PRO_0000056441.
FT   NP_BIND     249    254       NAD (By similarity).
FT   ACT_SITE    272    272       Proton acceptor (By similarity).
FT   ACT_SITE    306    306       Nucleophile (By similarity).
FT   SITE        173    173       Transition state stabilizer (By
FT                                similarity).
FT   MOD_RES     250    250       Phosphoserine.
FT   MOD_RES     251    251       Phosphothreonine.
FT   MOD_RES     262    262       Phosphoserine.
FT   MOD_RES     491    491       Phosphothreonine.
FT   CROSSLNK      3      3       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CONFLICT    121    121       L -> FK (in Ref. 1; AAB01219).
SQ   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
//