ID   UGA2_YEAST              Reviewed;         497 AA.
AC   P38067; D6VQ07; E9PAD1;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   27-MAR-2024, entry version 181.
DE   RecName: Full=Succinate-semialdehyde dehydrogenase [NADP(+)];
DE            Short=SSDH;
DE            EC=1.2.1.16;
GN   Name=UGA2; Synonyms=UGA5; OrderedLocusNames=YBR006W; ORFNames=YBR0112;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NAD(+) + succinate semialdehyde = 2 H(+) + NADH +
CC         succinate; Xref=Rhea:RHEA:13217, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57706, ChEBI:CHEBI:57945; EC=1.2.1.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NADP(+) + succinate semialdehyde = 2 H(+) + NADPH +
CC         succinate; Xref=Rhea:RHEA:13213, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:57706,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.16;
CC   -!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; Z35875; CAA84943.1; -; Genomic_DNA.
DR   EMBL; Z35876; CAA84945.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07127.1; -; Genomic_DNA.
DR   PIR; S45858; S45858.
DR   RefSeq; NP_009560.1; NM_001178354.1.
DR   AlphaFoldDB; P38067; -.
DR   SMR; P38067; -.
DR   BioGRID; 32707; 64.
DR   DIP; DIP-1759N; -.
DR   IntAct; P38067; 3.
DR   MINT; P38067; -.
DR   STRING; 4932.YBR006W; -.
DR   MaxQB; P38067; -.
DR   PaxDb; 4932-YBR006W; -.
DR   PeptideAtlas; P38067; -.
DR   EnsemblFungi; YBR006W_mRNA; YBR006W; YBR006W.
DR   GeneID; 852291; -.
DR   KEGG; sce:YBR006W; -.
DR   AGR; SGD:S000000210; -.
DR   SGD; S000000210; UGA2.
DR   VEuPathDB; FungiDB:YBR006W; -.
DR   eggNOG; KOG2451; Eukaryota.
DR   GeneTree; ENSGT00930000151038; -.
DR   HOGENOM; CLU_005391_5_1_1; -.
DR   InParanoid; P38067; -.
DR   OMA; IVTGMPT; -.
DR   OrthoDB; 216092at2759; -.
DR   BioCyc; MetaCyc:YBR006W-MONOMER; -.
DR   BioCyc; YEAST:YBR006W-MONOMER; -.
DR   Reactome; R-SCE-916853; Degradation of GABA.
DR   UniPathway; UPA00733; -.
DR   BioGRID-ORCS; 852291; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P38067; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38067; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0004777; F:succinate-semialdehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0036243; F:succinate-semialdehyde dehydrogenase (NADP+) activity; IEA:RHEA.
DR   GO; GO:0009013; F:succinate-semialdehyde dehydrogenase [NAD(P)+] activity; IMP:SGD.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR   GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IMP:SGD.
DR   GO; GO:0006540; P:glutamate decarboxylation to succinate; IMP:SGD.
DR   CDD; cd07103; ALDH_F5_SSADH_GabD; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR010102; Succ_semiAld_DH.
DR   NCBIfam; TIGR01780; SSADH; 1.
DR   PANTHER; PTHR43353; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43353:SF5; SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..497
FT                   /note="Succinate-semialdehyde dehydrogenase [NADP(+)]"
FT                   /id="PRO_0000056568"
FT   ACT_SITE        264
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        298
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   SITE            164
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   497 AA;  54189 MW;  F33252EEE24B9B40 CRC64;
     MTLSKYSKPT LNDPNLFRES GYIDGKWVKG TDEVFEVVDP ASGEIIARVP EQPVSVVEEA
     IDVAYETFKT YKNTTPRERA KWLRNMYNLM LENLDDLATI ITLENGKALG EAKGEIKYAA
     SYFEWYAEEA PRLYGATIQP LNPHNRVFTI RQPVGVCGII CPWNFPSAMI TRKAAAALAV
     GCTVVIKPDS QTPLSALAMA YLAEKAGFPK GSFNVILSHA NTPKLGKTLC ESPKVKKVTF
     TGSTNVGKIL MKQSSSTLKK LSFELGGNAP FIVFEDADLD QALEQAMACK FRGLGQTCVC
     ANRLYVHSSI IDKFAKLLAE RVKKFVIGHG LDPKTTHGCV INSSAIEKVE RHKQDAIDKG
     AKVVLEGGRL TELGPNFYAP VILSHVPSTA IVSKEETFGP LCPIFSFDTM EEVVGYANDT
     EFGLAAYVFS KNVNTLYTVS EALETGMVSC NTGVFSDCSI PFGGVKESGF GREGSLYGIE
     DYTVLKTITI GNLPNSI
//