(data stored in SCRATCH zone)

SWISSPROT: Q757K5_ASHGO

ID   Q757K5_ASHGO            Unreviewed;       495 AA.
AC   Q757K5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 102.
DE   RecName: Full=Succinate-semialdehyde dehydrogenase {ECO:0000256|RuleBase:RU365091};
DE            EC=1.2.1.16 {ECO:0000256|RuleBase:RU365091};
GN   ORFNames=AGOS_AER007W {ECO:0000313|EMBL:AAS52691.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS52691.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS52691.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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         Evidence={ECO:0000256|RuleBase:RU365091};
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         Evidence={ECO:0000256|RuleBase:RU365091};
CC   -!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation.
CC       {ECO:0000256|RuleBase:RU365091}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; AE016818; AAS52691.1; -; Genomic_DNA.
DR   RefSeq; NP_984867.1; NM_210221.1.
DR   STRING; 33169.AAS52691; -.
DR   EnsemblFungi; AAS52691; AAS52691; AGOS_AER007W.
DR   GeneID; 4621066; -.
DR   KEGG; ago:AGOS_AER007W; -.
DR   HOGENOM; HOG000271509; -.
DR   InParanoid; Q757K5; -.
DR   KO; K00135; -.
DR   OMA; IITWENG; -.
DR   UniPathway; UPA00733; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0004777; F:succinate-semialdehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0009013; F:succinate-semialdehyde dehydrogenase [NAD(P)+] activity; IBA:GO_Central.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
DR   GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006540; P:glutamate decarboxylation to succinate; IEA:EnsemblFungi.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 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   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   TIGRFAMs; TIGR01780; SSADH; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q757K5.
DR   SWISS-2DPAGE; Q757K5.
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591}.
FT   DOMAIN          26..487
FT                   /note="Aldedh"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        263
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   495 AA;  53676 MW;  886DC1BCC59BB0B5 CRC64;
     MGFQSFKPTF RNEDLVRRGA YINGEWITSA KESFNVTDPA TDQVIAELPD FDSGEAEAAL
     KAAHASFQSY KKTSPTQRSE WLRNLYDLIM ENAEDLAAIV TWENGKSLRE ALVEIRYGAT
     FFKWFSEEAL RLYGTTIQPS NPGNRAFTIR QPVGVCALIC PWNFPNAMIS RKAAPALAAG
     CTVIIKPDPQ TPLSSLALAH LAEKAGFPPG VINVVPTSKY TKDIGVLLCE SSLVRKVSFT
     GSTAVGKILM QQAASTVKKV SFELGGNAPV IIMGDADMEK TVEEVLATKF RGMGQTCICA
     NRLYVHRSII DDFSSRLVKK VEGLKLGNGF QEGVTHGSLI NNAAIEKVER HAKDAIERGA
     KVLLPGGRAP ELGPHFYSPT VLSDVKPDSV LTREETFGPL CAMIPFDTVE EVVGYANDTQ
     YGLASYVFSE NIKTVYSIAE ALDFGMVACN TGLFSDSMVP FGGIKESGFG IEGSLHGIND
     YTVLKTVTIG NVPTL
//

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