UniProt: A0A0D9R5W7

Database: UniProt
Entry: A0A0D9R5W7_CHLSB

LinkDB:  A0A0D9R5W7_CHLSB 
Original site:  A0A0D9R5W7_CHLSB

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Ontology (10)   
   GO (10)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (3)   
   ENSEMBL-UP (3)   
DNA sequence (3)   
   EMBL (3)   
Protein domain (10)   
   InterPro (7)   
   Pfam (1)   
   PROSITE (2)   
All databases (27)   

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ID   A0A0D9R5W7_CHLSB        Unreviewed;       447 AA.
AC   A0A0D9R5W7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Succinate-semialdehyde dehydrogenase {ECO:0000256|RuleBase:RU365091};
DE            EC=1.2.1.24 {ECO:0000256|RuleBase:RU365091};
GN   Name=ALDH5A1 {ECO:0000313|Ensembl:ENSCSAP00000004006.1};
OS   Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000004006.1, ECO:0000313|Proteomes:UP000029965};
RN   [1] {ECO:0000313|Ensembl:ENSCSAP00000004006.1, ECO:0000313|Proteomes:UP000029965}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAP00000004006.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Catalyzes one step in the degradation of the inhibitory
CC       neurotransmitter gamma-aminobutyric acid (GABA).
CC       {ECO:0000256|ARBA:ARBA00003743}.
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=1.2.1.24;
CC         Evidence={ECO:0000256|RuleBase:RU365091};
CC   -!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation.
CC       {ECO:0000256|ARBA:ARBA00005176, ECO:0000256|RuleBase:RU365091}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC       ECO:0000256|RuleBase:RU365091}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173,
CC       ECO:0000256|RuleBase:RU365091}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; AQIB01159542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01159543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01159544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A0D9R5W7; -.
DR   STRING; 60711.ENSCSAP00000004006; -.
DR   Ensembl; ENSCSAT00000005791.1; ENSCSAP00000004006.1; ENSCSAG00000007743.1.
DR   eggNOG; KOG2451; Eukaryota.
DR   GeneTree; ENSGT00930000151038; -.
DR   OMA; CTHEEVF; -.
DR   UniPathway; UPA00733; -.
DR   Proteomes; UP000029965; Chromosome 17.
DR   Bgee; ENSCSAG00000007743; Expressed in liver and 7 other cell types or tissues.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0004777; F:succinate-semialdehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007417; P:central nervous system development; IEA:Ensembl.
DR   GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006536; P:glutamate metabolic process; IEA:Ensembl.
DR   GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR   GO; GO:0006105; P:succinate metabolic process; IEA:Ensembl.
DR   GO; GO:0051932; P:synaptic transmission, GABAergic; IEA:Ensembl.
DR   CDD; cd07103; ALDH_F5_SSADH_GabD; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
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; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Mitochondrion {ECO:0000256|RuleBase:RU365091};
KW   NAD {ECO:0000256|RuleBase:RU365091};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003345};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029965}.
FT   DOMAIN          2..442
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        218
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ   SEQUENCE   447 AA;  48164 MW;  6A1B9389FE0DA951 CRC64;
     MVADCGVSEA RAAVRAAYEA FCSWREVSAK ERSSLLRKWY NLMIQNKDDL ARIITAESGK
     PLKEAHGEIL YSAFFLEWFS EEARRVYGDI IYTPAKDKRA LVLKQPVGVA AVITPWNFPS
     AMITRKVGAA LAAGCTVVVK PAEDTPFSAL ALAELASQAG IPPGVYNVIP CSRKNAKEVG
     EAICTDPLVS KISFTGSTTT GKILLHHAAN SVKRVSMELG GLAPFIVFDS ANVDQAVAGA
     LASKFRNAGQ TCVCSNRFLV QRGIHDAFVK AFAEAMKKNL HVGNGFEEGT TQGPLINEKA
     VEKVEKQVND AVSKGATIVT GGKRHHLGKN FFEPTLLSNV TQDMLCTHEE TFGPLAPVIK
     FDTEEEAIAI ANATDVGLAG YFYSQDPAQI WRVAEQLEVG MVGVNEGLIS SVECPFGGVK
     QSGLGREGSK YGIDEYLELK YVCYGGL
//

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