ID SSDH_PANPA Reviewed; 535 AA. AC Q3MSM4; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2005, sequence version 1. DT 02-SEP-2026, entry version 86. DE RecName: Full=Succinate-semialdehyde dehydrogenase, mitochondrial; DE EC=1.2.1.24; DE AltName: Full=Aldehyde dehydrogenase family 5 member A1; DE AltName: Full=NAD(+)-dependent succinic semialdehyde dehydrogenase; DE Flags: Precursor; GN Name=ALDH5A1; OS Pan paniscus (Pygmy chimpanzee) (Bonobo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pan. OX NCBI_TaxID=9597; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Blasi P., Palmerio F., Aiello A., Rocchi M., Malaspina P., Novelletto A.; RT "Human succinic semialdehyde dehydrogenase variation in higher primates: RT intra and inter specific data."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes one step in the degradation of the inhibitory CC neurotransmitter gamma-aminobutyric acid (GABA). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=succinate semialdehyde + NAD(+) + H2O = succinate + NADH + 2 CC H(+); Xref=Rhea:RHEA:13217, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30031, ChEBI:CHEBI:57540, ChEBI:CHEBI:57706, CC ChEBI:CHEBI:57945; EC=1.2.1.24; CC -!- ACTIVITY REGULATION: Redox-regulated. Inhibited under oxidizing CC conditions (By similarity). {ECO:0000250}. CC -!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ891037; CAI69937.1; -; mRNA. DR RefSeq; NP_001266175.1; NM_001279246.1. DR AlphaFoldDB; Q3MSM4; -. DR SMR; Q3MSM4; -. DR STRING; 9597.ENSPPAP00000025067; -. DR GeneID; 100973567; -. DR KEGG; pps:100973567; -. DR CTD; 7915; -. DR eggNOG; KOG2451; Eukaryota. DR BRENDA; 1.2.1.24; 9016. DR UniPathway; UPA00733; -. DR Proteomes; UP000240080; Unplaced. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB. DR GO; GO:0004777; F:succinate-semialdehyde dehydrogenase (NAD+) activity; ISS:UniProtKB. DR GO; GO:0007417; P:central nervous system development; ISS:UniProtKB. DR GO; GO:0009450; P:GABA catabolic process; ISS:UniProtKB. DR GO; GO:0006105; P:succinate metabolic process; ISS:UniProtKB. DR CDD; cd07103; ALDH_F5_SSADH_GabD; 1. DR FunFam; 3.40.605.10:FF:000026; Aldehyde dehydrogenase, putative; 1. DR FunFam; 3.40.309.10:FF:000004; Succinate-semialdehyde dehydrogenase I; 1. DR FunFam; 3.40.605.10:FF:000096; Succinate-semialdehyde dehydrogenase, mitochondrial; 1. DR Gene3D; 3.40.605.10; Aldehyde Dehydrogenase, Chain A, domain 1; 1. DR Gene3D; 3.40.309.10; Aldehyde Dehydrogenase, Chain A, domain 2; 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; IPR050740; Aldehyde_DH_Superfamily. 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 2: Evidence at transcript level; KW Acetylation; Disulfide bond; Mitochondrion; NAD; Oxidoreductase; KW Phosphoprotein; Reference proteome; Transit peptide. FT TRANSIT 1..47 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 48..535 FT /note="Succinate-semialdehyde dehydrogenase, mitochondrial" FT /id="PRO_0000042902" FT ACT_SITE 306 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007, FT ECO:0000255|PROSITE-ProRule:PRU10008" FT ACT_SITE 340 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007, FT ECO:0000255|PROSITE-ProRule:PRU10008" FT BINDING 213 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 213 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 228..231 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 284..289 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250" FT BINDING 334 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 498 FT /ligand="substrate" FT /evidence="ECO:0000250" FT SITE 205 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250" FT MOD_RES 126 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P51649" FT MOD_RES 126 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8BWF0" FT MOD_RES 135 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8BWF0" FT MOD_RES 184 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8BWF0" FT MOD_RES 265 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8BWF0" FT MOD_RES 265 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q8BWF0" FT MOD_RES 365 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8BWF0" FT MOD_RES 402 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8BWF0" FT MOD_RES 411 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8BWF0" FT MOD_RES 499 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P51649" FT DISULFID 340..342 FT /note="In inhibited form" FT /evidence="ECO:0000250" SQ SEQUENCE 535 AA; 57188 MW; C78625F5251EFBC2 CRC64; MATCIWLRSC GARRLGWTFP GCRLRPRAGG LVPASGPAPG PAQLRCYAGG LAGLSAALLR TDSFVGGRWL PAAATFPVQD PASGAALGMV ADCGVREARA AVRAAYEAFC CWREVSAKER SSLLRKWYNL MIQNKDDLAR IITAESGKPL KEAHGEILYS AFFLEWFSEE ARRVYGDIIY TPAKDRRALV LKQPIGVAAV ITPWNFPSAM ITRKVGAALA AGCTVVVKPA EDTPFSALAL AELASQAGIP SGVYNVIPCS RKNAKEVGEA ICTDPLVSKI SFTGSTTTGK ILLHHAANSV KRVSMELGGL APFIVFDSAN VDQAVAGAMA SKFRNTGQTC VCSNQFLVQR GIHDAFVKAF AEAMKKNLRV GNGFEEGTTQ GPLINEKAVE KVEKQVNDAV SKGATVVTGG KRHQLGKNFF EPTLLCNVTQ DMLCTHEETF GPLAPVIKFD TEEEAIAIAN AADVGLAGYF YSQDPAQIWR VAEQLEVGMV GVNEGLISSV ECPFGGVKQS GLGREGSKYG IDEYLELKYV CYGGL //