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 16-JUN-2009, entry version 25. DE RecName: Full=Succinate-semialdehyde dehydrogenase, mitochondrial; DE EC=1.2.1.24; DE AltName: Full=NAD(+)-dependent succinic semialdehyde dehydrogenase; DE AltName: Full=Aldehyde dehydrogenase family 5 member A1; DE Flags: Precursor; GN Name=ALDH5A1; OS Pan paniscus (Pygmy chimpanzee) (Bonobo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9597; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Blasi P., Palmerio F., Aiello A., Rocchi M., Malaspina P., RA Novelletto A.; RT "Human succinic semialdehyde dehydrogenase variation in higher RT primates: intra and inter specific data."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: Succinate semialdehyde + NAD(+) + H(2)O = CC succinate + NADH. CC -!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ891037; CAI69937.1; -; mRNA. DR HOVERGEN; Q3MSM4; -. DR BRENDA; 1.2.1.24; 289054. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0005625; C:soluble fraction; ISS:UniProtKB. DR GO; GO:0004777; F:succinate-semialdehyde dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0007417; P:central nervous system development; ISS:UniProtKB. DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; ISS:UniProtKB. DR GO; GO:0055114; P:oxidation reduction; ISS:UniProtKB. DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH. DR InterPro; IPR010102; Succ_semiAld_DH. DR Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1. DR PANTHER; PTHR11699; Aldehyde_dehyd; 1. DR Pfam; PF00171; Aldedh; 1. DR TIGRFAMs; TIGR01780; SSADH; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 2: Evidence at transcript level; KW Mitochondrion; NAD; Oxidoreductase; Transit peptide. FT TRANSIT 1 47 Mitochondrion (Potential). FT CHAIN 48 535 Succinate-semialdehyde dehydrogenase, FT mitochondrial. FT /FTId=PRO_0000042902. FT NP_BIND 284 289 NADP (By similarity). FT ACT_SITE 306 306 Proton acceptor (By similarity). FT ACT_SITE 340 340 Nucleophile (By similarity). FT SITE 205 205 Transition state stabilizer (By FT similarity). 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 //