ID SSDH_HYLLA Reviewed; 535 AA. AC Q3MSM3; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2005, sequence version 1. DT 22-JUL-2008, entry version 22. 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 Hylobates lar (Common gibbon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hylobatidae; Hylobates. OX NCBI_TaxID=9580; 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; AJ891038; CAI69938.1; -; mRNA. DR HOVERGEN; Q3MSM3; -. 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_DHase_CS. DR InterPro; IPR016162; Ald_DHase_N. DR InterPro; IPR015590; Aldehyde_DHase. DR InterPro; IPR010102; Succ_semiAld_DHase. 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_0000042903. 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; 57112 MW; 1D55DC672C6787B8 CRC64; MATCFWLRSC GARRLGSTFP GCRLRPRAGG LVPASGPAPG PAQLRCYAGG LAGLSAALLR TDSFVGGRWL PAAATFPVQD PASGAALGMV ADCGVREARA AVRAAYEAFC SWREVSAKER SSLLRKWYNL MIQNKDDLAR IITAESGKPL KEAHGEILYS AFFLEWFSEE ARRVYGDIIY TPAKDRRALV LKQPIGVAAV ITPWNFPSAM ITRKVGAALA AGCTVVVKPA EDTPFSALAL AELASQAGIP SGVYNVIPCS RKNAKEVGEA ICTDPLVSKI SFTGSTTTGK ILLHHAANSV KRVSMELGGL APFIVFDSAN VDQAVAGALA SKFRNTGQTC VCSNRFLVQR GIHDAFVKAF AEAMKKNLHV GNGFEEGTTQ GPLINEKAVE KVEKQVNDAV SKGATIVTGG KRHQLGKNFF EPTLLCNVTQ DMLCTHEETF GPLAPVIKFD TEEEAIAIAN AADVGLAGYF YSQDPAQIWR VAEQLEVGMV GVNEGLISSV ECPFGGVKQS GLGREGSKYG IDEYLELKYV CYGGL //