SSDH_GORGO
ID SSDH_GORGO Reviewed; 535 AA.
AC Q6A2H1;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
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 Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Blasi P., Malaspina P.;
RT "Comparative analysis of succinic semialdehyde dehydrogenase in non three
RT ape species.";
RL Submitted (JAN-2004) 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=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 -!- ACTIVITY REGULATION: Redox-regulated. Inhibited under oxydizing
CC conditions (By similarity). {ECO:0000250}.
CC -!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AJ621751; CAF21868.1; -; mRNA.
DR RefSeq; NP_001266541.1; NM_001279612.1.
DR AlphaFoldDB; Q6A2H1; -.
DR SMR; Q6A2H1; -.
DR STRING; 9593.ENSGGOP00000022293; -.
DR GeneID; 101149264; -.
DR KEGG; ggo:101149264; -.
DR CTD; 7915; -.
DR eggNOG; KOG2451; Eukaryota.
DR InParanoid; Q6A2H1; -.
DR OrthoDB; 899961at2759; -.
DR BRENDA; 1.2.1.24; 2496.
DR UniPathway; UPA00733; -.
DR Proteomes; UP000001519; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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:gamma-aminobutyric acid catabolic process; ISS:UniProtKB.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR GO; GO:0006105; P:succinate metabolic process; ISS:UniProtKB.
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; 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 Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 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 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_0000007183"
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; 57142 MW; B1FC5E4E92149214 CRC64;
MATCIWLRSC GARRLGSTFP GCRLRPRAGG LVPASGPAPG PAQLRCYAGG LAGLSAALLR
TDSFVGGRWL PAAATFPVQD PASGAALGMV ADCGVREARA AVRAAYEAFC RWREVSAKER
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
