ID   SSDH_RAT                Reviewed;         523 AA.
AC   P51650;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 2.
DT   27-MAR-2024, entry version 147.
DE   RecName: Full=Succinate-semialdehyde dehydrogenase, mitochondrial;
DE            Short=SSADH {ECO:0000303|PubMed:7814412};
DE            EC=1.2.1.24 {ECO:0000269|PubMed:7814412};
DE   AltName: Full=Aldehyde dehydrogenase family 5 member A1;
DE   AltName: Full=NAD(+)-dependent succinic semialdehyde dehydrogenase;
DE   Flags: Precursor;
GN   Name=Aldh5a1; Synonyms=Ssadh;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), PROTEIN SEQUENCE OF
RP   36-84; 92-101; 129-153; 162-172; 303-311; 419-425 AND 503-526, CATALYTIC
RP   ACTIVITY, AND TISSUE SPECIFICITY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=7814412; DOI=10.1074/jbc.270.1.461;
RA   Chambliss K.L., Caudle D.L., Hinson D.D., Moomaw C.R., Slaughter C.A.,
RA   Jakobs C., Gibson K.M.;
RT   "Molecular cloning of the mature NAD(+)-dependent succinic semialdehyde
RT   dehydrogenase from rat and human. cDNA isolation, evolutionary homology,
RT   and tissue expression.";
RL   J. Biol. Chem. 270:461-467(1995).
RN   [3]
RP   PROTEIN SEQUENCE OF 36-48; 161-172 AND 401-418, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA   Lubec G., Afjehi-Sadat L.;
RL   Submitted (NOV-2006) to UniProtKB.
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         Evidence={ECO:0000269|PubMed:7814412};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13218;
CC         Evidence={ECO:0000305|PubMed:7814412};
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 {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long {ECO:0000303|PubMed:7814412};
CC         IsoId=P51650-1; Sequence=Displayed;
CC       Name=Short {ECO:0000303|PubMed:7814412};
CC         IsoId=P51650-2; Sequence=VSP_001284;
CC   -!- TISSUE SPECIFICITY: Brain, pancreas, heart, liver, skeletal muscle,
CC       kidney. Lower in spleen, lung, kidney and testis.
CC       {ECO:0000269|PubMed:7814412}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AABR03105019; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L34821; AAA67058.1; -; mRNA.
DR   PIR; I61704; I61704.
DR   AlphaFoldDB; P51650; -.
DR   SMR; P51650; -.
DR   STRING; 10116.ENSRNOP00000035601; -.
DR   iPTMnet; P51650; -.
DR   PhosphoSitePlus; P51650; -.
DR   jPOST; P51650; -.
DR   PaxDb; 10116-ENSRNOP00000035601; -.
DR   PeptideAtlas; P51650; -.
DR   UCSC; RGD:621422; rat. [P51650-1]
DR   AGR; RGD:621422; -.
DR   RGD; 621422; Aldh5a1.
DR   eggNOG; KOG2451; Eukaryota.
DR   InParanoid; P51650; -.
DR   PhylomeDB; P51650; -.
DR   BRENDA; 1.2.1.3; 5301.
DR   Reactome; R-RNO-916853; Degradation of GABA.
DR   SABIO-RK; P51650; -.
DR   UniPathway; UPA00733; -.
DR   PRO; PR:P51650; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0031406; F:carboxylic acid binding; IPI:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0051287; F:NAD binding; IDA:RGD.
DR   GO; GO:0004777; F:succinate-semialdehyde dehydrogenase (NAD+) activity; IDA: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:0009448; P:gamma-aminobutyric acid metabolic process; ISO:RGD.
DR   GO; GO:0006536; P:glutamate metabolic process; ISO:RGD.
DR   GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR   GO; GO:0006105; P:succinate metabolic process; IDA:UniProtKB.
DR   GO; GO:0051932; P:synaptic transmission, GABAergic; ISO:RGD.
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.
DR   World-2DPAGE; 0004:P51650; -.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Direct protein sequencing;
KW   Disulfide bond; Mitochondrion; NAD; Oxidoreductase; Phosphoprotein;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..35
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:7814412, ECO:0000269|Ref.3"
FT   CHAIN           36..523
FT                   /note="Succinate-semialdehyde dehydrogenase, mitochondrial"
FT                   /id="PRO_0000056567"
FT   ACT_SITE        294
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        328
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         201
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         216..219
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         272..277
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         322
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         486
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            193
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         114
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P51649"
FT   MOD_RES         114
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWF0"
FT   MOD_RES         123
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWF0"
FT   MOD_RES         172
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWF0"
FT   MOD_RES         253
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWF0"
FT   MOD_RES         253
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWF0"
FT   MOD_RES         353
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWF0"
FT   MOD_RES         390
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWF0"
FT   MOD_RES         399
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BWF0"
FT   MOD_RES         487
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P51649"
FT   DISULFID        328..330
FT                   /note="In inhibited form"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         107..134
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000303|PubMed:7814412"
FT                   /id="VSP_001284"
SQ   SEQUENCE   523 AA;  56131 MW;  4CA521139C9FA98F CRC64;
     MATCFLLRNF CAARPALRPP GRLLREPAGA QRRSYVGGPA DLHADLLRGD SFVGGRWLPT
     PATFPVYDPA SGAKLGTVAD CGVPEARAAV RAAYDAFSSW KEISVKERSS LLRKWYDLMI
     QNKDELAKII TAESGKPLKE AQGEILYSAF FLEWFSEEAR RVYGDIIYTS AKDKRGLVLK
     QPVGVASIIT PWNFPSAMIT RKVGAALAAG CTVVVKPAED TPYSALALAQ LANQAGIPPG
     VYNVIPCSRT KAKEVGEVLC TDPLVSKISF TGSTATGKIL LHHAANSVKR VSMELGGLAP
     FIVFDSANVD QAVAGAMASK FRNAGQTCVC SNRFLVQRGI HDSFVTKFAE AMKKSLRVGN
     GFEEGTTQGP LINEKAVEKV EKHVNDAVAK GATVVTGGKR HQSGGNFFEP TLLSNVTRDM
     LCITEETFGP VAPVIKFDKE EEAVAIANAA DVGLAGYFYS QDPAQIWRVA EQLEVGMVGV
     NEGLISSVEC PFGGVKQSGL GREGSKYGID EYLEVKYVCY GGL
//