true
1996-10-01
2024-01-24
146
SSDH_RAT
Genome sequence of the Brown Norway rat yields insights into mammalian evolution.
Gibbs R.A.
Weinstock G.M.
Metzker M.L.
Muzny D.M.
Sodergren E.J.
Scherer S.
Scott G.
Steffen D.
Worley K.C.
Burch P.E.
Okwuonu G.
Hines S.
Lewis L.
Deramo C.
Delgado O.
Dugan-Rocha S.
Miner G.
Morgan M.
Hawes A.
Gill R.
Holt R.A.
Adams M.D.
Amanatides P.G.
Baden-Tillson H.
Barnstead M.
Chin S.
Evans C.A.
Ferriera S.
Fosler C.
Glodek A.
Gu Z.
Jennings D.
Kraft C.L.
Nguyen T.
Pfannkoch C.M.
Sitter C.
Sutton G.G.
Venter J.C.
Woodage T.
Smith D.
Lee H.-M.
Gustafson E.
Cahill P.
Kana A.
Doucette-Stamm L.
Weinstock K.
Fechtel K.
Weiss R.B.
Dunn D.M.
Green E.D.
Blakesley R.W.
Bouffard G.G.
De Jong P.J.
Osoegawa K.
Zhu B.
Marra M.
Schein J.
Bosdet I.
Fjell C.
Jones S.
Krzywinski M.
Mathewson C.
Siddiqui A.
Wye N.
McPherson J.
Zhao S.
Fraser C.M.
Shetty J.
Shatsman S.
Geer K.
Chen Y.
Abramzon S.
Nierman W.C.
Havlak P.H.
Chen R.
Durbin K.J.
Egan A.
Ren Y.
Song X.-Z.
Li B.
Liu Y.
Qin X.
Cawley S.
Cooney A.J.
D'Souza L.M.
Martin K.
Wu J.Q.
Gonzalez-Garay M.L.
Jackson A.R.
Kalafus K.J.
McLeod M.P.
Milosavljevic A.
Virk D.
Volkov A.
Wheeler D.A.
Zhang Z.
Bailey J.A.
Eichler E.E.
Tuzun E.
Birney E.
Mongin E.
Ureta-Vidal A.
Woodwark C.
Zdobnov E.
Bork P.
Suyama M.
Torrents D.
Alexandersson M.
Trask B.J.
Young J.M.
Huang H.
Wang H.
Xing H.
Daniels S.
Gietzen D.
Schmidt J.
Stevens K.
Vitt U.
Wingrove J.
Camara F.
Mar Alba M.
Abril J.F.
Guigo R.
Smit A.
Dubchak I.
Rubin E.M.
Couronne O.
Poliakov A.
Huebner N.
Ganten D.
Goesele C.
Hummel O.
Kreitler T.
Lee Y.-A.
Monti J.
Schulz H.
Zimdahl H.
Himmelbauer H.
Lehrach H.
Jacob H.J.
Bromberg S.
Gullings-Handley J.
Jensen-Seaman M.I.
Kwitek A.E.
Lazar J.
Pasko D.
Tonellato P.J.
Twigger S.
Ponting C.P.
Duarte J.M.
Rice S.
Goodstadt L.
Beatson S.A.
Emes R.D.
Winter E.E.
Webber C.
Brandt P.
Nyakatura G.
Adetobi M.
Chiaromonte F.
Elnitski L.
Eswara P.
Hardison R.C.
Hou M.
Kolbe D.
Makova K.
Miller W.
Nekrutenko A.
Riemer C.
Schwartz S.
Taylor J.
Yang S.
Zhang Y.
Lindpaintner K.
Andrews T.D.
Caccamo M.
Clamp M.
Clarke L.
Curwen V.
Durbin R.M.
Eyras E.
Searle S.M.
Cooper G.M.
Batzoglou S.
Brudno M.
Sidow A.
Stone E.A.
Payseur B.A.
Bourque G.
Lopez-Otin C.
Puente X.S.
Chakrabarti K.
Chatterji S.
Dewey C.
Pachter L.
Bray N.
Yap V.B.
Caspi A.
Tesler G.
Pevzner P.A.
Haussler D.
Roskin K.M.
Baertsch R.
Clawson H.
Furey T.S.
Hinrichs A.S.
Karolchik D.
Kent W.J.
Rosenbloom K.R.
Trumbower H.
Weirauch M.
Cooper D.N.
Stenson P.D.
Ma B.
Brent M.
Arumugam M.
Shteynberg D.
Copley R.R.
Taylor M.S.
Riethman H.
Mudunuri U.
Peterson J.
Guyer M.
Felsenfeld A.
Old S.
Mockrin S.
Collins F.S.
doi:10.1038/nature02426
2004
Nature
428
493-521
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
Brown Norway
Molecular cloning of the mature NAD(+)-dependent succinic semialdehyde dehydrogenase from rat and human. cDNA isolation, evolutionary homology, and tissue expression.
Chambliss K.L.
Caudle D.L.
Hinson D.D.
Moomaw C.R.
Slaughter C.A.
Jakobs C.
Gibson K.M.
doi:10.1074/jbc.270.1.461
1995
J. Biol. Chem.
270
461-467
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT)
PROTEIN SEQUENCE OF 36-84; 92-101; 129-153; 162-172; 303-311; 419-425 AND 503-526
CATALYTIC ACTIVITY
TISSUE SPECIFICITY
Sprague-Dawley
Brain
Lubec G.
Afjehi-Sadat L.
2006-11
UniProtKB
PROTEIN SEQUENCE OF 36-48; 161-172 AND 401-418
IDENTIFICATION BY MASS SPECTROMETRY
Spinal cord
rat
Aldh5a1
Eukaryota
5301
Degradation of GABA
ALDH_F5_SSADH_GabD
Ald_DH/histidinol_DH
Ald_DH_C
Ald_DH_CS_CYS
Ald_DH_CS_GLU
Ald_DH_N
Aldehyde_DH_dom
Succ_semiAld_DH
SSADH
SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL
SUCCINATE-SEMIALDEHYDE DEHYDROGENASE, MITOCHONDRIAL
Aldedh
ALDH-like
ALDEHYDE_DEHYDR_CYS
ALDEHYDE_DEHYDR_GLU
Succinate-semialdehyde dehydrogenase, mitochondrial
SSADH
1.2.1.24
Aldehyde dehydrogenase family 5 member A1
NAD(+)-dependent succinic semialdehyde dehydrogenase
Aldh5a1
Ssadh
Catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA).
Redox-regulated. Inhibited under oxydizing conditions (By similarity).
Homotetramer.
Brain, pancreas, heart, liver, skeletal muscle, kidney. Lower in spleen, lung, kidney and testis.
Belongs to the aldehyde dehydrogenase family.
Mitochondrion
1
35
Succinate-semialdehyde dehydrogenase, mitochondrial
52189
36
523
Proton acceptor
294
Nucleophile
328
201
216
219
272
277
322
486
Transition state stabilizer
193
N6-acetyllysine; alternate
114
N6-succinyllysine; alternate
N6-succinyllysine
123
N6-succinyllysine
172
N6-acetyllysine; alternate
253
N6-succinyllysine; alternate
N6-acetyllysine
353
N6-succinyllysine
390
N6-acetyllysine
399
Phosphoserine
487
In inhibited form
330
In isoform Short.
107
134
substrate
2008-04-08
2
true
56131
a3ea0bc821cbd87bf73e90c64ee314f0
Long
MATCFLLRNFCAARPALRPPGRLLREPAGAQRRSYVGGPADLHADLLRGDSFVGGRWLPTPATFPVYDPASGAKLGTVADCGVPEARAAVRAAYDAFSSWKEISVKERSSLLRKWYDLMIQNKDELAKIITAESGKPLKEAQGEILYSAFFLEWFSEEARRVYGDIIYTSAKDKRGLVLKQPVGVASIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPYSALALAQLANQAGIPPGVYNVIPCSRTKAKEVGEVLCTDPLVSKISFTGSTATGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNAGQTCVCSNRFLVQRGIHDSFVTKFAEAMKKSLRVGNGFEEGTTQGPLINEKAVEKVEKHVNDAVAKGATVVTGGKRHQSGGNFFEPTLLSNVTRDMLCITEETFGPVAPVIKFDKEEEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLEVKYVCYGGL
Short
MATCFLLRNFCAARPALRPPGRLLREPAGAQRRSYVGGPADLHADLLRGDSFVGGRWLPTPATFPVYDPASGAKLGTVADCGVPEARAAVRAAYDAFSSWKEISVKGKPLKEAQGEILYSAFFLEWFSEEARRVYGDIIYTSAKDKRGLVLKQPVGVASIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPYSALALAQLANQAGIPPGVYNVIPCSRTKAKEVGEVLCTDPLVSKISFTGSTATGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNAGQTCVCSNRFLVQRGIHDSFVTKFAEAMKKSLRVGNGFEEGTTQGPLINEKAVEKVEKHVNDAVAKGATVVTGGKRHQSGGNFFEPTLLSNVTRDMLCITEETFGPVAPVIKFDKEEEAVAIANAADVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLEVKYVCYGGL
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true