Reviewed, UniProtKB/Swiss-Prot Q8BWF0 (SSDH_MOUSE)

Names and origin

Protein names

Recommended name:
    Succinate-semialdehyde dehydrogenase, mitochondrial
    EC=1.2.1.24
Alternative name(s):
    NAD(+)-dependent succinic semialdehyde dehydrogenase
    Aldehyde dehydrogenase family 5 member A1

Gene names

Name:

Aldh5a1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	523 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Succinate semialdehyde + NAD+ + H2O = succinate + NADH.
Pathway	Amino-acid degradation; 4-aminobutanoate degradation.
Subunit structure	Homotetramer By similarity.
Subcellular location	Mitochondrion By similarity.
Sequence similarities	Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	acetate metabolic process Inferred from mutant phenotype. Source: MGI central nervous system development Inferred from sequence or structural similarity. Source: UniProtKB galactosylceramide metabolic process Inferred from mutant phenotype. Source: MGI gamma-aminobutyric acid catabolic process Inferred from sequence or structural similarity. Source: UniProtKB glucose metabolic process Inferred from mutant phenotype. Source: MGI glucosylceramide metabolic process Inferred from mutant phenotype. Source: MGI glutamate metabolic process Inferred from mutant phenotype. Source: MGI glutamine metabolic process Inferred from mutant phenotype. Source: MGI glutathione metabolic process Inferred from mutant phenotype. Source: MGI glycerophospholipid metabolic process Inferred from mutant phenotype. Source: MGI neurotransmitter catabolic process Inferred from mutant phenotype. Source: MGI post-embryonic development Inferred from mutant phenotype. Source: MGI respiratory electron transport chain Inferred from mutant phenotype. Source: MGI succinate metabolic process Inferred from mutant phenotype. Source: MGI
Cellular component	mitochondrion Inferred from direct assay. Source: UniProtKB
Molecular function	succinate-semialdehyde dehydrogenase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 35	35	Mitochondrion By similarity
	Chain	36 – 523	488	Succinate-semialdehyde dehydrogenase, mitochondrial		PRO_0000007185
Regions
	Nucleotide binding	272 – 277	6	NADP By similarity
Sites
	Active site	294	1	Proton acceptor By similarity
	Active site	328	1	Nucleophile By similarity
	Site	193	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	67	1	Phosphotyrosine Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q8BWF0-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: E0CF82E4F4FAE9D0	FASTA	523	55,968
	10 20 30 40 50 60 MATCFLLRSF WAARPALPPP GRFRPEPAGT PRRSYASGPG GLHADLLRGD SFVGGRWLPA 70 80 90 100 110 120 PATFPVYDPA SGAKLGTVAD CGVPEARAAV RAAYDAFNSW KGVSVKERSL LLRKWYDLMI 130 140 150 160 170 180 QNKDDLAKII TAESGKPLKE AQGEILYSAL FLEWFSEEAR RIYGDIIYTS AKDKRGLVLK 190 200 210 220 230 240 QPVGVAAIIT PWNFPSAMIT RKVGAALAAG CTVVVKPAED TPYSALALAQ LANQAGIPAG 250 260 270 280 290 300 VYNVIPCSRN KAKEVGEVLC TDPLVSKISF TGSTATGKIL LHHAANSVKR VSMELGGLAP 310 320 330 340 350 360 FIVFDSANVD QAVAGAMASK FRNAGQTCVC SNRFLVQRGI HDSFVTKFAE AMKKSLRVGN 370 380 390 400 410 420 GFEEGTTQGP LINEKAVEKV EKQVNDAVAK GATVVTGGKR HQSGGNFFEP TLLSNVTRDM 430 440 450 460 470 480 LCITEETFGP LAPVIKFDKE EEAVAIANAA EVGLAGYFYS QDPAQIWRVA EQLEVGMVGV 490 500 510 520 NEGLISSVEC PFGGVKQSGL GREGSKYGID EYLEVKYVCY GGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Kidney.
[2]	The mouse genome sequencing consortium Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 57-87; 115-123; 129-160; 162-172; 181-201; 254-289; 291-320; 323-333; 339-347; 358-375; 401-436; 469-496 AND 507-516, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[4]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-67, MASS SPECTROMETRY. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK052703 mRNA. Translation: BAC35105.1. AK144030 mRNA. Translation: BAE25663.1. AL589699 Genomic DNA. Translation: CAI26086.1.
IPI	IPI00273164.
RefSeq	NP_766120.1.
UniGene	Mm.393311 Mm.440292
3D structure databases
HSSP	HSSP built from PDB template 1BXS based on UniProtKB P51977.
ModBase	Search...
PTM databases
PhosphoSite	Q8BWF0.
Proteomic databases
PRIDE	Q8BWF0.
Genome annotation databases
Ensembl	ENSMUSG00000035936. Mus musculus. [Contig view]
GeneID	214579.
KEGG	mmu:214579.
NMPDR	fig|10090.3.peg.27594.
Organism-specific databases
MGI	MGI:2441982. Aldh5a1.
Phylogenomic databases
HOGENOM	Q8BWF0.
HOVERGEN	Q8BWF0.
OMA	Q8BWF0. IYTSAKD.
Enzyme and pathway databases
BRENDA	1.2.1.24. 244.
Gene expression databases
ArrayExpress	Q8BWF0.
Bgee	Q8BWF0.
CleanEx	MM_ALDH5A1.
GermOnline	ENSMUSG00000035936. Mus musculus.
Family and domain databases
InterPro	IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH. IPR010102. Succ_semiAld_DH. [Graphical view]
Gene3D	G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHER	PTHR11699. Aldehyde_dehyd. 1 hit.
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
TIGRFAMs	TIGR01780. SSADH. 1 hit.
PROSITE	PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	374368.
SOURCE	Search...

Entry information

Entry name

SSDH_MOUSE

Accession

Primary (citable) accession number: Q8BWF0
Secondary accession number(s): Q5SZW1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	March 1, 2003
Last modified:	June 16, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)