P51649 (SSDH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Succinate-semialdehyde dehydrogenase, mitochondrial
EC=1.2.1.24

Alternative name(s):
Aldehyde dehydrogenase family 5 member A1
NAD(+)-dependent succinic semialdehyde dehydrogenase

Gene names

Name:	ALDH5A1
Synonyms:	SSADH

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	535 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)

Function	Catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA). Ref.9
Catalytic activity	Succinate semialdehyde + NAD+ + H2O = succinate + NADH.
Enzyme regulation	Redox-regulated. Inhibited under oxydizing conditions. Inhibited by hydrogen peroxide H2O2. Ref.9
Pathway	Amino-acid degradation; 4-aminobutanoate degradation.
Subunit structure	Homotetramer. Ref.6
Subcellular location	Mitochondrion.
Tissue specificity	Brain, pancreas, heart, liver, skeletal muscle and kidney. Lower in placenta.
Involvement in disease	Defects in ALDH5A1 are the cause of succinate semialdehyde dehydrogenase deficiency (SSADH deficiency) [MIM:271980]. SSADH deficiency is a rare inborn error in the metabolism of 4-aminobutyric acid (GABA) which leads to accumulation of 4-hydroxybutyric acid in physiologic fluids of patients. The disease is characterized by severe ataxia and by mildly retarded psychomotor development.
Sequence similarities	Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Transit peptide
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Acetylation Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	acetate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB central nervous system development Inferred from mutant phenotype Ref.1. Source: UniProtKB galactosylceramide metabolic process Inferred from sequence or structural similarity. Source: UniProtKB gamma-aminobutyric acid catabolic process Inferred from direct assay Ref.1. Source: UniProtKB glucose metabolic process Inferred from sequence or structural similarity. Source: UniProtKB glutamate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB glutamine metabolic process Inferred from sequence or structural similarity. Source: UniProtKB glutathione metabolic process Inferred from sequence or structural similarity. Source: UniProtKB glycerophospholipid metabolic process Inferred from sequence or structural similarity. Source: UniProtKB neurotransmitter catabolic process Inferred from sequence or structural similarity. Source: UniProtKB neurotransmitter secretion Traceable author statement. Source: Reactome protein homotetramerization Inferred from direct assay. Source: UniProtKB respiratory electron transport chain Inferred from sequence or structural similarity. Source: UniProtKB short-chain fatty acid metabolic process Inferred from sequence or structural similarity. Source: UniProtKB succinate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	mitochondrial matrix Traceable author statement. Source: Reactome soluble fraction Inferred from direct assay. Source: UniProtKB
Molecular function	protein homodimerization activity Inferred by curator. Source: UniProtKB succinate-semialdehyde dehydrogenase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 47

47

Mitochondrion Potential

Chain

48 – 535

488

Succinate-semialdehyde dehydrogenase, mitochondrial

PRO_0000007184

Regions

Nucleotide binding

228 – 231

4

NAD

Nucleotide binding

284 – 289

6

NAD

Sites

Active site

306

1

Proton acceptor By similarity

Active site

340

1

Nucleophile By similarity

Binding site

213

1

NAD

Binding site

213

1

Substrate

Binding site

334

1

Substrate

Binding site

498

1

Substrate

Site

205

1

Transition state stabilizer By similarity

Amino acid modifications

Modified residue

126

1

N6-acetyllysine Ref.7

Modified residue

358

1

N6-acetyllysine Ref.7

Disulfide bond

340 ↔ 342

In inhibited form Ref.9

Natural variations

Natural variant

36

1

G → R. [dbSNP:rs4646832] Ref.12

VAR_026227

Natural variant

93

1

C → F in SSADH deficiency; 3% of activity. Ref.12

VAR_026199

Natural variant

176

1

G → R in SSADH deficiency; <1% of activity. Ref.12

VAR_026200

Natural variant

180

1

H → Y 83% of activity. [dbSNP:rs2760118] Ref.2 Ref.12

VAR_016758

Natural variant

182

1

P → L 48% of activity. [dbSNP:rs3765310] Ref.12

VAR_016759

Natural variant

223

1

C → Y in SSADH deficiency; 5% of activity. Ref.12

VAR_026201

Natural variant

233

1

T → M in SSADH deficiency; 4% of activity. Ref.12

VAR_026202

Natural variant

237

1

A → S 65% of activity. Ref.12

VAR_026228

Natural variant

255

1

N → S in SSADH deficiency; 17% of activity. Ref.12

VAR_026203

Natural variant

268

1

G → E in SSADH deficiency; <1% of activity. Ref.10 Ref.12

VAR_026204

Natural variant

335

1

N → K in SSADH deficiency; 1% of activity. Ref.12

VAR_026205

Natural variant

382

1

P → L in SSADH deficiency; 2% of activity. Ref.12

VAR_026206

Natural variant

382

1

P → Q in SSADH deficiency. Ref.12

VAR_026207

Natural variant

406

1

V → I Ref.12

VAR_026229

Natural variant

409

1

G → D in SSADH deficiency; <1% of activity. Ref.10 Ref.12

VAR_026208

Natural variant

487

1

V → E in SSADH deficiency. Ref.11

VAR_026209

Natural variant

533

1

G → R in SSADH deficiency; <1% of activity. Ref.12

VAR_026210

Experimental info

Mutagenesis

213

1

R → A: Reduces catalytic activity to less than 15% of wild-type. Ref.9

Mutagenesis

334

1

R → A: Reduces catalytic activity to less than 15% of wild-type. Ref.9

Mutagenesis

342

1

C → A: Loss of regulation by redox state. Ref.9

Mutagenesis

498

1

S → A: Reduces catalytic activity to less than 15% of wild-type. Ref.9

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

535

Helix Strand Turn

Details...

Beta strand

62 – 64

3

Helix

96 – 112

17

Helix

117 – 133

17

Helix

135 – 145

11

Helix

150 – 153

4

Helix

157 – 170

14

Helix

171 – 173

3

Beta strand

187 – 194

8

Beta strand

198 – 201

4

Beta strand

204 – 206

3

Helix

209 – 212

4

Turn

218 – 220

3

Beta strand

225 – 228

4

Helix

235 – 246

12

Beta strand

254 – 256

3

Helix

261 – 264

4

Turn

271 – 273

3

Beta strand

279 – 282

4

Helix

291 – 297

7

Turn

298 – 300

3

Beta strand

302 – 305

4

Beta strand

311 – 315

5

Helix

321 – 325

5

Helix

329 – 332

4

Beta strand

344 – 349

6

Helix

353 – 367

15

Helix

386 – 400

15

Beta strand

405 – 408

4

Beta strand

420 – 428

9

Helix

430 – 433

4

Beta strand

443 – 450

8

Helix

452 – 459

8

Helix

475 – 484

10

Helix

522 – 524

3

Beta strand

525 – 532

8

Sequences

	Sequence		Length	Mass (Da)
	P51649 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: C63A9431D3FA16C7	FASTA	535	57,215
	10 20 30 40 50 60 MATCIWLRSC GARRLGSTFP GCRLRPRAGG LVPASGPAPG PAQLRCYAGR LAGLSAALLR 70 80 90 100 110 120 TDSFVGGRWL PAAATFPVQD PASGAALGMV ADCGVREARA AVRAAYEAFC RWREVSAKER 130 140 150 160 170 180 SSLLRKWYNL MIQNKDDLAR IITAESGKPL KEAHGEILYS AFFLEWFSEE ARRVYGDIIH 190 200 210 220 230 240 TPAKDRRALV LKQPIGVAAV ITPWNFPSAM ITRKVGAALA AGCTVVVKPA EDTPFSALAL 250 260 270 280 290 300 AELASQAGIP SGVYNVIPCS RKNAKEVGEA ICTDPLVSKI SFTGSTTTGK ILLHHAANSV 310 320 330 340 350 360 KRVSMELGGL APFIVFDSAN VDQAVAGAMA SKFRNTGQTC VCSNQFLVQR GIHDAFVKAF 370 380 390 400 410 420 AEAMKKNLRV GNGFEEGTTQ GPLINEKAVE KVEKQVNDAV SKGATVVTGG KRHQLGKNFF 430 440 450 460 470 480 EPTLLCNVTQ DMLCTHEETF GPLAPVIKFD TEEEAIAIAN AADVGLAGYF YSQDPAQIWR 490 500 510 520 530 VAEQLEVGMV GVNEGLISSV ECPFGGVKQS GLGREGSKYG IDEYLELKYV CYGGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Two exon-skipping mutations as the molecular basis of succinic semialdehyde dehydrogenase deficiency (4-hydroxybutyric aciduria)." Chambliss K.L., Hinson D.D., Trettel F., Malaspina P., Novelletto A., Jakobs C., Gibson K.M. Am. J. Hum. Genet. 63:399-408(1998) [PubMed: 9683595] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lymphocyte.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT TYR-180. Tissue: Brain.
[3]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[5]	"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. J. Biol. Chem. 270:461-467(1995) [PubMed: 7814412] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 213-535. Tissue: Liver.
[6]	"Human succinic semialdehyde dehydrogenase. Molecular cloning and chromosomal localization." Trettel F., Malaspina P., Jodice C., Novelletto A., Slaughter C.A., Caudle D.L., Hinson D.D., Chambliss K.L., Gibson K.M. Adv. Exp. Med. Biol. 414:253-260(1997) [PubMed: 9059628] [Abstract] Cited for: SUBUNIT. Tissue: Brain.
[7]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-126 AND LYS-358, MASS SPECTROMETRY.
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]	"Redox-switch modulation of human SSADH by dynamic catalytic loop." Kim Y.-G., Lee S., Kwon O.-S., Park S.-Y., Lee S.-J., Park B.-J., Kim K.-J. EMBO J. 28:959-968(2009) [PubMed: 19300440] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 49-535 IN COMPLEX WITH PRODUCT AND ADP, FUNCTION, ENZYME REGULATION, DISULFIDE BOND, MUTAGENESIS OF ARG-213; ARG-334; CYS-342 AND SER-498.
[10]	"Prenatal diagnosis of succinic semialdehyde dehydrogenase deficiency: increased accuracy employing DNA, enzyme, and metabolite analyses." Hogema B.M., Akaboshi S., Taylor M., Salomons G.S., Jakobs C., Schutgens R.B., Wilcken B., Worthington S., Maropoulos G., Grompe M., Gibson K.M. Mol. Genet. Metab. 72:218-222(2001) [PubMed: 11243727] [Abstract] Cited for: VARIANTS SSADH DEFICIENCY GLU-268 AND ASP-409.
[11]	"Mutation analysis in a patient with succinic semialdehyde dehydrogenase deficiency: a compound heterozygote with 103-121del and 1460T>A of the ALDH5A1 gene." Aoshima T., Kajita M., Sekido Y., Ishiguro Y., Tsuge I., Kimura M., Yamaguchi S., Watanabe K., Shimokata K., Niwa T. Hum. Hered. 53:42-44(2002) [PubMed: 11901270] [Abstract] Cited for: VARIANT SSADH DEFICIENCY GLU-487.
[12]	"Mutational spectrum of the succinate semialdehyde dehydrogenase (ALDH5A1) gene and functional analysis of 27 novel disease-causing mutations in patients with SSADH deficiency." Akaboshi S., Hogema B.M., Novelletto A., Malaspina P., Salomons G.S., Maropoulos G.D., Jakobs C., Grompe M., Gibson K.M. Hum. Mutat. 22:442-450(2003) [PubMed: 14635103] [Abstract] Cited for: VARIANTS SSADH DEFICIENCY PHE-93; ARG-176; TYR-223; MET-233; SER-255; GLU-268; LYS-335; GLN-382; LEU-382; ASP-409 AND ARG-533, VARIANTS ARG-36; TYR-180; LEU-182; SER-237 AND ILE-406, CHARACTERIZATION OF VARIANTS ARG-36; PHE-93; ARG-176; TYR-180; LEU-182; TYR-223; MET-233; SER-237; SER-255; GLU-268; LYS-335; LEU-382; ASP-409 AND ARG-533.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y11192 mRNA. Translation: CAA72076.1.
AK315380 mRNA. Translation: BAG37773.1.
AL031230 Genomic DNA. Translation: CAA20248.1.
BC034321 mRNA. Translation: AAH34321.1.
L34820 mRNA. Translation: AAA67057.1.

IPI

IPI00019888.

PIR

A55773.

RefSeq

NP_001071.1. NM_001080.3.
NP_733936.1. NM_170740.1.

UniGene

Hs.371723.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2W8N	X-ray	2.00	A	49-535	[»]
2W8O	X-ray	3.40	A	49-535	[»]
2W8P	X-ray	2.30	A	49-535	[»]
2W8Q	X-ray	2.40	A	49-535	[»]
2W8R	X-ray	2.40	A	49-535	[»]

ProteinModelPortal

P51649.

SMR

P51649. Positions 56-535.

ModBase

Search...

Protein-protein interaction databases

IntAct

P51649. 1 interaction.

STRING

P51649.

PTM databases

PhosphoSite

P51649.

Polymorphism databases

DMDM

7531278.

Proteomic databases

PRIDE

P51649.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000357578; ENSP00000350191; ENSG00000112294.

GeneID

7915.

KEGG

hsa:7915.

UCSC

uc003neg.1. human.

Organism-specific databases

CTD

7915.

GeneCards

GC06P024444.

H-InvDB

HIX0005623.

HGNC

HGNC:408. ALDH5A1.

HPA

HPA029715.
HPA029716.

MIM

271980. phenotype.
610045. gene.

neXtProt

NX_P51649.

Orphanet

22. 4-hydroxybutyricaciduria.

PharmGKB

PA24702.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG06436.

HOVERGEN

HBG108515.

PhylomeDB

P51649.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-11540.

BRENDA

1.2.1.24. 2681.

Reactome

REACT_13685. Neuronal System.

Gene expression databases

ArrayExpress

P51649.

Bgee

P51649.

CleanEx

HS_ALDH5A1.

Genevestigator

P51649.

GermOnline

ENSG00000112294. Homo sapiens.

Family and domain databases

InterPro

IPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR010102. Succ_semiAld_DH.
[Graphical view]

Gene3D

G3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit.
G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.

KO

K00139.

Pfam

PF00171. Aldedh. 1 hit.
[Graphical view]

SUPFAM

SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.

TIGRFAMs

TIGR01780. SSADH. 1 hit.

PROSITE

PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00534. Chlormerodrin.
DB00157. NADH.
DB00139. Succinic acid.

NextBio

30381.

SOURCE

Search...

Entry information

Entry name

SSDH_HUMAN

Accession

Primary (citable) accession number: P51649
Secondary accession number(s): B2RD26

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	May 30, 2000
Last modified:	December 14, 2011
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.