Aspartate-semialdehyde dehydrogenase

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Q9ETB0 (Q9ETB0_YERPE) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 100. History...

Clusters with 100%, 90%, 50% identity |

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Recommended name:
Aspartate-semialdehyde dehydrogenase HAMAP-Rule MF_02121
Short name=ASA dehydrogenase HAMAP-Rule MF_02121
Short name=ASADH HAMAP-Rule MF_02121
EC=1.2.1.11 HAMAP-Rule MF_02121

Alternative name(s):
Aspartate-beta-semialdehyde dehydrogenase HAMAP-Rule MF_02121

Gene names

Name:	asd HAMAP-Rule MF_02121 EMBL AAG22007.1
Synonyms:	asd2 EMBL AAS63476.1
Ordered Locus Names:	y3880 EMBL AAM87425.1, YP_3311 EMBL AAS63476.1, YPO3949 EMBL CAL22530.1

Organism

Yersinia pestis [Reference proteome] [HAMAP] EMBL AAG22007.1

Taxonomic identifier

632 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Yersinia

Protein attributes

Sequence length	367 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate By similarity. HAMAP-Rule MF_02121
Catalytic activity	L-aspartate 4-semialdehyde + phosphate + NADP⁺ = L-4-aspartyl phosphate + NADPH. RuleBase RU004501 HAMAP-Rule MF_02121
Pathway	Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. RuleBase RU004502 HAMAP-Rule MF_02121 Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. RuleBase RU004502 HAMAP-Rule MF_02121 Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. RuleBase RU004502 HAMAP-Rule MF_02121
Subunit structure	Homodimer By similarity. HAMAP-Rule MF_02121
Sequence similarities	Belongs to the aspartate-semialdehyde dehydrogenase family. RuleBase RU004041 HAMAP-Rule MF_02121

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Diaminopimelate biosynthesis HAMAP-Rule MF_02121 Lysine biosynthesis HAMAP-Rule MF_02121 Methionine biosynthesis HAMAP-Rule MF_02121 Threonine biosynthesis HAMAP-Rule MF_02121
Ligand	NADP RuleBase RU004501 HAMAP-Rule MF_02121
Molecular function	Oxidoreductase RuleBase RU004501 HAMAP-Rule MF_02121
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' L-methionine biosynthetic process Inferred from electronic annotation. Source: HAMAP diaminopimelate biosynthetic process Inferred from electronic annotation. Source: HAMAP isoleucine biosynthetic process Inferred from electronic annotation. Source: InterPro lysine biosynthetic process via diaminopimelate Inferred from electronic annotation. Source: HAMAP threonine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular_function	N-acetyl-gamma-glutamyl-phosphate reductase activity Inferred from electronic annotation. Source: InterPro NAD binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from electronic annotation. Source: HAMAP aspartate-semialdehyde dehydrogenase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Nucleotide binding

10 – 13

NADP By similarity HAMAP-Rule MF_02121

Nucleotide binding

37 – 38

NADP By similarity HAMAP-Rule MF_02121

Nucleotide binding

165 – 166

NADP By similarity HAMAP-Rule MF_02121

Sites

Active site

135

Acyl-thioester intermediate By similarity PIRSR PIRSR000148-1 HAMAP-Rule MF_02121

Active site

274

Proton acceptor By similarity PIRSR PIRSR000148-1 HAMAP-Rule MF_02121

Binding site

NADP By similarity HAMAP-Rule MF_02121

Binding site

102

Phosphate By similarity HAMAP-Rule MF_02121

Binding site

162

Substrate By similarity HAMAP-Rule MF_02121

Binding site

193

NADP; via carbonyl oxygen By similarity HAMAP-Rule MF_02121

Binding site

241

Substrate By similarity HAMAP-Rule MF_02121

Binding site

244

Phosphate By similarity HAMAP-Rule MF_02121

Binding site

267

Substrate By similarity HAMAP-Rule MF_02121

Binding site

350

NADP By similarity HAMAP-Rule MF_02121

Sequences

Sequence

Length

Mass (Da)

Tools

Q9ETB0 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: EFFEE5C4625B6DE4
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FASTA

367

40,191

        10         20         30         40         50         60 
MKNVGFIGWR GMVGSVLMQR MIEERDFDGI RPVFFSTSQH GQAAPAFAGH QGTLQDAYDI 

        70         80         90        100        110        120 
DALSALDIII TCQGGDYTNQ IYPKLREIGW QGYWIDAASS LRMQDDTIII LDPVNHDVIK 

       130        140        150        160        170        180 
QGLDKGIKTF AGGNCTVSLM LMSLGGLFAN NLVEWASVAT YQAASGGGAR HMRELLTQMG 

       190        200        210        220        230        240 
MLHAGVAKEL QDPASAILDI ERKVTSTTRS GTLPTDNFGV PLAGSLIPWI DKALDNGQSR 

       250        260        270        280        290        300 
EEWKGQAETN KILSTSTLIP VDGLCVRVGA LRCHSQAFTL KLKKDVPLAE IEQMLATHND 

       310        320        330        340        350        360 
WVRVIPNDRE LSMRELTPAA VTGTLNTPVG RLRKLNMGPE YLSAFTVGDQ LLWGAAEPLR 


RMLRILL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genetic relatedness of Yersinia." Lindler L.E., Popek M., Huang X. Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: KIM EMBL AAG22007.1.
[2]	"Genome sequence of Yersinia pestis, the causative agent of plague." Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., Chillingworth T., Cronin A., Davies R.M. Barrell B.G. Nature 413:523-527(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CO-92 / Biovar Orientalis and CO92 EMBL CAL22530.1.
[3]	"Genome sequence of Yersinia pestis KIM." Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A., Nilles M.L. , Matson J.S., Blattner F.R., Perry R.D. J. Bacteriol. 184:4601-4611(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KIM EMBL AAM87425.1 and KIM10+ / Biovar Mediaevalis.
[4]	"Annotation and evolutionary relationships of a small regulatory RNA gene micF and its target ompF in Yersinia species." Delihas N. BMC Microbiol. 3:13-13(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: CO92 EMBL CAL22530.1.
[5]	"Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans." Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R. Yang R. DNA Res. 11:179-197(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 91001 EMBL AAS63476.1 and 91001 / Biovar Mediaevalis.
[6]	"Genetics of metabolic variations between Yersinia pestis biovars and the proposal of a new biovar, microtus." Zhou D., Tong Z., Song Y., Han Y., Pei D., Pang X., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R., Du Z., Wang J., Guo Z., Wang J., Huang P., Yang R. J. Bacteriol. 186:5147-5152(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: 91001 EMBL AAS63476.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF282318 Genomic DNA. Translation: AAG22007.1. AE009952 Genomic DNA. Translation: AAM87425.1. AE017042 Genomic DNA. Translation: AAS63476.1. AL590842 Genomic DNA. Translation: CAL22530.1.
PIR	AG0480.
RefSeq	NP_671174.1. NC_004088.1. NP_994599.1. NC_005810.1. YP_002348820.1. NC_003143.1.
3D structure databases
HSSP	HSSP built from PDB template 1GL3 based on UniProtKB P00353.
ModBase	Search...
Protein-protein interaction databases
STRING	214092.YPO3949.
Protocols and materials databases
DNASU	1148827.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAM87425; AAM87425; y3880. AAS63476; AAS63476; YP_3311.
GeneID	1148827. 1176788. 2763780.
KEGG	ype:YPO3949. ypk:y3880. ypm:YP_3311.
Phylogenomic databases
HOGENOM	HOG000161376.
KO	K00133.
OMA	SCQGGDY.
ProtClustDB	PRK06598.
Enzyme and pathway databases
UniPathway	UPA00034; UER00016. UPA00050; UER00463. UPA00051; UER00464.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
HAMAP	MF_02121. ASADH.
InterPro	IPR000319. Asp-semialdehyde_DH_CS. IPR011534. Asp_ADH_gamma-type. IPR012080. Asp_semialdehyde_DH. IPR016040. NAD(P)-bd_dom. IPR000534. Semialdehyde_DH_NAD-bd. IPR012280. Semialdhyde_DH_dimer_dom. [Graphical view]
Pfam	PF01118. Semialdhyde_dh. 1 hit. PF02774. Semialdhyde_dhC. 1 hit. [Graphical view]
PIRSF	PIRSF000148. ASA_dh. 1 hit.
SMART	SM00859. Semialdhyde_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR01745. asd_gamma. 1 hit.
PROSITE	PS01103. ASD. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q9ETB0_YERPE

Accession

Primary (citable) accession number: Q9ETB0
Secondary accession number(s): Q74QZ1, Q7CFY8

Entry history

Integrated into UniProtKB/TrEMBL:	March 1, 2001
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information