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Protein

Aspartate-semialdehyde dehydrogenase

Gene

asd

Organism
Yersinia pestis
Status
Unreviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.UniRule annotation

Catalytic activityi

L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH.UniRule annotation

Pathwayi: L-lysine biosynthesis via DAP pathway

This protein is involved in step 2 of the subpathway that synthesizes (S)-tetrahydrodipicolinate from L-aspartate.UniRule annotation
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Aspartokinase (AU253_09460), Aspartokinase (lysC)
  2. Aspartate-semialdehyde dehydrogenase (AU253_11705), Aspartate-semialdehyde dehydrogenase (asd), Aspartate-semialdehyde dehydrogenase (AVO31_11570)
  3. 4-hydroxy-tetrahydrodipicolinate synthase (dapA), 4-hydroxy-tetrahydrodipicolinate synthase (dapA)
  4. 4-hydroxy-tetrahydrodipicolinate reductase (dapB), 4-hydroxy-tetrahydrodipicolinate reductase (dapB)
This subpathway is part of the pathway L-lysine biosynthesis via DAP pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-tetrahydrodipicolinate from L-aspartate, the pathway L-lysine biosynthesis via DAP pathway and in Amino-acid biosynthesis.

Pathwayi: L-methionine biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes L-homoserine from L-aspartate.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Aspartokinase (AU253_09460), Aspartokinase (lysC)
  2. Aspartate-semialdehyde dehydrogenase (AU253_11705), Aspartate-semialdehyde dehydrogenase (asd), Aspartate-semialdehyde dehydrogenase (AVO31_11570)
  3. no protein annotated in this organism
This subpathway is part of the pathway L-methionine biosynthesis via de novo pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-homoserine from L-aspartate, the pathway L-methionine biosynthesis via de novo pathway and in Amino-acid biosynthesis.

Pathwayi: L-threonine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-threonine from L-aspartate.UniRule annotation
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Aspartokinase (AU253_09460), Aspartokinase (lysC)
  2. Aspartate-semialdehyde dehydrogenase (AU253_11705), Aspartate-semialdehyde dehydrogenase (asd), Aspartate-semialdehyde dehydrogenase (AVO31_11570)
  3. no protein annotated in this organism
  4. Homoserine kinase (thrB), Homoserine kinase (thrB)
  5. no protein annotated in this organism
This subpathway is part of the pathway L-threonine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-threonine from L-aspartate, the pathway L-threonine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei73NADPUniRule annotation1
Binding sitei102PhosphateUniRule annotation1
Active sitei135Acyl-thioester intermediateUniRule annotation1
Binding sitei162SubstrateUniRule annotation1
Binding sitei193NADP; via carbonyl oxygenUniRule annotation1
Binding sitei241SubstrateUniRule annotation1
Binding sitei244PhosphateUniRule annotation1
Binding sitei267SubstrateUniRule annotation1
Active sitei274Proton acceptorUniRule annotation1
Binding sitei350NADPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 13NADPUniRule annotation4
Nucleotide bindingi37 – 38NADPUniRule annotation2
Nucleotide bindingi165 – 166NADPUniRule annotation2

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotation

Keywords - Biological processi

Amino-acid biosynthesis, Diaminopimelate biosynthesisUniRule annotation, Lysine biosynthesisUniRule annotation, Methionine biosynthesisUniRule annotation, Threonine biosynthesisUniRule annotation

Keywords - Ligandi

NADPUniRule annotation

Enzyme and pathway databases

UniPathwayiUPA00034; UER00016.
UPA00050; UER00463.
UPA00051; UER00464.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate-semialdehyde dehydrogenaseUniRule annotation (EC:1.2.1.11UniRule annotation)
Short name:
ASA dehydrogenaseUniRule annotation
Short name:
ASADHUniRule annotation
Alternative name(s):
Aspartate-beta-semialdehyde dehydrogenaseUniRule annotation
Gene namesi
Name:asdUniRule annotationImported
Synonyms:asd2Imported
Ordered Locus Names:y3880Imported, YP_3311Imported, YPO3949Imported
OrganismiYersinia pestisImported
Taxonomic identifieri632 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesYersiniaceaeYersinia
Proteomesi
  • UP000000815 Componenti: Chromosome
  • UP000001019 Componenti: Chromosome
  • UP000002490 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Proteomic databases

PRIDEiQ9ETB0.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi187410.y3880.

Structurei

3D structure databases

ProteinModelPortaliQ9ETB0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 122Semialdhyde_dhInterPro annotationAdd BLAST120

Sequence similaritiesi

Belongs to the aspartate-semialdehyde dehydrogenase family.UniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiENOG4105CM3. Bacteria.
COG0136. LUCA.
HOGENOMiHOG000161376.
KOiK00133.
OMAiSCQGGDY.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_02121. ASADH. 1 hit.
InterProiIPR000319. 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]
PfamiPF01118. Semialdhyde_dh. 1 hit.
PF02774. Semialdhyde_dhC. 1 hit.
[Graphical view]
PIRSFiPIRSF000148. ASA_dh. 1 hit.
SMARTiSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01745. asd_gamma. 1 hit.
PROSITEiPS01103. ASD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ETB0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNVGFIGWR GMVGSVLMQR MIEERDFDGI RPVFFSTSQH GQAAPAFAGH
60 70 80 90 100
QGTLQDAYDI DALSALDIII TCQGGDYTNQ IYPKLREIGW QGYWIDAASS
110 120 130 140 150
LRMQDDTIII LDPVNHDVIK QGLDKGIKTF AGGNCTVSLM LMSLGGLFAN
160 170 180 190 200
NLVEWASVAT YQAASGGGAR HMRELLTQMG MLHAGVAKEL QDPASAILDI
210 220 230 240 250
ERKVTSTTRS GTLPTDNFGV PLAGSLIPWI DKALDNGQSR EEWKGQAETN
260 270 280 290 300
KILSTSTLIP VDGLCVRVGA LRCHSQAFTL KLKKDVPLAE IEQMLATHND
310 320 330 340 350
WVRVIPNDRE LSMRELTPAA VTGTLNTPVG RLRKLNMGPE YLSAFTVGDQ
360
LLWGAAEPLR RMLRILL
Length:367
Mass (Da):40,191
Last modified:March 1, 2001 - v1
Checksum:iEFFEE5C4625B6DE4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF282318 Genomic DNA. Translation: AAG22007.1.
AE009952 Genomic DNA. Translation: AAM87425.1.
AE017042 Genomic DNA. Translation: AAS63476.1.
AL590842 Genomic DNA. Translation: CAL22530.1.
PIRiAG0480.
RefSeqiWP_002209507.1. NZ_LQBA01000064.1.
YP_002348820.1. NC_003143.1.

Genome annotation databases

EnsemblBacteriaiAAM87425; AAM87425; y3880.
AAS63476; AAS63476; YP_3311.
GeneIDi1176788.
KEGGiype:YPO3949.
ypj:CH55_2628.
ypk:y3880.
ypl:CH46_1108.
ypm:YP_3311.
ypv:BZ15_3756.
ypw:CH59_1896.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF282318 Genomic DNA. Translation: AAG22007.1.
AE009952 Genomic DNA. Translation: AAM87425.1.
AE017042 Genomic DNA. Translation: AAS63476.1.
AL590842 Genomic DNA. Translation: CAL22530.1.
PIRiAG0480.
RefSeqiWP_002209507.1. NZ_LQBA01000064.1.
YP_002348820.1. NC_003143.1.

3D structure databases

ProteinModelPortaliQ9ETB0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi187410.y3880.

Proteomic databases

PRIDEiQ9ETB0.

Protocols and materials databases

DNASUi1148827.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM87425; AAM87425; y3880.
AAS63476; AAS63476; YP_3311.
GeneIDi1176788.
KEGGiype:YPO3949.
ypj:CH55_2628.
ypk:y3880.
ypl:CH46_1108.
ypm:YP_3311.
ypv:BZ15_3756.
ypw:CH59_1896.

Phylogenomic databases

eggNOGiENOG4105CM3. Bacteria.
COG0136. LUCA.
HOGENOMiHOG000161376.
KOiK00133.
OMAiSCQGGDY.

Enzyme and pathway databases

UniPathwayiUPA00034; UER00016.
UPA00050; UER00463.
UPA00051; UER00464.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_02121. ASADH. 1 hit.
InterProiIPR000319. 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]
PfamiPF01118. Semialdhyde_dh. 1 hit.
PF02774. Semialdhyde_dhC. 1 hit.
[Graphical view]
PIRSFiPIRSF000148. ASA_dh. 1 hit.
SMARTiSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01745. asd_gamma. 1 hit.
PROSITEiPS01103. ASD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiQ9ETB0_YERPE
AccessioniPrimary (citable) accession number: Q9ETB0
Secondary accession number(s): Q74QZ1, Q7CFY8
Entry historyi
Integrated into UniProtKB/TrEMBL: March 1, 2001
Last sequence update: March 1, 2001
Last modified: November 2, 2016
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.