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Protein

Aspartate-semialdehyde dehydrogenase

Gene

HOM2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Pathwayi: L-lysine biosynthesis via DAP pathway

This protein is involved in step 2 of the subpathway that synthesizes (S)-tetrahydrodipicolinate from L-aspartate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Aspartokinase (HOM3)
  2. Aspartate-semialdehyde dehydrogenase (HOM2)
  3. no protein annotated in this organism
  4. no protein annotated in this organism
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.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Aspartokinase (HOM3)
  2. Aspartate-semialdehyde dehydrogenase (HOM2)
  3. Homoserine dehydrogenase (HOM6)
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.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Aspartokinase (HOM3)
  2. Aspartate-semialdehyde dehydrogenase (HOM2)
  3. Homoserine dehydrogenase (HOM6)
  4. Homoserine kinase (THR1)
  5. Threonine synthase (THR4)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei112 – 1121PhosphateBy similarity
Active sitei156 – 1561Acyl-thioester intermediateBy similarity
Binding sitei184 – 1841SubstrateBy similarity
Binding sitei211 – 2111SubstrateBy similarity
Binding sitei214 – 2141PhosphateBy similarity
Binding sitei249 – 2491SubstrateBy similarity
Active sitei256 – 2561Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 164NADPBy similarity
Nucleotide bindingi40 – 412NADPBy similarity
Nucleotide bindingi187 – 1882NADPBy similarity
Nucleotide bindingi343 – 3442NADPBy similarity

GO - Molecular functioni

GO - Biological processi

  • aspartate metabolic process Source: InterPro
  • homoserine biosynthetic process Source: SGD
  • isoleucine biosynthetic process Source: InterPro
  • lysine biosynthetic process via diaminopimelate Source: UniProtKB-UniPathway
  • methionine biosynthetic process Source: SGD
  • threonine biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Lysine biosynthesis, Methionine biosynthesis, Threonine biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciYEAST:YDR158W-MONOMER.
UniPathwayiUPA00034; UER00016.
UPA00050; UER00463.
UPA00051; UER00464.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate-semialdehyde dehydrogenase (EC:1.2.1.11)
Short name:
ASA dehydrogenase
Short name:
ASADH
Alternative name(s):
Aspartate-beta-semialdehyde dehydrogenase
Gene namesi
Name:HOM2
Ordered Locus Names:YDR158W
ORF Names:YD8358.12
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR158W.
SGDiS000002565. HOM2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 365365Aspartate-semialdehyde dehydrogenasePRO_0000141400Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131PhosphothreonineCombined sources
Modified residuei318 – 3181PhosphoserineCombined sources
Modified residuei323 – 3231PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP13663.
PeptideAtlasiP13663.

2D gel databases

SWISS-2DPAGEP13663.

PTM databases

iPTMnetiP13663.

Expressioni

Inductioni

By high concentrations of Met (general AA biosynthesis control).

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi32209. 135 interactions.
DIPiDIP-5204N.
IntActiP13663. 17 interactions.
MINTiMINT-535737.

Structurei

3D structure databases

ProteinModelPortaliP13663.
SMRiP13663. Positions 5-365.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000013358.
InParanoidiP13663.
KOiK00133.
OMAiASCHRVP.
OrthoDBiEOG7XDBRM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_02121. ASADH.
InterProiIPR000319. Asp-semialdehyde_DH_CS.
IPR005676. Asp_semi-ald_DH_pep-lack.
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.
TIGRFAMsiTIGR00978. asd_EA. 1 hit.
PROSITEiPS01103. ASD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P13663-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGKKIAGVL GATGSVGQRF ILLLANHPHF ELKVLGASSR SAGKKYVDAV
60 70 80 90 100
NWKQTDLLPE SATDIIVSEC KSEFFKECDI VFSGLDADYA GAIEKEFMEA
110 120 130 140 150
GIAIVSNAKN YRREQDVPLI VPVVNPEHLD IVAQKLDTAK AQGKPRPGFI
160 170 180 190 200
ICISNCSTAG LVAPLKPLIE KFGPIDALTT TTLQAISGAG FSPGVPGIDI
210 220 230 240 250
LDNIIPYIGG EEDKMEWETK KILAPLAEDK THVKLLTPEE IKVSAQCNRV
260 270 280 290 300
AVSDGHTECI SLRFKNRPAP SVEQVKTCLK EYVCDAYKLG CHSAPKQTIH
310 320 330 340 350
VLEQPDRPQP RLDRNRDSGY GVSVGRIRED PLLDFKMVVL SHNTIIGAAG
360
SGVLIAEILL ARNLI
Length:365
Mass (Da):39,544
Last modified:January 1, 1990 - v1
Checksum:iD33096DA8C2B6424
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15649 Genomic DNA. Translation: CAA33675.1.
Z50046 Genomic DNA. Translation: CAA90378.1.
AY557698 Genomic DNA. Translation: AAS56024.1.
BK006938 Genomic DNA. Translation: DAA11998.1.
PIRiJQ0198.
RefSeqiNP_010442.3. NM_001180465.3.

Genome annotation databases

EnsemblFungiiYDR158W; YDR158W; YDR158W.
GeneIDi851736.
KEGGisce:YDR158W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15649 Genomic DNA. Translation: CAA33675.1.
Z50046 Genomic DNA. Translation: CAA90378.1.
AY557698 Genomic DNA. Translation: AAS56024.1.
BK006938 Genomic DNA. Translation: DAA11998.1.
PIRiJQ0198.
RefSeqiNP_010442.3. NM_001180465.3.

3D structure databases

ProteinModelPortaliP13663.
SMRiP13663. Positions 5-365.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32209. 135 interactions.
DIPiDIP-5204N.
IntActiP13663. 17 interactions.
MINTiMINT-535737.

PTM databases

iPTMnetiP13663.

2D gel databases

SWISS-2DPAGEP13663.

Proteomic databases

MaxQBiP13663.
PeptideAtlasiP13663.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR158W; YDR158W; YDR158W.
GeneIDi851736.
KEGGisce:YDR158W.

Organism-specific databases

EuPathDBiFungiDB:YDR158W.
SGDiS000002565. HOM2.

Phylogenomic databases

HOGENOMiHOG000013358.
InParanoidiP13663.
KOiK00133.
OMAiASCHRVP.
OrthoDBiEOG7XDBRM.

Enzyme and pathway databases

UniPathwayiUPA00034; UER00016.
UPA00050; UER00463.
UPA00051; UER00464.
BioCyciYEAST:YDR158W-MONOMER.

Miscellaneous databases

NextBioi969463.
PROiP13663.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_02121. ASADH.
InterProiIPR000319. Asp-semialdehyde_DH_CS.
IPR005676. Asp_semi-ald_DH_pep-lack.
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.
TIGRFAMsiTIGR00978. asd_EA. 1 hit.
PROSITEiPS01103. ASD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the HOM2 gene of Saccharomyces cerevisiae and regulation of its expression."
    Thomas D., Surdin-Kerjan Y.
    Mol. Gen. Genet. 217:149-154(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: CC494-7D.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318 AND SER-323, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDHAS_YEAST
AccessioniPrimary (citable) accession number: P13663
Secondary accession number(s): D6VSD8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: May 11, 2016
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 18400 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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.