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Protein

Probable aspartate-semialdehyde dehydrogenase

Gene

SPCC1827.06c

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission 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. Probable aspartokinase (SPBC19F5.04)
  2. Probable aspartate-semialdehyde dehydrogenase (SPCC1827.06c)
  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. Probable aspartokinase (SPBC19F5.04)
  2. Probable aspartate-semialdehyde dehydrogenase (SPCC1827.06c)
  3. Probable homoserine dehydrogenase (SPBC776.03)
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. Probable aspartokinase (SPBC19F5.04)
  2. Probable aspartate-semialdehyde dehydrogenase (SPCC1827.06c)
  3. Probable homoserine dehydrogenase (SPBC776.03)
  4. Probable homoserine kinase (SPBC4C3.03)
  5. Threonine synthase (thrc)
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 sitei111 – 1111PhosphateBy similarity
Active sitei151 – 1511Acyl-thioester intermediateBy similarity
Binding sitei179 – 1791SubstrateBy similarity
Binding sitei205 – 2051SubstrateBy similarity
Binding sitei208 – 2081PhosphateBy similarity
Binding sitei240 – 2401SubstrateBy similarity
Active sitei247 – 2471Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 154NADPBy similarity
Nucleotide bindingi39 – 402NADPBy similarity
Nucleotide bindingi182 – 1832NADPBy similarity
Nucleotide bindingi335 – 3362NADPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

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

Keywords - Ligandi

NADP

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Probable aspartate-semialdehyde dehydrogenase (EC:1.2.1.11)
Short name:
ASA dehydrogenase
Short name:
ASADH
Alternative name(s):
Aspartate-beta-semialdehyde dehydrogenase
Gene namesi
ORF Names:SPCC1827.06c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC1827.06c.
PomBaseiSPCC1827.06c.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 357357Probable aspartate-semialdehyde dehydrogenasePRO_0000141399Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei323 – 3231Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP78780.

PTM databases

iPTMnetiP78780.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi275837. 2 interactions.
IntActiP78780. 1 interaction.
MINTiMINT-4691224.

Structurei

3D structure databases

ProteinModelPortaliP78780.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000013358.
InParanoidiP78780.
KOiK00133.
OMAiASCHRVP.
OrthoDBiEOG7XDBRM.
PhylomeDBiP78780.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_02121. ASADH.
InterProiIPR005676. 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.

Sequencei

Sequence statusi: Complete.

P78780-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIKKVGILG ATGTVGQRFI TLLSDHPEFK IAVLGASARS AGKPYAVATK
60 70 80 90 100
WKQSIAMPKE ISQMSVKACD PKEFSECDIV FSGLDADFAG EIEKSFRDAN
110 120 130 140 150
LVIVSNAKNY RREPTVPLVV PTVNTDHLDV IKYQRQENKL DRGCIITNSN
160 170 180 190 200
CSTAAVVVPL KALQDAFGPI AQTNVVSMQA ISGAGYPGVS SLDILDNIVP
210 220 230 240 250
FIGGEEEKIE WETRKILGSV NSTISGYELT DNVVSAQCNR VPVIDGHLMC
260 270 280 290 300
ISVKFAKTSP TPDQVREVLA NYVSEPQKLG CYSAPKQAIY VFDDSTPDRP
310 320 330 340 350
QPRLDRNNEN GYAVSVGRIR SDSIFDIKFV SLVHNTVLGA AGAGILNAEV

AVKKGLM
Length:357
Mass (Da):38,550
Last modified:May 1, 1999 - v2
Checksum:iD3B0478617AE2848
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA19314.1.
D89129 mRNA. Translation: BAA13791.1.
PIRiT41167.
T42373.
RefSeqiNP_588552.1. NM_001023539.2.

Genome annotation databases

EnsemblFungiiSPCC1827.06c.1; SPCC1827.06c.1:pep; SPCC1827.06c.
GeneIDi2539267.
KEGGispo:SPCC1827.06c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA19314.1.
D89129 mRNA. Translation: BAA13791.1.
PIRiT41167.
T42373.
RefSeqiNP_588552.1. NM_001023539.2.

3D structure databases

ProteinModelPortaliP78780.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275837. 2 interactions.
IntActiP78780. 1 interaction.
MINTiMINT-4691224.

PTM databases

iPTMnetiP78780.

Proteomic databases

MaxQBiP78780.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC1827.06c.1; SPCC1827.06c.1:pep; SPCC1827.06c.
GeneIDi2539267.
KEGGispo:SPCC1827.06c.

Organism-specific databases

EuPathDBiFungiDB:SPCC1827.06c.
PomBaseiSPCC1827.06c.

Phylogenomic databases

HOGENOMiHOG000013358.
InParanoidiP78780.
KOiK00133.
OMAiASCHRVP.
OrthoDBiEOG7XDBRM.
PhylomeDBiP78780.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP78780.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_02121. ASADH.
InterProiIPR005676. 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.
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
    Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
    DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-357.
    Strain: PR745.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiDHAS_SCHPO
AccessioniPrimary (citable) accession number: P78780
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: May 1, 1999
Last modified: June 8, 2016
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

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.