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Protein

4-hydroxy-tetrahydrodipicolinate synthase

Gene

dapA

Organism
Staphylococcus aureus (strain N315)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).UniRule annotation

Catalytic activityi

Pyruvate + L-aspartate-4-semialdehyde = (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H2O.UniRule annotation

Pathway:iL-lysine biosynthesis via DAP pathway

This protein is involved in step 3 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. no protein annotated in this organism
  2. no protein annotated in this organism
  3. 4-hydroxy-tetrahydrodipicolinate synthase (dapA)
  4. 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei46 – 461Part of a proton relay during catalysisUniRule annotation
Binding sitei47 – 471PyruvateUniRule annotation
Sitei109 – 1091Part of a proton relay during catalysisUniRule annotation
Active sitei135 – 1351Proton donor/acceptorUniRule annotation
Active sitei163 – 1631Schiff-base intermediate with substrateUniRule annotation
Binding sitei206 – 2061Pyruvate; via carbonyl oxygenUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Diaminopimelate biosynthesis, Lysine biosynthesis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BioCyciSAUR158879:GJCB-1294-MONOMER.
UniPathwayiUPA00034; UER00017.

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxy-tetrahydrodipicolinate synthaseUniRule annotation (EC:4.3.3.7UniRule annotation)
Short name:
HTPA synthaseUniRule annotation
Gene namesi
Name:dapAUniRule annotation
Ordered Locus Names:SA1227
OrganismiStaphylococcus aureus (strain N315)
Taxonomic identifieri158879 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000751 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2952954-hydroxy-tetrahydrodipicolinate synthasePRO_0000103156Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP63948.
SMRiP63948. Positions 2-293.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the DapA family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0329.
HOGENOMiHOG000173604.
KOiK01714.
OMAiMDFTSNG.
OrthoDBiEOG6W7235.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00418. DapA.
InterProiIPR013785. Aldolase_TIM.
IPR005263. DapA.
IPR002220. DapA-like.
IPR020625. Schiff_base-form_aldolases_AS.
[Graphical view]
PANTHERiPTHR12128. PTHR12128. 1 hit.
PfamiPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFiPIRSF001365. DHDPS. 1 hit.
PRINTSiPR00146. DHPICSNTHASE.
TIGRFAMsiTIGR00674. dapA. 1 hit.
PROSITEiPS00666. DHDPS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P63948-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTHLFEGVGV ALTTPFTNNK VNLEALKAHV NFLLENNAQA IIVNGTTAES
60 70 80 90 100
PTLTTDEKER ILKTVIDLVD KRVPVIAGTG TNDTEKSIQA SFQAKALGAD
110 120 130 140 150
AIMLITPYYN KTNQRGLVKH FEAITDAVKL PVVLYNVPSR TNMTIEPETV
160 170 180 190 200
EILSQHPYIV ALKDATNDFE YLEEVKKRID TNSFALYSGN DDNVVEYYQR
210 220 230 240 250
GGQGVISVIA NVIPKEFQAL YDAQQSGLDI QDQFKPIGTL LSALSVDINP
260 270 280 290
IPIKALTSYL EFGNYELRLP LVSLEDTDTK VLREAYDTFK AGENE
Length:295
Mass (Da):32,660
Last modified:October 11, 2004 - v1
Checksum:iEAD1E6DD4CE05A17
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA. Translation: BAB42487.1.
PIRiC89916.
RefSeqiWP_000149278.1. NC_002745.2.

Genome annotation databases

EnsemblBacteriaiBAB42487; BAB42487; BAB42487.
KEGGisau:SA1227.
PATRICi19574704. VBIStaAur116463_1321.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000018 Genomic DNA. Translation: BAB42487.1.
PIRiC89916.
RefSeqiWP_000149278.1. NC_002745.2.

3D structure databases

ProteinModelPortaliP63948.
SMRiP63948. Positions 2-293.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB42487; BAB42487; BAB42487.
KEGGisau:SA1227.
PATRICi19574704. VBIStaAur116463_1321.

Phylogenomic databases

eggNOGiCOG0329.
HOGENOMiHOG000173604.
KOiK01714.
OMAiMDFTSNG.
OrthoDBiEOG6W7235.

Enzyme and pathway databases

UniPathwayiUPA00034; UER00017.
BioCyciSAUR158879:GJCB-1294-MONOMER.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00418. DapA.
InterProiIPR013785. Aldolase_TIM.
IPR005263. DapA.
IPR002220. DapA-like.
IPR020625. Schiff_base-form_aldolases_AS.
[Graphical view]
PANTHERiPTHR12128. PTHR12128. 1 hit.
PfamiPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFiPIRSF001365. DHDPS. 1 hit.
PRINTSiPR00146. DHPICSNTHASE.
TIGRFAMsiTIGR00674. dapA. 1 hit.
PROSITEiPS00666. DHDPS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: N315.

Entry informationi

Entry nameiDAPA_STAAN
AccessioniPrimary (citable) accession number: P63948
Secondary accession number(s): Q99U89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: July 22, 2015
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB.Curated

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.