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Protein

4-hydroxy-tetrahydrodipicolinate synthase 2

Gene

dapA2

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
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

Pathwayi: L-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. Aspartokinase (SCO3615)
  2. Aspartate-semialdehyde dehydrogenase (asd), Aspartate-semialdehyde dehydrogenase (asd)
  3. 4-hydroxy-tetrahydrodipicolinate synthase 2 (dapA2), 4-hydroxy-tetrahydrodipicolinate synthase 1 (dapA1)
  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
Sitei53 – 531Part of a proton relay during catalysisUniRule annotation
Binding sitei54 – 541PyruvateUniRule annotation
Sitei116 – 1161Part of a proton relay during catalysisUniRule annotation
Active sitei142 – 1421Proton donor/acceptorUniRule annotation
Active sitei170 – 1701Schiff-base intermediate with substrateUniRule annotation
Binding sitei210 – 2101Pyruvate; 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

UniPathwayiUPA00034; UER00017.

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxy-tetrahydrodipicolinate synthase 2UniRule annotation (EC:4.3.3.7UniRule annotation)
Short name:
HTPA synthase 2UniRule annotation
Gene namesi
Name:dapA2UniRule annotation
Ordered Locus Names:SCO5744
ORF Names:SC9A10.08
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
Proteomesi
  • UP000001973 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 – 2992994-hydroxy-tetrahydrodipicolinate synthase 2PRO_0000103165Add
BLAST

Proteomic databases

PRIDEiO86841.

Interactioni

Subunit structurei

Homotetramer; dimer of dimers.UniRule annotation

Protein-protein interaction databases

STRINGi100226.SCO5744.

Structurei

3D structure databases

ProteinModelPortaliO86841.
SMRiO86841. Positions 8-297.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the DapA family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CDP. Bacteria.
COG0329. LUCA.
HOGENOMiHOG000173604.
InParanoidiO86841.
KOiK01714.
OMAiRSGLAWY.
OrthoDBiEOG6W7235.
PhylomeDBiO86841.

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.
IPR020624. Schiff_base-form_aldolases_CS.
[Graphical view]
PANTHERiPTHR12128. PTHR12128. 1 hit.
PfamiPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFiPIRSF001365. DHDPS. 1 hit.
PRINTSiPR00146. DHPICSNTHASE.
SMARTiSM01130. DHDPS. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00674. dapA. 1 hit.
PROSITEiPS00665. DHDPS_1. 1 hit.
PS00666. DHDPS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O86841-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPTSTPQTP FGRVLTAMVT PFTADGALDL DGAQRLAAHL VDAGNDGLII
60 70 80 90 100
NGTTGESPTT SDAEKADLVR AVVEAVGDRA HVVAGVGTNN TQHSIELARA
110 120 130 140 150
AERVGAHGLL LVTPYYNKPP QEGLYLHFTA IADAAGLPVM LYDIPGRSGV
160 170 180 190 200
PINTETLVRL AEHPRIVANK DAKGDLGRAS WAIARSGLAW YSGDDMLNLP
210 220 230 240 250
LLAVGAVGFV SVVGHVVTPE LRAMVDAHVA GDVQKALEIH QKLLPVFTGM
260 270 280 290
FRTQGVMTTK GALALQGLPA GPLRAPMVGL TPEETEQLKI DLAAGGVQL
Length:299
Mass (Da):31,175
Last modified:November 1, 1998 - v1
Checksum:i44FC9B2094E69676
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939124 Genomic DNA. Translation: CAA20295.1.
PIRiT35844.
RefSeqiNP_629869.1. NC_003888.3.
WP_011030431.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAA20295; CAA20295; CAA20295.
GeneIDi1101183.
KEGGisco:SCO5744.
PATRICi23741362. VBIStrCoe124346_5832.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL939124 Genomic DNA. Translation: CAA20295.1.
PIRiT35844.
RefSeqiNP_629869.1. NC_003888.3.
WP_011030431.1. NC_003888.3.

3D structure databases

ProteinModelPortaliO86841.
SMRiO86841. Positions 8-297.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi100226.SCO5744.

Proteomic databases

PRIDEiO86841.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAA20295; CAA20295; CAA20295.
GeneIDi1101183.
KEGGisco:SCO5744.
PATRICi23741362. VBIStrCoe124346_5832.

Phylogenomic databases

eggNOGiENOG4105CDP. Bacteria.
COG0329. LUCA.
HOGENOMiHOG000173604.
InParanoidiO86841.
KOiK01714.
OMAiRSGLAWY.
OrthoDBiEOG6W7235.
PhylomeDBiO86841.

Enzyme and pathway databases

UniPathwayiUPA00034; UER00017.

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.
IPR020624. Schiff_base-form_aldolases_CS.
[Graphical view]
PANTHERiPTHR12128. PTHR12128. 1 hit.
PfamiPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFiPIRSF001365. DHDPS. 1 hit.
PRINTSiPR00146. DHPICSNTHASE.
SMARTiSM01130. DHDPS. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00674. dapA. 1 hit.
PROSITEiPS00665. DHDPS_1. 1 hit.
PS00666. DHDPS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-471 / A3(2) / M145.

Entry informationi

Entry nameiDAPA2_STRCO
AccessioniPrimary (citable) accession number: O86841
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: November 1, 1998
Last modified: May 11, 2016
This is version 113 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.