Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

4-hydroxy-tetrahydrodipicolinate synthase

Gene

dapA

Organism
Prochlorococcus marinus (strain SARG / CCMP1375 / SS120)
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. no protein annotated in this organism
  2. Aspartate-semialdehyde dehydrogenase (asd)
  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
Sitei54 – 541Part of a proton relay during catalysisUniRule annotation
Binding sitei55 – 551PyruvateUniRule annotation
Sitei117 – 1171Part of a proton relay during catalysisUniRule annotation
Active sitei144 – 1441Proton donor/acceptorUniRule annotation
Active sitei172 – 1721Schiff-base intermediate with substrateUniRule annotation
Binding sitei214 – 2141Pyruvate; 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

BioCyciPMAR167539:GJN2-1857-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:Pro_1813
OrganismiProchlorococcus marinus (strain SARG / CCMP1375 / SS120)
Taxonomic identifieri167539 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus
Proteomesi
  • UP000001420 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 – 3023024-hydroxy-tetrahydrodipicolinate synthasePRO_0000103135Add
BLAST

Interactioni

Subunit structurei

Homotetramer; dimer of dimers.UniRule annotation

Protein-protein interaction databases

STRINGi167539.Pro1813.

Structurei

3D structure databases

ProteinModelPortaliP49423.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the DapA family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CDP. Bacteria.
COG0329. LUCA.
KOiK01714.
OMAiGMDACVP.
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.
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.

P49423-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTVPEISSA PFGRLLTAMV TPFDTAGAVD FALAARLARY LVDQGSDGLI
60 70 80 90 100
VCGTTGESPT LSWEEQYQLL ETVRNAVNGS AKVLAGTGSN STSEAIHATA
110 120 130 140 150
KAAEAGADGA LVVVPYYNKP PQAGLESHFR AVAQAAPDLP LMLYNIPGRT
160 170 180 190 200
GCSISPITVQ RLMNCSNIVS FKAASGTTNE VTDLRIRCGS RLAIYSGDDG
210 220 230 240 250
LLLPMLSVGA VGVVSVASHI VGMRLKAMIE AYFAGENSLA LSHHEQLQPL
260 270 280 290 300
FKALFATTNP IPVKAALELI GWPVGAPRSP LLPLENQMKN ELMKTISALL

QT
Length:302
Mass (Da):31,764
Last modified:September 26, 2003 - v2
Checksum:i7C6B2871C7A2E0D6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31T → P in CAA92211 (Ref. 1) Curated
Sequence conflicti85 – 851A → P in CAA92211 (Ref. 1) Curated
Sequence conflicti202 – 2021L → P in CAA92211 (Ref. 1) Curated
Sequence conflicti202 – 2021L → P in CAA85785 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z68126 Genomic DNA. Translation: CAA92211.1.
AE017126 Genomic DNA. Translation: AAQ00857.1.
Z37733 Genomic DNA. Translation: CAA85785.1.
PIRiS51751.
RefSeqiNP_876204.1. NC_005042.1.
WP_011125962.1. NC_005042.1.

Genome annotation databases

EnsemblBacteriaiAAQ00857; AAQ00857; Pro_1813.
GeneIDi1463196.
KEGGipma:Pro_1813.
PATRICi23030479. VBIProMar8617_1915.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z68126 Genomic DNA. Translation: CAA92211.1.
AE017126 Genomic DNA. Translation: AAQ00857.1.
Z37733 Genomic DNA. Translation: CAA85785.1.
PIRiS51751.
RefSeqiNP_876204.1. NC_005042.1.
WP_011125962.1. NC_005042.1.

3D structure databases

ProteinModelPortaliP49423.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi167539.Pro1813.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAQ00857; AAQ00857; Pro_1813.
GeneIDi1463196.
KEGGipma:Pro_1813.
PATRICi23030479. VBIProMar8617_1915.

Phylogenomic databases

eggNOGiENOG4105CDP. Bacteria.
COG0329. LUCA.
KOiK01714.
OMAiGMDACVP.
OrthoDBiEOG6W7235.

Enzyme and pathway databases

UniPathwayiUPA00034; UER00017.
BioCyciPMAR167539:GJN2-1857-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.
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

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of a dihydrodipicolinate synthase (DHDPS) gene from the photoautotrophic prokaryote Prochlorococcus marinus CCMP 1375 (Prochlorophyta)."
    Lorenz M., Boerner T., Hess W.R.
    Endocyt. Cell Res. 11:59-68(1995)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: SARG / CCMP1375 / SS120.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SARG / CCMP1375 / SS120.
  3. "Sequencing and determination of copy numbers of RAPD fragments amplified by repetitive primers in the prokaryote Prochlorococcus marinus."
    Lorenz M., Partensky F., Boerner T., Hess W.R.
    Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-302.
    Strain: SARG / CCMP1375 / SS120.

Entry informationi

Entry nameiDAPA_PROMA
AccessioniPrimary (citable) accession number: P49423
Secondary accession number(s): Q51920
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: September 26, 2003
Last modified: May 11, 2016
This is version 103 of the entry and version 2 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.