SubmitCancel

Skip Header

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

F0SDL3

- F0SDL3_PEDSD

UniProt

F0SDL3 - F0SDL3_PEDSD

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

4-hydroxy-tetrahydrodipicolinate synthase

Gene
dapA, Pedsa_0154
Organism
Pedobacter saltans (strain ATCC 51119 / DSM 12145 / JCM 21818 / LMG 10337 / NBRC 100064 / NCIMB 13643)
Status
Unreviewed - 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) By similarity.UniRule annotationSAAS annotations

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei46 – 461Part of a proton relay during catalysis By similarityUniRule annotation
Binding sitei47 – 471Pyruvate By similarityUniRule annotation
Sitei109 – 1091Part of a proton relay during catalysis By similarityUniRule annotation
Active sitei135 – 1351Proton donor/acceptor By similarityUniRule annotation
Active sitei164 – 1641Schiff-base intermediate with substrate By similarityUniRule annotation
Binding sitei206 – 2061Pyruvate; via carbonyl oxygen By similarityUniRule annotation

GO - Molecular functioni

  1. 4-hydroxy-tetrahydrodipicolinate synthase Source: UniProtKB-EC
  2. amine-lyase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. diaminopimelate biosynthetic process Source: UniProtKB-HAMAP
  2. lysine biosynthetic process via diaminopimelate Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationSAAS annotationsImported

Keywords - Biological processi

Amino-acid biosynthesis, Diaminopimelate biosynthesisUniRule annotationSAAS annotations, Lysine biosynthesisUniRule annotationSAAS annotations

Keywords - Ligandi

Schiff baseUniRule annotationSAAS annotations

Enzyme and pathway databases

BioCyciPSAL762903:GHB2-155-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:Pedsa_0154Imported
OrganismiPedobacter saltans (strain ATCC 51119 / DSM 12145 / JCM 21818 / LMG 10337 / NBRC 100064 / NCIMB 13643)Imported
Taxonomic identifieri762903 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesSphingobacteriiaSphingobacterialesSphingobacteriaceaePedobacter
ProteomesiUP000000310: Chromosome

Subcellular locationi

Cytoplasm By similarity UniRule annotationSAAS annotations

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotationSAAS annotations

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919 PredictedImportedAdd
BLAST
Chaini20 – 292273 PredictedImportedPRO_5000720397Add
BLAST

Interactioni

Subunit structurei

Homotetramer; dimer of dimers By similarity.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliF0SDL3.

Family & Domainsi

Sequence similaritiesi

Belongs to the DapA family.UniRule annotation

Keywords - Domaini

SignalImported

Phylogenomic databases

KOiK01714.
OMAiLADHENI.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

F0SDL3-1 [UniParc]FASTAAdd to Basket

« Hide

MSRFLGTGVA MVTPFQANGS IDFDGLAATI EHLINGKVEY IVVLGTTAES    50
ATLSKDEKKQ VFKFVTERVN GRIPLVAGIG GNNTTEVVAE VNQFEMVGYE 100
AILSVVPYYN KPTQEGIYQH YKSIAQAAKL PIILYNVPGR TGVSMSAETT 150
IRLAREFKNI IATKEASGSF DQFNAIMADK PEGFELISGD DPITLPMVAL 200
GAIGVISVVG NAFPVKFSEM VRLSLNGDFK AARPLHSSFL EFTRLCFVES 250
NPCGVKAAMK ELGIIEDYVR LPLTPIGDST RAKVVAEVAK LK 292
Length:292
Mass (Da):31,574
Last modified:May 3, 2011 - v1
Checksum:i871A8139E06C7B61
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002545 Genomic DNA. Translation: ADY50740.1.
RefSeqiWP_013631243.1. NC_015177.1.
YP_004272562.1. NC_015177.1.

Genome annotation databases

EnsemblBacteriaiADY50740; ADY50740; Pedsa_0154.
GeneIDi10229685.
KEGGipsn:Pedsa_0154.
PATRICi47000875. VBIPedSal163994_0162.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP002545 Genomic DNA. Translation: ADY50740.1 .
RefSeqi WP_013631243.1. NC_015177.1.
YP_004272562.1. NC_015177.1.

3D structure databases

ProteinModelPortali F0SDL3.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ADY50740 ; ADY50740 ; Pedsa_0154 .
GeneIDi 10229685.
KEGGi psn:Pedsa_0154.
PATRICi 47000875. VBIPedSal163994_0162.

Phylogenomic databases

KOi K01714.
OMAi LADHENI.

Enzyme and pathway databases

UniPathwayi UPA00034 ; UER00017 .
BioCyci PSAL762903:GHB2-155-MONOMER.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_00418. DapA.
InterProi IPR013785. Aldolase_TIM.
IPR005263. DapA.
IPR002220. DapA-like.
[Graphical view ]
PANTHERi PTHR12128. PTHR12128. 1 hit.
Pfami PF00701. DHDPS. 1 hit.
[Graphical view ]
PIRSFi PIRSF001365. DHDPS. 1 hit.
PRINTSi PR00146. DHPICSNTHASE.
TIGRFAMsi TIGR00674. dapA. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51119 / DSM 12145 / JCM 21818 / LMG 10337 / NBRC 100064 / NCIMB 13643.

Entry informationi

Entry nameiF0SDL3_PEDSD
AccessioniPrimary (citable) accession number: F0SDL3
Entry historyi
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: May 3, 2011
Last modified: September 3, 2014
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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.UniRule annotation

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

Similar proteinsi