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B3ETX1 (B3ETX1_AMOA5) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
4-hydroxy-tetrahydrodipicolinate synthase HAMAP-Rule MF_00418
Short name=HTPA synthase HAMAP-Rule MF_00418
EC=4.3.3.7 HAMAP-Rule MF_00418
Gene names
Name:dapA HAMAP-Rule MF_00418
Ordered Locus Names:Aasi_1369 EMBL ACE06673.1
OrganismAmoebophilus asiaticus (strain 5a2) [Complete proteome] [HAMAP] EMBL ACE06673.1
Taxonomic identifier452471 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Candidatus Amoebophilus ›

Protein attributes

Sequence length295 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA) By similarity. SAAS SAAS005263 HAMAP-Rule MF_00418

Catalytic activity

Pyruvate + L-aspartate-4-semialdehyde = (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H2O. SAAS SAAS005263 HAMAP-Rule MF_00418

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. HAMAP-Rule MF_00418 SAAS SAAS005263

Subunit structure

Homotetramer; dimer of dimers By similarity. HAMAP-Rule MF_00418

Subcellular location

Cytoplasm By similarity SAAS SAAS005263 HAMAP-Rule MF_00418.

Sequence similarities

Belongs to the DapA family. HAMAP-Rule MF_00418

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 (PubMed:8993314 and PubMed:20503968) 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 (PubMed:20503968). HAMAP-Rule MF_00418

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Sites

Active site1361Proton donor/acceptor By similarity HAMAP-Rule MF_00418
Active site1641Schiff-base intermediate with substrate By similarity HAMAP-Rule MF_00418
Binding site481Pyruvate By similarity HAMAP-Rule MF_00418
Binding site2061Pyruvate; via carbonyl oxygen By similarity HAMAP-Rule MF_00418
Site471Part of a proton relay during catalysis By similarity HAMAP-Rule MF_00418
Site1101Part of a proton relay during catalysis By similarity HAMAP-Rule MF_00418

Sequences

Sequence LengthMass (Da)Tools
B3ETX1 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: 16A826D6FB56CCCA

FASTA29532,001
        10         20         30         40         50         60 
MIEKLKGTGV ALVTPFDEKL QVDFEGLAKL LQINTAGGVN YWVVHGTTGE AATTTSREKK 

        70         80         90        100        110        120 
EILGFIQANN PNAIPIVYGL GGNNTNDLIK QIDEMDFSGI DFVMAVSPYY NKPSQEGIYL 

       130        140        150        160        170        180 
HYKMLADVCP IPILLYNVPS RTGSSIAPET VIKLSSHPNI IGIKEASGNL VSCIEIARKK 

       190        200        210        220        230        240 
PVDFLLISGD DVLTVPIMSI GGVGVISTLA NAFPKQMTAM VQAALNKDFQ LAAEHQFELF 

       250        260        270        280        290 
PLHQLIAQGG NPVATKQMLA ALGICKNYVR LPLAPLDTLF IEQMQAAMQP WLYKA

« Hide

References

[1]"Complete sequence of Candidatus Amoebophilus asiaticus 5a2."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Horn M., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 5a2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001102 Genomic DNA. Translation: ACE06673.1.
RefSeqYP_001958402.1. NC_010830.1.

3D structure databases

ProteinModelPortalB3ETX1.
ModBaseSearch...

Protein-protein interaction databases

STRING452471.Aasi_1369.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACE06673; ACE06673; Aasi_1369.
GeneID6377617.
KEGGaas:Aasi_1369.
PATRIC21268511. VBICanAmo76781_1579.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0329.
HOGENOMHOG000173604.
KOK01714.
OMALTTMTEK.

Enzyme and pathway databases

BioCycAASI452471:GKEN-1499-MONOMER.
UniPathwayUPA00034; UER00017.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00418. DapA.
InterProIPR013785. Aldolase_TIM.
IPR002220. Dihydrodipicolinate_synth-like.
IPR020625. Dihydrodipicolinate_synth_AS.
IPR005263. Dihydrodipicolinate_synth_DapA.
[Graphical view]
PANTHERPTHR12128. PTHR12128. 1 hit.
PfamPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFPIRSF001365. DHDPS. 1 hit.
PRINTSPR00146. DHPICSNTHASE.
TIGRFAMsTIGR00674. dapA. 1 hit.
PROSITEPS00666. DHDPS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameB3ETX1_AMOA5
AccessionPrimary (citable) accession number: B3ETX1
Entry history
Integrated into UniProtKB/TrEMBL: July 22, 2008
Last sequence update: July 22, 2008
Last modified: May 29, 2013
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info