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Q0HLM3 (DAPB_SHESM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
4-hydroxy-tetrahydrodipicolinate reductase

Short name=HTPA reductase
EC=1.17.1.8
Gene names
Name:dapB
Ordered Locus Names:Shewmr4_0964
OrganismShewanella sp. (strain MR-4) [Complete proteome] [HAMAP]
Taxonomic identifier60480 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length270 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate By similarity. HAMAP-Rule MF_00102

Catalytic activity

(S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + NAD(P)+ + H2O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NAD(P)H. HAMAP-Rule MF_00102

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. HAMAP-Rule MF_00102

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00102.

Sequence similarities

Belongs to the DapB family.

Caution

Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2702704-hydroxy-tetrahydrodipicolinate reductase HAMAP-Rule MF_00102
PRO_1000008639

Regions

Nucleotide binding11 – 166NAD(P) By similarity
Nucleotide binding101 – 1033NAD(P) By similarity
Nucleotide binding125 – 1284NAD(P) By similarity
Region168 – 1692Substrate binding By similarity

Sites

Active site1581Proton donor/acceptor By similarity
Active site1621Proton donor By similarity
Binding site371NAD By similarity
Binding site381NADP By similarity
Binding site1591Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0HLM3 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 92CC873EB4AD46F4

FASTA27029,279
        10         20         30         40         50         60 
MGGQVRVAIV GAGGRMGRTL IESAYHQEHI RLGAAIERPG SSLVGVDAGE LAGVGKLNVL 

        70         80         90        100        110        120 
VMDSLDYATD DFDVLIDFTA PEASIVHLDW CVRHKKAMVI GTTGFNHAQK EQINAFAEQT 

       130        140        150        160        170        180 
PVVMAPNMSV GVNLMWKLLE LAAEVMGDYT DIEIIEGHHR HKKDAPSGTA LKMGEVIAKT 

       190        200        210        220        230        240 
LGRDLEKCAV YGREGITGER DRETIGFATV RAGDLVGEHT AMFADIGERL EITHKASSRM 

       250        260        270 
TFANGAMRAA HWLVEQKPGL YDMQQVLGLN 

« Hide

References

[1]"Complete sequence of Shewanella sp. MR-4."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K., Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MR-4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000446 Genomic DNA. Translation: ABI38044.1.
RefSeqYP_733101.1. NC_008321.1.

3D structure databases

ProteinModelPortalQ0HLM3.
SMRQ0HLM3. Positions 5-270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING60480.Shewmr4_0964.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI38044; ABI38044; Shewmr4_0964.
GeneID4251615.
KEGGshe:Shewmr4_0964.
PATRIC23578406. VBISheSp133532_1000.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0289.
HOGENOMHOG000227153.
KOK00215.
OMAIVMAPNM.
OrthoDBEOG6SV5DS.
ProtClustDBPRK00048.

Enzyme and pathway databases

BioCycSSP60480:GI2N-994-MONOMER.
UniPathwayUPA00034; UER00018.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00102. DapB.
InterProIPR022663. DapB_C.
IPR000846. DapB_N.
IPR022664. DapB_N_CS.
IPR011770. Dihydrodipicolinate_Rdtase.
IPR023940. Dihydrodipicolinate_Rdtase_bac.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR20836. PTHR20836. 1 hit.
PfamPF05173. DapB_C. 1 hit.
PF01113. DapB_N. 1 hit.
[Graphical view]
PIRSFPIRSF000161. DHPR. 1 hit.
TIGRFAMsTIGR00036. dapB. 1 hit.
PROSITEPS01298. DAPB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDAPB_SHESM
AccessionPrimary (citable) accession number: Q0HLM3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 3, 2006
Last modified: February 19, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways