Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9PK30 (DAPB_CHLMU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 71. 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:
Dihydrodipicolinate reductase

Short name=DHPR
EC=1.3.1.26
Gene names
Name:dapB
Ordered Locus Names:TC_0643
OrganismChlamydia muridarum [Complete proteome] [HAMAP]
Taxonomic identifier83560 [NCBI]
Taxonomic lineageBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-2,3,4,5-tetrahydrodipicolinate + NAD(P)+ = (S)-2,3-dihydrodipicolinate + NAD(P)H. HAMAP MF_00102

Pathway

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

Subcellular location

Cytoplasm By similarity HAMAP MF_00102.

Sequence similarities

Belongs to the dihydrodipicolinate reductase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Diaminopimelate biosynthesis
Lysine biosynthesis
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processdiaminopimelate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNADPH binding

Inferred from electronic annotation. Source: InterPro

dihydrodipicolinate reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 246246Dihydrodipicolinate reductase HAMAP MF_00102
PRO_0000141427

Sequences

Sequence LengthMass (Da)Tools
Q9PK30 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: E5E0586AAF84FE32

FASTA24627,397
        10         20         30         40         50         60 
MKKSVGLIGN TGRMGGLLTE ALRSHPRCLL GKGFSRRSQT LLKEVVLEND ILIDFSAPEV 

        70         80         90        100        110        120 
TETLMDILLV TPKPVIIGTT GFSDNSVIRD KLSLLSEYVP VIFSPNMSLG AYVQRRLTAC 

       130        140        150        160        170        180 
AAKLFDASYD VRILETHHRT KVDAISGTAL SLAEAICSAK KDHFGDEQEP CIEMFGSRVG 

       190        200        210        220        230        240 
NIFGEHEVSF VGKNERFVIR HEAFSRQTFS DGVLIILRKI MEERLPAGYY TSDVLYESLF 


QEVVFD 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE002160 Genomic DNA. Translation: AAF39471.1.
PIRC81679.
RefSeqNP_297017.1. NC_002620.2.

3D structure databases

ProteinModelPortalQ9PK30.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1246004.
GenomeReviewsGene locus TC_0643 in contig AE002160_GR.
KEGGcmu:TC0643.
PATRIC20372740. VBIChlMur19118_0682.
TIGRTC_0643.

Phylogenomic databases

HOGENOMHBG594002.
OMADEIGIHA.
PhylomeDBQ9PK30.
ProtClustDBPRK00048.

Enzyme and pathway databases

BioCycCMUR243161:TC_0643-MONOMER.

Family and domain databases

HAMAPMF_00102. DapB.
[Tree]
InterProIPR022663. DapB_C.
IPR000846. DapB_N.
IPR022664. DapB_N_CS.
IPR011770. Dihydrodipicolinate_Rdtase.
IPR023940. Dihydrodipicolinate_Rdtase_bac.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK00215.
PANTHERPTHR20836. DapB_bac/pln. 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_CHLMU
AccessionPrimary (citable) accession number: Q9PK30
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families