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Protein

4-hydroxy-tetrahydrodipicolinate reductase

Gene

dapB

Organism
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.UniRule annotation

Catalytic activityi

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

Pathwayi: L-lysine biosynthesis via DAP pathway

This protein is involved in step 4 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. Aspartokinase (lysC)
  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
Active sitei134 – 1341Proton donor/acceptorUniRule annotation
Binding sitei135 – 1351SubstrateUniRule annotation
Active sitei138 – 1381Proton donorUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi9 – 146NAD(P)UniRule annotation
Nucleotide bindingi77 – 793NAD(P)UniRule annotation
Nucleotide bindingi104 – 1074NAD(P)UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Diaminopimelate biosynthesis, Lysine biosynthesis

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

UniPathwayiUPA00034; UER00018.

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxy-tetrahydrodipicolinate reductaseUniRule annotation (EC:1.17.1.8UniRule annotation)
Short name:
HTPA reductaseUniRule annotation
Gene namesi
Name:dapBUniRule annotation
Ordered Locus Names:CE1866
OrganismiCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Taxonomic identifieri196164 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
Proteomesi
  • UP000001409 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 – 2482484-hydroxy-tetrahydrodipicolinate reductasePRO_0000141434Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi196164.HMPREF0290_1898.

Structurei

3D structure databases

ProteinModelPortaliQ8RQN0.
SMRiQ8RQN0. Positions 3-248.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni144 – 1452Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the DapB family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105DUK. Bacteria.
COG0289. LUCA.
HOGENOMiHOG000227154.
KOiK00215.
OrthoDBiEOG6SV5DS.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00102. DapB.
InterProiIPR022663. DapB_C.
IPR000846. DapB_N.
IPR022664. DapB_N_CS.
IPR023940. DHDPR_bac.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR20836. PTHR20836. 1 hit.
PfamiPF05173. DapB_C. 1 hit.
PF01113. DapB_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000161. DHPR. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00036. dapB. 1 hit.
PROSITEiPS01298. DAPB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8RQN0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIKVGVLGA KGRVGQTIVA AVNDTDDLEL VAEVDHDDDL SLLVDSGAEV
60 70 80 90 100
VVDFTTPNAV MGNLEFCINN GISAVVGTTG FDEDRLAQVR SWCASNEGVG
110 120 130 140 150
VLIAPNFAIS AVLTMVFARQ AARFFESAEV IELHHPNKLD APSGTAIHTA
160 170 180 190 200
QGIAEARREA GMAAQPDATE QALDGSRGAD VDGIPVHAVR MSGMVAHEAV
210 220 230 240
IFGTQGQTLT IKQDSYDRNS FAPGVLVGIR NIAQHPGLTV GLEHYLDL
Length:248
Mass (Da):26,055
Last modified:June 1, 2002 - v1
Checksum:iDE8253756BF460DC
GO

Sequence cautioni

The sequence BAC18676.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB083130 Genomic DNA. Translation: BAB88821.1.
BA000035 Genomic DNA. Translation: BAC18676.1. Different initiation.
RefSeqiWP_006767864.1. NZ_GG700683.1.

Genome annotation databases

EnsemblBacteriaiBAC18676; BAC18676; BAC18676.
KEGGicef:CE1866.
PATRICi21489883. VBICorEff9312_1855.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB083130 Genomic DNA. Translation: BAB88821.1.
BA000035 Genomic DNA. Translation: BAC18676.1. Different initiation.
RefSeqiWP_006767864.1. NZ_GG700683.1.

3D structure databases

ProteinModelPortaliQ8RQN0.
SMRiQ8RQN0. Positions 3-248.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196164.HMPREF0290_1898.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC18676; BAC18676; BAC18676.
KEGGicef:CE1866.
PATRICi21489883. VBICorEff9312_1855.

Phylogenomic databases

eggNOGiENOG4105DUK. Bacteria.
COG0289. LUCA.
HOGENOMiHOG000227154.
KOiK00215.
OrthoDBiEOG6SV5DS.

Enzyme and pathway databases

UniPathwayiUPA00034; UER00018.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00102. DapB.
InterProiIPR022663. DapB_C.
IPR000846. DapB_N.
IPR022664. DapB_N_CS.
IPR023940. DHDPR_bac.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR20836. PTHR20836. 1 hit.
PfamiPF05173. DapB_C. 1 hit.
PF01113. DapB_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000161. DHPR. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00036. dapB. 1 hit.
PROSITEiPS01298. DAPB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "dapB, dapA of Corynebacterium efficiens."
    Itaya H., Kimura E., Kawahara Y., Sugimoto S.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.
  2. "Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
    Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
    Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Entry informationi

Entry nameiDAPB_COREF
AccessioniPrimary (citable) accession number: Q8RQN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: June 1, 2002
Last modified: December 9, 2015
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.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.