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ECOLI:DAPB

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) dapB (ECO:0000255 with HAMAP-Rule:MF_00102)
Protein Name(s) 4-hydroxy-tetrahydrodipicolinate reductase (ECO:0000255 with HAMAP-Rule:MF_00102)

HTPA reductase (ECO:0000255 with HAMAP-Rule:MF_00102)

External Links
UniProt P04036
EMBL M10611
U00096
AP009048
J01597
PIR A00375
RefSeq NP_414572.1
YP_488337.1
PDB 1ARZ
1DIH
1DRU
1DRV
1DRW
PDBsum 1ARZ
1DIH
1DRU
1DRV
1DRW
ProteinModelPortal P04036
SMR P04036
DIP DIP-9399N
IntAct P04036
STRING 511145.b0031
BindingDB P04036
SWISS-2DPAGE P04036
PaxDb P04036
PRIDE P04036
EnsemblBacteria AAC73142
BAB96600
GeneID 12932496
944762
KEGG ecj:Y75_p0031
eco:b0031
PATRIC 32115153
EchoBASE EB0202
EcoGene EG10206
eggNOG COG0289
HOGENOM HOG000227153
InParanoid P04036
KO K00215
OMA CAVYARE
OrthoDB EOG6SV5DS
PhylomeDB P04036
BioCyc EcoCyc:DIHYDROPICRED-MONOMER
ECOL316407:JW0029-MONOMER
MetaCyc:DIHYDROPICRED-MONOMER
UniPathway UPA00034
EvolutionaryTrace P04036
PRO PR:P04036
Proteomes UP000000318
UP000000625
Genevestigator P04036
GO GO:0005829
GO:0008839
GO:0042802
GO:0051287
GO:0070402
GO:0016726
GO:0008652
GO:0019877
GO:0009089
Gene3D 3.40.50.720
HAMAP MF_00102
InterPro IPR022663
IPR000846
IPR022664
IPR011770
IPR023940
IPR016040
PANTHER PTHR20836
Pfam PF05173
PF01113
PIRSF PIRSF000161
TIGRFAMs TIGR00036
PROSITE PS01298

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

part_of

GO:0005829

cytosol

PMID:16858726[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0019877

diaminopimelate biosynthetic process

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10206
PANTHER:PTN000464618
UniProtKB:P9WP23

P

Seeded From UniProt

complete

enables

GO:0008839

4-hydroxy-tetrahydrodipicolinate reductase

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10206
PANTHER:PTN000464618
TAIR:locus:2051854
TAIR:locus:2080482
TAIR:locus:2173043
UniProtKB:P9WP23

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10206
PANTHER:PTN000464634

C

Seeded From UniProt

complete

involved_in

GO:0019877

diaminopimelate biosynthetic process

PMID:4151489[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0008652

cellular amino acid biosynthetic process

PMID:4151489[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:7893644[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0019877

diaminopimelate biosynthetic process

PMID:4926684[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008839

4-hydroxy-tetrahydrodipicolinate reductase

PMID:7893644[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008839

4-hydroxy-tetrahydrodipicolinate reductase

PMID:20503968[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0008839

4-hydroxy-tetrahydrodipicolinate reductase

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000846
InterPro:IPR022663
InterPro:IPR022664
InterPro:IPR023940

F

Seeded From UniProt

complete

involved_in

GO:0009089

lysine biosynthetic process via diaminopimelate

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000846
InterPro:IPR022663
InterPro:IPR022664
InterPro:IPR023940

P

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000846
InterPro:IPR022663
InterPro:IPR022664
InterPro:IPR023940

P

Seeded From UniProt

complete

enables

GO:0008839

4-hydroxy-tetrahydrodipicolinate reductase

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.17.1.8

F

Seeded From UniProt

complete

involved_in

GO:0009089

lysine biosynthetic process via diaminopimelate

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000034378

P

Seeded From UniProt

complete

enables

GO:0016726

oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000034378

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000034378

C

Seeded From UniProt

complete

enables

GO:0050661

NADP binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000034378

F

Seeded From UniProt

complete

enables

GO:0051287

NAD binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000034378

F

Seeded From UniProt

complete

involved_in

GO:0019877

diaminopimelate biosynthetic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000034378

P

Seeded From UniProt

complete

involved_in

GO:0008652

cellular amino acid biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0028

P

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

involved_in

GO:0019877

diaminopimelate biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0220

P

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

involved_in

GO:0009085

lysine biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0457

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

involved_in

GO:0009089

lysine biosynthetic process via diaminopimelate

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00034

P

Seeded From UniProt

complete

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Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
  2. ↑ 2.0 2.1 2.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  3. ↑ 3.0 3.1 Tamir, H & Gilvarg, C (1974) Dihydrodipicolinic acid reductase. J. Biol. Chem. 249 3034-40 PubMed GONUTS page
  4. ↑ 4.0 4.1 Reddy, SG et al. (1995) Expression, purification, and characterization of Escherichia coli dihydrodipicolinate reductase. Biochemistry 34 3492-501 PubMed GONUTS page
  5. ↑ Bukhari, AI & Taylor, AL (1971) Genetic analysis of diaminopimelic acid- and lysine-requiring mutants of Escherichia coli. J. Bacteriol. 105 844-54 PubMed GONUTS page
  6. ↑ Devenish, SR et al. (2010) NMR studies uncover alternate substrates for dihydrodipicolinate synthase and suggest that dihydrodipicolinate reductase is also a dehydratase. J. Med. Chem. 53 4808-12 PubMed GONUTS page
  7. ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
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