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P44859

- DAPF_HAEIN

UniProt

P44859 - DAPF_HAEIN

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Protein

Diaminopimelate epimerase

Gene
dapF, HI_0750
Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan. Only accepts DAP isomers with the L configuration.1 Publication

Catalytic activityi

LL-2,6-diaminoheptanedioate = meso-diaminoheptanedioate.1 Publication

Enzyme regulationi

Inhibited by LL-aziridino (LL-AziDAP), DL-aziridino (DL-AziDAP), (2S,3R,6S)-2,6-diamino-3-fluoropimelate (L,L-3-fluoro-DAP) and (2R,3S,6S)-2,6-diamino-3-fluoropimelate (D,L-3-fluoro-DAP).2 Publications

Kineticsi

Kcat is 128 and 82 (sec-1) for L,L-DAP and D,L-DAP, respectively.

  1. KM=0.7 mM for L,L-DAP (at pH 7.8)1 Publication
  2. KM=1.1 mM for D,L-DAP (at pH 7.8)

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei11 – 111Substrate
Binding sitei44 – 441Substrate
Binding sitei64 – 641Substrate
Active sitei73 – 731Proton donor/acceptor2 Publications
Binding sitei157 – 1571Substrate
Sitei159 – 1591Important for catalytic activity Reviewed prediction
Binding sitei190 – 1901Substrate
Sitei208 – 2081Important for catalytic activity Reviewed prediction
Active sitei217 – 2171Proton donor/acceptor2 Publications

GO - Molecular functioni

  1. diaminopimelate epimerase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. lysine biosynthetic process via diaminopimelate Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Amino-acid biosynthesis, Lysine biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00034; UER00025.

Names & Taxonomyi

Protein namesi
Recommended name:
Diaminopimelate epimerase (EC:5.1.1.7)
Short name:
DAP epimerase
Alternative name(s):
PLP-Independent Amino Acid Racemases
Gene namesi
Name:dapF
Ordered Locus Names:HI_0750
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
ProteomesiUP000000579: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi73 – 731C → A: Inactive as epimerases, but it is able to rapidly catalyze the HF eliminatio via abstraction of the C-2 hydrogen of the D,L-3-fluoro-DAP analog and is essentially unable to catalyze the same elimination with the L,L-3-fluoro-DAP analog. 2 Publications
Mutagenesisi73 – 731C → S: It is able to catalyze both epimerization of DAP and HF elimination of L,L-3-fluoro-DAP and D,L-3-fluoro-DAP. Able to slowly eliminate HF but does not catalyze epimerization; when associated with S-217. 2 Publications
Mutagenesisi217 – 2171C → A: Inactive as epimerases. It is able to rapidly catalyze the HF eliminatio via abstraction of the C-2 hydrogen of the L,L-3-fluoro-DAP analog and is essentially unable to catalyze the same elimination with the D,L-3-fluoro-DAP analog. 2 Publications
Mutagenesisi217 – 2171C → S: It is able to catalyze both epimerization of DAP and HF elimination of L,L-3-fluoro-DAP and D,L-3-fluoro-DAP. Able to slowly eliminate HF but does not catalyze epimerization; when associated with S-73. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 274274Diaminopimelate epimeraseUniRule annotationPRO_0000149842Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi73 ↔ 2171 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

STRINGi71421.HI0750.

Structurei

Secondary structure

1
274
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 87
Beta strandi11 – 177
Beta strandi19 – 213
Helixi27 – 348
Turni36 – 383
Beta strandi43 – 497
Beta strandi56 – 649
Beta strandi69 – 713
Helixi74 – 8613
Beta strandi93 – 986
Beta strandi103 – 1086
Beta strandi114 – 1174
Helixi125 – 1273
Beta strandi137 – 1426
Beta strandi147 – 16317
Turni167 – 1693
Helixi172 – 1809
Beta strandi190 – 1989
Beta strandi201 – 2088
Turni209 – 2113
Helixi218 – 23013
Beta strandi236 – 2427
Beta strandi245 – 2517
Beta strandi258 – 2625
Beta strandi265 – 2717

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BWZX-ray2.72A1-274[»]
1GQZX-ray1.75A1-274[»]
2GKEX-ray1.35A1-274[»]
2GKJX-ray1.70A1-274[»]
2Q9HX-ray2.30A1-274[»]
2Q9JX-ray2.20A1-274[»]
ProteinModelPortaliP44859.
SMRiP44859. Positions 1-274.

Miscellaneous databases

EvolutionaryTraceiP44859.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni8 – 92SubstrateUniRule annotation
Regioni73 – 753Substrate bindingUniRule annotation
Regioni208 – 2092Substrate bindingUniRule annotation
Regioni218 – 2192Substrate bindingUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0253.
KOiK01778.
OMAiLIVEPPY.
OrthoDBiEOG6ND0M5.
PhylomeDBiP44859.

Family and domain databases

HAMAPiMF_00197. DAP_epimerase.
InterProiIPR018510. DAP_epimerase_AS.
IPR001653. DAP_epimerase_DapF.
[Graphical view]
PANTHERiPTHR31689. PTHR31689. 1 hit.
PfamiPF01678. DAP_epimerase. 2 hits.
[Graphical view]
TIGRFAMsiTIGR00652. DapF. 1 hit.
PROSITEiPS01326. DAP_EPIMERASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P44859-1 [UniParc]FASTAAdd to Basket

« Hide

MQFSKMHGLG NDFVVVDGVT QNVFFTPETI RRLANRHCGI GFDQLLIVEA    50
PYDPELDFHY RIFNADGSEV SQCGNGARCF ARFVTLKGLT NKKDISVSTQ 100
KGNMVLTVKD DNQIRVNMGE PIWEPAKIPF TANKFEKNYI LRTDIQTVLC 150
GAVSMGNPHC VVQVDDIQTA NVEQLGPLLE SHERFPERVN AGFMQIINKE 200
HIKLRVYERG AGETQACGSG ACAAVAVGIM QGLLNNNVQV DLPGGSLMIE 250
WNGVGHPLYM TGEATHIYDG FITL 274
Length:274
Mass (Da):30,249
Last modified:November 1, 1995 - v1
Checksum:i321B3CDAFFE81EDA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L42023 Genomic DNA. Translation: AAC22409.1.
PIRiF64090.
RefSeqiNP_438909.1. NC_000907.1.

Genome annotation databases

EnsemblBacteriaiAAC22409; AAC22409; HI_0750.
GeneIDi949560.
KEGGihin:HI0750.
PATRICi20190143. VBIHaeInf48452_0787.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L42023 Genomic DNA. Translation: AAC22409.1 .
PIRi F64090.
RefSeqi NP_438909.1. NC_000907.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BWZ X-ray 2.72 A 1-274 [» ]
1GQZ X-ray 1.75 A 1-274 [» ]
2GKE X-ray 1.35 A 1-274 [» ]
2GKJ X-ray 1.70 A 1-274 [» ]
2Q9H X-ray 2.30 A 1-274 [» ]
2Q9J X-ray 2.20 A 1-274 [» ]
ProteinModelPortali P44859.
SMRi P44859. Positions 1-274.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 71421.HI0750.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC22409 ; AAC22409 ; HI_0750 .
GeneIDi 949560.
KEGGi hin:HI0750.
PATRICi 20190143. VBIHaeInf48452_0787.

Phylogenomic databases

eggNOGi COG0253.
KOi K01778.
OMAi LIVEPPY.
OrthoDBi EOG6ND0M5.
PhylomeDBi P44859.

Enzyme and pathway databases

UniPathwayi UPA00034 ; UER00025 .

Miscellaneous databases

EvolutionaryTracei P44859.

Family and domain databases

HAMAPi MF_00197. DAP_epimerase.
InterProi IPR018510. DAP_epimerase_AS.
IPR001653. DAP_epimerase_DapF.
[Graphical view ]
PANTHERi PTHR31689. PTHR31689. 1 hit.
Pfami PF01678. DAP_epimerase. 2 hits.
[Graphical view ]
TIGRFAMsi TIGR00652. DapF. 1 hit.
PROSITEi PS01326. DAP_EPIMERASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
  2. "Chemical mechanism of Haemophilus influenzae diaminopimelate epimerase."
    Koo C.W., Blanchard J.S.
    Biochemistry 38:4416-4422(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, BIOPHYSICOCHEMICAL PROPERTIES.
  3. "Identification of active site cysteine residues that function as general bases: diaminopimelate epimerase."
    Koo C.W., Sutherland A., Vederas J.C., Blanchard J.S.
    J. Am. Chem. Soc. 122:6122-6123(2000)
    Cited for: MUTAGENESIS OF CYS-73 AND CYS-217, ACTIVE SITE, ENZYME REGULATION.
  4. "Structural symmetry: the three-dimensional structure of Haemophilus influenzae diaminopimelate epimerase."
    Cirilli M., Zheng R., Scapin G., Blanchard J.S.
    Biochemistry 37:16452-16458(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.72 ANGSTROMS), ACTIVE SITE, DISULFIDE BOND, SUBUNIT.
  5. "Refinement of Haemophilus influenzae diaminopimelic acid epimerase (DapF) at 1.75 A resolution suggests a mechanism for stereocontrol during catalysis."
    Lloyd A.J., Huyton T., Turkenburg J., Roper D.I.
    Acta Crystallogr. D 60:397-400(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), REACTION MECHANISM.
  6. "Structural insights into stereochemical inversion by diaminopimelate epimerase: an antibacterial drug target."
    Pillai B., Cherney M.M., Diaper C.M., Sutherland A., Blanchard J.S., Vederas J.C., James M.N.
    Proc. Natl. Acad. Sci. U.S.A. 103:8668-8673(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, SUBSTRATE SPECIFICITY, ENZYME REGULATION.
  7. "Dynamics of catalysis revealed from the crystal structures of mutants of diaminopimelate epimerase."
    Pillai B., Cherney M., Diaper C.M., Sutherland A., Blanchard J.S., Vederas J.C., James M.N.
    Biochem. Biophys. Res. Commun. 363:547-553(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF MUTANT SER-73 AND SER-217 IN COMPLEX WITH SUBSTRATE ANALOGS, MUTAGENESIS OF CYS-73 AND CYS-217.

Entry informationi

Entry nameiDAPF_HAEIN
AccessioniPrimary (citable) accession number: P44859
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Haemophilus influenzae
    Haemophilus influenzae (strain Rd): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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