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Protein

LL-diaminopimelate aminotransferase

Gene

dapL

Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate. Is also able to catalyze the reverse reaction in vitro, i.e. the transamination of LL-diaminopimelate with 2-oxoglutarate to produce tetrahydrodipicolinate and glutamate. Cannot use m-DAP, lysine or ornithine as the amino-group donor, when using 2-oxoglutarate as the amino-group acceptor. Cannot use pyruvate, indole 3-pyruvate, oxaloacetate or phenyl pyruvate as the amino-group acceptor, when using LL-DAP as the amino-group donor.1 Publication

Catalytic activityi

LL-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H2O.UniRule annotation1 Publication

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Kineticsi

  1. KM=37 µM for LL-2,6-diaminopimelate1 Publication
  2. KM=14 µM for L-2,3,4,5-tetrahydrodipicolinate1 Publication
  3. KM=0.40 mM for 2-oxoglutarate1 Publication
  4. KM=4.3 mM for glutamate1 Publication
  1. Vmax=10.6 µmol/min/mg enzyme for the forward reaction (tetrahydrodipicolinate synthesis)1 Publication
  2. Vmax=0.450 µmol/min/mg enzyme for the reverse reaction (LL-DAP synthesis)1 Publication

Pathwayi: L-lysine biosynthesis via DAP pathway

This protein is involved in step 1 of the subpathway that synthesizes LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (aminotransferase route).UniRule annotation1 Publication
Proteins known to be involved in this subpathway in this organism are:
  1. LL-diaminopimelate aminotransferase (dapL)
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 LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (aminotransferase route), the pathway L-lysine biosynthesis via DAP pathway and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei15SubstrateUniRule annotation1
Binding sitei42Substrate; via amide nitrogenUniRule annotation1
Binding sitei72Pyridoxal phosphateUniRule annotation1
Binding sitei109SubstrateUniRule annotation1
Binding sitei132Pyridoxal phosphateUniRule annotation1
Binding sitei132SubstrateUniRule annotation1
Binding sitei187Pyridoxal phosphateUniRule annotation1
Binding sitei187SubstrateUniRule annotation1
Binding sitei218Pyridoxal phosphateUniRule annotation1
Binding sitei257Pyridoxal phosphateUniRule annotation1
Binding sitei292Pyridoxal phosphateUniRule annotation1
Binding sitei292SubstrateUniRule annotation1
Binding sitei388SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAminotransferase, Transferase
LigandPyridoxal phosphate

Enzyme and pathway databases

BRENDAi2.6.1.83 2986
SABIO-RKiQ72NJ3
UniPathwayi
UPA00034;UER00466

Names & Taxonomyi

Protein namesi
Recommended name:
LL-diaminopimelate aminotransferase1 PublicationUniRule annotation (EC:2.6.1.83UniRule annotation1 Publication)
Short name:
DAP-AT1 PublicationUniRule annotation
Short name:
DAP-aminotransferase1 PublicationUniRule annotation
Short name:
LL-DAP-aminotransferase1 PublicationUniRule annotation
Gene namesi
Name:dapLUniRule annotation
Ordered Locus Names:LIC_12841
OrganismiLeptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
Taxonomic identifieri267671 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesLeptospiralesLeptospiraceaeLeptospira
Proteomesi
  • UP000007037 Componenti: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003422481 – 408LL-diaminopimelate aminotransferaseAdd BLAST408

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei249N6-(pyridoxal phosphate)lysineUniRule annotation1

Proteomic databases

PaxDbiQ72NJ3

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi267671.LIC12841

Structurei

3D structure databases

ProteinModelPortaliQ72NJ3
SMRiQ72NJ3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni108 – 109Pyridoxal phosphate bindingUniRule annotation2
Regioni246 – 248Pyridoxal phosphate bindingUniRule annotation3

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4107QSS Bacteria
COG0436 LUCA
KOiK10206
OMAiTGTRCAF

Family and domain databases

Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 2 hits
HAMAPiMF_01642 DapL_aminotrans_1, 1 hit
InterProiView protein in InterPro
IPR004839 Aminotransferase_I/II
IPR019942 DapL/ALD1
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
PANTHERiPTHR43144 PTHR43144, 1 hit
PfamiView protein in Pfam
PF00155 Aminotran_1_2, 1 hit
SUPFAMiSSF53383 SSF53383, 1 hit
TIGRFAMsiTIGR03542 DAPAT_plant, 1 hit

Sequencei

Sequence statusi: Complete.

Q72NJ3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MANINENYLK LKAGYLFPEI SKRVKIYSEK NPSAKIIRLG IGDVTLPIVP
60 70 80 90 100
SVVDAMVEAS KEMGTVGGFH GYGPEQGYSF LLKSIADHDY GSLGIKIDES
110 120 130 140 150
EIFVSDGSKC DCGNIQEIFS TDSKIAVADP VYPVYVDTNV MAGRTGEIGP
160 170 180 190 200
DGRYSNLIYM PATKENGFQP EIPKEKADIV YLCYPNNPTG TVTTKESLKA
210 220 230 240 250
WVEYAKKNNS IILYDSAYEA FISEPGVPRS IYEVEGAKEV AIEFRSFSKT
260 270 280 290 300
AGFTGLRCAY IVIPKELKGR TRSGEEVSLN SLWNRRHTTK FNGVSYVTQK
310 320 330 340 350
GAEACYSPQG KKEIQTSIAY YMANASKIRD GLKKAGYEVF GGVNAPYIWL
360 370 380 390 400
KTSDNLSSWD FFDKLLNKAQ VVGTPGSGFG PAGEGYFRLS AFGKKEDVEE

AIARITSL
Length:408
Mass (Da):44,819
Last modified:July 5, 2004 - v1
Checksum:i078F8359FBA99D2A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016823 Genomic DNA Translation: AAS71394.1
RefSeqiWP_001284168.1, NC_005823.1

Genome annotation databases

EnsemblBacteriaiAAS71394; AAS71394; LIC_12841
KEGGilic:LIC_12841

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016823 Genomic DNA Translation: AAS71394.1
RefSeqiWP_001284168.1, NC_005823.1

3D structure databases

ProteinModelPortaliQ72NJ3
SMRiQ72NJ3
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi267671.LIC12841

Proteomic databases

PaxDbiQ72NJ3

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAS71394; AAS71394; LIC_12841
KEGGilic:LIC_12841

Phylogenomic databases

eggNOGiENOG4107QSS Bacteria
COG0436 LUCA
KOiK10206
OMAiTGTRCAF

Enzyme and pathway databases

UniPathwayi
UPA00034;UER00466

BRENDAi2.6.1.83 2986
SABIO-RKiQ72NJ3

Family and domain databases

Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 2 hits
HAMAPiMF_01642 DapL_aminotrans_1, 1 hit
InterProiView protein in InterPro
IPR004839 Aminotransferase_I/II
IPR019942 DapL/ALD1
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
PANTHERiPTHR43144 PTHR43144, 1 hit
PfamiView protein in Pfam
PF00155 Aminotran_1_2, 1 hit
SUPFAMiSSF53383 SSF53383, 1 hit
TIGRFAMsiTIGR03542 DAPAT_plant, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiDAPAT_LEPIC
AccessioniPrimary (citable) accession number: Q72NJ3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: July 5, 2004
Last modified: October 10, 2018
This is version 94 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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Main funding by: National Institutes of Health

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