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Protein

LL-diaminopimelate aminotransferase

Gene

dapL

Organism
Moorella thermoacetica (strain ATCC 39073 / JCM 9320)
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. Can also use m-DAP instead of LL-DAP as the amino-group donor, and oxaloacetate instead of 2-oxoglutarate as the amino-group acceptor.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=60.4 µM for LL-2,6-diaminopimelate1 Publication
  2. KM=14 µM for L-2,3,4,5-tetrahydrodipicolinate1 Publication
  3. KM=0.30 mM for 2-oxoglutarate1 Publication
  4. KM=4.2 mM for glutamate1 Publication
  1. Vmax=0.25 µmol/min/mg enzyme for the forward reaction (tetrahydrodipicolinate synthesis)1 Publication
  2. Vmax=0.006 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 sitei13SubstrateUniRule annotation1
Binding sitei38Substrate; via amide nitrogenUniRule annotation1
Binding sitei102SubstrateUniRule annotation1
Binding sitei126Pyridoxal phosphateUniRule annotation1
Binding sitei126SubstrateUniRule annotation1
Binding sitei176Pyridoxal phosphateUniRule annotation1
Binding sitei176SubstrateUniRule annotation1
Binding sitei207Pyridoxal phosphateUniRule annotation1
Binding sitei246Pyridoxal phosphateUniRule annotation1
Binding sitei364SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAminotransferase, Transferase
LigandPyridoxal phosphate

Enzyme and pathway databases

BioCyciMTHE264732:G1G5J-924-MONOMER
BRENDAi2.6.1.83 1528
SABIO-RKiQ2RK33
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:Moth_0889
OrganismiMoorella thermoacetica (strain ATCC 39073 / JCM 9320)
Taxonomic identifieri264732 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeMoorella groupMoorella
Proteomesi
  • UP000007053 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003422501 – 390LL-diaminopimelate aminotransferaseAdd BLAST390

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei238N6-(pyridoxal phosphate)lysineUniRule annotation1

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi264732.Moth_0889

Structurei

3D structure databases

ProteinModelPortaliQ2RK33
SMRiQ2RK33
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni101 – 102Pyridoxal phosphate bindingUniRule annotation2
Regioni235 – 237Pyridoxal phosphate bindingUniRule annotation3

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CHM Bacteria
COG0436 LUCA
HOGENOMiHOG000223051
KOiK10206
OMAiPYAFINP
OrthoDBiPOG091H09WQ

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
IPR019881 DAP-NH2Trfase_DapL_Desulfo
IPR019942 DapL/ALD1
IPR004838 NHTrfase_class1_PyrdxlP-BS
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
PfamiView protein in Pfam
PF00155 Aminotran_1_2, 1 hit
SUPFAMiSSF53383 SSF53383, 1 hit
TIGRFAMsiTIGR03540 DapC_direct, 1 hit
PROSITEiView protein in PROSITE
PS00105 AA_TRANSFER_CLASS_1, 1 hit

Sequencei

Sequence statusi: Complete.

Q2RK33-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQEARRIREL PPYLFARIEK KIAEARERGV DIISLGIGDP DMPTPSHVID
60 70 80 90 100
KLVAEAHNPE NHRYPTSEGL LAFRQAVADW YQRLYGVDLD PRREVVTLIG
110 120 130 140 150
SKEGIAHISL CYVDPGDINL VPDPGYPVYN IGTLLAGGES YFMPLTAANG
160 170 180 190 200
FLPDLGAIPS DVARRAKLMF INYPNNPTGA VADLKFFQEV VEFARSYDLI
210 220 230 240 250
VCHDAAYSEI TYDGYRAPSF LQAPGAKEVG IEFNSVSKPY NMTGWRLGWA
260 270 280 290 300
CGRADVIEAL ARIKSNIDSG AFQAVQYAGI AALTGPQEGL AEVRRVYQER
310 320 330 340 350
RDIIVEGFNS LGWHLEKPKA TFYVWAPVPR GYTSASFAEM VLEKAGVIIT
360 370 380 390
PGNGYGNYGE GYFRIALTIS KERMQEAIER LRRVLGKVEF
Length:390
Mass (Da):43,318
Last modified:January 24, 2006 - v1
Checksum:i6500EC02D5A17860
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000232 Genomic DNA Translation: ABC19206.1
RefSeqiWP_011392408.1, NC_007644.1
YP_429749.1, NC_007644.1

Genome annotation databases

EnsemblBacteriaiABC19206; ABC19206; Moth_0889
GeneIDi3831430
KEGGimta:Moth_0889
PATRICifig|264732.11.peg.956

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000232 Genomic DNA Translation: ABC19206.1
RefSeqiWP_011392408.1, NC_007644.1
YP_429749.1, NC_007644.1

3D structure databases

ProteinModelPortaliQ2RK33
SMRiQ2RK33
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi264732.Moth_0889

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABC19206; ABC19206; Moth_0889
GeneIDi3831430
KEGGimta:Moth_0889
PATRICifig|264732.11.peg.956

Phylogenomic databases

eggNOGiENOG4105CHM Bacteria
COG0436 LUCA
HOGENOMiHOG000223051
KOiK10206
OMAiPYAFINP
OrthoDBiPOG091H09WQ

Enzyme and pathway databases

UniPathwayi
UPA00034;UER00466

BioCyciMTHE264732:G1G5J-924-MONOMER
BRENDAi2.6.1.83 1528
SABIO-RKiQ2RK33

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
IPR019881 DAP-NH2Trfase_DapL_Desulfo
IPR019942 DapL/ALD1
IPR004838 NHTrfase_class1_PyrdxlP-BS
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
PfamiView protein in Pfam
PF00155 Aminotran_1_2, 1 hit
SUPFAMiSSF53383 SSF53383, 1 hit
TIGRFAMsiTIGR03540 DapC_direct, 1 hit
PROSITEiView protein in PROSITE
PS00105 AA_TRANSFER_CLASS_1, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiDAPAT_MOOTA
AccessioniPrimary (citable) accession number: Q2RK33
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: January 24, 2006
Last modified: October 10, 2018
This is version 83 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, Reference 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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