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A3MFT3

- HEM1_BURM7

UniProt

A3MFT3 - HEM1_BURM7

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Burkholderia mallei (strain NCTC 10247)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).UniRule annotation

Catalytic activityi

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei58 – 581NucleophileUniRule annotation
Sitei106 – 1061Important for activityUniRule annotation
Binding sitei116 – 1161SubstrateUniRule annotation
Binding sitei127 – 1271SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi196 – 2016NADPUniRule annotation

GO - Molecular functioni

  1. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
  2. NADP binding Source: InterPro

GO - Biological processi

  1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciBMAL320389:GH97-5461-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTRUniRule annotation
Gene namesi
Name:hemAUniRule annotation
Ordered Locus Names:BMA10247_A1942
OrganismiBurkholderia mallei (strain NCTC 10247)
Taxonomic identifieri320389 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
ProteomesiUP000002284: Chromosome II

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 434434Glutamyl-tRNA reductasePRO_0000335014Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi320389.BMA10247_A1942.

Structurei

3D structure databases

ProteinModelPortaliA3MFT3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni57 – 604Substrate bindingUniRule annotation
Regioni121 – 1233Substrate bindingUniRule annotation

Domaini

Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.UniRule annotation

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109650.
KOiK02492.
OMAiHEVTGEY.
OrthoDBiEOG6C2WN5.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFiPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMiSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A3MFT3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDMQLLTIGI NHHTAPVALR ERVAFPLEQI KPALSTFKSV FLGHPAPNAP
60 70 80 90 100
EAAILSTCNR TELYCATNDR AARDAAIRWM SDYHRIPADE LAPHVYALPQ
110 120 130 140 150
SEAVRHAFRV ASGLDSMVLG ETQILGQMKN AVRTASEAGS LGTYLNQLFQ
160 170 180 190 200
RTFAVAKEVR GTTEIGAQSV SMAAAAVRLA QRIFEQVAQQ RVLFIGAGEM
210 220 230 240 250
IELCATHFAA QGPRELVVAN RTAERGAKLA ERFGGRAMPL ADLPARMHEF
260 270 280 290 300
DIIVSCTAST LPIIGLGAVE RAVKARRHRP IFMVDLAVPR DIEPEVGKLK
310 320 330 340 350
DVFLYTVDDL GAIVREGNAS RQAAVAQAEA IIETRVQNFM QWLDARSIVP
360 370 380 390 400
VIRHMHTQAD ALRRAEVERA RKMLARGDDP DAVLDALSQA LTNKLIHGPT
410 420 430
SALNRANGAD RDSLIDLMRG FYQHAPRSSD TSDR
Length:434
Mass (Da):47,546
Last modified:April 3, 2007 - v1
Checksum:iD9DC915D8233453A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000547 Genomic DNA. Translation: ABO03720.1.
RefSeqiYP_001079119.1. NC_009079.1.

Genome annotation databases

EnsemblBacteriaiABO03720; ABO03720; BMA10247_A1942.
GeneIDi4889654.
KEGGibmn:BMA10247_A1942.
PATRICi19141485. VBIBurMal96640_1812.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000547 Genomic DNA. Translation: ABO03720.1 .
RefSeqi YP_001079119.1. NC_009079.1.

3D structure databases

ProteinModelPortali A3MFT3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 320389.BMA10247_A1942.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABO03720 ; ABO03720 ; BMA10247_A1942 .
GeneIDi 4889654.
KEGGi bmn:BMA10247_A1942.
PATRICi 19141485. VBIBurMal96640_1812.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109650.
KOi K02492.
OMAi HEVTGEY.
OrthoDBi EOG6C2WN5.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci BMAL320389:GH97-5461-MONOMER.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_00087. Glu_tRNA_reductase.
InterProi IPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view ]
Pfami PF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMi SSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsi TIGR01035. hemA. 1 hit.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. DeShazer D., Woods D.E., Nierman W.C.
    Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NCTC 10247.

Entry informationi

Entry nameiHEM1_BURM7
AccessioniPrimary (citable) accession number: A3MFT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 3, 2007
Last modified: October 1, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA.UniRule annotation

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3