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A2BJB7

- HEM1_HYPBU

UniProt

A2BJB7 - HEM1_HYPBU

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Hyperthermus butylicus (strain DSM 5456 / JCM 9403)
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 sitei50 – 501NucleophileUniRule annotation
Sitei89 – 891Important for activityUniRule annotation
Binding sitei99 – 991SubstrateUniRule annotation
Binding sitei110 – 1101SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi179 – 1846NADPUniRule 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

BioCyciHBUT415426:GC56-206-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:Hbut_0206
OrganismiHyperthermus butylicus (strain DSM 5456 / JCM 9403)
Taxonomic identifieri415426 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesPyrodictiaceaeHyperthermus
ProteomesiUP000002593: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 411411Glutamyl-tRNA reductasePRO_0000335089Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi415426.Hbut_0206.

Structurei

3D structure databases

ProteinModelPortaliA2BJB7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni104 – 1063Substrate 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.
KOiK02492.
OMAiEHMIEDE.

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.
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.

Sequencei

Sequence statusi: Complete.

A2BJB7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPRLLEELTA VILTHRDAPL DVVGSFESRV GEAYQILRGV VDEAVVLATC
60 70 80 90 100
NRFEVYALPR RGFVETVIGF LGEASRYARI LHGMDVVRHL FRVAAGLESA
110 120 130 140 150
IIGENEILGQ VARAYEEARR RGVAGKYLGL LFSQAVRTGK LVRSRTRISY
160 170 180 190 200
GNVGAPGAAV KLAREAAGGF DGKHVVVVGA GEAGSIMASL VREEAPTARI
210 220 230 240 250
SIVNRSVDRA RELAGKVRGE AYGLDMLPKL LAAADVVLVA VTVNEPVIKR
260 270 280 290 300
SMLEDVGRHL VVVDISNPPA VEQPIPSNVY YAGLRDVEKV IKEVLAVRIR
310 320 330 340 350
EVPKAEAIVE EQVALLRKLW LKRGADEAIA EIMRYANRVM EEEVEELVSR
360 370 380 390 400
LRGLGVDGAA LLVARSFAYS LTKKLLRPLI LYAHEAALEG SLSKLEEIAQ
410
KYRDELARRQ H
Length:411
Mass (Da):45,007
Last modified:February 20, 2007 - v1
Checksum:iC744C393B3D4C4FE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000493 Genomic DNA. Translation: ABM80078.1.
RefSeqiYP_001012423.1. NC_008818.1.

Genome annotation databases

EnsemblBacteriaiABM80078; ABM80078; Hbut_0206.
GeneIDi4782332.
KEGGihbu:Hbut_0206.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000493 Genomic DNA. Translation: ABM80078.1 .
RefSeqi YP_001012423.1. NC_008818.1.

3D structure databases

ProteinModelPortali A2BJB7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 415426.Hbut_0206.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABM80078 ; ABM80078 ; Hbut_0206 .
GeneIDi 4782332.
KEGGi hbu:Hbut_0206.

Phylogenomic databases

eggNOGi COG0373.
KOi K02492.
OMAi EHMIEDE.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci HBUT415426:GC56-206-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.
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.
ProtoNeti Search...

Publicationsi

  1. "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C."
    Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M., She Q., Garrett R.A., Klenk H.-P.
    Archaea 2:127-135(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 5456 / JCM 9403.

Entry informationi

Entry nameiHEM1_HYPBU
AccessioniPrimary (citable) accession number: A2BJB7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 20, 2007
Last modified: October 29, 2014
This is version 66 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, Reference proteome

Documents

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

External Data

Dasty 3