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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432)
Status
Reviewed-Annotation score: 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 sitei49 – 491NucleophileUniRule annotation
Sitei114 – 1141Important for activityUniRule annotation
Binding sitei124 – 1241SubstrateUniRule annotation
Binding sitei135 – 1351SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi204 – 2096NADPUniRule 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

BioCyciBCAV471853:GI1Z-4062-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:Bcav_4009
OrganismiBeutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432)
Taxonomic identifieri471853 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeBeutenbergiaceaeBeutenbergia
ProteomesiUP000007962: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 441441Glutamyl-tRNA reductasePRO_1000202630Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi471853.Bcav_4009.

Structurei

3D structure databases

ProteinModelPortaliC5C5B0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 514Substrate bindingUniRule annotation
Regioni129 – 1313Substrate 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.
HOGENOMiHOG000109649.
KOiK02492.
OMAiEHAPAEH.
OrthoDBiEOG6MWNBM.

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. 2 hits.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

C5C5B0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLLSVSASHR DADLADLERL SSGVGRVWAD APLVAHGLDG AGVVLLATCN
60 70 80 90 100
RFEVYLDVAD GTDPQRALAV VRDLVRTVPE SPLAAPGADD DAAGPGPDPS
110 120 130 140 150
AALRVRVGDD AARHLFGVAS GLDSIVVGER EIAGQVRRAI AAARRAGTTT
160 170 180 190 200
GALERLFAQA QRTSRAVEAG TGLAAAGRSV VGVALDLAAR SAPPWPLARV
210 220 230 240 250
VLIGTGSYAG ASLAALRARG CTDVRVHSES GRAEEFARAR EAEAVPPGEL
260 270 280 290 300
LTAIADADVV VSCRGSVRPV LDAAAVAGAR AAAERRAEER AGHAVGTAVQ
310 320 330 340 350
PRPLVVVDLA LHRDVDPAVG SVDGVELLDL GTIRAHAPAA ATRDVERARE
360 370 380 390 400
IVDDAVAQHA LVRAAREMDP AITRLRGRVR EVLDAEVGRL PVGPVSREDA
410 420 430 440
ERALHRLAAT LAHAPTEAAR EAARAGRGEE YVEALRLLFP D
Length:441
Mass (Da):45,703
Last modified:July 28, 2009 - v1
Checksum:i0AF8243E92066449
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001618 Genomic DNA. Translation: ACQ82250.1.
RefSeqiYP_002884012.1. NC_012669.1.

Genome annotation databases

EnsemblBacteriaiACQ82250; ACQ82250; Bcav_4009.
GeneIDi7861107.
KEGGibcv:Bcav_4009.
PATRICi21098740. VBIBeuCav91323_4061.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001618 Genomic DNA. Translation: ACQ82250.1.
RefSeqiYP_002884012.1. NC_012669.1.

3D structure databases

ProteinModelPortaliC5C5B0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi471853.Bcav_4009.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACQ82250; ACQ82250; Bcav_4009.
GeneIDi7861107.
KEGGibcv:Bcav_4009.
PATRICi21098740. VBIBeuCav91323_4061.

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109649.
KOiK02492.
OMAiEHAPAEH.
OrthoDBiEOG6MWNBM.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316.
BioCyciBCAV471853:GI1Z-4062-MONOMER.

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. 2 hits.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-8 / DSM 12333 / NBRC 16432.

Entry informationi

Entry nameiHEM1_BEUC1
AccessioniPrimary (citable) accession number: C5C5B0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: January 7, 2015
This is version 45 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.