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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii)
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: protoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamyl-tRNA reductase (hemA)
  2. Glutamate-1-semialdehyde 2,1-aminomutase (hemL)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu), the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei50NucleophileUniRule annotation1
Sitei99Important for activityUniRule annotation1
Binding sitei109SubstrateUniRule annotation1
Binding sitei120SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi189 – 194NADPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

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:ESA_01496
OrganismiCronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii)
Taxonomic identifieri290339 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeCronobacter
Proteomesi
  • UP000000260 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003350291 – 418Glutamyl-tRNA reductaseAdd BLAST418

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi290339.ESA_01496.

Structurei

3D structure databases

ProteinModelPortaliA7MKC0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni49 – 52Substrate bindingUniRule annotation4
Regioni114 – 116Substrate bindingUniRule annotation3

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

eggNOGiENOG4105C7E. Bacteria.
COG0373. LUCA.
HOGENOMiHOG000109650.
KOiK02492.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase. 1 hit.
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.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A7MKC0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLLALGINH KTAPVSLRER VTFSPDTLDQ ALESLLSQPM VQGGVVLSTC
60 70 80 90 100
NRTELYLSVE EQDNLHDKLV RWLCDYHNLD EEEVRNSLYW HHDNDAVSHL
110 120 130 140 150
MRVASGLDSL VLGEPQILGQ VKKAFADSGR GHANASELER MFQKSFSVAK
160 170 180 190 200
RVRTETDIGA SAVSVAFAAC TLARQIFESL STVTVMLVGA GETIELAARH
210 220 230 240 250
LREHNVQKMI IANRTRERAQ RLADEVGAEV IGLGDIDERL KDADIIISST
260 270 280 290 300
ASPLPIIGKG MMERALKARR NQPMLLVDIA VPRDVEPEVG KLANAYLYSV
310 320 330 340 350
DDLQSIIQHN LAQRKAAAVQ AESIVEQEAC EFMAWLRAQS VSETIREYRA
360 370 380 390 400
QADQVREELT SKALAALRTG GDAEAIMQDL ARKLTNRLIH TPTKSLQQAA
410
RDGDDERLHI LRNSLGLE
Length:418
Mass (Da):46,312
Last modified:May 20, 2008 - v2
Checksum:i95E16F973C273DFD
GO

Sequence cautioni

The sequence ABU76754 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000783 Genomic DNA. Translation: ABU76754.1. Different initiation.
RefSeqiWP_004386063.1. NC_009778.1.

Genome annotation databases

EnsemblBacteriaiABU76754; ABU76754; ESA_01496.
GeneIDi5549361.
KEGGiesa:ESA_01496.
PATRICi20395071. VBICroSak107175_1327.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000783 Genomic DNA. Translation: ABU76754.1. Different initiation.
RefSeqiWP_004386063.1. NC_009778.1.

3D structure databases

ProteinModelPortaliA7MKC0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi290339.ESA_01496.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABU76754; ABU76754; ESA_01496.
GeneIDi5549361.
KEGGiesa:ESA_01496.
PATRICi20395071. VBICroSak107175_1327.

Phylogenomic databases

eggNOGiENOG4105C7E. Bacteria.
COG0373. LUCA.
HOGENOMiHOG000109650.
KOiK02492.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase. 1 hit.
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.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHEM1_CROS8
AccessioniPrimary (citable) accession number: A7MKC0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: November 2, 2016
This is version 62 of the entry and version 2 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

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 one 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.