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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Escherichia coli M114
Status
Unreviewed-Annotation score: -Protein inferred from homologyi

Functioni

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

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

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.Imported

Catalytic activityi

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.UniRule annotationSAAS 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 annotationSAAS 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 sitei73NucleophileUniRule annotation1
Sitei122Important for activityUniRule annotation1
Binding sitei132SubstrateUniRule annotation1
Binding sitei143SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi212 – 217NADPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductaseUniRule annotationSAAS annotation
Biological processPorphyrin biosynthesisUniRule annotationSAAS annotation
LigandNADPUniRule annotationSAAS annotation

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductaseUniRule annotationSAAS annotation (EC:1.2.1.70UniRule annotationSAAS annotation)
Short name:
GluTRUniRule annotation
Gene namesi
Name:hemAUniRule annotation
ORF Names:ERYG_04412Imported
OrganismiEscherichia coli M114Imported
Taxonomic identifieri656416 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000037133 Componenti: Unassembled WGS sequence

Interactioni

Subunit structurei

Homodimer.UniRule annotationSAAS annotation

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini29 – 179GlutR_NInterPro annotationAdd BLAST151
Domaini195 – 329Shikimate_DHInterPro annotationAdd BLAST135
Domaini343 – 439GlutR_dimerInterPro annotationAdd BLAST97

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni72 – 75Substrate bindingUniRule annotation4
Regioni137 – 139Substrate bindingUniRule annotation3

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili361 – 381Sequence analysisAdd BLAST21

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 annotationSAAS annotation

Keywords - Domaini

Coiled coilSequence analysis

Family and domain databases

Gene3Di3.30.460.30, 1 hit
HAMAPiMF_00087 Glu_tRNA_reductase, 1 hit
InterProiView protein in InterPro
IPR000343 4pyrrol_synth_GluRdtase
IPR015896 4pyrrol_synth_GluRdtase_dimer
IPR015895 4pyrrol_synth_GluRdtase_N
IPR018214 GluRdtase_CS
IPR036453 GluRdtase_dimer_dom_sf
IPR036343 GluRdtase_N_sf
IPR036291 NAD(P)-bd_dom_sf
IPR006151 Shikm_DH/Glu-tRNA_Rdtase
PfamiView protein in Pfam
PF00745 GlutR_dimer, 1 hit
PF05201 GlutR_N, 1 hit
PF01488 Shikimate_DH, 1 hit
PIRSFiPIRSF000445 4pyrrol_synth_GluRdtase, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
SSF69075 SSF69075, 1 hit
SSF69742 SSF69742, 1 hit
TIGRFAMsiTIGR01035 hemA, 1 hit
PROSITEiView protein in PROSITE
PS00747 GLUTR, 1 hit

Sequencei

Sequence statusi: Complete.

A0A0K9T6B7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MILRILYDAS RLTLSTLVLF PADMTLLALG INHKTAPVSL RERVSFSPDK
60 70 80 90 100
LDQALDSLLA QPMVQGGVVL STCNRTELYL SVEEQDNLQE ALIRWLCDYH
110 120 130 140 150
NLNEEDLRKS LYWHQDNDAV SHLMRVASGL DSLVLGEPQI LGQVKKAFAD
160 170 180 190 200
SQKGHMKASE LERMFQKSFS VAKRVRTETD IGASAVSVAF AACTLARQIF
210 220 230 240 250
ESLSTVTVLL VGAGETIELV ARHLREHKVQ KMIIANRTRE RAQILADEVG
260 270 280 290 300
AEVIALSDID ERLREADIII SSTASPLPII GKGMVERALK SRRNQPMLLV
310 320 330 340 350
DIAVPRDVEP EVGKLANAYL YSVDDLQSII SHNLAQRKAA AVEAETIVAQ
360 370 380 390 400
ETSEFMAWLR AQSASETIRE YRSQAEQVRD ELTAKALAAL EQGGDAQAIM
410 420 430 440
QDLAWKLTNR LIHAPTKSLQ QAARDGDNER LNILRDSLGL E
Length:441
Mass (Da):48,911
Last modified:November 11, 2015 - v1
Checksum:i95164B272B0E2C8E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AEMV01000070 Genomic DNA Translation: KNA39615.1

Genome annotation databases

EnsemblBacteriaiKNA39615; KNA39615; ERYG_04412
PATRICifig|656416.3.peg.4691

Similar proteinsi

Entry informationi

Entry nameiA0A0K9T6B7_ECOLX
AccessioniPrimary (citable) accession number: A0A0K9T6B7
Entry historyiIntegrated into UniProtKB/TrEMBL: November 11, 2015
Last sequence update: November 11, 2015
Last modified: March 28, 2018
This is version 18 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

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