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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Streptococcus sanguinis (strain SK36)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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

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

Keywordsi

Molecular functionOxidoreductase
Biological processPorphyrin biosynthesis
LigandNADP

Enzyme and pathway databases

BioCyciSSAN388919:G1G6Q-503-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:SSA_0484
OrganismiStreptococcus sanguinis (strain SK36)
Taxonomic identifieri388919 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000002148 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000047061 – 417Glutamyl-tRNA reductaseAdd BLAST417

Proteomic databases

PRIDEiA3CL77

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi388919.SSA_0484

Structurei

3D structure databases

ProteinModelPortaliA3CL77
SMRiA3CL77
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
HOGENOMiHOG000109651
KOiK02492
OMAiFAFKCAA

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
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

Sequencei

Sequence statusi: Complete.

A3CL77-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHLLYVGLTH RETPLTILEK AHFSDQEGLK ALKLLKREKS ILENIILSTC
60 70 80 90 100
NRTELYLVVD QLHTGRYYSK HFLADWFQIP VKELEEYLVF REGDEALRHL
110 120 130 140 150
LRVSIGLESK IVGESQVLGQ LKQAFLTAQD AGTTGIVLNQ AFKQALTFAK
160 170 180 190 200
RMHDTYRIND RPISIGLTAI QELDRMGLDY STKKIAVIGL GEIGQLVTKY
210 220 230 240 250
ALQRPFESVM LLNRTVSKAQ AFLTEDRVSA HGWDELEEVL ADADVVFSAV
260 270 280 290 300
KTEEYIIFPS MLKEGAIVFD LCLPRSCHPS SSLKLYNIEN LTNQLEQYKA
310 320 330 340 350
ERQEIAGRIA LEIDEELVKF ADWRQQLGII PLIQEIRDKA LEAQASAMES
360 370 380 390 400
LNRKIPDLTE REQKQISKHM KSIINQVLKE PILQLKELSV GEHSDYDIAL
410
IAKIFGLHRE RGKDEGH
Length:417
Mass (Da):47,561
Last modified:March 20, 2007 - v1
Checksum:i91D4A9FFB2B8E0D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000387 Genomic DNA Translation: ABN43932.1
RefSeqiWP_011836538.1, NC_009009.1
YP_001034482.1, NC_009009.1

Genome annotation databases

EnsemblBacteriaiABN43932; ABN43932; SSA_0484
GeneIDi4806219
KEGGissa:SSA_0484
PATRICifig|388919.9.peg.468

Similar proteinsi

Entry informationi

Entry nameiHEM1_STRSV
AccessioniPrimary (citable) accession number: A3CL77
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 20, 2007
Last modified: May 23, 2018
This is version 91 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

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