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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium acetobutylicum)
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 sitei46NucleophileUniRule annotation1
Sitei91Important for activityUniRule annotation1
Binding sitei101SubstrateUniRule annotation1
Binding sitei112SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi177 – 182NADPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processPorphyrin biosynthesis
LigandNADP

Enzyme and pathway databases

BioCyciCBEI290402:G1G93-1360-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:Cbei_1283
OrganismiClostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium acetobutylicum)
Taxonomic identifieri290402 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
Proteomesi
  • UP000000565 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000754041 – 401Glutamyl-tRNA reductaseAdd BLAST401

Proteomic databases

PRIDEiA6LSY3

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi290402.Cbei_1283

Structurei

3D structure databases

ProteinModelPortaliA6LSY3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni45 – 48Substrate bindingUniRule annotation4
Regioni106 – 108Substrate 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
HOGENOMiHOG000090159
KOiK02492
OMAiFAFKCAA
OrthoDBiPOG091H05DA

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
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
SSF69742 SSF69742, 1 hit
TIGRFAMsiTIGR01035 hemA, 1 hit
PROSITEiView protein in PROSITE
PS00747 GLUTR, 1 hit

Sequencei

Sequence statusi: Complete.

A6LSY3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIGLIGIRKN TPLEIREKFI VKSKKYNEYF GELLKELNEV VILATCNRTE
60 70 80 90 100
IYFNASLNEE ELLKKIFDIF NWDYEYKKYV FITNNKDAYR HLFEVCSGFH
110 120 130 140 150
SKILGEDQIL GQVKDAYEEA LEFKAVSLEL HRLFQEAITC GKRFRKEAKL
160 170 180 190 200
FEIPVSSSSI VVSEAIKREC TKFMVLGYGE VGQLVMKYLL SHKIQTVYLV
210 220 230 240 250
VRNPKIKDEI QDERVKVITF EEKNKYINSI ECIISCTSAP HPVVKTEDIS
260 270 280 290 300
ESGSRLVIYD LSVPRDVEKE VALLSRTEVY NIDTISRIDD ENKKLRKDKM
310 320 330 340 350
EDNRHIMNKY LKEYDEWLKL RSISHVIKNL KTVGNDVYEK RVQTFSHKSK
360 370 380 390 400
DKNDIALAHK LIKSTSDFYI NRAIEVIKEE TLKGCGEEWI GIIEKIFMTK

E
Length:401
Mass (Da):46,919
Last modified:July 24, 2007 - v1
Checksum:i813E3FA143D8A58A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000721 Genomic DNA Translation: ABR33463.1
RefSeqiWP_011968617.1, NC_009617.1

Genome annotation databases

EnsemblBacteriaiABR33463; ABR33463; Cbei_1283
KEGGicbe:Cbei_1283

Similar proteinsi

Entry informationi

Entry nameiHEM1_CLOB8
AccessioniPrimary (citable) accession number: A6LSY3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: July 24, 2007
Last modified: March 28, 2018
This is version 81 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

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