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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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 sitei49NucleophileUniRule annotation1
Sitei79Important for activityUniRule annotation1
Binding sitei89SubstrateUniRule annotation1
Binding sitei100SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi165 – 170NADPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processPorphyrin biosynthesis
LigandNADP

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:TV0590
ORF Names:TVG0579613
OrganismiThermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
Taxonomic identifieri273116 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma
Proteomesi
  • UP000001017 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001141131 – 409Glutamyl-tRNA reductaseAdd BLAST409

Proteomic databases

PRIDEiQ97B68

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi273116.TVN0590

Structurei

Secondary structure

1409
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi145 – 156Combined sources12
Beta strandi160 – 164Combined sources5
Helixi168 – 173Combined sources6
Helixi174 – 176Combined sources3
Turni179 – 181Combined sources3
Beta strandi183 – 189Combined sources7
Helixi191 – 201Combined sources11
Beta strandi204 – 207Combined sources4
Helixi211 – 216Combined sources6
Beta strandi219 – 223Combined sources5
Helixi234 – 236Combined sources3
Beta strandi242 – 245Combined sources4
Beta strandi258 – 260Combined sources3
Helixi261 – 274Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3OJ0X-ray1.65A141-281[»]
ProteinModelPortaliQ97B68
SMRiQ97B68
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ97B68

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni48 – 51Substrate bindingUniRule annotation4
Regioni94 – 96Substrate 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

eggNOGiarCOG01036 Archaea
COG0373 LUCA
KOiK02492
OMAiYGSATCE
OrthoDBiPOG093Z06M3

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
PROSITEiView protein in PROSITE
PS00747 GLUTR, 1 hit

Sequencei

Sequence statusi: Complete.

Q97B68-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLMNIVTLIS WDFKRNNESF QRAIINGYDY WSRILDDHGV EKYVILLTCN
60 70 80 90 100
RVELYYRGDP FDVQEKGYNI ISDDMAINHL FHVAAGLDSM SIGENEVLKQ
110 120 130 140 150
VKQAYEKSSS MGKSDKFLSL IFQRAISVGK LVRSKTGIGK GKVSIPSIVY
160 170 180 190 200
DIVRKNGGNK ILLVGNGMLA SEIAPYFSYP QYKVTVAGRN IDHVRAFAEK
210 220 230 240 250
YEYEYVLIND IDSLIKNNDV IITATSSKTP IVEERSLMPG KLFIDLGNPP
260 270 280 290 300
NIERGNNVIT LDEIYEISKK NEMLREEKIN QAEILIENEM KATMNKIKDL
310 320 330 340 350
MIDDIFSQFY RFASVVQTME IQKFRKMHPE VNENDLEALA HSIINKILNV
360 370 380 390 400
PVTTLKAVSR SQGNSDFNRL FESFSSNFND IVSAALQSYE GLRDTQSLRD

RTRQLLQKS
Length:409
Mass (Da):46,691
Last modified:October 1, 2001 - v1
Checksum:i8CF23510B233D830
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000011 Genomic DNA Translation: BAB59732.1

Genome annotation databases

EnsemblBacteriaiBAB59732; BAB59732; BAB59732
KEGGitvo:TVG0579613

Similar proteinsi

Entry informationi

Entry nameiHEM1_THEVO
AccessioniPrimary (citable) accession number: Q97B68
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: October 1, 2001
Last modified: May 23, 2018
This is version 111 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

3D-structure, Complete proteome

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