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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: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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

Pathway: 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei49 – 491NucleophileUniRule annotation
Sitei79 – 791Important for activityUniRule annotation
Binding sitei89 – 891SubstrateUniRule annotation
Binding sitei100 – 1001SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi165 – 1706NADPUniRule annotation

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

BioCyciTVOL273116:GC31-614-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:TV0590
ORF Names:TVG0579613
OrganismiThermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
Taxonomic identifieri273116 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma
ProteomesiUP000001017 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 409409Glutamyl-tRNA reductasePRO_0000114113Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi273116.TVN0590.

Structurei

Secondary structure

1
409
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi145 – 15612Combined sources
Beta strandi160 – 1645Combined sources
Helixi168 – 1736Combined sources
Helixi174 – 1763Combined sources
Turni179 – 1813Combined sources
Beta strandi183 – 1897Combined sources
Helixi191 – 20111Combined sources
Beta strandi204 – 2074Combined sources
Helixi211 – 2166Combined sources
Beta strandi219 – 2235Combined sources
Helixi234 – 2363Combined sources
Beta strandi242 – 2454Combined sources
Beta strandi258 – 2603Combined sources
Helixi261 – 27414Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ97B68.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 514Substrate bindingUniRule annotation
Regioni94 – 963Substrate bindingUniRule annotation

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

eggNOGiCOG0373.
KOiK02492.
OMAiMSIGENE.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase.
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.
SUPFAMiSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

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.
RefSeqiNP_111109.1. NC_002689.2.

Genome annotation databases

EnsemblBacteriaiBAB59732; BAB59732; BAB59732.
GeneIDi1441696.
KEGGitvo:TVN0590.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000011 Genomic DNA. Translation: BAB59732.1.
RefSeqiNP_111109.1. NC_002689.2.

3D structure databases

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

Protein-protein interaction databases

STRINGi273116.TVN0590.

Protocols and materials databases

DNASUi1441696.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB59732; BAB59732; BAB59732.
GeneIDi1441696.
KEGGitvo:TVN0590.

Phylogenomic databases

eggNOGiCOG0373.
KOiK02492.
OMAiMSIGENE.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316.
BioCyciTVOL273116:GC31-614-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ97B68.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase.
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.
SUPFAMiSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1.

Entry informationi

Entry nameiHEM1_THEVO
AccessioniPrimary (citable) accession number: Q97B68
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: October 1, 2001
Last modified: May 27, 2015
This is version 95 of the entry and version 1 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

3D-structure, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.