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Q97B68

- HEM1_THEVO

UniProt

Q97B68 - HEM1_THEVO

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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: 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

Pathwayi

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

  1. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
  2. NADP binding Source: InterPro

GO - Biological processi

  1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
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: 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 – 15612
Beta strandi160 – 1645
Helixi168 – 1736
Helixi174 – 1763
Turni179 – 1813
Beta strandi183 – 1897
Helixi191 – 20111
Beta strandi204 – 2074
Helixi211 – 2166
Beta strandi219 – 2235
Helixi234 – 2363
Beta strandi242 – 2454
Beta strandi258 – 2603
Helixi261 – 27414

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiEHMIEDE.

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
BA000011 Genomic DNA. Translation: BAB59732.1 .
RefSeqi NP_111109.1. NC_002689.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3OJ0 X-ray 1.65 A 141-281 [» ]
ProteinModelPortali Q97B68.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 273116.TVN0590.

Protocols and materials databases

DNASUi 1441696.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB59732 ; BAB59732 ; BAB59732 .
GeneIDi 1441696.
KEGGi tvo:TVN0590.

Phylogenomic databases

eggNOGi COG0373.
KOi K02492.
OMAi EHMIEDE.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci TVOL273116:GC31-614-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q97B68.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_00087. Glu_tRNA_reductase.
InterProi IPR000343. 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 ]
Pfami PF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMi SSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 1, 2014
This is version 91 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