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Q97B68

- HEM1_THEVO

UniProt

Q97B68 - HEM1_THEVO

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Protein
Glutamyl-tRNA reductase
Gene
hemA, TV0590, TVG0579613
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) By similarity.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 – 491Nucleophile By similarity
Sitei79 – 791Important for activity By similarity
Binding sitei89 – 891Substrate By similarity
Binding sitei100 – 1001Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi165 – 1706NADP By similarity

GO - Molecular functioni

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

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 reductase (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:hemA
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 reductaseUniRule annotation
PRO_0000114113Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi273116.TVN0590.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ97B68.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 514Substrate binding By similarity
Regioni94 – 963Substrate binding By similarity

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 By similarity.UniRule annotation

Sequence similaritiesi

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

MLMNIVTLIS WDFKRNNESF QRAIINGYDY WSRILDDHGV EKYVILLTCN    50
RVELYYRGDP FDVQEKGYNI ISDDMAINHL FHVAAGLDSM SIGENEVLKQ 100
VKQAYEKSSS MGKSDKFLSL IFQRAISVGK LVRSKTGIGK GKVSIPSIVY 150
DIVRKNGGNK ILLVGNGMLA SEIAPYFSYP QYKVTVAGRN IDHVRAFAEK 200
YEYEYVLIND IDSLIKNNDV IITATSSKTP IVEERSLMPG KLFIDLGNPP 250
NIERGNNVIT LDEIYEISKK NEMLREEKIN QAEILIENEM KATMNKIKDL 300
MIDDIFSQFY RFASVVQTME IQKFRKMHPE VNENDLEALA HSIINKILNV 350
PVTTLKAVSR SQGNSDFNRL FESFSSNFND IVSAALQSYE GLRDTQSLRD 400
RTRQLLQKS 409
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: September 3, 2014
This is version 90 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 By similarity.

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

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