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A4WJE1

- HEM11_PYRAR

UniProt

A4WJE1 - HEM11_PYRAR

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Protein
Glutamyl-tRNA reductase 1
Gene
hemA1, Pars_0928
Organism
Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

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 sitei46 – 461Nucleophile By similarity
Sitei86 – 861Important for activity By similarity
Binding sitei96 – 961Substrate By similarity
Binding sitei107 – 1071Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi175 – 1806NADP 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

BioCyciPARS340102:GHGQ-939-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase 1 (EC:1.2.1.70)
Short name:
GluTR 1
Gene namesi
Name:hemA1
Ordered Locus Names:Pars_0928
OrganismiPyrobaculum arsenaticum (strain DSM 13514 / JCM 11321)
Taxonomic identifieri340102 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum
ProteomesiUP000001567: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 387387Glutamyl-tRNA reductase 1UniRule annotation
PRO_0000335096Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi340102.Pars_0928.

Structurei

3D structure databases

ProteinModelPortaliA4WJE1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 484Substrate binding By similarity
Regioni101 – 1033Substrate 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.
HOGENOMiHOG000112880.
KOiK02492.
OMAiVANGVHR.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
SUPFAMiSSF69742. SSF69742. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A4WJE1-1 [UniParc]FASTAAdd to Basket

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MDLVNGLVAL SLTHKELGVD ELSKVANGVH RVCVSLRQPL FVLHTCNRVE    50
AYLYNPPDEV VEIVKSGYAP YVEKVVERRG VDAARHLFRV AAGLESMLIG 100
ETDVLGQLEE AFDRQVRAGY TRELLKTVVE RAIRVGKRVR TETGISRGPR 150
GLGSLSILYV KEKIDLTNAR VCVIGAGSVG RGLVKELIDA GARRLVVVNR 200
SVEKAADLGV EVWPLSERSV ERCLEDFDVV FTAVATFEPI IKSVPRDARV 250
RIIVDMGMPR NTAAGLPVEV VTIDSLRDLA DRFNAMRDAE IKKAEEIVEE 300
ELVALERLLR IRWVEEVSAK LLEYWFKIAE EEGERAGGLE AKIAARTTVK 350
RTLLPVVNYL KKVAVSDIDE AYRIISVLRL SYGLKDL 387
Length:387
Mass (Da):43,082
Last modified:May 29, 2007 - v1
Checksum:iD8AFB667A047C5FA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000660 Genomic DNA. Translation: ABP50508.1.
RefSeqiWP_011900415.1. NC_009376.1.
YP_001153160.1. NC_009376.1.

Genome annotation databases

EnsemblBacteriaiABP50508; ABP50508; Pars_0928.
GeneIDi5054302.
KEGGipas:Pars_0928.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000660 Genomic DNA. Translation: ABP50508.1 .
RefSeqi WP_011900415.1. NC_009376.1.
YP_001153160.1. NC_009376.1.

3D structure databases

ProteinModelPortali A4WJE1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 340102.Pars_0928.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABP50508 ; ABP50508 ; Pars_0928 .
GeneIDi 5054302.
KEGGi pas:Pars_0928.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000112880.
KOi K02492.
OMAi VANGVHR.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci PARS340102:GHGQ-939-MONOMER.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_00087. Glu_tRNA_reductase.
InterProi IPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view ]
Pfami PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view ]
SUPFAMi SSF69742. SSF69742. 1 hit.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 13514 / JCM 11321.

Entry informationi

Entry nameiHEM11_PYRAR
AccessioniPrimary (citable) accession number: A4WJE1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 29, 2007
Last modified: September 3, 2014
This is version 58 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

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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