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Q1IWG2

- HEM1_DEIGD

UniProt

Q1IWG2 - HEM1_DEIGD

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Deinococcus geothermalis (strain DSM 11300)
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).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 sitei54 – 541NucleophileUniRule annotation
Sitei95 – 951Important for activityUniRule annotation
Binding sitei105 – 1051SubstrateUniRule annotation
Binding sitei116 – 1161SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi185 – 1906NADPUniRule 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

BioCyciDGEO319795:GHMU-2176-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:Dgeo_2128
OrganismiDeinococcus geothermalis (strain DSM 11300)
Taxonomic identifieri319795 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
ProteomesiUP000002431: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 349349Glutamyl-tRNA reductasePRO_0000335027Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi319795.Dgeo_2128.

Structurei

3D structure databases

ProteinModelPortaliQ1IWG2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 564Substrate bindingUniRule annotation
Regioni110 – 1123Substrate 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.
HOGENOMiHOG000109651.
KOiK02492.
OrthoDBiEOG6MWNBM.

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]
PIRSFiPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMiSSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q1IWG2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPPLAPLDFA VIGLNHQTAP VEVREQAAVR AGDEGKVLQH LSRYAREVML
60 70 80 90 100
LNTCNRTEVY LAGLQGDPLR AFESGWGRAL DGHLYVHRGE AAATHLYRVA
110 120 130 140 150
AGLDSLVIGE TQIQGQVKRA WQEAHARGLS GTLLNKVAQG ALAAGKRVRS
160 170 180 190 200
ETGLSDKVVS VSSAAVELAE AALGELRHRT ALILGAGETA ELTLTHLRAA
210 220 230 240 250
GVQDVIVVNR TEARARQLAD KLGGRACAAE YLHEVLPEAD VVIASSAAPH
260 270 280 290 300
YVLHGEGVRA ALAKRPERPI FLIDISVPRI LDPDIRAVSG AHLYNLDDLT
310 320 330 340
AIVSRNLQSR RAALPYAEAI IREAVADLLR WHLTREAQLG RRAVALASD
Length:349
Mass (Da):37,531
Last modified:May 20, 2008 - v2
Checksum:i9B1FA1D2703A99E9
GO

Sequence cautioni

The sequence ABF46422.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000359 Genomic DNA. Translation: ABF46422.1. Different initiation.
RefSeqiYP_605591.1. NC_008025.1.

Genome annotation databases

EnsemblBacteriaiABF46422; ABF46422; Dgeo_2128.
GeneIDi4058863.
KEGGidge:Dgeo_2128.
PATRICi21626231. VBIDeiGeo41128_2727.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000359 Genomic DNA. Translation: ABF46422.1 . Different initiation.
RefSeqi YP_605591.1. NC_008025.1.

3D structure databases

ProteinModelPortali Q1IWG2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 319795.Dgeo_2128.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABF46422 ; ABF46422 ; Dgeo_2128 .
GeneIDi 4058863.
KEGGi dge:Dgeo_2128.
PATRICi 21626231. VBIDeiGeo41128_2727.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
KOi K02492.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci DGEO319795:GHMU-2176-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 ]
PIRSFi PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMi SSF69742. SSF69742. 1 hit.
TIGRFAMsi TIGR01035. hemA. 1 hit.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 11300.

Entry informationi

Entry nameiHEM1_DEIGD
AccessioniPrimary (citable) accession number: Q1IWG2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: October 1, 2014
This is version 73 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3