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B2VEH8

- HEM1_ERWT9

UniProt

B2VEH8 - HEM1_ERWT9

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Protein
Glutamyl-tRNA reductase
Gene
hemA, ETA_18800
Organism
Erwinia tasmaniensis (strain DSM 17950 / Et1/99)
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 sitei50 – 501Nucleophile By similarity
Sitei99 – 991Important for activity By similarity
Binding sitei109 – 1091Substrate By similarity
Binding sitei120 – 1201Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi189 – 1946NADP By similarity

GO - Molecular functioni

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

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

BioCyciETAS465817:GI36-1943-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:ETA_18800
OrganismiErwinia tasmaniensis (strain DSM 17950 / Et1/99)
Taxonomic identifieri338565 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeErwinia
ProteomesiUP000001726: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 418418Glutamyl-tRNA reductaseUniRule annotation
PRO_1000093135Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi465817.ETA_18800.

Structurei

3D structure databases

ProteinModelPortaliB2VEH8.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni114 – 1163Substrate 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.
HOGENOMiHOG000109650.
KOiK02492.
OMAiLAHKLTN.
OrthoDBiEOG6MWNBM.

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.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B2VEH8-1 [UniParc]FASTAAdd to Basket

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MTLLALGINH KTAPVALRER VTFTPDTLEQ ALNSLMAQPL IQGGVVLSTC    50
NRTELYLSVE QQENLQDQLI AWLCDYHQLS PDEVLKSLYW HHGNEAVSHL 100
MRVASGLDSL VLGEPQILGQ VKKAFADSQR GHSLSGELER MFQKSFSVAK 150
RVRTETEIGA SAVSVAFAAC TLARQIFESL TTVNVLLVGA GETIELAARH 200
LHQHKVKKLM IANRTRERAQ VLAAEVEAEV ISLADIDERL AEADIIISST 250
ASPLPIIGKG MVERALKKRR NQPMLLVDIA VPRDVEPDVG KLPNAYLYSV 300
DDLQAIIESN MAQRQAAAVE AETIVVQESS DFMSWLRAQS AVETIREYRA 350
QADEARAELE ARAIQSLQQG ADAEKVLRDL AHKLTNRLIH APTKSLQQAA 400
RDGDGERLQI LRDGLGLE 418
Length:418
Mass (Da):46,078
Last modified:July 1, 2008 - v1
Checksum:i120A00FEEF8C7ABE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU468135 Genomic DNA. Translation: CAO96926.1.
RefSeqiYP_001907813.1. NC_010694.1.

Genome annotation databases

EnsemblBacteriaiCAO96926; CAO96926; ETA_18800.
GeneIDi6299659.
KEGGieta:ETA_18800.
PATRICi20429597. VBIErwTas9546_1967.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU468135 Genomic DNA. Translation: CAO96926.1 .
RefSeqi YP_001907813.1. NC_010694.1.

3D structure databases

ProteinModelPortali B2VEH8.
ModBasei Search...

Protein-protein interaction databases

STRINGi 465817.ETA_18800.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAO96926 ; CAO96926 ; ETA_18800 .
GeneIDi 6299659.
KEGGi eta:ETA_18800.
PATRICi 20429597. VBIErwTas9546_1967.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109650.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci ETAS465817:GI36-1943-MONOMER.

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.
TIGRFAMsi TIGR01035. hemA. 1 hit.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic bacterium in the genus Erwinia."
    Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R., Geider K.
    Environ. Microbiol. 10:2211-2222(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 17950 / Et1/99.

Entry informationi

Entry nameiHEM1_ERWT9
AccessioniPrimary (citable) accession number: B2VEH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: September 3, 2014
This is version 47 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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