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A5IED6

- HEM1_LEGPC

UniProt

A5IED6 - HEM1_LEGPC

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Protein
Glutamyl-tRNA reductase
Gene
hemA, LPC_1803
Organism
Legionella pneumophila (strain Corby)
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
Sitei95 – 951Important for activity By similarity
Binding sitei105 – 1051Substrate By similarity
Binding sitei116 – 1161Substrate By similarity

Regions

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

BioCyciLPNE400673:GCIT-2460-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:LPC_1803
OrganismiLegionella pneumophila (strain Corby)
Taxonomic identifieri400673 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella
ProteomesiUP000001569: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 424424Glutamyl-tRNA reductaseUniRule annotation
PRO_0000335049Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi400673.LPC_1803.

Structurei

3D structure databases

ProteinModelPortaliA5IED6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni110 – 1123Substrate 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.
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.
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.

Sequencei

Sequence statusi: Complete.

A5IED6-1 [UniParc]FASTAAdd to Basket

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MVFVACGLNH KTAPIHVREK VALQPAMQDS LLSSLLDLPE VNEAAILSTC    50
NRTEIYCDTN TPEVLGNWLA HEHQLSEELL SQFLYIHQGK EGIKHTLRVA 100
SGLDSMMIGE PQILGQMKQA YQHACRLGTV KTQLRPVFEY IFRASKRIRT 150
RSGIGANPVS IAYAAVQLIG QLFKNYHSLS VFLIGSGETA SLVAKYLHQH 200
GVHRFLIASR TLENAQKLAE TFGGKTLSIG DIPQYLPLAD VVISATACPL 250
PFINKSLVEH ALEQRNHAPM FLLDLAVPRD IEGNVNELEQ VHLYNVDDLQ 300
SMIEKGMNER RNAALQAEQL IESELDNYIR WHRSLRAKDV ICDYRNQMHT 350
LAQQELQRAL KKISAGQNQQ DVLNEFSMRL VNKLTHNPTI GLRQIAWDNR 400
EDLLDLARYL FDTTANQSLY EEIS 424
Length:424
Mass (Da):47,883
Last modified:May 20, 2008 - v2
Checksum:iF5463C08FE291233
GO

Sequence cautioni

The sequence ABQ55736.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000675 Genomic DNA. Translation: ABQ55736.1. Different initiation.
RefSeqiYP_001251082.1. NC_009494.2.

Genome annotation databases

EnsemblBacteriaiABQ55736; ABQ55736; LPC_1803.
GeneIDi5181611.
KEGGilpc:LPC_1803.
PATRICi22310125. VBILegPne45588_1877.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000675 Genomic DNA. Translation: ABQ55736.1 . Different initiation.
RefSeqi YP_001251082.1. NC_009494.2.

3D structure databases

ProteinModelPortali A5IED6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 400673.LPC_1803.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABQ55736 ; ABQ55736 ; LPC_1803 .
GeneIDi 5181611.
KEGGi lpc:LPC_1803.
PATRICi 22310125. VBILegPne45588_1877.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci LPNE400673:GCIT-2460-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.
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.
ProtoNeti Search...

Publicationsi

  1. "Identification and characterization of a new conjugation/ type IVA secretion system (trb/tra) of L. pneumophila Corby localized on a mobile genomic island."
    Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E., Steinert M., Buchrieser C., Hacker J., Heuner K.
    Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Corby.

Entry informationi

Entry nameiHEM1_LEGPC
AccessioniPrimary (citable) accession number: A5IED6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: May 14, 2014
This is version 57 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 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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