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B0R6C0

- HEM1_HALS3

UniProt

B0R6C0 - HEM1_HALS3

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Protein
Glutamyl-tRNA reductase
Gene
hemA, OE_3496R
Organism
Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)
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 sitei53 – 531Nucleophile 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 bindingi184 – 1896NADP 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

BioCyciHSAL478009:GJVF-1440-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:OE_3496R
OrganismiHalobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)
Taxonomic identifieri478009 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHalobacterium
ProteomesiUP000001321: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 436436Glutamyl-tRNA reductaseUniRule annotation
PRO_1000093142Add
BLAST

Proteomic databases

PRIDEiB0R6C0.

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi478009.OE3496R.

Structurei

3D structure databases

ProteinModelPortaliB0R6C0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni52 – 554Substrate 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.
HOGENOMiHOG000109651.
KOiK02492.
OMAiYREADAN.

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.

B0R6C0-1 [UniParc]FASTAAdd to Basket

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MNGNTGVVSG VRVSHETASL DELAAASAAS TEAALDALLE QPPVEEAFVL    50
QTCHRVEAYV VTADQASGRR ALGGAGFNPA GGGAISMGHE DSLRHLLRVA 100
AGLESLVVGE DQILGQLRDA YDAAKDAGGI DHVLREAVTK AMHVGERART 150
ETAINEGATS LGTAAVRLAE RKTQLADARA VVVGAGEMGA LAAKAFASAT 200
VAEIVIANRT PARAVRVADM VSVPAEATTL ADARGRLDAA DVVVTATGSP 250
EHVLPASAFA DAGDTVVVDL AQPRDVAPGA GGHDGVAVHD LDDLEAVTAA 300
TRERREDAAR EVEAMIETEF ERLLTQYKRK RADEVIARMY ESADRLKSRE 350
VQTAVHRLEA ESGSLSADER EVVESMADAL VSQLLAAPTK SLRDAAAEDD 400
WSTIATALEL FNPEFEDGMP FDASRGGDAA SAESED 436
Length:436
Mass (Da):45,450
Last modified:April 8, 2008 - v1
Checksum:i3016F114705F6987
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM774415 Genomic DNA. Translation: CAP14289.1.
RefSeqiYP_001689635.1. NC_010364.1.

Genome annotation databases

EnsemblBacteriaiCAP14289; CAP14289; OE_3496R.
GeneIDi5953600.
KEGGihsl:OE3496R.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM774415 Genomic DNA. Translation: CAP14289.1 .
RefSeqi YP_001689635.1. NC_010364.1.

3D structure databases

ProteinModelPortali B0R6C0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 478009.OE3496R.

Proteomic databases

PRIDEi B0R6C0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAP14289 ; CAP14289 ; OE_3496R .
GeneIDi 5953600.
KEGGi hsl:OE3496R.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
KOi K02492.
OMAi YREADAN.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci HSAL478009:GJVF-1440-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. "Evolution in the laboratory: the genome of Halobacterium salinarum strain R1 compared to that of strain NRC-1."
    Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K., Ruepp A., Soppa J., Tittor J., Oesterhelt D.
    Genomics 91:335-346(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29341 / DSM 671 / R1.

Entry informationi

Entry nameiHEM1_HALS3
AccessioniPrimary (citable) accession number: B0R6C0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: September 3, 2014
This is version 53 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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