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B0R6C0

- HEM1_HALS3

UniProt

B0R6C0 - HEM1_HALS3

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Protein

Glutamyl-tRNA reductase

Gene

hemA

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).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 – 531NucleophileUniRule annotation
Sitei95 – 951Important for activityUniRule annotation
Binding sitei105 – 1051SubstrateUniRule annotation
Binding sitei116 – 1161SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi184 – 1896NADPUniRule 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

BioCyciHSAL478009:GJVF-1440-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: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 reductasePRO_1000093142Add
BLAST

Proteomic databases

PRIDEiB0R6C0.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi478009.OE3496R.

Structurei

3D structure databases

ProteinModelPortaliB0R6C0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

« Hide

        10         20         30         40         50
MNGNTGVVSG VRVSHETASL DELAAASAAS TEAALDALLE QPPVEEAFVL
60 70 80 90 100
QTCHRVEAYV VTADQASGRR ALGGAGFNPA GGGAISMGHE DSLRHLLRVA
110 120 130 140 150
AGLESLVVGE DQILGQLRDA YDAAKDAGGI DHVLREAVTK AMHVGERART
160 170 180 190 200
ETAINEGATS LGTAAVRLAE RKTQLADARA VVVGAGEMGA LAAKAFASAT
210 220 230 240 250
VAEIVIANRT PARAVRVADM VSVPAEATTL ADARGRLDAA DVVVTATGSP
260 270 280 290 300
EHVLPASAFA DAGDTVVVDL AQPRDVAPGA GGHDGVAVHD LDDLEAVTAA
310 320 330 340 350
TRERREDAAR EVEAMIETEF ERLLTQYKRK RADEVIARMY ESADRLKSRE
360 370 380 390 400
VQTAVHRLEA ESGSLSADER EVVESMADAL VSQLLAAPTK SLRDAAAEDD
410 420 430
WSTIATALEL FNPEFEDGMP FDASRGGDAA SAESED
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.
RefSeqiWP_010903296.1. NC_010364.1.
YP_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 WP_010903296.1. NC_010364.1.
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: October 29, 2014
This is version 55 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.UniRule annotation

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