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B1YBN0

- HEM1_PYRNV

UniProt

B1YBN0 - HEM1_PYRNV

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Protein
Glutamyl-tRNA reductase
Gene
hemA, Tneu_1917
Organism
Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / V24Sta) (Thermoproteus neutrophilus)
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 sitei48 – 481Nucleophile By similarity
Sitei88 – 881Important for activity By similarity
Binding sitei98 – 981Substrate By similarity
Binding sitei109 – 1091Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi177 – 1826NADP 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

BioCyciTNEU444157:GHL2-1966-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:Tneu_1917
OrganismiPyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / V24Sta) (Thermoproteus neutrophilus)
Taxonomic identifieri444157 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum
ProteomesiUP000001694: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 393393Glutamyl-tRNA reductaseUniRule annotation
PRO_1000093175Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi444157.Tneu_1917.

Structurei

3D structure databases

ProteinModelPortaliB1YBN0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni47 – 504Substrate binding By similarity
Regioni103 – 1053Substrate 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.
HOGENOMiHOG000112880.
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]
PfamiPF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
SUPFAMiSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B1YBN0-1 [UniParc]FASTAAdd to Basket

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MDLLAPLSAV VLTYREVSAE ALGKVGQEMK RCIERRARAF PMYVLHTCSR    50
VEAYLYGAPP EEVQEVAEAY RRYVDSVRVI TGAEAARHLF RVAAGLDSIL 100
IGETDVLGQV EEAFDRQVRA GYTRGLLKTV VERAVRVGKR VRTETAISRG 150
PRGLGSLSII YVSRLLDLRQ AKAAVLGAGA VGSGLAMELA SRGVGKLYIL 200
NRTFEKAREV AAKTGGEARP LTREEVERCL RECDVVFSSV HSMEYVIDRV 250
PEGASVKIVV DLGVPQTVAP GLPVKVVRIE DLRQVAEQYN AERAAEVAKA 300
EAIVEEELAA LPRLLARRYV EETVAALLET AMTAAEEEGA RAGCDAAALA 350
AKTTVKRVLL PLVEKMKKMA EDGQMEEAVR LANVLTQAVG RKT 393
Length:393
Mass (Da):42,756
Last modified:May 20, 2008 - v1
Checksum:i27D03C3CC36DF232
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001014 Genomic DNA. Translation: ACB40832.1.
RefSeqiWP_012351251.1. NC_010525.1.
YP_001795278.1. NC_010525.1.

Genome annotation databases

EnsemblBacteriaiACB40832; ACB40832; Tneu_1917.
GeneIDi6164814.
KEGGitne:Tneu_1917.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001014 Genomic DNA. Translation: ACB40832.1 .
RefSeqi WP_012351251.1. NC_010525.1.
YP_001795278.1. NC_010525.1.

3D structure databases

ProteinModelPortali B1YBN0.
ModBasei Search...

Protein-protein interaction databases

STRINGi 444157.Tneu_1917.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACB40832 ; ACB40832 ; Tneu_1917 .
GeneIDi 6164814.
KEGGi tne:Tneu_1917.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000112880.
KOi K02492.
OMAi YREADAN.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci TNEU444157:GHL2-1966-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 PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view ]
SUPFAMi SSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 2338 / JCM 9278 / V24Sta.

Entry informationi

Entry nameiHEM1_PYRNV
AccessioniPrimary (citable) accession number: B1YBN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: September 3, 2014
This is version 50 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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