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Protein

Glutamyl-tRNA reductase 1

Gene

hemA1

Organism
Pyrobaculum calidifontis (strain JCM 11548 / VA1)
Status
Reviewed-Annotation score: 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

Pathway: protoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamyl-tRNA reductase 2 (hemA2), Glutamyl-tRNA reductase 1 (hemA1)
  2. Glutamate-1-semialdehyde 2,1-aminomutase (hemL)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu), the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei43 – 431NucleophileUniRule annotation
Sitei83 – 831Important for activityUniRule annotation
Binding sitei93 – 931SubstrateUniRule annotation
Binding sitei104 – 1041SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi172 – 1776NADPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciPCAL410359:GIX2-1515-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase 1UniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTR 1UniRule annotation
Gene namesi
Name:hemA1UniRule annotation
Ordered Locus Names:Pcal_1481
OrganismiPyrobaculum calidifontis (strain JCM 11548 / VA1)
Taxonomic identifieri410359 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum
ProteomesiUP000001431 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 380380Glutamyl-tRNA reductase 1PRO_0000335098Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi410359.Pcal_1481.

Structurei

3D structure databases

ProteinModelPortaliA3MW83.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni42 – 454Substrate bindingUniRule annotation
Regioni98 – 1003Substrate 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.
HOGENOMiHOG000112880.
KOiK02492.
OMAiVHIEREG.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
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]
SUPFAMiSSF69742. SSF69742. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A3MW83-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLVDKLYALS LSHKRLSVDE LSEISRNVHK TCYNVQAFVF HTCNRVEVYL
60 70 80 90 100
YDADAGPAEH IKRSYGPYVE KVAEFRGVEA ARHLFRVAAG LESMLIGETD
110 120 130 140 150
VLGQLEEAYE SQVRRGNLRG LLKTVVERAV AVGKRVRTET GISRGPRGLG
160 170 180 190 200
SLSIVYLSRR LPLREISVCV IGAGAVGRGV VKELIDAGVR RVAVVNRTVE
210 220 230 240 250
KAADLGVEVR PLTSENVEWC LREFDVVYTA VSSFEPVVVY VPPGSRVKLV
260 270 280 290 300
VDLGVPRNTA PNLPVEVVTL DHLRELAEEF NRQRAEEVSK AEKIVEEEVA
310 320 330 340 350
RLEEVLRRRW VELEMSALLK KWFAVAEEEG ERAGGGPARL AAMSTVKRTL
360 370 380
LPLVNYIKEV AVKDLAVAEG LLQVLKSAYA
Length:380
Mass (Da):42,139
Last modified:April 3, 2007 - v1
Checksum:i02E622F27C210096
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000561 Genomic DNA. Translation: ABO08900.1.
RefSeqiWP_011850158.1. NC_009073.1.
YP_001056366.1. NC_009073.1.

Genome annotation databases

EnsemblBacteriaiABO08900; ABO08900; Pcal_1481.
GeneIDi4910204.
KEGGipcl:Pcal_1481.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000561 Genomic DNA. Translation: ABO08900.1.
RefSeqiWP_011850158.1. NC_009073.1.
YP_001056366.1. NC_009073.1.

3D structure databases

ProteinModelPortaliA3MW83.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi410359.Pcal_1481.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABO08900; ABO08900; Pcal_1481.
GeneIDi4910204.
KEGGipcl:Pcal_1481.

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000112880.
KOiK02492.
OMAiVHIEREG.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316.
BioCyciPCAL410359:GIX2-1515-MONOMER.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
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]
SUPFAMiSSF69742. SSF69742. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JCM 11548 / VA1.

Entry informationi

Entry nameiHEM11_PYRCJ
AccessioniPrimary (citable) accession number: A3MW83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 3, 2007
Last modified: May 27, 2015
This is version 66 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.