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Protein

Glutamyl-tRNA reductase 1

Gene

hemA1

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

Functioni

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).UniRule annotation

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

Catalytic activityi

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.UniRule annotation

Pathwayi: 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)DescriptionActionsGraphical viewLength
Active sitei43NucleophileUniRule annotation1
Sitei83Important for activityUniRule annotation1
Binding sitei93SubstrateUniRule annotation1
Binding sitei104SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi172 – 177NADPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processPorphyrin biosynthesis
LigandNADP

Enzyme and pathway databases

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
Proteomesi
  • UP000001431 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003350981 – 380Glutamyl-tRNA reductase 1Add BLAST380

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi410359.Pcal_1481

Structurei

3D structure databases

ProteinModelPortaliA3MW83
SMRiA3MW83
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni42 – 45Substrate bindingUniRule annotation4
Regioni98 – 100Substrate bindingUniRule annotation3

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

eggNOGiarCOG01036 Archaea
COG0373 LUCA
HOGENOMiHOG000112880
KOiK02492
OMAiMANLVIK
OrthoDBiPOG093Z06M3

Family and domain databases

Gene3Di3.30.460.30, 1 hit
HAMAPiMF_00087 Glu_tRNA_reductase, 1 hit
InterProiView protein in InterPro
IPR000343 4pyrrol_synth_GluRdtase
IPR015895 4pyrrol_synth_GluRdtase_N
IPR018214 GluRdtase_CS
IPR036343 GluRdtase_N_sf
IPR036291 NAD(P)-bd_dom_sf
IPR006151 Shikm_DH/Glu-tRNA_Rdtase
PfamiView protein in Pfam
PF05201 GlutR_N, 1 hit
PF01488 Shikimate_DH, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
SSF69742 SSF69742, 1 hit
PROSITEiView protein in PROSITE
PS00747 GLUTR, 1 hit

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

Genome annotation databases

EnsemblBacteriaiABO08900; ABO08900; Pcal_1481
KEGGipcl:Pcal_1481

Similar proteinsi

Entry informationi

Entry nameiHEM11_PYRCJ
AccessioniPrimary (citable) accession number: A3MW83
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 3, 2007
Last modified: March 28, 2018
This is version 76 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome
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Main funding by: National Institutes of Health