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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Salinibacter ruber (strain DSM 13855 / M31)
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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei49 – 491NucleophileUniRule annotation
Sitei94 – 941Important for activityUniRule annotation
Binding sitei104 – 1041SubstrateUniRule annotation
Binding sitei115 – 1151SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi189 – 1946NADPUniRule 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

BioCyciSRUB309807:GJJD-1552-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:SRU_1555
OrganismiSalinibacter ruber (strain DSM 13855 / M31)
Taxonomic identifieri309807 [NCBI]
Taxonomic lineageiBacteriaBacteroidetesBacteroidetes Order II. Incertae sedisRhodothermaceaeSalinibacter
ProteomesiUP000008674 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 479479Glutamyl-tRNA reductasePRO_0000335070Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi309807.SRU_1555.

Structurei

3D structure databases

ProteinModelPortaliQ2S2A5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 514Substrate bindingUniRule annotation
Regioni109 – 1113Substrate 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.
HOGENOMiHOG000106238.
KOiK02492.
OrthoDBiEOG6MWNBM.

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.
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.

Sequencei

Sequence statusi: Complete.

Q2S2A5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRFYAVGLNH ECTSLEQTET FALSAEEQEA LYANLSLSAD AEVVVLSTCN
60 70 80 90 100
RTEAYLYGTE ADLRQVKALI GQGGGTRWPE ETAFQERDEA AVRHLLQVTS
110 120 130 140 150
GLRSVVLGER QIFAQVKAAY ERAVDAGGIH SVMHRLFHTA FRAAKRVSSE
160 170 180 190 200
TGLGRGAASV STAAVEMARQ DLSEAGGEGL RNTEIVLVGA GKMGRLALEA
210 220 230 240 250
LADESLASLT VVNRSPDRAR EVASPFGGDT EPWADRHRAV ATADLALVAT
260 270 280 290 300
GASDPVLHAP ALPAPDEATL VVDVAMPRNV DPAVDERPGY RLYDLDDLEA
310 320 330 340 350
WTAEVRERRA DAVPEAESIC EELLEDFVTW VFHQQALQPA IQAIRSTFDT
360 370 380 390 400
IREQEVDRHA HRTGMDREEV DRLTESIMQK LLAVPIVRLK NVDPESIDFV
410 420 430 440 450
QGIELLHALF APSDESDAGR SLAEAPDADT PDLGEAPSRC PYMTHDPGGD
460 470
GTETEEVQKA LRLSAAHQAA SHSEEVRGG
Length:479
Mass (Da):51,933
Last modified:May 20, 2008 - v2
Checksum:iCCBDCF4F287BBB5D
GO

Sequence cautioni

The sequence ABC43868.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000159 Genomic DNA. Translation: ABC43868.1. Different initiation.
RefSeqiYP_445676.1. NC_007677.1.

Genome annotation databases

EnsemblBacteriaiABC43868; ABC43868; SRU_1555.
GeneIDi3851349.
KEGGisru:SRU_1555.
PATRICi23425545. VBISalRub86502_1609.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000159 Genomic DNA. Translation: ABC43868.1. Different initiation.
RefSeqiYP_445676.1. NC_007677.1.

3D structure databases

ProteinModelPortaliQ2S2A5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi309807.SRU_1555.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABC43868; ABC43868; SRU_1555.
GeneIDi3851349.
KEGGisru:SRU_1555.
PATRICi23425545. VBISalRub86502_1609.

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000106238.
KOiK02492.
OrthoDBiEOG6MWNBM.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316.
BioCyciSRUB309807:GJJD-1552-MONOMER.

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.
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.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 13855 / M31.

Entry informationi

Entry nameiHEM1_SALRD
AccessioniPrimary (citable) accession number: Q2S2A5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: January 7, 2015
This is version 75 of the entry and version 2 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, Reference 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.