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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Roseiflexus castenholzii (strain DSM 13941 / HLO8)
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 sitei48 – 481NucleophileUniRule annotation
Sitei97 – 971Important for activityUniRule annotation
Binding sitei107 – 1071SubstrateUniRule annotation
Binding sitei118 – 1181SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi187 – 1926NADPUniRule annotation

GO - Molecular functioni

  1. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
  2. NADP binding Source: InterPro

GO - Biological processi

  1. chlorophyll biosynthetic process Source: UniProtKB-HAMAP
  2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Chlorophyll biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciRCAS383372:GH89-2048-MONOMER.
UniPathwayiUPA00251; UER00316.
UPA00668.

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:Rcas_2026
OrganismiRoseiflexus castenholzii (strain DSM 13941 / HLO8)
Taxonomic identifieri383372 [NCBI]
Taxonomic lineageiBacteriaChloroflexiChloroflexiaChloroflexalesRoseiflexineaeRoseiflexaceaeRoseiflexus
ProteomesiUP000000263: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 425425Glutamyl-tRNA reductasePRO_1000075420Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi383372.Rcas_2026.

Structurei

3D structure databases

ProteinModelPortaliA7NKU4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni47 – 504Substrate bindingUniRule annotation
Regioni112 – 1143Substrate 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.
HOGENOMiHOG000109649.
KOiK02492.
OMAiGAHSISM.
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.
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.

A7NKU4-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MHITLIGVHQ RNTPVTVRER LAFSLRELPD ALLALRRYVE EGIILSTCNR
60 70 80 90 100
VEVCAVTHDS VGGDAALKSF LAEQRGVDQA VFVPSLYIYH NEAVVRHLYR
110 120 130 140 150
LAAGLDSMVL GEDQIVGQIK EALAIAHASG AIGPVLHRVL HGALAAGKRA
160 170 180 190 200
RTHTGIASGH VSVVSVAIDA LRQHADLLKQ GRALVIGAGH MAELTLKHLI
210 220 230 240 250
AEGCSAITVI NRTETRASAL AQRYGVAWRP WGDLSDALAM SDMVVSCTSA
260 270 280 290 300
PGIVVSWQMV ERAAVGRSVP LLLFDLAVPR DIDQRVVEIP GVHLYDVDAL
310 320 330 340 350
EPICVTNRAM RAAEAQRAEA IIDGEVAKFM EWWVAQQAVP TIRALRERAE
360 370 380 390 400
AIRDAEIRRA LARCPELSPQ QRETVVALST AIINKLLHEP IVALRDPEAG
410 420
SELVSAVRRL FNIDDATVHP SAKVT
Length:425
Mass (Da):46,118
Last modified:October 2, 2007 - v1
Checksum:iD17749B8F9E3140D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000804 Genomic DNA. Translation: ABU58114.1.
RefSeqiYP_001432132.1. NC_009767.1.

Genome annotation databases

EnsemblBacteriaiABU58114; ABU58114; Rcas_2026.
GeneIDi5539504.
KEGGirca:Rcas_2026.
PATRICi23342441. VBIRosCas91182_2289.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000804 Genomic DNA. Translation: ABU58114.1.
RefSeqiYP_001432132.1. NC_009767.1.

3D structure databases

ProteinModelPortaliA7NKU4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi383372.Rcas_2026.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABU58114; ABU58114; Rcas_2026.
GeneIDi5539504.
KEGGirca:Rcas_2026.
PATRICi23342441. VBIRosCas91182_2289.

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109649.
KOiK02492.
OMAiGAHSISM.
OrthoDBiEOG6MWNBM.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316.
UPA00668.
BioCyciRCAS383372:GH89-2048-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.
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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 13941 / HLO8.

Entry informationi

Entry nameiHEM1_ROSCS
AccessioniPrimary (citable) accession number: A7NKU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 2, 2007
Last modified: February 4, 2015
This is version 61 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.