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Q0SF26

- HEM1_RHOSR

UniProt

Q0SF26 - HEM1_RHOSR

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Protein

Glutamyl-tRNA reductase

Gene
hemA, RHA1_ro02053
Organism
Rhodococcus sp. (strain RHA1)
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 sitei50 – 501Nucleophile By similarity
Sitei99 – 991Important for activity By similarity
Binding sitei109 – 1091Substrate By similarity
Binding sitei120 – 1201Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi191 – 1966NADP By similarity

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

BioCyciRJOS101510:GJJ1-2051-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:RHA1_ro02053
OrganismiRhodococcus sp. (strain RHA1)
Taxonomic identifieri101510 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus
ProteomesiUP000008710: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 479479Glutamyl-tRNA reductaseUniRule annotationPRO_0000335065Add
BLAST

Proteomic databases

PRIDEiQ0SF26.

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi101510.RHA1_ro02053.

Structurei

3D structure databases

ProteinModelPortaliQ0SF26.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni114 – 1163Substrate 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.
HOGENOMiHOG000109649.
KOiK02492.
OMAiLAHKLTN.
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.

Q0SF26-1 [UniParc]FASTAAdd to Basket

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MSVLLVGVSH RTAPVPVLER VAVTDTDRPK LTDKLLASSH ISEAMIVSTC    50
NRVEIYAVVD AFHGALAEVG ELLADHSGLD LTDLHRHAYV RYSEAAAEHL 100
FAVASGLDSM VIGEQQILGQ IRTAYASSDA QQAAGRTLHE LAQQALRVGK 150
RVHSETGIDS AGASVVSVAL DRAAGIVGDG GLTGRTAVVV GAGSMGGLSV 200
AHLTRAGIGR IVVVNRTKER AEHLADTARA NGVEAEALEL SELPAAMAQA 250
DVLVTCTGAV GAVVTLADTH RALAQPGRDA ERPLVICDLG LPRDVEPAVS 300
GLPGVTVLDM ESLQRDPAAG AAASDADAAR TIVAAELANY LAGQRLAEVT 350
PTVTALRQRA ADVVEAELMR LDSRLPGLDD PERDEVARTV RRVVDKLLHA 400
PTVRVKQLAS APGGDSYAAA LRELFELSPG SVEAVAKPTD LGGATDLSAI 450
DITDGFIAGQ DPRLRRFVTD DNHGKESQA 479
Length:479
Mass (Da):49,932
Last modified:September 5, 2006 - v1
Checksum:i77CE63C13CC79C2C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000431 Genomic DNA. Translation: ABG93860.1.
RefSeqiYP_702018.1. NC_008268.1.

Genome annotation databases

EnsemblBacteriaiABG93860; ABG93860; RHA1_ro02053.
GeneIDi4218099.
KEGGirha:RHA1_ro02053.
PATRICi23202953. VBIRhoJos26306_2078.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000431 Genomic DNA. Translation: ABG93860.1 .
RefSeqi YP_702018.1. NC_008268.1.

3D structure databases

ProteinModelPortali Q0SF26.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 101510.RHA1_ro02053.

Proteomic databases

PRIDEi Q0SF26.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABG93860 ; ABG93860 ; RHA1_ro02053 .
GeneIDi 4218099.
KEGGi rha:RHA1_ro02053.
PATRICi 23202953. VBIRhoJos26306_2078.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109649.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci RJOS101510:GJJ1-2051-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 PF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMi SSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsi TIGR01035. hemA. 1 hit.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RHA1.

Entry informationi

Entry nameiHEM1_RHOSR
AccessioniPrimary (citable) accession number: Q0SF26
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: September 5, 2006
Last modified: September 3, 2014
This is version 73 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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