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C1AZ44

- HEM1_RHOOB

UniProt

C1AZ44 - HEM1_RHOOB

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Protein
Glutamyl-tRNA reductase
Gene
hemA, ROP_17250
Organism
Rhodococcus opacus (strain B4)
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. NADP binding Source: InterPro
  2. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP

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

BioCyciROPA632772:GH0Q-1749-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:ROP_17250
OrganismiRhodococcus opacus (strain B4)
Taxonomic identifieri632772 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus
ProteomesiUP000002212: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 478478Glutamyl-tRNA reductaseUniRule annotation
PRO_1000190538Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi632772.ROP_17250.

Structurei

3D structure databases

ProteinModelPortaliC1AZ44.

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.
OMAiPYLYVHY.
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.

C1AZ44-1 [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 DRAAGIVGAG GLTGRTAVVV GAGSMGGLSV 200
AHLTRAGIGR IVVVNRTRER AEHLADTARS NGVAAEALEL AELPDAMAQA 250
DVLVTCTGAV GAVVTLADTH RALAQPGRDS ERPLVICDLG LPRDVEPAVS 300
GLPGVTVLDM ESLQRDPAAG AAASDADAAR TIVAAELANY LAGQRLAEVT 350
PTVTALRQRA ADVVEAELMR LDSRLPGLDD PERDEVARTV RRVVDKLLHA 400
PTVRVKQLAS APGGDSYAAA LRELFELSPG SVEAVAKPTE LGGADLGAID 450
ITDGFIAGQD PRLRRFVADD NRGKESQA 478
Length:478
Mass (Da):49,790
Last modified:May 26, 2009 - v1
Checksum:iBF23CC81F2D15D75
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP011115 Genomic DNA. Translation: BAH49972.1.
RefSeqiYP_002778917.1. NC_012522.1.

Genome annotation databases

EnsemblBacteriaiBAH49972; BAH49972; ROP_17250.
GeneIDi7741679.
KEGGirop:ROP_17250.
PATRICi23220677. VBIRhoOpa21106_1733.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP011115 Genomic DNA. Translation: BAH49972.1 .
RefSeqi YP_002778917.1. NC_012522.1.

3D structure databases

ProteinModelPortali C1AZ44.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 632772.ROP_17250.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAH49972 ; BAH49972 ; ROP_17250 .
GeneIDi 7741679.
KEGGi rop:ROP_17250.
PATRICi 23220677. VBIRhoOpa21106_1733.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci ROPA632772:GH0Q-1749-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. "Comparison of the complete genome sequences of Rhodococcus erythropolis PR4 and Rhodococcus opacus B4."
    Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.
    Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: B4.

Entry informationi

Entry nameiHEM1_RHOOB
AccessioniPrimary (citable) accession number: C1AZ44
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 26, 2009
Last modified: September 3, 2014
This is version 43 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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