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Q83H91

- HEM1_TROW8

UniProt

Q83H91 - HEM1_TROW8

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Protein
Glutamyl-tRNA reductase
Gene
hemA, TW750
Organism
Tropheryma whipplei (strain TW08/27) (Whipple's bacillus)
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 sitei46 – 461Nucleophile By similarity
Sitei101 – 1011Important for activity By similarity
Binding sitei111 – 1111Substrate By similarity
Binding sitei122 – 1221Substrate 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

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:TW750
OrganismiTropheryma whipplei (strain TW08/27) (Whipple's bacillus)
Taxonomic identifieri218496 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeTropheryma
ProteomesiUP000001413: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 447447Glutamyl-tRNA reductaseUniRule annotation
PRO_0000114081Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi218496.TW750.

Structurei

3D structure databases

ProteinModelPortaliQ83H91.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 484Substrate binding By similarity
Regioni116 – 1183Substrate 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.
OMAiMIICEEL.
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.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q83H91-1 [UniParc]FASTAAdd to Basket

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MLLCVSANHK KTSFTVLEQL ARVSPDFASE LVEAEDIDGA AILSTCNRFE    50
VYIDAIQKGD QDDVCKTGLL VQNRIGELCN ISPSTIIEQT SFLAGCEVSR 100
HLFSVATGLE SMIIGETEIA GQVKRALTYA QKCRTTSPEL ERLFQRASAV 150
NRHIRQSTKI NEVGQSLVSL SLDLASSRIG DWSGVRAIIV GTGKYASKAL 200
ALLKERGVVD ISVYSPSGHV NNICNTEGVR NIFNLQTALS GCDLVVGCSS 250
VDKPVITKQD IETAQASGSR TSRVRPVGRP STDLTAIEAS NRSRHVLIDL 300
GLPRNFDPAI SDLPTADLID LDMLRVHAPF DNLAAEKMAH ELAIESSSQF 350
VNDCKQHEAT PVIVSFRNYL ESLTQTSLRR TDNCKHAQHA LKHFVNSLIH 400
IPLTRCKQLA ANGESHKFAE SMEILFDVKT DCTEGTQYQS SCGKSFD 447
Length:447
Mass (Da):48,838
Last modified:June 1, 2003 - v1
Checksum:i7E5EF8E73584B2F1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX251412 Genomic DNA. Translation: CAD67409.1.
RefSeqiNP_789671.1. NC_004551.1.

Genome annotation databases

EnsemblBacteriaiCAD67409; CAD67409; TW750.
GeneIDi1064950.
KEGGitws:TW750.
PATRICi24000213. VBITroWhi42739_0910.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX251412 Genomic DNA. Translation: CAD67409.1 .
RefSeqi NP_789671.1. NC_004551.1.

3D structure databases

ProteinModelPortali Q83H91.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 218496.TW750.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAD67409 ; CAD67409 ; TW750 .
GeneIDi 1064950.
KEGGi tws:TW750.
PATRICi 24000213. VBITroWhi42739_0910.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .

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.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TW08/27.

Entry informationi

Entry nameiHEM1_TROW8
AccessioniPrimary (citable) accession number: Q83H91
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: September 3, 2014
This is version 80 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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