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Q2JFS1

- HEM1_FRASC

UniProt

Q2JFS1 - HEM1_FRASC

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Protein
Glutamyl-tRNA reductase
Gene
hemA, Francci3_0485
Organism
Frankia sp. (strain CcI3)
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 bindingi226 – 2316NADP 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

BioCyciFSP106370:GI1F-498-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:Francci3_0485
OrganismiFrankia sp. (strain CcI3)
Taxonomic identifieri106370 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesFrankineaeFrankiaceaeFrankia
ProteomesiUP000001937: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473Glutamyl-tRNA reductaseUniRule annotation
PRO_0000335039Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi106370.Francci3_0485.

Structurei

3D structure databases

ProteinModelPortaliQ2JFS1.

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.
OMAiAITCGKK.
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.

Q2JFS1-1 [UniParc]FASTAAdd to Basket

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MSLLVVGLNH QTAPTSLLER TSVSAEDIPK VLHDLAEGTH VSEAVVLSTC    50
NRIEIYAEVE TFHGGVADIS DQLSRICGID LGDLAGHLYV HHEARAIGHL 100
FSVVCGLDSM LVGESQILGQ VRTAFRAGQA AGVAGSALSG LFQAALRVGK 150
RAHSETSIDA AGASIVSVGV RLAASGLGLH SEVPAVPVAP PGGRALDGGG 200
VAAEGPRHAV TPEPPPLAGT RVLLIGAGAV GSLAAQTVRR AGAGEVVIAN 250
RTAARAARVA EAHEARVVGL TDLAHEITMA DLVISSTGAS GLVVEHELVA 300
AALPGRAGRP LVFLDLALPH DIDPGVRELP GVSLIDLDAL RIALDGAQVT 350
HDVEAVRALV AAEVASFLDR RRAGRVAPTV VALRAHAAAV VRSELARLHT 400
RLPDLDDREW SLVEGSVRRV VDKLLHAPTV RVQELAGAPG GDAYAEALRE 450
LFDLPREVPA VVSAPDLDLL ERS 473
Length:473
Mass (Da):48,915
Last modified:March 7, 2006 - v1
Checksum:iEF7A0429CA48907B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000249 Genomic DNA. Translation: ABD09871.1.
RefSeqiYP_479600.1. NC_007777.1.

Genome annotation databases

EnsemblBacteriaiABD09871; ABD09871; Francci3_0485.
GeneIDi3903005.
KEGGifra:Francci3_0485.
PATRICi21923820. VBIFraSp10456_0539.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000249 Genomic DNA. Translation: ABD09871.1 .
RefSeqi YP_479600.1. NC_007777.1.

3D structure databases

ProteinModelPortali Q2JFS1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 106370.Francci3_0485.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABD09871 ; ABD09871 ; Francci3_0485 .
GeneIDi 3903005.
KEGGi fra:Francci3_0485.
PATRICi 21923820. VBIFraSp10456_0539.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci FSP106370:GI1F-498-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.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CcI3.

Entry informationi

Entry nameiHEM1_FRASC
AccessioniPrimary (citable) accession number: Q2JFS1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 7, 2006
Last modified: September 3, 2014
This is version 74 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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