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A6W5L7

- HEM1_KINRD

UniProt

A6W5L7 - HEM1_KINRD

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Protein
Glutamyl-tRNA reductase
Gene
hemA, Krad_0617
Organism
Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216)
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 bindingi189 – 1946NADP By similarity

GO - Molecular functioni

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

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

BioCyciKRAD266940:GI4N-1622-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:Krad_0617
OrganismiKineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216)
Taxonomic identifieri266940 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesKineosporiineaeKineosporiaceaeKineococcus
ProteomesiUP000001116: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 442442Glutamyl-tRNA reductaseUniRule annotation
PRO_1000075411Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi266940.Krad_0617.

Structurei

3D structure databases

ProteinModelPortaliA6W5L7.

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.

A6W5L7-1 [UniParc]FASTAAdd to Basket

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MALMVVGLSH RTASLEVLER AAFDARGAEE VLRALTASPH VEEAFVLSTC    50
NRVELYCDVS RFHGGVADIG DVLCRRIGRG LDELGDQLYV HYEDAGVEHL 100
FKVACGLDSM AVGESQILGQ LRLALRGLHE RGLAGGTLDR LLQTALRVGK 150
RAHSETRLDA AGASLVDTAM TRAAGVVGEL PGRRALVVGA GAMSALVATT 200
LARAGLDVVV ANRTPDRAQR LAAAVGGRAT GLDDLRAEVA AADLVVSCTG 250
AVGHVLDVAT VASALLDRPE RPLFLADLAL PRDVHPDVAT LRGAHLVDLE 300
GLGADLASSA VAQDLRAVRA IVAEEVAAHA ASLRAADVAP TVVALRAQAR 350
HVVEVEMRRL ASRVDLDDTT RSEVDRAVHR IVEKLLHTPT VRVKELAEAP 400
GGVGYAAALR ALFDLEVTAQ GGALPGDAPL SGTVADAVGH VS 442
Length:442
Mass (Da):46,057
Last modified:August 21, 2007 - v1
Checksum:i4B30DCD0C27FCB32
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000750 Genomic DNA. Translation: ABS02106.1.
RefSeqiWP_012085052.1. NC_009664.2.
YP_001360370.1. NC_009664.2.

Genome annotation databases

EnsemblBacteriaiABS02106; ABS02106; Krad_0617.
GeneIDi5336359.
KEGGikra:Krad_0617.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000750 Genomic DNA. Translation: ABS02106.1 .
RefSeqi WP_012085052.1. NC_009664.2.
YP_001360370.1. NC_009664.2.

3D structure databases

ProteinModelPortali A6W5L7.
ModBasei Search...

Protein-protein interaction databases

STRINGi 266940.Krad_0617.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABS02106 ; ABS02106 ; Krad_0617 .
GeneIDi 5336359.
KEGGi kra:Krad_0617.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci KRAD266940:GI4N-1622-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: ATCC BAA-149 / DSM 14245 / SRS30216.

Entry informationi

Entry nameiHEM1_KINRD
AccessioniPrimary (citable) accession number: A6W5L7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: August 21, 2007
Last modified: September 3, 2014
This is version 60 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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