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A1R8A6

- HEM1_ARTAT

UniProt

A1R8A6 - HEM1_ARTAT

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Arthrobacter aurescens (strain TC1)
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).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 sitei48 – 481NucleophileUniRule annotation
Sitei100 – 1001Important for activityUniRule annotation
Binding sitei110 – 1101SubstrateUniRule annotation
Binding sitei121 – 1211SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi192 – 1976NADPUniRule annotation

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

BioCyciAAUR290340:GI59-2755-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTRUniRule annotation
Gene namesi
Name:hemAUniRule annotation
Ordered Locus Names:AAur_2756
OrganismiArthrobacter aurescens (strain TC1)
Taxonomic identifieri290340 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter
ProteomesiUP000000637: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 440440Glutamyl-tRNA reductasePRO_0000335009Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi290340.AAur_2756.

Structurei

3D structure databases

ProteinModelPortaliA1R8A6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni47 – 504Substrate bindingUniRule annotation
Regioni115 – 1173Substrate bindingUniRule annotation

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.UniRule annotation

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109649.
KOiK02492.
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.

A1R8A6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVLFSLVATH ADIDLETVAQ LSNGSSELAS AALTDSSVVS GAVVLATCNR
60 70 80 90 100
YEVYGETANG ADLEAARSAL VSQISELSGL NEQLVSRSFA THTGPDVTRH
110 120 130 140 150
LFAVSAGLDS AVVGEREIAG QVRRALITAQ QEGTASSGLV RLFQAASKTA
160 170 180 190 200
KDVGAQTALG SRGLSIVSVA LDLATDLAEN DDWTTKKVVV FGTGAYAGAT
210 220 230 240 250
MSLLRERGCT DISVYSSSGR AEGFVATRGG TALDADTLPA AVAAADVMIG
260 270 280 290 300
CSGSDNRVEA ADLARVRANS GKPLIAIDLA LTHDFDPAVG ELDGVELLTL
310 320 330 340 350
ESVRLAAPQE QAESLSQASA IVNGAATSFE SEREARSVDT AIVALRRHTM
360 370 380 390 400
NVLDAEMEKV RARHGCTAAA EEVEFALRRM VKQLLHIPTV RARELAANGQ
410 420 430 440
QDDYVAALEA LYGIQVEQPQ AAAPASECPV DHEQLRSESA
Length:440
Mass (Da):45,893
Last modified:May 20, 2008 - v2
Checksum:iFC01F5CD3ADA7D8C
GO

Sequence cautioni

The sequence ABM08676.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000474 Genomic DNA. Translation: ABM08676.1. Different initiation.
RefSeqiYP_948468.1. NC_008711.1.

Genome annotation databases

EnsemblBacteriaiABM08676; ABM08676; AAur_2756.
GeneIDi4638618.
KEGGiaau:AAur_2756.
PATRICi20980978. VBIArtAur67810_2798.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000474 Genomic DNA. Translation: ABM08676.1 . Different initiation.
RefSeqi YP_948468.1. NC_008711.1.

3D structure databases

ProteinModelPortali A1R8A6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 290340.AAur_2756.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABM08676 ; ABM08676 ; AAur_2756 .
GeneIDi 4638618.
KEGGi aau:AAur_2756.
PATRICi 20980978. VBIArtAur67810_2798.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci AAUR290340:GI59-2755-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: TC1.

Entry informationi

Entry nameiHEM1_ARTAT
AccessioniPrimary (citable) accession number: A1R8A6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: October 1, 2014
This is version 68 of the entry and version 2 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.UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3