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Q6AHF6

- HEM1_LEIXX

UniProt

Q6AHF6 - HEM1_LEIXX

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Leifsonia xyli subsp. xyli (strain CTCB07)
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 sitei47 – 471NucleophileUniRule annotation
Sitei101 – 1011Important for activityUniRule annotation
Binding sitei111 – 1111SubstrateUniRule annotation
Binding sitei122 – 1221SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi191 – 1966NADPUniRule 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

BioCyciLXYL281090:GH0X-94-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:Lxx01050
OrganismiLeifsonia xyli subsp. xyli (strain CTCB07)
Taxonomic identifieri281090 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrobacteriaceaeLeifsonia
ProteomesiUP000001306: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432Glutamyl-tRNA reductasePRO_0000114034Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi281090.Lxx01050.

Structurei

3D structure databases

ProteinModelPortaliQ6AHF6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni46 – 494Substrate bindingUniRule annotation
Regioni116 – 1183Substrate 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.
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.

Q6AHF6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLICFSSSHR TAAFDLLDQL ERHAPAVATA LAEHSELVTG SVVLATCNRF
60 70 80 90 100
EAYLDIDEPL PAARAVSAET VIAAVGNAAG IDADLLRSSS RVYCDDAAAE
110 120 130 140 150
HLLSVSSGLD SVVVGEGEIA GQVRRALTTA RQAGTVSQDL ERLFQVASRT
160 170 180 190 200
SRGVKNRTGI ATAGRSIVRL ALDLAESRVS DWSRMRVLLI GTGKYAGASL
210 220 230 240 250
AALRDRGVAD VQVHSPSGRA EKFALSHGVT AVPAGGLGAA LAHAHLIVTC
260 270 280 290 300
TTVRDYTLTP GNFGQAQQQD GIERRLVIDL GLPRNVDSAV AELPGVELLD
310 320 330 340 350
LETISLHAPV AELNAADDAR EIVGAAAAEF AAQTAEQAVK PALIALRKHV
360 370 380 390 400
FDILDAEIAR ARTRGDSSEQ TEAALRHLAG VLLHTPSVRA RELARAGDAQ
410 420 430
RFADAAETLF GLRIEEAPVH PRLIAVDRVT AS
Length:432
Mass (Da):45,469
Last modified:September 13, 2004 - v1
Checksum:iEE221EFFFBE4DED5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016822 Genomic DNA. Translation: AAT88189.1.
RefSeqiWP_011185194.1. NC_006087.1.
YP_061294.1. NC_006087.1.

Genome annotation databases

EnsemblBacteriaiAAT88189; AAT88189; Lxx01050.
GeneIDi2938311.
KEGGilxx:Lxx01050.
PATRICi22333648. VBILeiXyl11655_0102.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016822 Genomic DNA. Translation: AAT88189.1 .
RefSeqi WP_011185194.1. NC_006087.1.
YP_061294.1. NC_006087.1.

3D structure databases

ProteinModelPortali Q6AHF6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 281090.Lxx01050.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAT88189 ; AAT88189 ; Lxx01050 .
GeneIDi 2938311.
KEGGi lxx:Lxx01050.
PATRICi 22333648. VBILeiXyl11655_0102.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci LXYL281090:GH0X-94-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: CTCB07.

Entry informationi

Entry nameiHEM1_LEIXX
AccessioniPrimary (citable) accession number: Q6AHF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: September 13, 2004
Last modified: October 1, 2014
This is version 79 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.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