SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q6AHF6

- HEM1_LEIXX

UniProt

Q6AHF6 - HEM1_LEIXX

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glutamyl-tRNA reductase

Gene
hemA, Lxx01050
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) 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 sitei47 – 471Nucleophile 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. 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 reductase (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:hemA
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 reductaseUniRule annotationPRO_0000114034Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi281090.Lxx01050.

Structurei

3D structure databases

ProteinModelPortaliQ6AHF6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni46 – 494Substrate 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.
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

MLICFSSSHR TAAFDLLDQL ERHAPAVATA LAEHSELVTG SVVLATCNRF    50
EAYLDIDEPL PAARAVSAET VIAAVGNAAG IDADLLRSSS RVYCDDAAAE 100
HLLSVSSGLD SVVVGEGEIA GQVRRALTTA RQAGTVSQDL ERLFQVASRT 150
SRGVKNRTGI ATAGRSIVRL ALDLAESRVS DWSRMRVLLI GTGKYAGASL 200
AALRDRGVAD VQVHSPSGRA EKFALSHGVT AVPAGGLGAA LAHAHLIVTC 250
TTVRDYTLTP GNFGQAQQQD GIERRLVIDL GLPRNVDSAV AELPGVELLD 300
LETISLHAPV AELNAADDAR EIVGAAAAEF AAQTAEQAVK PALIALRKHV 350
FDILDAEIAR ARTRGDSSEQ TEAALRHLAG VLLHTPSVRA RELARAGDAQ 400
RFADAAETLF GLRIEEAPVH PRLIAVDRVT AS 432
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: September 3, 2014
This is version 78 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

Similar proteinsi