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.

A8A9U3

- HEM1_IGNH4

UniProt

A8A9U3 - HEM1_IGNH4

(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, Igni_0512
Organism
Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125)
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 sitei59 – 591Nucleophile By similarity
Sitei106 – 1061Important for activity By similarity
Binding sitei116 – 1161Substrate By similarity
Binding sitei127 – 1271Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi195 – 2006NADP 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

BioCyciIHOS453591:GHYN-527-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:Igni_0512
OrganismiIgnicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125)
Taxonomic identifieri453591 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeIgnicoccus
ProteomesiUP000000262: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 441441Glutamyl-tRNA reductaseUniRule annotation
PRO_0000335090Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi453591.Igni_0512.

Structurei

3D structure databases

ProteinModelPortaliA8A9U3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 614Substrate binding By similarity
Regioni121 – 1233Substrate 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.
KOiK02492.
OMAiEHMIEDE.

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.

A8A9U3-1 [UniParc]FASTAAdd to Basket

« Hide

MPAAARVPLF VDDLVMVGVN YKTSGKELVE KAQFPDPLAA YSAISRIPAV    50
REVVLLQTCN RVEVYAITTN KKATVESIKS LLEARAGEPI PEEKFVIYYG 100
TDAVRHLFRV AAGLESMVLG EPDILRQVRE AAEFAAKEGY IGKALKLTFE 150
NAVRVGKRVR TETALGKGSI GIPSASVKLL EELIGLEGKK LLVVGAGMAG 200
RVVAVNAAKR GAKVIIVNRT LSKAKELAEE VGGEAYPLEE LPRLLREADA 250
VVVAVGGGSK VITRDAVAEV NKKLVIVDIS EPPAVDPGVS LNPYVIYKDM 300
LAVAEVANRG LEKRKSEIKR AEDIIEAELN KFVNFAQRVL ADKILRELME 350
KVEQIRINEL SKAMAKVPQE YAEVLDKMTS SLVKKVLKDV ILKVREAAGK 400
GDLTTLRIVA EVFDLKESLN NIEIIYDYNG VEQELKRKLE L 441
Length:441
Mass (Da):48,266
Last modified:October 23, 2007 - v1
Checksum:i4053407C2ACE2C4A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000816 Genomic DNA. Translation: ABU81695.1.
RefSeqiWP_011998547.1. NC_009776.1.
YP_001435102.1. NC_009776.1.

Genome annotation databases

EnsemblBacteriaiABU81695; ABU81695; Igni_0512.
GeneIDi5562776.
KEGGiiho:Igni_0512.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000816 Genomic DNA. Translation: ABU81695.1 .
RefSeqi WP_011998547.1. NC_009776.1.
YP_001435102.1. NC_009776.1.

3D structure databases

ProteinModelPortali A8A9U3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 453591.Igni_0512.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABU81695 ; ABU81695 ; Igni_0512 .
GeneIDi 5562776.
KEGGi iho:Igni_0512.

Phylogenomic databases

eggNOGi COG0373.
KOi K02492.
OMAi EHMIEDE.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci IHOS453591:GHYN-527-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: KIN4/I / DSM 18386 / JCM 14125.

Entry informationi

Entry nameiHEM1_IGNH4
AccessioniPrimary (citable) accession number: A8A9U3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 23, 2007
Last modified: September 3, 2014
This is version 56 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