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Q82TH3

- HEM1_NITEU

UniProt

Q82TH3 - HEM1_NITEU

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Protein

Glutamyl-tRNA reductase

Gene
hemA, NE1914
Organism
Nitrosomonas europaea (strain ATCC 19718 / NBRC 14298)
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
Sitei95 – 951Important for activity By similarity
Binding sitei105 – 1051Substrate By similarity
Binding sitei116 – 1161Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi185 – 1906NADP 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

BioCyciNEUR228410:GJNO-1950-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:NE1914
OrganismiNitrosomonas europaea (strain ATCC 19718 / NBRC 14298)
Taxonomic identifieri228410 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas
ProteomesiUP000001416: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 416416Glutamyl-tRNA reductaseUniRule annotationPRO_0000114048Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi228410.NE1914.

Structurei

3D structure databases

ProteinModelPortaliQ82TH3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni110 – 1123Substrate 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.
HOGENOMiHOG000109650.
KOiK02492.
OMAiKMLHGTM.
OrthoDBiEOG6MWNBM.
PhylomeDBiQ82TH3.

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.

Q82TH3-1 [UniParc]FASTAAdd to Basket

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MQLFAFGVNH HTAPLDIREH VAFSEESMQH ALHDLVGHQL VKEAAIVSTC    50
NRTEIYCNTD TPDKAVGWLA DFHHLRFGDL EPYLYRLLRE QAVKHAFRVA 100
SGLDSMVLGE PQILGQMKNA VKSAEQAGTL GLLLHKMFQR TFFVAKEVRT 150
STEIGACSVS MAAASARLAE RIFGNISEQK VLFIGAGEMI ELCAAHFVAR 200
HPVHVTVANR TVERAEALAR RFNAHPISLG ELPDQLALHD IVVTSTASPL 250
PILGKGMLER AIKQRKHRPV FIVDLAVPRD VEAEVAELDD VFLYYVDDLA 300
DIVKEGLDNR QGAVTQAETI IESNVVDFMH WVATRQSVPT IRALRNQAER 350
YRRHELARAH KLLAKGEDPE KVLESLSSGL TNKFLHLPSS VLNHATDDER 400
EQLIELVNRL YQLHHS 416
Length:416
Mass (Da):46,558
Last modified:June 1, 2003 - v1
Checksum:i72CB44C31905CCD3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL954747 Genomic DNA. Translation: CAD85825.1.
RefSeqiNP_841936.1. NC_004757.1.
WP_011112451.1. NC_004757.1.

Genome annotation databases

EnsemblBacteriaiCAD85825; CAD85825; NE1914.
GeneIDi1082871.
KEGGineu:NE1914.
PATRICi22715121. VBINitEur56163_2147.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL954747 Genomic DNA. Translation: CAD85825.1 .
RefSeqi NP_841936.1. NC_004757.1.
WP_011112451.1. NC_004757.1.

3D structure databases

ProteinModelPortali Q82TH3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 228410.NE1914.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAD85825 ; CAD85825 ; NE1914 .
GeneIDi 1082871.
KEGGi neu:NE1914.
PATRICi 22715121. VBINitEur56163_2147.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109650.
KOi K02492.
OMAi KMLHGTM.
OrthoDBi EOG6MWNBM.
PhylomeDBi Q82TH3.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci NEUR228410:GJNO-1950-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. "Complete genome sequence of the ammonia-oxidizing bacterium and obligate chemolithoautotroph Nitrosomonas europaea."
    Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L., Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A., Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.
    J. Bacteriol. 185:2759-2773(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 19718 / NBRC 14298.

Entry informationi

Entry nameiHEM1_NITEU
AccessioniPrimary (citable) accession number: Q82TH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: September 3, 2014
This is version 85 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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