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Q5P7G6

- HEM1_AROAE

UniProt

Q5P7G6 - HEM1_AROAE

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Protein

Glutamyl-tRNA reductase

Gene
hemA, AZOSEA06230, ebA1179
Organism
Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1))
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

BioCyciAARO76114:GJTA-636-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:AZOSEA06230
ORF Names:ebA1179
OrganismiAromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1))
Taxonomic identifieri76114 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAromatoleum
ProteomesiUP000006552: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 418418Glutamyl-tRNA reductaseUniRule annotationPRO_1000004594Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi76114.ebA1179.

Structurei

3D structure databases

ProteinModelPortaliQ5P7G6.

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.

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.

Q5P7G6-1 [UniParc]FASTAAdd to Basket

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MQLYALGLNH HTAPLTIREQ VAFQPERLDD ALHDLTHERT VREAAILSTC    50
NRTELYFATE QPQHAADWLA RFHHMPLSEV SPYLYTYPQR DAIRHVFRVA 100
SGLDSMVLGE PQILGQVKDA VRRAEEAGTM GTLLHKLFQN TFAVAKEVRS 150
TTAIGANIVS MAAAALHLSE RIFERMSDQR VLFIGAGEMI ELCAAYFAGA 200
CPKRIAVANR TEARAQLVAH RFGAEVMRLD VVGEMLPHFD VVVSCTASPL 250
PIVGLGMVER AIKARRHRPI VMVDLAVPRD IEAEVGELDD VFLYTVDDLA 300
QIVDAGLESR QQAVLEAEEI IDSRVNGFLH WMQARDAVPT IRALRQHAET 350
VRAVELERAT RLLAKGEDPR KVLDALSHGL INKLMHSPTR YLNQSEGEQQ 400
ADASRLVQQL FNLSNSPD 418
Length:418
Mass (Da):46,624
Last modified:January 4, 2005 - v1
Checksum:i308581D58B76AC8C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR555306 Genomic DNA. Translation: CAI06745.1.
RefSeqiYP_157646.1. NC_006513.1.

Genome annotation databases

EnsemblBacteriaiCAI06745; CAI06745; ebA1179.
GeneIDi3179696.
KEGGieba:ebA1179.
PATRICi20967337. VBIAroAro98752_0635.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR555306 Genomic DNA. Translation: CAI06745.1 .
RefSeqi YP_157646.1. NC_006513.1.

3D structure databases

ProteinModelPortali Q5P7G6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 76114.ebA1179.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAI06745 ; CAI06745 ; ebA1179 .
GeneIDi 3179696.
KEGGi eba:ebA1179.
PATRICi 20967337. VBIAroAro98752_0635.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci AARO76114:GJTA-636-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. "The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1."
    Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.
    Arch. Microbiol. 183:27-36(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: EbN1.

Entry informationi

Entry nameiHEM1_AROAE
AccessioniPrimary (citable) accession number: Q5P7G6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 4, 2005
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

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