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Q1CUR3

- HEM1_HELPH

UniProt

Q1CUR3 - HEM1_HELPH

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Helicobacter pylori (strain HPAG1)
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 sitei59 – 591NucleophileUniRule annotation
Sitei111 – 1111Important for activityUniRule annotation
Binding sitei121 – 1211SubstrateUniRule annotation
Binding sitei132 – 1321SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi203 – 2086NADPUniRule 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

BioCyciHPYL357544:GH1F-250-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:HPAG1_0242
OrganismiHelicobacter pylori (strain HPAG1)
Taxonomic identifieri357544 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
ProteomesiUP000008835: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 449449Glutamyl-tRNA reductasePRO_1000004627Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi357544.HPAG1_0242.

Structurei

3D structure databases

ProteinModelPortaliQ1CUR3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 614Substrate bindingUniRule annotation
Regioni126 – 1283Substrate 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.
HOGENOMiHOG000109651.
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.

Q1CUR3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MELETHLSKY FTLAFTHKSM SLEMREKLAI NSSATLKEFL QTIKNHCPNI
60 70 80 90 100
KECMVLSTCN RFEIYASLRH GAHANEQKSA LLKILAQNKK MSVSDLEKCV
110 120 130 140 150
LMNTDESAVH HVFSVCSSLD SLVVGETQIT GQMKNAYKFA FEEKFCSKDL
160 170 180 190 200
TRLLHFAFKC AAKVRNLTGI SKQGVSISSV AVKEALNIFE KERIKDKKAL
210 220 230 240 250
VIGLGEMAQL VIKHLLNKQF EALILGRNAA KFEDFIKELE EPKKVSFQNI
260 270 280 290 300
ENLNAYINEY ELLFCATSSP HFIVQNSMLK ETIFRRFWFD LAVPRNIEKP
310 320 330 340 350
VLDNIFLYSV DDLEPMVKEN VGNRQESRTK AYEIVGLATM EFYQWIQSLE
360 370 380 390 400
VEPLIKDLRE LARISAQKEL QKALKKRYVP KEYESNIEKI LHNAFNTFLH
410 420 430 440
HPTIALKKNA QKEESDVLVG AIKNLFNLDK SNANHAQNLN LYKCEYYEE
Length:449
Mass (Da):51,652
Last modified:July 11, 2006 - v1
Checksum:i0EF2F4F5815F4C74
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000241 Genomic DNA. Translation: ABF84309.1.
RefSeqiYP_626983.1. NC_008086.1.

Genome annotation databases

EnsemblBacteriaiABF84309; ABF84309; HPAG1_0242.
GeneIDi4097976.
KEGGihpa:HPAG1_0242.
PATRICi20601807. VBIHelPyl56048_0255.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000241 Genomic DNA. Translation: ABF84309.1 .
RefSeqi YP_626983.1. NC_008086.1.

3D structure databases

ProteinModelPortali Q1CUR3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 357544.HPAG1_0242.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABF84309 ; ABF84309 ; HPAG1_0242 .
GeneIDi 4097976.
KEGGi hpa:HPAG1_0242.
PATRICi 20601807. VBIHelPyl56048_0255.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
KOi K02492.
OMAi KMLHGTM.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci HPYL357544:GH1F-250-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 complete genome sequence of a chronic atrophic gastritis Helicobacter pylori strain: evolution during disease progression."
    Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A., Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G., Gordon J.I.
    Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HPAG1.

Entry informationi

Entry nameiHEM1_HELPH
AccessioniPrimary (citable) accession number: Q1CUR3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 11, 2006
Last modified: October 1, 2014
This is version 70 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3