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P56125

- HEM1_HELPY

UniProt

P56125 - HEM1_HELPY

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Protein
Glutamyl-tRNA reductase
Gene
hemA, HP_0239
Organism
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
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
Sitei111 – 1111Important for activity By similarity
Binding sitei121 – 1211Substrate By similarity
Binding sitei132 – 1321Substrate By similarity

Regions

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

BioCyciHPY:HP0239-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:HP_0239
OrganismiHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Taxonomic identifieri85962 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
ProteomesiUP000000429: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 449449Glutamyl-tRNA reductaseUniRule annotation
PRO_0000114032Add
BLAST

Proteomic databases

PRIDEiP56125.

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi85962.HP0239.

Structurei

3D structure databases

ProteinModelPortaliP56125.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 614Substrate binding By similarity
Regioni126 – 1283Substrate 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.
OMAiHEVTGEY.
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.

P56125-1 [UniParc]FASTAAdd to Basket

« Hide

MELETHLSKY FTLAFTHKSM SLEMREKLAI NSNATLKEFL QTIKNHCPNI    50
KECMVLSTCN RFEIYASLKH GANTNEQKNA LLKILAQNKK MSVSDLEKCV 100
LMNTDESAVH HVFSVCSSLD SLVVGETQIT GQMKNAYKFA FEEKFCSKDL 150
TRLLHFAFKC AAKVRNLTGI SKQGVSISSV AVKEALNIFE KERIKDKKAL 200
VIGLGEMAQL VIKHLLNKQF EALILGRNAA KFEDFIKELE EPKKVSFQNI 250
ENLNAYINEY ELLFCATSSP HFIVQNRMLK ETIFRRFWFD LAVPRNIEKP 300
VLDNIFLYSV DDLEPMVREN VENRQESRMR AYEIVGLATM EFYQWIQSLE 350
VEPVIKDLRE LARISAQKEL QKALKKRYVP KEYENNIEKI LHNAFNTFLH 400
NPTIALKKNA QKEESDVLVG AIKNLFNLDK SNANHAQNLN LYKCEYYEE 449
Length:449
Mass (Da):51,902
Last modified:November 1, 1997 - v1
Checksum:iC4B12225DE4D83CB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000511 Genomic DNA. Translation: AAD07306.1.
PIRiG64549.
RefSeqiNP_207037.1. NC_000915.1.
YP_006934166.1. NC_018939.1.

Genome annotation databases

EnsemblBacteriaiAAD07306; AAD07306; HP_0239.
GeneIDi13869423.
898973.
KEGGiheo:C694_01210.
hpy:HP0239.
PATRICi20591703. VBIHelPyl33062_0250.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000511 Genomic DNA. Translation: AAD07306.1 .
PIRi G64549.
RefSeqi NP_207037.1. NC_000915.1.
YP_006934166.1. NC_018939.1.

3D structure databases

ProteinModelPortali P56125.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 85962.HP0239.

Proteomic databases

PRIDEi P56125.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD07306 ; AAD07306 ; HP_0239 .
GeneIDi 13869423.
898973.
KEGGi heo:C694_01210.
hpy:HP0239.
PATRICi 20591703. VBIHelPyl33062_0250.

Phylogenomic databases

eggNOGi COG0373.
KOi K02492.
OMAi HEVTGEY.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci HPY:HP0239-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: ATCC 700392 / 26695.

Entry informationi

Entry nameiHEM1_HELPY
AccessioniPrimary (citable) accession number: P56125
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 3, 2014
This is version 102 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, Reference proteome

Documents

  1. Helicobacter pylori
    Helicobacter pylori (strain 26695): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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