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B5ZA06

- HEM1_HELPG

UniProt

B5ZA06 - HEM1_HELPG

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Protein
Glutamyl-tRNA reductase
Gene
hemA, HPG27_219
Organism
Helicobacter pylori (strain G27)
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
Complete GO annotation...

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

BioCyciHPYL563041:GC38-227-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:HPG27_219
OrganismiHelicobacter pylori (strain G27)
Taxonomic identifieri563041 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
ProteomesiUP000001735: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 449449Glutamyl-tRNA reductaseUniRule annotation
PRO_1000093144Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi563041.HPG27_219.

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.
HOGENOMiHOG000109651.
KOiK02492.
OMAiLAHKLTN.
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.

B5ZA06-1 [UniParc]FASTAAdd to Basket

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MELETHLSKY FTLAFTHKSM SLEMREKLAI NSSATLKEFL QTIKTHCPNI    50
KECMVLSTCN RFEIYASLKH NTHANEQKNA LLKILAQNKK MSMSDLEKCV 100
LMNTDESAVH HVFSVCSSLD SLVVGETQIT GQMKNAYRFA FEEKFCSKDL 150
TRLLHFAFKC AAKVRNLTGI SKQGVSISSV AVKEALNIFE KERIKDKKAL 200
VIGLGEMAQL VIKHLLNKQF EVLILGRNAA KFEDFIKELE EPKKVSFQNI 250
ENLNAYINAY ALLFCATSSP HFIVQNRMLK ETSFRRFWFD LAVPRNIEKP 300
VFNNIFLYSV DDLEPMVREN VGNRQESRTR AYEIVGLATM EFYQWIQSLE 350
VEPLIKDLRE LARISAQKEL QKALKKRYVP KEYEGNIEKI LHNAFNTFLH 400
HPTIALKKNA QKEESDVLVG AIKNLFNLDK STTCHAQNLN LYKCEYYEE 449
Length:449
Mass (Da):51,805
Last modified:November 25, 2008 - v1
Checksum:iBD38F20F6E95404E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001173 Genomic DNA. Translation: ACI26986.1.
RefSeqiWP_000418382.1. NC_011333.1.
YP_002265852.1. NC_011333.1.

Genome annotation databases

EnsemblBacteriaiACI26986; ACI26986; HPG27_219.
GeneIDi6963104.
KEGGihpg:HPG27_219.
PATRICi20598371. VBIHelPyl113476_0246.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001173 Genomic DNA. Translation: ACI26986.1 .
RefSeqi WP_000418382.1. NC_011333.1.
YP_002265852.1. NC_011333.1.

3D structure databases

ModBasei Search...

Protein-protein interaction databases

STRINGi 563041.HPG27_219.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACI26986 ; ACI26986 ; HPG27_219 .
GeneIDi 6963104.
KEGGi hpg:HPG27_219.
PATRICi 20598371. VBIHelPyl113476_0246.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci HPYL563041:GC38-227-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: G27.

Entry informationi

Entry nameiHEM1_HELPG
AccessioniPrimary (citable) accession number: B5ZA06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 25, 2008
Last modified: September 3, 2014
This is version 46 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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