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Q7VFF1

- HEM1_HELHP

UniProt

Q7VFF1 - HEM1_HELHP

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Protein

Glutamyl-tRNA reductase

Gene
hemA, HH_1725
Organism
Helicobacter hepaticus (strain ATCC 51449 / 3B1)
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 sitei56 – 561Nucleophile By similarity
Sitei105 – 1051Important for activity By similarity
Binding sitei115 – 1151Substrate By similarity
Binding sitei126 – 1261Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi199 – 2046NADP 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

BioCyciHHEP235279:GHUA-1765-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:HH_1725
OrganismiHelicobacter hepaticus (strain ATCC 51449 / 3B1)
Taxonomic identifieri235279 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
ProteomesiUP000002495: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 440440Glutamyl-tRNA reductaseUniRule annotationPRO_0000114031Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi235279.HH1725.

Structurei

3D structure databases

ProteinModelPortaliQ7VFF1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni55 – 584Substrate binding By similarity
Regioni120 – 1223Substrate 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.
OMAiSINIESW.
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.

Q7VFF1-1 [UniParc]FASTAAdd to Basket

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MQEKMEVQYM VVSFSHKNVD IATREKLSFS QEEIVPFLQE INVCDSIRES    50
ILLCTCNRVE LYVSMIDKKR AREHIYECFC THKNIALEDI KNIALMRLNQ 100
YAIYHIFSVA SSLDSLVIGE TQITGQLKLA YKLAFENALC AKDMTRLMHF 150
AFKCAASVRK ETDISAHSVS VASTAVRMAE QKLALCDKTL ENLPVLVIGS 200
GEMGRLACKH LQNANAQITL VSRTKENARK LALELDSSIN IESWEHLEQL 250
LGQYEVLFSA TSAPNCIIQS KMVQVSQKQR WWFDLALPRD IENIQMENLH 300
IFCVDDLEEI VQEHKNARED SAKKAQKILE RYSVEFFKWL QTLGIDPIIK 350
HIRYLAKQSA LKELDRAVKK GFLPASYQQN VEKILHGAFN TFLHQPTIRL 400
KQASENPQGD PIIEAMKNVF DISDDVVMLN GYKCEKDTIF 440
Length:440
Mass (Da):50,370
Last modified:October 1, 2003 - v1
Checksum:i6F1675038CD6B9D1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017125 Genomic DNA. Translation: AAP78322.1.
RefSeqiNP_861256.1. NC_004917.1.
WP_011116564.1. NC_004917.1.

Genome annotation databases

EnsemblBacteriaiAAP78322; AAP78322; HH_1725.
GeneIDi1492272.
KEGGihhe:HH1725.
PATRICi20590888. VBIHelHep90276_1702.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017125 Genomic DNA. Translation: AAP78322.1 .
RefSeqi NP_861256.1. NC_004917.1.
WP_011116564.1. NC_004917.1.

3D structure databases

ProteinModelPortali Q7VFF1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 235279.HH1725.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAP78322 ; AAP78322 ; HH_1725 .
GeneIDi 1492272.
KEGGi hhe:HH1725.
PATRICi 20590888. VBIHelHep90276_1702.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci HHEP235279:GHUA-1765-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 51449 / 3B1.

Entry informationi

Entry nameiHEM1_HELHP
AccessioniPrimary (citable) accession number: Q7VFF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: September 3, 2014
This is version 83 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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