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Q7VFF1

- HEM1_HELHP

UniProt

Q7VFF1 - HEM1_HELHP

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Protein

Glutamyl-tRNA reductase

Gene

hemA

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).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 – 561NucleophileUniRule annotation
Sitei105 – 1051Important for activityUniRule annotation
Binding sitei115 – 1151SubstrateUniRule annotation
Binding sitei126 – 1261SubstrateUniRule annotation

Regions

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

BioCyciHHEP235279:GHUA-1765-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: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 reductasePRO_0000114031Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi235279.HH1725.

Structurei

3D structure databases

ProteinModelPortaliQ7VFF1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni55 – 584Substrate bindingUniRule annotation
Regioni120 – 1223Substrate 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.
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

« Hide

        10         20         30         40         50
MQEKMEVQYM VVSFSHKNVD IATREKLSFS QEEIVPFLQE INVCDSIRES
60 70 80 90 100
ILLCTCNRVE LYVSMIDKKR AREHIYECFC THKNIALEDI KNIALMRLNQ
110 120 130 140 150
YAIYHIFSVA SSLDSLVIGE TQITGQLKLA YKLAFENALC AKDMTRLMHF
160 170 180 190 200
AFKCAASVRK ETDISAHSVS VASTAVRMAE QKLALCDKTL ENLPVLVIGS
210 220 230 240 250
GEMGRLACKH LQNANAQITL VSRTKENARK LALELDSSIN IESWEHLEQL
260 270 280 290 300
LGQYEVLFSA TSAPNCIIQS KMVQVSQKQR WWFDLALPRD IENIQMENLH
310 320 330 340 350
IFCVDDLEEI VQEHKNARED SAKKAQKILE RYSVEFFKWL QTLGIDPIIK
360 370 380 390 400
HIRYLAKQSA LKELDRAVKK GFLPASYQQN VEKILHGAFN TFLHQPTIRL
410 420 430 440
KQASENPQGD PIIEAMKNVF DISDDVVMLN GYKCEKDTIF
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: October 1, 2014
This is version 84 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, Reference proteome

Documents

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

External Data

Dasty 3