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Q17W63

- HEM1_HELAH

UniProt

Q17W63 - HEM1_HELAH

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Helicobacter acinonychis (strain Sheeba)
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 sitei57 – 571NucleophileUniRule annotation
Sitei109 – 1091Important for activityUniRule annotation
Binding sitei119 – 1191SubstrateUniRule annotation
Binding sitei130 – 1301SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi201 – 2066NADPUniRule 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

BioCyciHACI382638:GJAU-1278-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:Hac_1379
OrganismiHelicobacter acinonychis (strain Sheeba)
Taxonomic identifieri382638 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
ProteomesiUP000000775: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 447447Glutamyl-tRNA reductasePRO_0000335045Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi382638.Hac_1379.

Structurei

3D structure databases

ProteinModelPortaliQ17W63.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni56 – 594Substrate bindingUniRule annotation
Regioni124 – 1263Substrate 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.
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.

Q17W63-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MELETTKYFI LAFTHKSMSL EMREKLAINS PAILKEFLQT IKNYCPNIKE
60 70 80 90 100
CMVLSTCNRF EIYASLKHNT HADEQKNALL KILAQNKKMS VSDLEKCVLM
110 120 130 140 150
STDESAVHHV FSVCSSLDSL VVGETQITGQ MKNAYKFAFE EKFCSKDLTR
160 170 180 190 200
LLHFAFKCAA KVRNLTGISK QGVSISSVAV KEALSIFEKE KIEDKKALVI
210 220 230 240 250
GLGEMSQLVI KHLLNKQFEV LVLGRNAAKF EDFLKELEEP KKVSFQNIEN
260 270 280 290 300
LNAYINAYEL LFCATSSPNF IVQNCMVKET IFRRFWFDLA VPRNIEKPIF
310 320 330 340 350
NNIFLYSVDD LEPMVRENVE NRQESRMKAY EIVGLATMEF YQWIQSLEVE
360 370 380 390 400
PLIKDLRELA RISAQKELQK AVKKRYVPKE YESNIEKILH NAFNAFLHHP
410 420 430 440
TIALKKNAQK EESDVLVGTI KNLFNLDKSS TNHAQNLNLY KCEYYEE
Length:447
Mass (Da):51,599
Last modified:July 25, 2006 - v1
Checksum:i72A3F222978A27FE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM260522 Genomic DNA. Translation: CAK00113.1.
RefSeqiYP_665112.1. NC_008229.1.

Genome annotation databases

EnsemblBacteriaiCAK00113; CAK00113; Hac_1379.
GeneIDi4177421.
KEGGihac:Hac_1379.
PATRICi20586596. VBIHelAci71660_1302.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM260522 Genomic DNA. Translation: CAK00113.1 .
RefSeqi YP_665112.1. NC_008229.1.

3D structure databases

ProteinModelPortali Q17W63.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 382638.Hac_1379.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAK00113 ; CAK00113 ; Hac_1379 .
GeneIDi 4177421.
KEGGi hac:Hac_1379.
PATRICi 20586596. VBIHelAci71660_1302.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci HACI382638:GJAU-1278-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. "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a host jump from early humans to large felines."
    Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G., Gressmann H., Achtman M., Schuster S.C.
    PLoS Genet. 2:1097-1110(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sheeba.

Entry informationi

Entry nameiHEM1_HELAH
AccessioniPrimary (citable) accession number: Q17W63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: July 25, 2006
Last modified: October 1, 2014
This is version 74 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