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O67314

- HEM1_AQUAE

UniProt

O67314 - HEM1_AQUAE

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Aquifex aeolicus (strain VF5)
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 sitei51 – 511NucleophileUniRule annotation
Sitei97 – 971Important for activityUniRule annotation
Binding sitei107 – 1071SubstrateUniRule annotation
Binding sitei118 – 1181SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi187 – 1926NADPUniRule 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

BioCyciAAEO224324:GJBH-916-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:aq_1279
OrganismiAquifex aeolicus (strain VF5)
Taxonomic identifieri224324 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
ProteomesiUP000000798: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 406406Glutamyl-tRNA reductasePRO_0000113987Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi224324.aq_1279.

Structurei

3D structure databases

ProteinModelPortaliO67314.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 534Substrate bindingUniRule annotation
Regioni112 – 1143Substrate 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.
InParanoidiO67314.
KOiK02492.
OMAiLAHKLTN.
OrthoDBiEOG6MWNBM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFiPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMiSSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O67314-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGEIFVAGVN FKVAPVEVRE KLACSLEETK KVLPILKRET PLEEVMLLST
60 70 80 90 100
CNRVEVYAYN FVENSEDLIN KLLEIKRLNP SFKRYFFVKR GEEAVYHIFK
110 120 130 140 150
VASSLDSMVI GEPQIVAQFK EAYRVAKEAG TVGKILNRVY EKALRASKRV
160 170 180 190 200
RTETGISRSA VSVSYAAVEL AKKIFGDLKE AKVLLIGAGE MGELAANYLR
210 220 230 240 250
RFGAKLHITN RTYERALKLV KELSGNVLRF EELKEYLPLM DIVIVSTGAK
260 270 280 290 300
DYILKREDFE RSVRERHYEP QFVIDIAVPR NVDPEAGNVE GVFLYDIDDL
310 320 330 340 350
KQVVEENLKE RIKEAQRGEI ILWDEVKKFM NWYESLKAEP YILELKASVE
360 370 380 390 400
GKEVSPYIKK LVHRAIKEIK RNPEVADIIL RIFKEVEKNE PRRKELSNVY

NGTHGA
Length:406
Mass (Da):46,648
Last modified:August 1, 1998 - v1
Checksum:i77F3ECC488FC4394
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000657 Genomic DNA. Translation: AAC07274.1.
PIRiG70410.
RefSeqiNP_213878.1. NC_000918.1.
WP_010880816.1. NC_000918.1.

Genome annotation databases

EnsemblBacteriaiAAC07274; AAC07274; aq_1279.
GeneIDi1192752.
KEGGiaae:aq_1279.
PATRICi20959764. VBIAquAeo85532_0999.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000657 Genomic DNA. Translation: AAC07274.1 .
PIRi G70410.
RefSeqi NP_213878.1. NC_000918.1.
WP_010880816.1. NC_000918.1.

3D structure databases

ProteinModelPortali O67314.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224324.aq_1279.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC07274 ; AAC07274 ; aq_1279 .
GeneIDi 1192752.
KEGGi aae:aq_1279.
PATRICi 20959764. VBIAquAeo85532_0999.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
InParanoidi O67314.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci AAEO224324:GJBH-916-MONOMER.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_00087. Glu_tRNA_reductase.
InterProi IPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view ]
Pfami PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMi 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: VF5.

Entry informationi

Entry nameiHEM1_AQUAE
AccessioniPrimary (citable) accession number: O67314
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: October 29, 2014
This is version 108 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