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A1RQP7

- HEM1_PYRIL

UniProt

A1RQP7 - HEM1_PYRIL

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Pyrobaculum islandicum (strain DSM 4184 / JCM 9189)
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 sitei48 – 481NucleophileUniRule annotation
Sitei88 – 881Important for activityUniRule annotation
Binding sitei98 – 981SubstrateUniRule annotation
Binding sitei109 – 1091SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi177 – 1826NADPUniRule 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

BioCyciPISL384616:GC8H-98-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:Pisl_0096
OrganismiPyrobaculum islandicum (strain DSM 4184 / JCM 9189)
Taxonomic identifieri384616 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum
ProteomesiUP000002595: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 393393Glutamyl-tRNA reductasePRO_1000004679Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi384616.Pisl_0096.

Structurei

3D structure databases

ProteinModelPortaliA1RQP7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni47 – 504Substrate bindingUniRule annotation
Regioni103 – 1053Substrate 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.
HOGENOMiHOG000112880.
KOiK02492.
OMAiYREADAN.

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]
PfamiPF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
SUPFAMiSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A1RQP7-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MDLLSPLSAI VLTYREVDTD TLGKIGEEMR KCLEQMGRGT PIYVLHTCGR
60 70 80 90 100
VEAYLYGASP EEVQTVAETY RKYVNSVRII AGVEAARHLF RVAAGLDSML
110 120 130 140 150
IGETDVLGQL EEAFDRQVRA GYTRGLLKTI VERAVRVGKR VRTETAISRG
160 170 180 190 200
PRGLGSLSII YVSRLLDMRQ AKVAVLGAGA VGAGLAMELA ARGVKKLYIL
210 220 230 240 250
NRTLEKAKEV AAKTGGEARP LTKEEVERCL RECDVVFSSV HSMEYIIDKI
260 270 280 290 300
PEGASVKVVV DLGVPQTVAS GLPVKVVRIE DLREIAEQYN AERASEIAKA
310 320 330 340 350
EAIVEEELAI LPKLLARRYI EETVSTFIET AMLAAEEEGA RAGCNTATLA
360 370 380 390
ARTTVKRILL PLVERLKKMA EDGQIEEAVK LAQMLSQTIG RKI
Length:393
Mass (Da):43,011
Last modified:February 6, 2007 - v1
Checksum:iD5B0DC67046AF16A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000504 Genomic DNA. Translation: ABL87279.1.
RefSeqiWP_011761856.1. NC_008701.1.
YP_929622.1. NC_008701.1.

Genome annotation databases

EnsemblBacteriaiABL87279; ABL87279; Pisl_0096.
GeneIDi4616972.
KEGGipis:Pisl_0096.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000504 Genomic DNA. Translation: ABL87279.1 .
RefSeqi WP_011761856.1. NC_008701.1.
YP_929622.1. NC_008701.1.

3D structure databases

ProteinModelPortali A1RQP7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 384616.Pisl_0096.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABL87279 ; ABL87279 ; Pisl_0096 .
GeneIDi 4616972.
KEGGi pis:Pisl_0096.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000112880.
KOi K02492.
OMAi YREADAN.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci PISL384616:GC8H-98-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 PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view ]
SUPFAMi SSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete sequence of Pyrobaculum islandicum DSM 4184."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.
    , Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.
    Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 4184 / JCM 9189.

Entry informationi

Entry nameiHEM1_PYRIL
AccessioniPrimary (citable) accession number: A1RQP7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: October 1, 2014
This is version 59 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