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Q9RRE5

- HEM1_DEIRA

UniProt

Q9RRE5 - HEM1_DEIRA

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
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 sitei54 – 541NucleophileUniRule annotation
Sitei95 – 951Important for activityUniRule annotation
Binding sitei105 – 1051SubstrateUniRule annotation
Binding sitei116 – 1161SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi185 – 1906NADPUniRule 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

BioCyciDRAD243230:GH46-2600-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:DR_2547
OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Taxonomic identifieri243230 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
ProteomesiUP000002524: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 350350Glutamyl-tRNA reductasePRO_0000114019Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi243230.DR_2547.

Structurei

3D structure databases

ProteinModelPortaliQ9RRE5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 564Substrate bindingUniRule annotation
Regioni110 – 1123Substrate 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.
InParanoidiQ9RRE5.
KOiK02492.
OMAiMIICEEL.
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.

Q9RRE5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPQPAPLDFV VVGLNHQTAP VEVRERVAVR PEEEGALLGH LARHADEVLL
60 70 80 90 100
LATCNRTEVY LAGVHGDPLA AFEGAWGHAL LDHLYVYRGE AAVRHLYRVT
110 120 130 140 150
AGLDSLVIGE TQIQGQVKRA WQSARERGLS GTLMNKVVQG ALAAGKRVRS
160 170 180 190 200
HTGLSDKVVS VSSAAVELAQ AALGELSQRR ALILGAGETA ELTLTHLRAA
210 220 230 240 250
GVQDVLVVNR TAERARALAE KLGGRACPAE ELSAALPEVD VVIASSAAPH
260 270 280 290 300
YVVTAQNVRE ALAGRPGRAM FLIDISVPRI LDPEIASVPG AHLYNLDDLT
310 320 330 340 350
AVVQRNMQSR RAALPQAEAI IRELGSDLSR WYLTRETQLA RQAELALACD
Length:350
Mass (Da):37,529
Last modified:May 1, 2000 - v1
Checksum:i72B9BC71CA368507
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000513 Genomic DNA. Translation: AAF12088.1.
PIRiF75259.
RefSeqiNP_296267.1. NC_001263.1.
WP_010889172.1. NC_001263.1.

Genome annotation databases

EnsemblBacteriaiAAF12088; AAF12088; DR_2547.
GeneIDi1798429.
KEGGidra:DR_2547.
PATRICi21632833. VBIDeiRad64572_2790.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000513 Genomic DNA. Translation: AAF12088.1 .
PIRi F75259.
RefSeqi NP_296267.1. NC_001263.1.
WP_010889172.1. NC_001263.1.

3D structure databases

ProteinModelPortali Q9RRE5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243230.DR_2547.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAF12088 ; AAF12088 ; DR_2547 .
GeneIDi 1798429.
KEGGi dra:DR_2547.
PATRICi 21632833. VBIDeiRad64572_2790.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
InParanoidi Q9RRE5.
KOi K02492.
OMAi MIICEEL.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci DRAD243230:GH46-2600-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: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.

Entry informationi

Entry nameiHEM1_DEIRA
AccessioniPrimary (citable) accession number: Q9RRE5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 104 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