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Q9RRE5

- HEM1_DEIRA

UniProt

Q9RRE5 - HEM1_DEIRA

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Protein
Glutamyl-tRNA reductase
Gene
hemA, DR_2547
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) By similarity.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 – 541Nucleophile By similarity
Sitei95 – 951Important for activity By similarity
Binding sitei105 – 1051Substrate By similarity
Binding sitei116 – 1161Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi185 – 1906NADP By similarity

GO - Molecular functioni

  1. NADP binding Source: InterPro
  2. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP

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 reductase (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:hemA
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 reductaseUniRule annotation
PRO_0000114019Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi243230.DR_2547.

Structurei

3D structure databases

ProteinModelPortaliQ9RRE5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 564Substrate binding By similarity
Regioni110 – 1123Substrate binding By similarity

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 By similarity.UniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109651.
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

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MPQPAPLDFV VVGLNHQTAP VEVRERVAVR PEEEGALLGH LARHADEVLL    50
LATCNRTEVY LAGVHGDPLA AFEGAWGHAL LDHLYVYRGE AAVRHLYRVT 100
AGLDSLVIGE TQIQGQVKRA WQSARERGLS GTLMNKVVQG ALAAGKRVRS 150
HTGLSDKVVS VSSAAVELAQ AALGELSQRR ALILGAGETA ELTLTHLRAA 200
GVQDVLVVNR TAERARALAE KLGGRACPAE ELSAALPEVD VVIASSAAPH 250
YVVTAQNVRE ALAGRPGRAM FLIDISVPRI LDPEIASVPG AHLYNLDDLT 300
AVVQRNMQSR RAALPQAEAI IRELGSDLSR WYLTRETQLA RQAELALACD 350
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.
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: September 3, 2014
This is version 102 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 By similarity.

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

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