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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Corynebacterium jeikeium (strain K411)
Status
Reviewed-Annotation score: 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 sitei59 – 591NucleophileUniRule annotation
Sitei108 – 1081Important for activityUniRule annotation
Binding sitei118 – 1181SubstrateUniRule annotation
Binding sitei129 – 1291SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi214 – 2196NADPUniRule 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

BioCyciCJEI306537:GJ8V-1955-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:jk1902
OrganismiCorynebacterium jeikeium (strain K411)
Taxonomic identifieri306537 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
ProteomesiUP000000545: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 497497Glutamyl-tRNA reductasePRO_5000134241Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi306537.jk1902.

Structurei

3D structure databases

ProteinModelPortaliQ4JSX4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 614Substrate bindingUniRule annotation
Regioni123 – 1253Substrate 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.
HOGENOMiHOG000109649.
KOiK02492.
OMAiGAHSISM.
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.

Q4JSX4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGSTRTGSA SVLLVGLSFR SAPVTMLEQA TVADADLPKM QLSLVDNDVI
60 70 80 90 100
SESLVLSTCN RMEFYTVANA FHSGLDHVVD TIAQFSGLQT AELEPHLYVH
110 120 130 140 150
YADSAAEHML KVASGLDSMV IGEQQIIGQL RSAYQSANET GTVGRTLHDL
160 170 180 190 200
TQRALRTGKR VHSETAIDSA GASMVSFALD QALRYIEPAR ALSAVVDDAP
210 220 230 240 250
LSQPLAGHRA LIIGAGAMAS LASTHLGKLG IDHVTVANRT LSRAENLVNH
260 270 280 290 300
ARQAGVDASA VPLDGVTDCL SAVDIVVSAT GAVGNVVTEQ DVRAAVGAAG
310 320 330 340 350
GVASVAGRRG TKVMIDLSMP ADIEHSVAEI DGVKLLNIEE LTTMAGDRVQ
360 370 380 390 400
DESPARAIVA DELQSFLEQQ RAQSVVPTVK ALRQKAGEVM AEELMALERL
410 420 430 440 450
TPDMSEADRA AVVKSMKRVV DKLLHTPTVQ AKKLSAGGQQ VSYPDALAAL
460 470 480 490
FNLPNGMVDS VTQPGQADSS AAQTAGTSAR ADQIPSAARV GRVVREA
Length:497
Mass (Da):52,036
Last modified:August 2, 2005 - v1
Checksum:i3EEAF7564A2ABC2D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR931997 Genomic DNA. Translation: CAI38083.1.
RefSeqiWP_011274210.1. NC_007164.1.
YP_251701.1. NC_007164.1.

Genome annotation databases

EnsemblBacteriaiCAI38083; CAI38083; jk1902.
GeneIDi3433802.
KEGGicjk:jk1902.
PATRICi21514774. VBICorJei31838_1929.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR931997 Genomic DNA. Translation: CAI38083.1.
RefSeqiWP_011274210.1. NC_007164.1.
YP_251701.1. NC_007164.1.

3D structure databases

ProteinModelPortaliQ4JSX4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi306537.jk1902.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAI38083; CAI38083; jk1902.
GeneIDi3433802.
KEGGicjk:jk1902.
PATRICi21514774. VBICorJei31838_1929.

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109649.
KOiK02492.
OMAiGAHSISM.
OrthoDBiEOG6MWNBM.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316.
BioCyciCJEI306537:GJ8V-1955-MONOMER.

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]
ProtoNetiSearch...

Publicationsi

  1. "Complete genome sequence and analysis of the multiresistant nosocomial pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the human skin flora."
    Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A., Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F., Rupp O., Schneiker S., Viehoever P., Puehler A.
    J. Bacteriol. 187:4671-4682(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K411.

Entry informationi

Entry nameiHEM1_CORJK
AccessioniPrimary (citable) accession number: Q4JSX4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: August 2, 2005
Last modified: March 4, 2015
This is version 80 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.