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Q4JSX4

- HEM1_CORJK

UniProt

Q4JSX4 - HEM1_CORJK

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Protein

Glutamyl-tRNA reductase

Gene
hemA, jk1902
Organism
Corynebacterium jeikeium (strain K411)
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 sitei59 – 591Nucleophile By similarity
Sitei108 – 1081Important for activity By similarity
Binding sitei118 – 1181Substrate By similarity
Binding sitei129 – 1291Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi214 – 2196NADP By similarity

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 reductase (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:hemA
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 reductaseUniRule annotationPRO_5000134241Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi306537.jk1902.

Structurei

3D structure databases

ProteinModelPortaliQ4JSX4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 614Substrate binding By similarity
Regioni123 – 1253Substrate 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.
HOGENOMiHOG000109649.
KOiK02492.
OMAiPYLYVHY.
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

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MSGSTRTGSA SVLLVGLSFR SAPVTMLEQA TVADADLPKM QLSLVDNDVI    50
SESLVLSTCN RMEFYTVANA FHSGLDHVVD TIAQFSGLQT AELEPHLYVH 100
YADSAAEHML KVASGLDSMV IGEQQIIGQL RSAYQSANET GTVGRTLHDL 150
TQRALRTGKR VHSETAIDSA GASMVSFALD QALRYIEPAR ALSAVVDDAP 200
LSQPLAGHRA LIIGAGAMAS LASTHLGKLG IDHVTVANRT LSRAENLVNH 250
ARQAGVDASA VPLDGVTDCL SAVDIVVSAT GAVGNVVTEQ DVRAAVGAAG 300
GVASVAGRRG TKVMIDLSMP ADIEHSVAEI DGVKLLNIEE LTTMAGDRVQ 350
DESPARAIVA DELQSFLEQQ RAQSVVPTVK ALRQKAGEVM AEELMALERL 400
TPDMSEADRA AVVKSMKRVV DKLLHTPTVQ AKKLSAGGQQ VSYPDALAAL 450
FNLPNGMVDS VTQPGQADSS AAQTAGTSAR ADQIPSAARV GRVVREA 497
Length:497
Mass (Da):52,036
Last modified:August 2, 2005 - v1
Checksum:i3EEAF7564A2ABC2D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
CR931997 Genomic DNA. Translation: CAI38083.1 .
RefSeqi WP_011274210.1. NC_007164.1.
YP_251701.1. NC_007164.1.

3D structure databases

ProteinModelPortali Q4JSX4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 306537.jk1902.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAI38083 ; CAI38083 ; jk1902 .
GeneIDi 3433802.
KEGGi cjk:jk1902.
PATRICi 21514774. VBICorJei31838_1929.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109649.
KOi K02492.
OMAi PYLYVHY.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CJEI306537:GJ8V-1955-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 PF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMi SSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsi TIGR01035. hemA. 1 hit.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 76 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

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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