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Q8FSF8

- HEM1_COREF

UniProt

Q8FSF8 - HEM1_COREF

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
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
Sitei97 – 971Important for activityUniRule annotation
Binding sitei107 – 1071SubstrateUniRule annotation
Binding sitei118 – 1181SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi194 – 1996NADPUniRule 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

BioCyciCEFF196164:GJW8-444-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:CE0435
OrganismiCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Taxonomic identifieri196164 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
ProteomesiUP000001409: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 466466Glutamyl-tRNA reductasePRO_0000114016Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi196164.CE0435.

Structurei

3D structure databases

ProteinModelPortaliQ8FSF8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni47 – 504Substrate bindingUniRule annotation
Regioni112 – 1143Substrate 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

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.

Q8FSF8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLVVGMSHRS APVALLERLS MDDSVRGQTT SALVERPSLS EALIVSTCNR
60 70 80 90 100
LEVYTVTSSF HTGVNDVVEV LHEISGVDIE TLRGYLYVRY ADAAAEHMLV
110 120 130 140 150
VASGLDSMVV GEQQIIGQVR TAYQQATEAG TVGPALHALA QTALHTGKRV
160 170 180 190 200
HTETDIDEAG ASMVSFAIDR ALTQMGIDPA SDKPLAGKTA LVLGAGAMSS
210 220 230 240 250
LAATHLGREG VDKLIMANRT RERAERLASH SLEAGVPAEV VDFADRASVL
260 270 280 290 300
DRVDMVVSAT GADDFTVKPA DIPAGVQLML VDLSMPRDID DACAEVPGVD
310 320 330 340 350
LVNIERLHRA KREDPTGAAA EGADALAIVR EELEAFTSEQ RIRDVVPAVS
360 370 380 390 400
ALRKRANELL LDELDRLQAR TPDISQEDWK EVTRTVRRVM DKFLHEPTVR
410 420 430 440 450
VKKLAARSGS VSYESALQEL FGLEAVQTTA PPAITSVNAS DLPDAGIVAI
460
VNSPSTTGQS VSVDGS
Length:466
Mass (Da):49,685
Last modified:March 1, 2003 - v1
Checksum:i23A441F510CDCF11
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000035 Genomic DNA. Translation: BAC17245.1.
RefSeqiNP_737045.1. NC_004369.1.

Genome annotation databases

EnsemblBacteriaiBAC17245; BAC17245; BAC17245.
GeneIDi1032556.
KEGGicef:CE0435.
PATRICi21487026. VBICorEff9312_0459.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000035 Genomic DNA. Translation: BAC17245.1 .
RefSeqi NP_737045.1. NC_004369.1.

3D structure databases

ProteinModelPortali Q8FSF8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 196164.CE0435.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC17245 ; BAC17245 ; BAC17245 .
GeneIDi 1032556.
KEGGi cef:CE0435.
PATRICi 21487026. VBICorEff9312_0459.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CEFF196164:GJW8-444-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. "Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
    Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
    Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Entry informationi

Entry nameiHEM1_COREF
AccessioniPrimary (citable) accession number: Q8FSF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: March 1, 2003
Last modified: October 1, 2014
This is version 88 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