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Q0ST14

- HEM1_CLOPS

UniProt

Q0ST14 - HEM1_CLOPS

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Protein
Glutamyl-tRNA reductase
Gene
hemA, CPR_1424
Organism
Clostridium perfringens (strain SM101 / Type A)
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 sitei46 – 461Nucleophile By similarity
Sitei93 – 931Important for activity By similarity
Binding sitei103 – 1031Substrate By similarity
Binding sitei114 – 1141Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi179 – 1846NADP 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

BioCyciCPER289380:GI76-1437-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:CPR_1424
OrganismiClostridium perfringens (strain SM101 / Type A)
Taxonomic identifieri289380 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
ProteomesiUP000001824: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 400400Glutamyl-tRNA reductaseUniRule annotation
PRO_1000004613Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi289380.CPR_1424.

Structurei

3D structure databases

ProteinModelPortaliQ0ST14.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 484Substrate binding By similarity
Regioni108 – 1103Substrate 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.
HOGENOMiHOG000090159.
KOiK02492.
OMAiHEVTGEY.
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.
SUPFAMiSSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q0ST14-1 [UniParc]FASTAAdd to Basket

« Hide

MIGVIGVKRN VDIAIREKLA LYPKKHKKYV GELLNSFKEV VILNTCNRTE    50
IYFNCTEEIS EDEIFDKIFN VFNWNDDLKK YMFLSKEKRA VTHLMEVICG 100
FHSRILGEDQ ILGQIKDAYK TAISDNSISS ELQKMFEIAI ACGKKFKTKC 150
KMFEVPVSSV SISINSALLK GCRKFMVLGY GEIGKLAIKH LLSHKVECIY 200
LIVRDKSKAS DLEGEIVEIL DFNEKNHVIN EVDCIVSCTA APHTVVRNED 250
IKTEGDIIHI YDLAVPRDVD KELSEKERVI LKDIDEISKI DDKNKKIRKE 300
RMEEYKHIVE ESIEEFLNWL KIREVSSKIR NIKIRENEIC SERIKTFSNK 350
GNGENAKLAE RMIKSTADAY VNRAIELLKS EALKGSDSSC AEIIEKIFLT 400
Length:400
Mass (Da):45,912
Last modified:September 5, 2006 - v1
Checksum:i4BB8852FE0459CE9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000312 Genomic DNA. Translation: ABG85577.1.
RefSeqiWP_011592388.1. NC_008262.1.
YP_698743.1. NC_008262.1.

Genome annotation databases

EnsemblBacteriaiABG85577; ABG85577; CPR_1424.
GeneIDi4205064.
KEGGicpr:CPR_1424.
PATRICi19491139. VBICloPer122123_1399.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000312 Genomic DNA. Translation: ABG85577.1 .
RefSeqi WP_011592388.1. NC_008262.1.
YP_698743.1. NC_008262.1.

3D structure databases

ProteinModelPortali Q0ST14.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 289380.CPR_1424.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABG85577 ; ABG85577 ; CPR_1424 .
GeneIDi 4205064.
KEGGi cpr:CPR_1424.
PATRICi 19491139. VBICloPer122123_1399.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000090159.
KOi K02492.
OMAi HEVTGEY.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CPER289380:GI76-1437-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 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: SM101 / Type A.

Entry informationi

Entry nameiHEM1_CLOPS
AccessioniPrimary (citable) accession number: Q0ST14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 5, 2006
Last modified: September 3, 2014
This is version 68 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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