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P0C2E3

- HEM1_CLOPE

UniProt

P0C2E3 - HEM1_CLOPE

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Clostridium perfringens (strain 13 / 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).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 – 461NucleophileUniRule annotation
Sitei93 – 931Important for activityUniRule annotation
Binding sitei103 – 1031SubstrateUniRule annotation
Binding sitei114 – 1141SubstrateUniRule annotation

Regions

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

BioCyciCPER195102:GJFM-1483-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:CPE1437
OrganismiClostridium perfringens (strain 13 / Type A)
Taxonomic identifieri195102 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium
ProteomesiUP000000818: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 400400Glutamyl-tRNA reductasePRO_0000114013Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi195102.CPE1437.

Structurei

3D structure databases

ProteinModelPortaliP0C2E3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 484Substrate bindingUniRule annotation
Regioni108 – 1103Substrate 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.
HOGENOMiHOG000090159.
KOiK02492.
OMAiAITCGKK.
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.

P0C2E3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIGVIGVKRN VDIAIREKLA LYPKKHKKYV GELLNSFKEV VILNTCNRTE
60 70 80 90 100
IYFNCTEEIS EDEIFDKIFN VFNWNDDLKK YMFLSKEKRA VTHLMEVICG
110 120 130 140 150
FHSRILGEDQ ILGQIKDAYK TAISDNSISS ELQKMFEIAI ACGKKFKTEC
160 170 180 190 200
KMFEVPVSSV SISINSALLK GCRKFMVLGY GEIGKLAIKH LLSHKVECIY
210 220 230 240 250
LIVRDKSKAS DLEGEIVEVL DFNEKNQVIN EVDCIVSCTA APHTVVRNED
260 270 280 290 300
IKTEGDIIHI YDLAVPRDVD KELSEKERVI LKDIDEISKI DDKNKKIRKE
310 320 330 340 350
RMEEYKHIVE ESIEEFLNWL KIREVSSKIR NIKIRENEIC SERIKTFSNK
360 370 380 390 400
GNGENAKLAE RMIKSTADAY VNRAIELLKS EALKGSDSSC AEIIEKIFLT
Length:400
Mass (Da):45,890
Last modified:January 23, 2007 - v1
Checksum:i037AC2CFD4F60DEE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000016 Genomic DNA. Translation: BAB81143.1.
RefSeqiNP_562353.1. NC_003366.1.

Genome annotation databases

EnsemblBacteriaiBAB81143; BAB81143; BAB81143.
GeneIDi989747.
KEGGicpe:CPE1437.
PATRICi19496823. VBICloPer59675_1507.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000016 Genomic DNA. Translation: BAB81143.1 .
RefSeqi NP_562353.1. NC_003366.1.

3D structure databases

ProteinModelPortali P0C2E3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 195102.CPE1437.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB81143 ; BAB81143 ; BAB81143 .
GeneIDi 989747.
KEGGi cpe:CPE1437.
PATRICi 19496823. VBICloPer59675_1507.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CPER195102:GJFM-1483-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: 13 / Type A.

Entry informationi

Entry nameiHEM1_CLOPE
AccessioniPrimary (citable) accession number: P0C2E3
Secondary accession number(s): Q9ZND3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: October 1, 2014
This is version 63 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