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Q252N9

- HEM1_CHLFF

UniProt

Q252N9 - HEM1_CHLFF

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Protein

Glutamyl-tRNA reductase

Gene
hemA, CF0977
Organism
Chlamydophila felis (strain Fe/C-56)
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 sitei51 – 511Nucleophile By similarity
Sitei92 – 921Important for activity By similarity
Binding sitei102 – 1021Substrate By similarity
Binding sitei113 – 1131Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi181 – 1866NADP 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

BioCyciCFEL264202:GJCG-1016-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:CF0977
OrganismiChlamydophila felis (strain Fe/C-56)
Taxonomic identifieri264202 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila
ProteomesiUP000001260: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 338338Glutamyl-tRNA reductaseUniRule annotationPRO_0000335021Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi264202.CF0977.

Structurei

3D structure databases

ProteinModelPortaliQ252N9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 534Substrate binding By similarity
Regioni107 – 1093Substrate 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.
HOGENOMiHOG000110628.
KOiK02492.
OMAiCHRAELY.
OrthoDBiEOG6MWNBM.

Family and domain databases

HAMAPiMF_00087. Glu_tRNA_reductase.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
[Graphical view]
PfamiPF05201. GlutR_N. 1 hit.
[Graphical view]
SUPFAMiSSF69742. SSF69742. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q252N9-1 [UniParc]FASTAAdd to Basket

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MVLGVVGISY REAALKEREA VINILKTFEA DTLLAQRFFG GDGSFVLLLT    50
CHRAEIYYFS KSNANVQSKL LSWISSLGTR PYCYQGLACF THLFTVTSGM 100
DSLIFGETEI QGQVKRAYIK AKTDRELPFA LHFLFQKALK EGKDFRSQVS 150
LSYPVVTMES IVEETLDLHG KSTKDKLLFI GYSDVNRKIA KGLSAKGYRN 200
LIFCSRKNIP IPYDTVARSQ LSFGKPYDVI FFGSSESARD FPGLSLESLA 250
GIPNRVVFDF NVPRTFTLVE RPEGISYLDM DFISERVQKK LQISKQCTNK 300
EKPFLALAAR KQWEVYEKKS SNISLSQIRT SRPKLLIL 338
Length:338
Mass (Da):38,262
Last modified:April 18, 2006 - v1
Checksum:i514B1BAA1E41A3B2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP006861 Genomic DNA. Translation: BAE81749.1.
RefSeqiWP_011458522.1. NC_007899.1.
YP_515894.1. NC_007899.1.

Genome annotation databases

GeneIDi3958483.
KEGGicfe:CF0977.
PATRICi20205669. VBIChlFel51660_1026.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP006861 Genomic DNA. Translation: BAE81749.1 .
RefSeqi WP_011458522.1. NC_007899.1.
YP_515894.1. NC_007899.1.

3D structure databases

ProteinModelPortali Q252N9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 264202.CF0977.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3958483.
KEGGi cfe:CF0977.
PATRICi 20205669. VBIChlFel51660_1026.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000110628.
KOi K02492.
OMAi CHRAELY.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CFEL264202:GJCG-1016-MONOMER.

Family and domain databases

HAMAPi MF_00087. Glu_tRNA_reductase.
InterProi IPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
[Graphical view ]
Pfami PF05201. GlutR_N. 1 hit.
[Graphical view ]
SUPFAMi SSF69742. SSF69742. 1 hit.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Fe/C-56.

Entry informationi

Entry nameiHEM1_CHLFF
AccessioniPrimary (citable) accession number: Q252N9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 18, 2006
Last modified: September 3, 2014
This is version 59 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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