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Q6MEC8

- HEM1_PARUW

UniProt

Q6MEC8 - HEM1_PARUW

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Protein
Glutamyl-tRNA reductase
Gene
hemA, pc0347
Organism
Protochlamydia amoebophila (strain UWE25)
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 sitei47 – 471Nucleophile 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 bindingi183 – 1886NADP 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

BioCyciPAMO264201:GH0M-356-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:pc0347
OrganismiProtochlamydia amoebophila (strain UWE25)
Taxonomic identifieri264201 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesParachlamydiaceaeCandidatus Protochlamydia
ProteomesiUP000000529: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 340340Glutamyl-tRNA reductaseUniRule annotation
PRO_0000114051Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi264201.pc0347.

Structurei

3D structure databases

ProteinModelPortaliQ6MEC8.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni46 – 494Substrate 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.
HOGENOMiHOG000112883.
KOiK02492.
OMAiAETEIQG.
OrthoDBiEOG6MWNBM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
SUPFAMiSSF69742. SSF69742. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6MEC8-1 [UniParc]FASTAAdd to Basket

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MRIGVIGINH KLADLKLRDA LAKACQKRFG ANQSVHDQHH FILLSTCNRT    50
EVYFSSHDLT ATHSYLLSIL RQDVKEDFDH KLYSFFGMDC FSHLTRVTSG 100
LDSAIVAETE IQGQVKNAYN LATTFLCLPK ELHFLFQKSM GIAKRIRSEL 150
HLGRGLPNLE HAILQTGKYF FRNTQQPKIL FVGASEINRK ILHFLKSKQY 200
SDMTICNRSE IRSKELAILY GLHLLPWCQL DSWHQYDWII FGTKSSEYLI 250
KPEKNFIPAD NDKLIMDLCV PRNVEPKLGQ NAKITLLNID QINRLLKIRH 300
RGMTQALIEA ENRVNLATYE HTNRYRQKED SKITIFAASA 340
Length:340
Mass (Da):39,232
Last modified:July 5, 2004 - v1
Checksum:i93824A5CBA5E3D40
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX908798 Genomic DNA. Translation: CAF23071.1.
RefSeqiYP_007346.1. NC_005861.1.

Genome annotation databases

EnsemblBacteriaiCAF23071; CAF23071; pc0347.
GeneIDi2779718.
KEGGipcu:pc0347.
PATRICi31995996. VBICanPro72727_0353.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX908798 Genomic DNA. Translation: CAF23071.1 .
RefSeqi YP_007346.1. NC_005861.1.

3D structure databases

ProteinModelPortali Q6MEC8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 264201.pc0347.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAF23071 ; CAF23071 ; pc0347 .
GeneIDi 2779718.
KEGGi pcu:pc0347.
PATRICi 31995996. VBICanPro72727_0353.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000112883.
KOi K02492.
OMAi AETEIQG.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci PAMO264201:GH0M-356-MONOMER.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_00087. Glu_tRNA_reductase.
InterProi IPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view ]
Pfami PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 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: UWE25.

Entry informationi

Entry nameiHEM1_PARUW
AccessioniPrimary (citable) accession number: Q6MEC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: July 5, 2004
Last modified: September 3, 2014
This is version 78 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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