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Q6MEC8

- HEM1_PARUW

UniProt

Q6MEC8 - HEM1_PARUW

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Protein

Glutamyl-tRNA reductase

Gene

hemA

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).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 – 471NucleophileUniRule annotation
Sitei93 – 931Important for activityUniRule annotation
Binding sitei103 – 1031SubstrateUniRule annotation
Binding sitei114 – 1141SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi183 – 1886NADPUniRule 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

BioCyciPAMO264201:GH0M-356-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: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 reductasePRO_0000114051Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi264201.pc0347.

Structurei

3D structure databases

ProteinModelPortaliQ6MEC8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni46 – 494Substrate 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.
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

« Hide

        10         20         30         40         50
MRIGVIGINH KLADLKLRDA LAKACQKRFG ANQSVHDQHH FILLSTCNRT
60 70 80 90 100
EVYFSSHDLT ATHSYLLSIL RQDVKEDFDH KLYSFFGMDC FSHLTRVTSG
110 120 130 140 150
LDSAIVAETE IQGQVKNAYN LATTFLCLPK ELHFLFQKSM GIAKRIRSEL
160 170 180 190 200
HLGRGLPNLE HAILQTGKYF FRNTQQPKIL FVGASEINRK ILHFLKSKQY
210 220 230 240 250
SDMTICNRSE IRSKELAILY GLHLLPWCQL DSWHQYDWII FGTKSSEYLI
260 270 280 290 300
KPEKNFIPAD NDKLIMDLCV PRNVEPKLGQ NAKITLLNID QINRLLKIRH
310 320 330 340
RGMTQALIEA ENRVNLATYE HTNRYRQKED SKITIFAASA
Length:340
Mass (Da):39,232
Last modified:July 5, 2004 - v1
Checksum:i93824A5CBA5E3D40
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: October 1, 2014
This is version 79 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