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Q9PLR2

- HEM1_CHLMU

UniProt

Q9PLR2 - HEM1_CHLMU

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Protein
Glutamyl-tRNA reductase
Gene
hemA, TC_0033
Organism
Chlamydia muridarum (strain MoPn / Nigg)
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 sitei61 – 611Nucleophile By similarity
Sitei100 – 1001Important for activity By similarity
Binding sitei110 – 1101Substrate By similarity
Binding sitei121 – 1211Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi189 – 1946NADP 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

BioCyciCMUR243161:GHYU-35-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:TC_0033
OrganismiChlamydia muridarum (strain MoPn / Nigg)
Taxonomic identifieri243161 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
ProteomesiUP000000800: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 333333Glutamyl-tRNA reductaseUniRule annotation
PRO_0000114005Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi243161.TC0033.

Structurei

3D structure databases

ProteinModelPortaliQ9PLR2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni60 – 634Substrate binding By similarity
Regioni115 – 1173Substrate 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.
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.

Q9PLR2-1 [UniParc]FASTAAdd to Basket

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MVREGEEHID EEFSLGVIGV SYRETALQQR EQVLQFLQQA QLSFYPKFPQ    50
EEGRSVLLST CHRVELYGMA TEAIFSTLEK EIREMGAIPY FYRNQDCFSH 100
LFCVVGGMDS LVLGETEIQG QVKRAYLQAI EEQKLAFALH FLFQKALKEG 150
KVFRTKRSSP STEITIPAFV QHELQKQKMA RSASLLFMGY SEINRSVAYY 200
LQKQGFSRIT FCSRQPLSLR SMDQVLREEV CFQDPYHVIF LGSSELRHAF 250
PRSLWEGVWD FPGRLVFDFA VPRALPVQPA CRDRYIDMEQ ISDWLRQHQK 300
EVFPLQLDSL REVGYRYWES LNRRLARRRY ASV 333
Length:333
Mass (Da):39,016
Last modified:October 1, 2000 - v1
Checksum:i81D9B761ECC8A986
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE002160 Genomic DNA. Translation: AAF38924.1.
PIRiE81748.
RefSeqiNP_296417.1. NC_002620.2.

Genome annotation databases

EnsemblBacteriaiAAF38924; AAF38924; TC_0033.
GeneIDi1245558.
KEGGicmu:TC_0033.
PATRICi20371402. VBIChlMur19118_0042.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE002160 Genomic DNA. Translation: AAF38924.1 .
PIRi E81748.
RefSeqi NP_296417.1. NC_002620.2.

3D structure databases

ProteinModelPortali Q9PLR2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243161.TC0033.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAF38924 ; AAF38924 ; TC_0033 .
GeneIDi 1245558.
KEGGi cmu:TC_0033.
PATRICi 20371402. VBIChlMur19118_0042.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CMUR243161:GHYU-35-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: MoPn / Nigg.

Entry informationi

Entry nameiHEM1_CHLMU
AccessioniPrimary (citable) accession number: Q9PLR2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 1, 2000
Last modified: September 3, 2014
This is version 89 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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