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B0B8N8

- HEM1_CHLT2

UniProt

B0B8N8 - HEM1_CHLT2

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Protein
Glutamyl-tRNA reductase
Gene
hemA, CTL0031
Organism
Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B)
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
Complete GO annotation...

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

BioCyciCTRA471472:GJ9M-33-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:CTL0031
OrganismiChlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B)
Taxonomic identifieri471472 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
ProteomesiUP000000795: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 335335Glutamyl-tRNA reductaseUniRule annotation
PRO_1000093124Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi471472.CTL0031.

Structurei

3D structure databases

ProteinModelPortaliB0B8N8.

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.
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.

B0B8N8-1 [UniParc]FASTAAdd to Basket

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MVREGEERIG NRVLLGVIGV SYRETTLQQR EQVLHILQQA QGSFRPEVFQ    50
EERDYVLLAT CHRVELYSVA PAELFDSLAQ EIKLLGVSPY FYRNQDCFAH 100
LFCVAGGLDS LVLGETEIQG QVKRAYLQAA REQKLSFALH FLFQKALKEG 150
KVFRAKGGAP YAAITIPILV DQELRRRQID KKASLLFIGY SEINRSVAYH 200
LRRQGFSCIT FCSRQQLPTL SMRQVVREEL CFQDPYRVVF LGSLELQYAL 250
PHSLWESIWD IPDRIVFDFA VPRALPSHTV FPHRYMDMDQ ISDWLREHRK 300
EVNSAHLDSL REVAYRYWNS LNQRLERHDC VGANA 335
Length:335
Mass (Da):38,868
Last modified:February 26, 2008 - v1
Checksum:i3BAE3959FB93A1A4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM884176 Genomic DNA. Translation: CAP03475.1.
RefSeqiYP_001654122.1. NC_010287.1.

Genome annotation databases

EnsemblBacteriaiCAP03475; CAP03475; CTL0031.
GeneIDi5858148.
KEGGictb:CTL0031.
PATRICi20375482. VBIChlTra32542_0034.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM884176 Genomic DNA. Translation: CAP03475.1 .
RefSeqi YP_001654122.1. NC_010287.1.

3D structure databases

ProteinModelPortali B0B8N8.
ModBasei Search...

Protein-protein interaction databases

STRINGi 471472.CTL0031.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAP03475 ; CAP03475 ; CTL0031 .
GeneIDi 5858148.
KEGGi ctb:CTL0031.
PATRICi 20375482. VBIChlTra32542_0034.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CTRA471472:GJ9M-33-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: 434/Bu / ATCC VR-902B.

Entry informationi

Entry nameiHEM1_CHLT2
AccessioniPrimary (citable) accession number: B0B8N8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 26, 2008
Last modified: September 3, 2014
This is version 45 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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