SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q824W1

- HEM1_CHLCV

UniProt

Q824W1 - HEM1_CHLCV

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Glutamyl-tRNA reductase
Gene
hemA, CCA_00028
Organism
Chlamydophila caviae (strain GPIC)
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. 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

BioCyciCCAV227941:GH8L-30-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:CCA_00028
OrganismiChlamydophila caviae (strain GPIC)
Taxonomic identifieri227941 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila
ProteomesiUP000002193: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 338338Glutamyl-tRNA reductaseUniRule annotation
PRO_0000114004Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi227941.CCA00028.

Structurei

3D structure databases

ProteinModelPortaliQ824W1.

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.
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.

Q824W1-1 [UniParc]FASTAAdd to Basket

« Hide

MVLGVVGISY REAALKEREA AINILKDFEA NTLFSQRFFG GEGSFVLLLT    50
CHRAEIYYFS KSNHNVQSEL LSRISALGAR PYCYQGLACF THLFTVTSGM 100
DSLISGETEI QGQVKRAYIK AKTDRELPFA LHFLFQKALK EGKDFRSQVS 150
LSHPVVTIES VVEQTLDLHG KSTKDKLLFI GYSDINRKVA NGLSAKGYRN 200
LIFCSRKNIS IPYATVARSQ LSFREPYDVI FFGSSESAKD FPGLSLENLA 250
SISNRVIFDF NVPRTFTLME RPKDIVCLDM DFISEQVQKK LQISKQCTNK 300
EKPFLALAAR KQWEVYEKKC SHISSSQLQT SRPKLLIL 338
Length:338
Mass (Da):38,246
Last modified:June 1, 2003 - v1
Checksum:i74BD254818939641
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE015925 Genomic DNA. Translation: AAP04780.1.
RefSeqiNP_828902.1. NC_003361.3.
WP_011006001.1. NC_003361.3.

Genome annotation databases

EnsemblBacteriaiAAP04780; AAP04780; CCA_00028.
GeneIDi1217697.
KEGGicca:CCA00028.
PATRICi20269038. VBIChlCav107360_0029.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE015925 Genomic DNA. Translation: AAP04780.1 .
RefSeqi NP_828902.1. NC_003361.3.
WP_011006001.1. NC_003361.3.

3D structure databases

ProteinModelPortali Q824W1.
ModBasei Search...

Protein-protein interaction databases

STRINGi 227941.CCA00028.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAP04780 ; AAP04780 ; CCA_00028 .
GeneIDi 1217697.
KEGGi cca:CCA00028.
PATRICi 20269038. VBIChlCav107360_0029.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CCAV227941:GH8L-30-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. "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC): examining the role of niche-specific genes in the evolution of the Chlamydiaceae."
    Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T., Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A., Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O., Salzberg S.L., Hsia R.-C., McClarty G.
    , Rank R.G., Bavoil P.M., Fraser C.M.
    Nucleic Acids Res. 31:2134-2147(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: GPIC.

Entry informationi

Entry nameiHEM1_CHLCV
AccessioniPrimary (citable) accession number: Q824W1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
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

Similar proteinsi