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Q9Z7J1

- HEM1_CHLPN

UniProt

Q9Z7J1 - HEM1_CHLPN

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Protein
Glutamyl-tRNA reductase
Gene
hemA, CPn_0714, CP_0032, CpB0741
Organism
Chlamydia pneumoniae (Chlamydophila pneumoniae)
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

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

BioCyciCPNE115711:GI7B-33-MONOMER.
CPNE115713:GHEY-745-MONOMER.
CPNE138677:GH8N-736-MONOMER.
CPNE182082:GH4N-763-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:CPn_0714, CP_0032, CpB0741
OrganismiChlamydia pneumoniae (Chlamydophila pneumoniae)
Taxonomic identifieri83558 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
ProteomesiUP000000424: Chromosome, UP000000583: Chromosome, UP000000801: Chromosome, UP000000802: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 339339Glutamyl-tRNA reductaseUniRule annotation
PRO_0000114006Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi115713.CPn0714.

Structurei

3D structure databases

ProteinModelPortaliQ9Z7J1.

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.
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.

Q9Z7J1-1 [UniParc]FASTAAdd to Basket

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MVLGVVGISY REAALKERER AIQYLQSFEK NLFLAQRFLG KGGAFIPLLT    50
CHRAELYYYS ESPEIAQAAL LSELTSQGIR PYRHRGLSCF THLFQVTSGI 100
DSLIFGETEI QGQVKRAYLK GSKERELPFD LHFLFQKALK EGKEYRSRIG 150
FPDHQVTIES VVQEILLSYD KSIYTNFLFV GYSDINRKVA AYLYQHGYHR 200
ITFCSRQQVT APYRTLSRET LSFRQPYDVI FFGSSESASQ FSDLSCESLA 250
SIPKRIVFDF NVPRTFLWKE TPTGFVYLDI DFISECVQKR LQCTKEGVNK 300
AKLLLTCAAK KQWEIYEKKS SHITQRQISS PRIPSVLSY 339
Length:339
Mass (Da):39,104
Last modified:May 1, 1999 - v1
Checksum:i814E823518D6B157
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE001363 Genomic DNA. Translation: AAD18853.1.
AE002161 Genomic DNA. Translation: AAF37927.1.
BA000008 Genomic DNA. Translation: BAA98921.1.
AE009440 Genomic DNA. Translation: AAP98670.1.
PIRiB72043.
G86579.
RefSeqiNP_224910.1. NC_000922.1.
NP_300770.1. NC_002491.1.
NP_444584.1. NC_002179.2.
NP_877013.1. NC_005043.1.

Genome annotation databases

EnsemblBacteriaiAAD18853; AAD18853; CPn_0714.
AAF37927; AAF37927; CP_0032.
AAP98670; AAP98670; CpB0741.
BAA98921; BAA98921; BAA98921.
GeneIDi1467420.
895228.
919483.
963654.
KEGGicpa:CP0032.
cpj:CPj0714.
cpn:CPn0714.
cpt:CpB0741.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE001363 Genomic DNA. Translation: AAD18853.1 .
AE002161 Genomic DNA. Translation: AAF37927.1 .
BA000008 Genomic DNA. Translation: BAA98921.1 .
AE009440 Genomic DNA. Translation: AAP98670.1 .
PIRi B72043.
G86579.
RefSeqi NP_224910.1. NC_000922.1.
NP_300770.1. NC_002491.1.
NP_444584.1. NC_002179.2.
NP_877013.1. NC_005043.1.

3D structure databases

ProteinModelPortali Q9Z7J1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 115713.CPn0714.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD18853 ; AAD18853 ; CPn_0714 .
AAF37927 ; AAF37927 ; CP_0032 .
AAP98670 ; AAP98670 ; CpB0741 .
BAA98921 ; BAA98921 ; BAA98921 .
GeneIDi 1467420.
895228.
919483.
963654.
KEGGi cpa:CP0032.
cpj:CPj0714.
cpn:CPn0714.
cpt:CpB0741.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CPNE115711:GI7B-33-MONOMER.
CPNE115713:GHEY-745-MONOMER.
CPNE138677:GH8N-736-MONOMER.
CPNE182082:GH4N-763-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: CWL029.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AR39.
  3. "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from Japan and CWL029 from USA."
    Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K., Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.
    Nucleic Acids Res. 28:2311-2314(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: J138.
  4. "The genome sequence of Chlamydia pneumoniae TW183 and comparison with other Chlamydia strains based on whole genome sequence analysis."
    Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P., Schneider S., Pohl T., Essig A., Marre R., Melchers K.
    Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TW-183.

Entry informationi

Entry nameiHEM1_CHLPN
AccessioniPrimary (citable) accession number: Q9Z7J1
Secondary accession number(s): Q9JQF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: September 3, 2014
This is version 100 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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