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Q888C2

- HEM1_PSESM

UniProt

Q888C2 - HEM1_PSESM

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Protein
Glutamyl-tRNA reductase
Gene
hemA, PSPTO_1108
Organism
Pseudomonas syringae pv. tomato (strain DC3000)
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 sitei50 – 501Nucleophile By similarity
Sitei97 – 971Important for activity By similarity
Binding sitei107 – 1071Substrate By similarity
Binding sitei118 – 1181Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi187 – 1926NADP 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

BioCyciPSYR223283:GJIX-1131-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:PSPTO_1108
OrganismiPseudomonas syringae pv. tomato (strain DC3000)
Taxonomic identifieri223283 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002515: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 425425Glutamyl-tRNA reductaseUniRule annotation
PRO_0000114060Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi223283.PSPTO_1108.

Structurei

3D structure databases

ProteinModelPortaliQ888C2.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni112 – 1143Substrate 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.
HOGENOMiHOG000109650.
KOiK02492.
OMAiLAHKLTN.
OrthoDBiEOG6MWNBM.
PhylomeDBiQ888C2.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFiPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMiSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q888C2-1 [UniParc]FASTAAdd to Basket

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MAFLALGINH KTASVDVRER VAFTPEQLVD ALQQLCHLTE SREAAILSTC    50
NRSELYIEHE HLGADSILAW LANYHHLSLE ELRASAYVHE DDAAVRHMMR 100
VASGLDSLVL GEPQILGQMK SAYAVAREAG TVGPLLGRLF QATFSAAKQV 150
RTDTAIGENP VSVAFAAVSL AKQIFSDLQR SQALLIGAGE TITLVARHLH 200
DLGVKRIVVA NRTLERASIL AAEFGAHAVL LSDIPAELVN SDIVISSTAS 250
QLPILGKGAV ESALKLRKHK PIFMVDIAVP RDIEPEVGEL DDVYLYSVDD 300
LHEVVAENLK SRQGAALAAE QLVSVGAEDF MSRLRELAAV DVLRAYRQQS 350
ERLRDEELSK AQRMLANGSN AEDVLIQLAR GLTNKLLHAP SVQLKKLSAE 400
GRVDALAMAQ ELFALGEGST DKTPQ 425
Length:425
Mass (Da):46,089
Last modified:June 1, 2003 - v1
Checksum:iEF9A771689EC5B1D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016853 Genomic DNA. Translation: AAO54637.1.
RefSeqiNP_790942.1. NC_004578.1.

Genome annotation databases

EnsemblBacteriaiAAO54637; AAO54637; PSPTO_1108.
GeneIDi1182744.
KEGGipst:PSPTO_1108.
PATRICi19993433. VBIPseSyr93040_1118.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016853 Genomic DNA. Translation: AAO54637.1 .
RefSeqi NP_790942.1. NC_004578.1.

3D structure databases

ProteinModelPortali Q888C2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 223283.PSPTO_1108.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAO54637 ; AAO54637 ; PSPTO_1108 .
GeneIDi 1182744.
KEGGi pst:PSPTO_1108.
PATRICi 19993433. VBIPseSyr93040_1118.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109650.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.
PhylomeDBi Q888C2.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci PSYR223283:GJIX-1131-MONOMER.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_00087. Glu_tRNA_reductase.
InterProi IPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view ]
Pfami PF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMi SSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsi TIGR01035. hemA. 1 hit.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DC3000.

Entry informationi

Entry nameiHEM1_PSESM
AccessioniPrimary (citable) accession number: Q888C2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: June 1, 2003
Last modified: September 3, 2014
This is version 91 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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