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Q6L0J9

- HEM1_PICTO

UniProt

Q6L0J9 - HEM1_PICTO

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Protein
Glutamyl-tRNA reductase
Gene
hemA, PTO0918
Organism
Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)
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
Sitei82 – 821Important for activity By similarity
Binding sitei92 – 921Substrate By similarity
Binding sitei103 – 1031Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi171 – 1766NADP 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

BioCyciPTOR263820:GHA3-959-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:PTO0918
OrganismiPicrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)
Taxonomic identifieri263820 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesPicrophilaceaePicrophilus
ProteomesiUP000000438: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 401401Glutamyl-tRNA reductaseUniRule annotation
PRO_0000114107Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi263820.PTO0918.

Structurei

3D structure databases

ProteinModelPortaliQ6L0J9.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni97 – 993Substrate 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.
HOGENOMiHOG000112884.
KOiK02492.
OMAiYREADAN.

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.

Q6L0J9-1 [UniParc]FASTAAdd to Basket

« Hide

MIIMIPIYAI TWNFRDTPEG FDKIVNNDYN YFESLCKKSS IDEFVILITC    50
NRVEIYAYTR NEIDKDLFKD SLIYNYPEST MHLLRVASGL ESMSIGENDI 100
MRQVKEAYEL SIKRKTSGKI LSYIFKKALN VGKEVRTQTS ISRGKTSIPA 150
ISLDICDNEY GINNKSILII GNGKMATDFS RYLKEYRPGN VTIAGRSIDH 200
ARNLAVLYGY SYDSIKNLNN LIKNSDIIIA ATSAGNYIVK DLGDLARNKY 250
FIDISKPENI DPEISKYARL LSINEIGKIL KRNEDEKKGE VEIAEVIINQ 300
EQKTIDEKLK EMMLDDVIAM FYKFANNVKK DELEELFLIQ DFNDEQKKDI 350
DAMTSSLINK ILAPYTNSVK QFIKENKNFD YILNEYKKML EQFMENIVKK 400
L 401
Length:401
Mass (Da):46,302
Last modified:July 5, 2004 - v1
Checksum:iC16EDBDE1B47E975
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017261 Genomic DNA. Translation: AAT43503.1.
RefSeqiYP_023696.1. NC_005877.1.

Genome annotation databases

EnsemblBacteriaiAAT43503; AAT43503; PTO0918.
GeneIDi2843948.
KEGGipto:PTO0918.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017261 Genomic DNA. Translation: AAT43503.1 .
RefSeqi YP_023696.1. NC_005877.1.

3D structure databases

ProteinModelPortali Q6L0J9.
ModBasei Search...

Protein-protein interaction databases

STRINGi 263820.PTO0918.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAT43503 ; AAT43503 ; PTO0918 .
GeneIDi 2843948.
KEGGi pto:PTO0918.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000112884.
KOi K02492.
OMAi YREADAN.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci PTOR263820:GHA3-959-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: ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828.

Entry informationi

Entry nameiHEM1_PICTO
AccessioniPrimary (citable) accession number: Q6L0J9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: July 5, 2004
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

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