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.

A3DIE8

- HEM1_CLOTH

UniProt

A3DIE8 - HEM1_CLOTH

(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, Cthe_2525
Organism
Clostridium thermocellum (strain ATCC 27405 / DSM 1237)
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 bindingi184 – 1896NADP By similarity

GO - Molecular functioni

  1. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
  2. NADP binding Source: InterPro

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

BioCyciCTHE203119:GIW8-2613-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:Cthe_2525
OrganismiClostridium thermocellum (strain ATCC 27405 / DSM 1237)
Taxonomic identifieri203119 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium
ProteomesiUP000002145: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 331331Glutamyl-tRNA reductaseUniRule annotationPRO_1000004614Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi203119.Cthe_2525.

Structurei

3D structure databases

ProteinModelPortaliA3DIE8.

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.
HOGENOMiHOG000069583.
KOiK02492.
OMAiNISRGPR.
OrthoDBiEOG6MWNBM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
SUPFAMiSSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.

Sequencei

Sequence statusi: Complete.

A3DIE8-1 [UniParc]FASTAAdd to Basket

« Hide

MNVIMAGIDY TLAPIDIREK FSFTKSTLQA VYNDLLKNEN IFGAVIVSTC    50
NRTELYLSCE EGLYINPFEL LCDAANFDYE EYSNMHVLRT GVDVIRHLCE 100
LACGVKSQIW GEDQIITQVR NAIELAREMN ASDSTLEVMF RIAVTSAKKV 150
KTTLKLSSTE RSIAYSALKI IKSKENISKA LVIGNGEIGR LMASILIENG 200
YDTTITLRRY RHGDNIIPLG AKTIEYVARY EKLKDCDVVI SATLSPHYTL 250
EIDKIDRIKY PRLFIDLAVP RDIDPKIKSL DNVELYDLDS IYAGEVDKNR 300
TEQMIQVKKI IDKYIFDYYR WYEYRKRLVL T 331
Length:331
Mass (Da):38,025
Last modified:March 20, 2007 - v1
Checksum:i180492694F8EB897
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000568 Genomic DNA. Translation: ABN53727.1.
RefSeqiYP_001038920.1. NC_009012.1.

Genome annotation databases

EnsemblBacteriaiABN53727; ABN53727; Cthe_2525.
GeneIDi4809281.
KEGGicth:Cthe_2525.
PATRICi19519058. VBICloThe47081_2688.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000568 Genomic DNA. Translation: ABN53727.1 .
RefSeqi YP_001038920.1. NC_009012.1.

3D structure databases

ProteinModelPortali A3DIE8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 203119.Cthe_2525.

Protocols and materials databases

DNASUi 4809281.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABN53727 ; ABN53727 ; Cthe_2525 .
GeneIDi 4809281.
KEGGi cth:Cthe_2525.
PATRICi 19519058. VBICloThe47081_2688.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000069583.
KOi K02492.
OMAi NISRGPR.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci CTHE203119:GIW8-2613-MONOMER.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_00087. Glu_tRNA_reductase.
InterProi IPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view ]
Pfami PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view ]
SUPFAMi SSF69742. SSF69742. 1 hit.
TIGRFAMsi TIGR01035. hemA. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 27405 / DSM 1237.

Entry informationi

Entry nameiHEM1_CLOTH
AccessioniPrimary (citable) accession number: A3DIE8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 20, 2007
Last modified: September 3, 2014
This is version 62 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