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Q1INI5 (HEM12_KORVE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamyl-tRNA reductase 2

Short name=GluTR 2
EC=1.2.1.70
Gene names
Name:hemA2
Ordered Locus Names:Acid345_2564
OrganismKoribacter versatilis (strain Ellin345) [Reference proteome] [HAMAP]
Taxonomic identifier204669 [NCBI]
Taxonomic lineageBacteriaAcidobacteriaCandidatus Koribacter

Protein attributes

Sequence length436 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA) By similarity. HAMAP-Rule MF_00087

Catalytic activity

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. HAMAP-Rule MF_00087

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. HAMAP-Rule MF_00087

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00087

Domain

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. HAMAP-Rule MF_00087

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.

Sequence similarities

Belongs to the glutamyl-tRNA reductase family.

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionNADP binding

Inferred from electronic annotation. Source: InterPro

glutamyl-tRNA reductase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 436436Glutamyl-tRNA reductase 2 HAMAP-Rule MF_00087
PRO_0000334999

Regions

Nucleotide binding186 – 1916NADP By similarity
Region49 – 524Substrate binding By similarity
Region111 – 1133Substrate binding By similarity

Sites

Active site501Nucleophile By similarity
Binding site1061Substrate By similarity
Binding site1171Substrate By similarity
Site961Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1INI5 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: 407B8A871D22A84C

FASTA43648,410
        10         20         30         40         50         60 
MNFFVIGVNH KTAPVEVRER FAIPESRLPE ATKLLASYPG IEEGMIVSTC NRVEMVARSV 

        70         80         90        100        110        120 
NGNADMRGFL KQLYNIDPAQ YEQYLYEYRS TEAVRHMFRV ASSLDSMVVG EPQILGQVKE 

       130        140        150        160        170        180 
AYATARAVGA VSSQLDALLT RAFAVAKRVR TDTSIASSSV SIASVAVELA KKIFGSLQGR 

       190        200        210        220        230        240 
SVYIVGAGKM CELAARHFVA HGVEKIYVAN RTYERGVAFA KKFNGEAVPI EHLYETVDKA 

       250        260        270        280        290        300 
DIVLSSTGAP IAIFRKEHGE KFLSRRKNRP MFFLDIAVPR DVDAKMNELD GIFVYDIDDL 

       310        320        330        340        350        360 
QQVVHSHISD RKDEAAHAEA IVNAEVEKFE ERLRTLDVVP TIVSLQEHLE TVRQAEIDRL 

       370        380        390        400        410        420 
RGRLGELSPE QEMAVDALTK GIINKIMHTP ITTLKTAAKE PESTTVIELV KRIFNLHEKA 

       430 
KDETVKTGPP QSGPGK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000360 Genomic DNA. Translation: ABF41565.1.
RefSeqYP_591639.1. NC_008009.1.

3D structure databases

ProteinModelPortalQ1INI5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING204669.Acid345_2564.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF41565; ABF41565; Acid345_2564.
GeneID4072208.
KEGGaba:Acid345_2564.
PATRIC31982188. VBICanKor57425_2730.

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
OMAAITCGKK.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycKVER204669:GHL8-2586-MONOMER.
UniPathwayUPA00251; UER00316.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00087. Glu_tRNA_reductase.
InterProIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR016040. NAD(P)-bd_dom.
IPR018214. Pyrrol_synth_GluRdtase_CS.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsTIGR01035. hemA. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM12_KORVE
AccessionPrimary (citable) accession number: Q1INI5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 13, 2006
Last modified: May 14, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways