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Q96563 (HEM12_HORVU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 86. 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
EC=1.2.1.70
Gene names
Name:HEMA2
OrganismHordeum vulgare (Barley)
Taxonomic identifier4513 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Protein attributes

Sequence length465 AA.
Sequence statusFragment.
Protein existenceEvidence at transcript level

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

Subcellular location

Plastidchloroplast 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 processChlorophyll biosynthesis
Porphyrin biosynthesis
   Cellular componentChloroplast
Plastid
   LigandNADP
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological_processchlorophyll biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

protoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionNADP binding

Inferred from electronic annotation. Source: InterPro

glutamyl-tRNA reductase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 465›465Glutamyl-tRNA reductase 2 HAMAP-Rule MF_00087
PRO_0000114114

Regions

Nucleotide binding204 – 2096NADP By similarity
Region62 – 654Substrate binding By similarity
Region127 – 1293Substrate binding By similarity
Compositional bias224 – 2274Poly-Val HAMAP-Rule MF_00087

Sites

Active site631Nucleophile By similarity
Binding site1221Substrate By similarity
Binding site1331Substrate By similarity
Site1121Important for activity By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
Q96563 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: E42A50A3E749CE6D

FASTA46551,675
        10         20         30         40         50         60 
QFKISADRYI KEKSSIAVIG LSVHTAPVDM REKLAVAEEL WPRAISELTS LNHIEEAAVL 

        70         80         90        100        110        120 
STCNRMEIYV VALSWNRGIR EVVDWMSKKS GIPASELREH LFMLRDSGAT RHLFEVSAGL 

       130        140        150        160        170        180 
DSLVLGEGQI LAQVKQVVRN GQNSGGLGKN IDRMFKDAIT AGKRARCETN ISAGAVSVSS 

       190        200        210        220        230        240 
AAVELAMMKL PKSECLSARM LLIGAGKMGK LVVKHLIAKG CKKVVVVNRS VERVDAIREE 

       250        260        270        280        290        300 
MKDIEIVYRP LTEMYEAAAD ADVVFTSTAS ESLLFTKEHA EALPPISLAM GGVRLFVDIS 

       310        320        330        340        350        360 
VPRNVGACLS QVEHARVYNV DDLKEVVEAN KEDRVRKAME AQAIITQELK RFEAWRDSLE 

       370        380        390        400        410        420 
TVPTIKKLRS YADRIRASEL DKCLQKIGED NLNKKTRRSI EELSTGIVNK LLHGPLQHLR 

       430        440        450        460 
CDGSDSRTLD ETLDNMHALN RMFNLDTEKA VLEQKIKAKV EKTQS 

« Hide

References

[1]"Members of a low-copy number gene family encoding glutamyl-tRNA reductase are differentially expressed in barley."
Bougri O., Grimm B.
Plant J. 9:867-878(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Bonus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X86102 mRNA. Translation: CAA60055.1.
PIRT05734.

3D structure databases

ProteinModelPortalQ96563.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneQ96563.

Enzyme and pathway databases

UniPathwayUPA00251; UER00316.

Gene expression databases

GenevestigatorQ96563.

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_HORVU
AccessionPrimary (citable) accession number: Q96563
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: February 19, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways