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Q96563

- HEM12_HORVU

UniProt

Q96563 - HEM12_HORVU

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Protein

Glutamyl-tRNA reductase 2

Gene
HEMA2
Organism
Hordeum vulgare (Barley)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

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 sitei63 – 631Nucleophile By similarity
Sitei112 – 1121Important for activity By similarity
Binding sitei122 – 1221Substrate By similarity
Binding sitei133 – 1331Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi204 – 2096NADP By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. chlorophyll biosynthetic process Source: UniProtKB-KW
  2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Chlorophyll biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase 2 (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:HEMA2
OrganismiHordeum vulgare (Barley)
Taxonomic identifieri4513 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Organism-specific databases

GrameneiQ96563.

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 465›465Glutamyl-tRNA reductase 2UniRule annotationPRO_0000114114Add
BLAST

Expressioni

Gene expression databases

GenevestigatoriQ96563.

Structurei

3D structure databases

ProteinModelPortaliQ96563.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni62 – 654Substrate binding By similarity
Regioni127 – 1293Substrate binding By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi224 – 2274Poly-ValUniRule annotation

Sequence similaritiesi

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: Fragment.

Q96563-1 [UniParc]FASTAAdd to Basket

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QFKISADRYI KEKSSIAVIG LSVHTAPVDM REKLAVAEEL WPRAISELTS    50
LNHIEEAAVL STCNRMEIYV VALSWNRGIR EVVDWMSKKS GIPASELREH 100
LFMLRDSGAT RHLFEVSAGL DSLVLGEGQI LAQVKQVVRN GQNSGGLGKN 150
IDRMFKDAIT AGKRARCETN ISAGAVSVSS AAVELAMMKL PKSECLSARM 200
LLIGAGKMGK LVVKHLIAKG CKKVVVVNRS VERVDAIREE MKDIEIVYRP 250
LTEMYEAAAD ADVVFTSTAS ESLLFTKEHA EALPPISLAM GGVRLFVDIS 300
VPRNVGACLS QVEHARVYNV DDLKEVVEAN KEDRVRKAME AQAIITQELK 350
RFEAWRDSLE TVPTIKKLRS YADRIRASEL DKCLQKIGED NLNKKTRRSI 400
EELSTGIVNK LLHGPLQHLR CDGSDSRTLD ETLDNMHALN RMFNLDTEKA 450
VLEQKIKAKV EKTQS 465
Length:465
Mass (Da):51,675
Last modified:February 1, 1997 - v1
Checksum:iE42A50A3E749CE6D
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X86102 mRNA. Translation: CAA60055.1.
PIRiT05734.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X86102 mRNA. Translation: CAA60055.1 .
PIRi T05734.

3D structure databases

ProteinModelPortali Q96563.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

Gramenei Q96563.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .

Gene expression databases

Genevestigatori Q96563.

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. "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.

Entry informationi

Entry nameiHEM12_HORVU
AccessioniPrimary (citable) accession number: Q96563
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: September 3, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant 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.

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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