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Q42843

- HEM11_HORVU

UniProt

Q42843 - HEM11_HORVU

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Protein

Glutamyl-tRNA reductase 1, chloroplastic

Gene

HEMA1

Organism
Hordeum vulgare (Barley)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).1 Publication

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei125 – 1251NucleophileBy similarity
Sitei174 – 1741Important for activityBy similarity
Binding sitei184 – 1841SubstrateBy similarity
Binding sitei195 – 1951SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi266 – 2716NADPBy 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 1, chloroplastic (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:HEMA1
OrganismiHordeum vulgare (Barley)
Taxonomic identifieri4513 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeHordeum

Organism-specific databases

GrameneiQ42843.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4343Chloroplast1 PublicationAdd
BLAST
Chaini44 – 527484Glutamyl-tRNA reductase 1, chloroplasticPRO_0000013311Add
BLAST

Expressioni

Gene expression databases

GenevestigatoriQ42843.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B29model-A76-460[»]
1B61model-A76-460[»]
ProteinModelPortaliQ42843.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni124 – 1274Substrate bindingBy similarity
Regioni189 – 1913Substrate bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi286 – 2894Poly-Val

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.Curated

Keywords - Domaini

Transit peptide

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q42843-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGATSATAA AGAFAAAKAR GPAAACPWLV AAGGRRRSGV VRCDAGGDAQ
60 70 80 90 100
AASKAASITA LEQFKISADR YMKEKSSIAV IGLSVHTAPV EMREKLAVAE
110 120 130 140 150
ELWPRAISEL TSLNHIEEAA VLSTCNRMEI YVVALSWNRG IREVVDWMSK
160 170 180 190 200
KSGIPASELR EHLFMLRDSD ATRHLFEVSA GLDSLVLGEG QILAQVKQVV
210 220 230 240 250
RNGQNSGGLG KNIDRMFKDA ITAGKRVRCE TNISAGAVSV SSAAVELAMM
260 270 280 290 300
KLPKSECLSA RMLLIGAGKM GKLVVKHLIA KGCKKVVVVN RSVERVDAIR
310 320 330 340 350
EEMKDIEIVY RPLTEMYEAA ADADVVFTST ASESLLFTKE HAEVLPPISL
360 370 380 390 400
AMGGVRLFVD ISVPRNVGAC LSEVEHARVY NVDDLKEVVE ANKEDRVRKA
410 420 430 440 450
MEAQTIITQE LKRFEAWRDS LETVPTIKKL RSYADRIRAS ELEKCLQKIG
460 470 480 490 500
EDNLNKKMRR SIEELSTGIV NKLLHGPLQH LRCDGSDSRT LDETLENMHA
510 520
LNRMFSLDTE KAVLEQKIKA KVEKTQS
Length:527
Mass (Da):57,653
Last modified:November 1, 1997 - v1
Checksum:iD329E56458BE1165
GO

Sequence cautioni

The sequence CAA60054.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92403 mRNA. Translation: CAA63140.1.
X86101 mRNA. Translation: CAA60054.1. Different initiation.
PIRiT05732.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92403 mRNA. Translation: CAA63140.1 .
X86101 mRNA. Translation: CAA60054.1 . Different initiation.
PIRi T05732.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B29 model - A 76-460 [» ]
1B61 model - A 76-460 [» ]
ProteinModelPortali Q42843.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

Gramenei Q42843.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .

Gene expression databases

Genevestigatori Q42843.

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. Klages.
  2. "Purification and partial characterisation of barley glutamyl-tRNA(Glu) reductase, the enzyme that directs glutamate to chlorophyll biosynthesis."
    Pontoppidan B., Kannangara C.G.
    Eur. J. Biochem. 225:529-537(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 44-65, CHARACTERIZATION.
  3. "Expression of catalytically active barley glutamyl tRNAGlu reductase in Escherichia coli as a fusion protein with glutathione S-transferase."
    Vothknecht U.C., Kannangara C.G., von Wettstein D.
    Proc. Natl. Acad. Sci. U.S.A. 93:9287-9291(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CHARACTERIZATION, HEME BINDING, SUBUNIT.
  4. "Predicted structure and fold recognition for the glutamyl tRNA reductase family of proteins."
    Brody S.S., Gough S.P., Kannangara C.G.
    Proteins 37:485-493(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF 76-460.

Entry informationi

Entry nameiHEM11_HORVU
AccessioniPrimary (citable) accession number: Q42843
Secondary accession number(s): Q42844
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 26, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Was shown to bind heme, but the precise role of heme is unclear.
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).By similarity

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3