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Protein

Glutamyl-tRNA reductase 1, chloroplastic

Gene

HEMA1

Organism
Cucumis sativus (Cucumber)
Status
Reviewed-Annotation score: 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

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei151 – 1511NucleophileBy similarity
Sitei200 – 2001Important for activityBy similarity
Binding sitei210 – 2101SubstrateBy similarity
Binding sitei221 – 2211SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi292 – 2976NADPBy 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
OrganismiCucumis sativus (Cucumber)
Taxonomic identifieri3659 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsCucurbitalesCucurbitaceaeBenincaseaeCucumis

Subcellular locationi

Plastidchloroplast By similarity

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? – 552Glutamyl-tRNA reductase 1, chloroplasticPRO_0000013309
Transit peptidei1 – ?ChloroplastSequence Analysis

Expressioni

Tissue specificityi

Primarily in cotyledons and hypocotyls of greening cucumber seedlings.

Structurei

3D structure databases

ProteinModelPortaliP93111.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni150 – 1534Substrate bindingBy similarity
Regioni215 – 2173Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

KOiK02492.

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]
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.

P93111-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVSTSFSGA KLEALLFKSA SNSSSTRNLS SSHLPGFCKS IRTRRILFQR
60 70 80 90 100
TGVSSFTPFK CELASSDVLV QNDEIDPPKS SNLSALEQLK TSAVDRYTKE
110 120 130 140 150
RSSIVVIGLS IHTTPVEMRE KLAIPEAEWP RAIGELCGLN HIEEAAVLST
160 170 180 190 200
CNRMEIYVVA LSQHRGVKEV TEWMSKTSGI PVSEICQHRF LLYNNDATQH
210 220 230 240 250
IFEVSAGLDS LVLGEGQILA QVKQVVKVGQ GVAGFGRNIS GLFKHAITVG
260 270 280 290 300
KRVRTETNIA AGAVSVSSAA VELALMKLPE PSHATARMLV IGAGKMGKLV
310 320 330 340 350
IKHLVAKGCT KMVVVNRSEE RVTAIREEMK DVEIIYKPLT EMLSCTAEAD
360 370 380 390 400
VIFTSTASES LLFTKEQVKD LPPVGHDVGG LRLFIDISVP RNVGACINNL
410 420 430 440 450
EDVRVYNVDD LKEVVAANKE DRLRKAMEAQ SIITEESKQF EAWRDSLETV
460 470 480 490 500
PTIKKLRAYA ERIRTAELEK CLSKMGDDIP KKTRRAVDDL SRGIVNKLLH
510 520 530 540 550
GPMQHLRCDG SDSRTLSETL ENMHALNRMF SLETEIAVLE QKIRAKVEQN

QK
Length:552
Mass (Da):60,895
Last modified:May 1, 1997 - v1
Checksum:i9C7A72AF24FF00F5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50407 mRNA. Translation: BAA08910.1.
PIRiT10186.
RefSeqiNP_001267503.1. NM_001280574.1.

Genome annotation databases

GeneIDi101220615.
KEGGicsv:101220615.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50407 mRNA. Translation: BAA08910.1.
PIRiT10186.
RefSeqiNP_001267503.1. NM_001280574.1.

3D structure databases

ProteinModelPortaliP93111.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi101220615.
KEGGicsv:101220615.

Phylogenomic databases

KOiK02492.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316.

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]
SUPFAMiSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Differential expression of two hemA mRNAs encoding glutamyl-tRNA reductase proteins in greening cucumber seedlings."
    Tanaka R., Yoshida K., Nakayashiki T., Masuda T., Tsuji H., Inokuchi H., Tanaka A.
    Plant Physiol. 110:1223-1230(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Aonagajibai.
    Tissue: Cotyledon.

Entry informationi

Entry nameiHEM11_CUCSA
AccessioniPrimary (citable) accession number: P93111
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: January 7, 2015
This is version 94 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).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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.