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P49295

- HEM12_CUCSA

UniProt

P49295 - HEM12_CUCSA

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Protein

Glutamyl-tRNA reductase 2, chloroplastic

Gene

HEMA2

Organism
Cucumis sativus (Cucumber)
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

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei143 – 1431NucleophileBy similarity
Sitei192 – 1921Important for activityBy similarity
Binding sitei202 – 2021SubstrateBy similarity
Binding sitei213 – 2131SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi284 – 2896NADPBy 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, chloroplastic (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:HEMA2
OrganismiCucumis sativus (Cucumber)
Taxonomic identifieri3659 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsCucurbitalesCucurbitaceaeBenincaseaeCucumis

Subcellular locationi

Plastidchloroplast By similarity

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
Chaini? – 542Glutamyl-tRNA reductase 2, chloroplasticPRO_0000013310
Transit peptidei1 – ?ChloroplastSequence Analysis

Expressioni

Tissue specificityi

Found in all tissues examined.

Structurei

3D structure databases

ProteinModelPortaliP49295.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni142 – 1454Substrate bindingBy similarity
Regioni207 – 2093Substrate 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.

P49295 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAAVGGLTT CFARPTPEFI APSTSYSAPV RVFFKPFKVR DLCCAGEVVG
60 70 80 90 100
VLSARSIPIS PRFELIRLVR MQPGLSALEL LKTSSVNRYT KERISIVVIG
110 120 130 140 150
LNVHTAPVEL REKLAIPEAQ WPPGIGELCA LNHIEEAAVL STCNRIEIYV
160 170 180 190 200
VALSQHRGVK EVTEWMSKRS GIPISELCKH RVLLYNTDAT QHLFEVSAGL
210 220 230 240 250
DSLVLGEGQI LAQVKHVVKT GQGVAGFDRK ISGLFKHAIT VGKRVRTETN
260 270 280 290 300
ISSGSFSVSS AAVELAQKKL PESSYATAKV MVVGAGKMGK LVIKHLVAKG
310 320 330 340 350
CRKMVVVNRT QDSVDAVEEL KDVEIIYKPL SKILACASEA DVIFTCTASK
360 370 380 390 400
TPLFTKEHVA MLPPAGTETG RRLFVDISVP RNVEQRVSDL ETVSVFNVDD
410 420 430 440 450
LKEVVAANKE DRLKKVQEAQ SIIGEEINKF EAWRDSLETV PTIKKFRAYV
460 470 480 490 500
ERIRAAELDK CLSKMGEDIP KKKKVAINDL SLGIANKLLH GPIQHLRCDG
510 520 530 540
NDSRTLDEIL QNMHAINRMF DLETDLSVLE EKIRAKVERG QK
Length:542
Mass (Da):59,707
Last modified:February 1, 1996 - v1
Checksum:iA576B3B96A0B6EEF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D67088 mRNA. Translation: BAA11091.1.
PIRiT10245.
RefSeqiNP_001267616.1. NM_001280687.1.

Genome annotation databases

GeneIDi101208135.
KEGGicsv:101208135.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D67088 mRNA. Translation: BAA11091.1 .
PIRi T10245.
RefSeqi NP_001267616.1. NM_001280687.1.

3D structure databases

ProteinModelPortali P49295.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 101208135.
KEGGi csv:101208135.

Phylogenomic databases

KOi K02492.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .

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 ]
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. "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 nameiHEM12_CUCSA
AccessioniPrimary (citable) accession number: P49295
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: October 29, 2014
This is version 93 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