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A2Z928

- HEM1_ORYSI

UniProt

A2Z928 - HEM1_ORYSI

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Protein
Glutamyl-tRNA reductase, chloroplastic
Gene
OsI_033071
Organism
Oryza sativa subsp. indica (Rice)
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 sitei135 – 1351Nucleophile By similarity
Sitei184 – 1841Important for activity By similarity
Binding sitei194 – 1941Substrate By similarity
Binding sitei205 – 2051Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi276 – 2816NADP By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. chlorophyll biosynthetic process Source: UniProtKB-KW
  2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
  3. response to oxidative stress Source: EnsemblPlants/Gramene
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, chloroplastic (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
ORF Names:OsI_033071
OrganismiOryza sativa subsp. indica (Rice)
Taxonomic identifieri39946 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

Organism-specific databases

GrameneiA2Z928.

Subcellular locationi

Plastidchloroplast By similarity UniRule annotation

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
Transit peptidei1 – 4848Chloroplast Reviewed prediction
Add
BLAST
Chaini49 – 537489Glutamyl-tRNA reductase, chloroplasticUniRule annotation
PRO_0000295656Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliA2Z928.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni134 – 1374Substrate binding By similarity
Regioni199 – 2013Substrate binding By similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109651.

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.

A2Z928-1 [UniParc]FASTAAdd to Basket

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MMASTTSATA AGGAFAAAKT RAGSSAAGGG ACARVAAGGR RRSGVVVRCD    50
AGVEAQAQAQ AVAKAASVAA LEQFKISADR YMKERSSIAV IGLSVHTAPV 100
EMREKLAVAE ELWPRAISEL TSLNHIEEAA VLSTCNRMEI YVVALSWNRG 150
IREVVDWMSK KSGIPASELR EHLFMLRDSD ATRHLFEVSA GLDSLVLGEG 200
QILAQVKQVV RSGQNSGGLG KNIDRMFKDA ITAGKRVRCE TNISSGAVSV 250
SSAAVELALM KLPKSECLSA RMLLIGAGKM GKLVVKHLIA KGCKKVVVVN 300
RSVERVDAIR EEMKDIEIVY RPLTEMYEAA AEADVVFTST ASETPLFTKE 350
HAEALPAISD AMGGVRLFVD ISVPRNVSAC VSEVGHARVY NVDDLKEVVE 400
ANKEDRLRKA MEAQTIITQE LKRFEAWRDS LETVPTIKKL RSYADRIRAS 450
ELEKCLQKIG EDSLTKKMRR SIEELSTGIV NKLLHGPLQH LRCDGSDSRT 500
LDETLENMHA LNRMFSLDTE KAIIEQKIKA KVEKSQN 537
Length:537
Mass (Da):58,435
Last modified:July 24, 2007 - v2
Checksum:i51414A99FFF50A9A
GO

Sequence cautioni

The sequence BAA25003.1 differs from that shown. Reason: Frameshift at positions 22 and 31.
The sequence EAY79112.1 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti151 – 1511I → L in BAA25003. 1 Publication
Sequence conflicti201 – 2011Q → E in BAA25003. 1 Publication
Sequence conflicti463 – 4631S → A in BAA25003. 1 Publication
Sequence conflicti468 – 4681M → T in BAA25003. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB011416 mRNA. Translation: BAA25003.1. Frameshift.
CM000135 Genomic DNA. Translation: EAY79112.1. Different initiation.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB011416 mRNA. Translation: BAA25003.1 . Frameshift.
CM000135 Genomic DNA. Translation: EAY79112.1 . Different initiation.

3D structure databases

ProteinModelPortali A2Z928.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

Gramenei A2Z928.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.

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

« Hide 'large scale' publications
  1. "Nucleotide sequence of a cDNA clone encoding glutamyl-tRNA reductase from rice."
    Nakayashiki T., Inokuchi H.
    Plant Gene Register PGR98-080
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. IR36.
  2. "The genomes of Oryza sativa: a history of duplications."
    Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.
    , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.
    PLoS Biol. 3:266-281(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. 93-11.

Entry informationi

Entry nameiHEM1_ORYSI
AccessioniPrimary (citable) accession number: A2Z928
Secondary accession number(s): O48674
, Q0IWL0, Q337F6, Q8LNE9, Q9FW00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: July 24, 2007
Last modified: September 3, 2014
This is version 56 of the entry and version 2 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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