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P49294 (HEM12_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamyl-tRNA reductase 2, chloroplastic

Short name=GluTR
EC=1.2.1.70
Gene names
Name:HEMA2
Ordered Locus Names:At1g09940
ORF Names:F21M12.33
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length530 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). Probably involved in wound-induced supply of heme to defensive hemoproteins outside plastids. Ref.1 Ref.6 Ref.8

Catalytic activity

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. HAMAP-Rule MF_00087

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. HAMAP-Rule MF_00087

Porphyrin-containing compound metabolism; chlorophyll biosynthesis. HAMAP-Rule MF_00087

Subcellular location

Plastidchloroplast By similarity HAMAP-Rule MF_00087.

Tissue specificity

Expressed in roots and flowers. Detected in leaves, hypocotyls and cotyledons. Ref.1 Ref.6 Ref.7 Ref.8

Induction

Not regulated by light. Up-regulated localy by wounding and reactive oxygen species. Not regulated by methyl jasmonate. Ref.6 Ref.7 Ref.8

Disruption phenotype

No visible phenotype, but decreased heme content in roots. Ref.8

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.

Sequence similarities

Belongs to the glutamyl-tRNA reductase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6464Chloroplast Potential
Chain65 – 530466Glutamyl-tRNA reductase 2, chloroplastic HAMAP-Rule MF_00087
PRO_0000013308

Regions

Nucleotide binding277 – 2826NADP By similarity
Region134 – 1374Substrate binding By similarity
Region199 – 2013Substrate binding By similarity

Sites

Active site1351Nucleophile By similarity
Binding site1941Substrate By similarity
Binding site2051Substrate By similarity
Site1841Important for activity By similarity

Experimental info

Sequence conflict2451A → G in BAF00558. Ref.5
Sequence conflict4101D → E in AAB01674. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P49294 [UniParc].

Last modified July 24, 2007. Version 2.
Checksum: 0C0224296BA3D0A8

FASTA53058,292
        10         20         30         40         50         60 
MAVSSAFVVT PKLEKLLANH HNPTYSSSPA PLDVIGIRAL PMNNRNKRGL IQRARCEISP 

        70         80         90        100        110        120 
SNKAASISAL EQLKTSAIDR YTKERSSIVV IGLSIHTAPV EMREKLAIPE AEWPRAIAEL 

       130        140        150        160        170        180 
CGLNHIEEAA VLSTCNRMEI YVLALSQHRG VKEVTEWMSK TSGIPVSEIC QHRFLLYNKD 

       190        200        210        220        230        240 
VTQHIFEVSA GLDSLVLGEG QILAQVKQVV KVGQGVNGFG RNISGLFKHA ITVGKRVRTE 

       250        260        270        280        290        300 
TNIAAGAVSV SSAAVELALM KLPESSHASS ARMLVVGAGK MGKLVIKHLV AKGCTKMVVV 

       310        320        330        340        350        360 
NRSEEKVAAV RNEMPPGVEI IYKPLDEMLS CAAEADVVFT STASETPLFL KEQVETLPPV 

       370        380        390        400        410        420 
RDARLFVDIS VPRNVGSCVA EIDGTRVFNV DDLKEVVAAN KEDRVRKAMD AQAIITDESK 

       430        440        450        460        470        480 
HFEAWRDSLE TVPTIKKLRG YTERIIAAEI EKSLPKMGID MNKKMRKTVD DLIRGIVNKL 

       490        500        510        520        530 
LHGPMQHLRC DGNDSRTLSE TLDNMQALNR MYGLDAEILE EKIRAKVEKK 

« Hide

References

« Hide 'large scale' references
[1]"A second and differentially expressed glutamyl-tRNA reductase gene from Arabidopsis thaliana."
Kumar A.M., Csankovszki G., Soell D.
Plant Mol. Biol. 30:419-426(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY.
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Arabidopsis ORF clones."
Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.
Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[6]"Divergent regulation of the HEMA gene family encoding glutamyl-tRNA reductase in Arabidopsis thaliana: expression of HEMA2 is regulated by sugars, but is independent of light and plastid signalling."
Ujwal M.L., McCormac A.C., Goulding A., Kumar A.M., Soell D., Terry M.J.
Plant Mol. Biol. 50:83-91(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION BY LIGHT.
[7]"Regulation of HEMA1 expression by phytochrome and a plastid signal during de-etiolation in Arabidopsis thaliana."
McCormac A.C., Fischer A., Kumar A.M., Soll D., Terry M.J.
Plant J. 25:549-561(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY LIGHT, TISSUE SPECIFICITY.
[8]"Induction of isoforms of tetrapyrrole biosynthetic enzymes, AtHEMA2 and AtFC1, under stress conditions and their physiological functions in Arabidopsis."
Nagai S., Koide M., Takahashi S., Kikuta A., Aono M., Sasaki-Sekimoto Y., Ohta H., Takamiya K., Masuda T.
Plant Physiol. 144:1039-1051(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION BY WOUNDING AND REACTIVE OXYGEN SPECIES, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U27118 Genomic DNA. Translation: AAB01674.1.
AC000132 Genomic DNA. Translation: AAB60749.1.
CP002684 Genomic DNA. Translation: AEE28519.1.
BT023439 mRNA. Translation: AAY56430.1.
AK228651 mRNA. Translation: BAF00558.1.
PIRG86233.
S65773.
RefSeqNP_172465.1. NM_100868.2.
UniGeneAt.27711.

3D structure databases

ProteinModelPortalP49294.
SMRP49294. Positions 88-415.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP49294.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G09940.1; AT1G09940.1; AT1G09940.
GeneID837528.
KEGGath:AT1G09940.

Organism-specific databases

TAIRAT1G09940.

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
InParanoidP49294.
KOK02492.
OMAIGCSGSD.
PhylomeDBP49294.
ProtClustDBPLN00203.

Enzyme and pathway databases

BioCycARA:AT1G09940-MONOMER.
MetaCyc:AT1G09940-MONOMER.
UniPathwayUPA00251; UER00316.
UPA00668.

Gene expression databases

GenevestigatorP49294.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00087. Glu_tRNA_reductase.
InterProIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR016040. NAD(P)-bd_dom.
IPR018214. Pyrrol_synth_GluRdtase_CS.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsTIGR01035. hemA. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM12_ARATH
AccessionPrimary (citable) accession number: P49294
Secondary accession number(s): O04950, Q0WQP1, Q4V3B7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: July 24, 2007
Last modified: April 16, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names