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P42804 (HEM11_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 122. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamyl-tRNA reductase 1, chloroplastic

Short name=GluTR
EC=1.2.1.70
Gene names
Name:HEMA1
Synonyms:HEMA
Ordered Locus Names:At1g58290
ORF Names:F19C14.9
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length543 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). Probably involved in the tetrapyrrole synthesis required for the chlorophyll biosynthesis. Ref.1 Ref.7

Catalytic activity

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

Enzyme regulation

Negatively regulated by FLU and heme. Ref.8 Ref.10

Pathway

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

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

Subunit structure

Part of the FLU-containing chloroplast membrane complex composed of FLU, CRD1, PORB, PORC, CHLP and HEMA1. Interacts (via C-terminus) with FLU, only in the absence of light. Ref.8 Ref.10

Subcellular location

Plastidchloroplast membrane Ref.1 Ref.10.

Tissue specificity

Strongly expressed in photosynthetic tissues. Detected in all tissues tested. Ref.1 Ref.6 Ref.7

Induction

Circadian-regulation. Up-regulated by light. Ref.1 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Domain

The N-terminus (65-92) is required for heme inhibition, but not for activity. 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FLUQ940U63EBI-2319900,EBI-2319882

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 6464Chloroplast Potential
Chain65 – 543479Glutamyl-tRNA reductase 1, chloroplastic HAMAP-Rule MF_00087
PRO_0000013307

Regions

Nucleotide binding285 – 2906NADP By similarity
Region143 – 1464Substrate binding By similarity
Region208 – 2103Substrate binding By similarity
Compositional bias23 – 3311Poly-Ser HAMAP-Rule MF_00087
Compositional bias305 – 3084Poly-Val HAMAP-Rule MF_00087

Sites

Active site1441Nucleophile By similarity
Binding site2031Substrate By similarity
Binding site2141Substrate By similarity
Site1931Important for activity By similarity

Experimental info

Sequence conflict621E → V in AAA19118. Ref.1
Sequence conflict1691K → N in AAA19118. Ref.1
Sequence conflict2911K → L in AAA19118. Ref.1
Sequence conflict4431V → G in BAE98482. Ref.5
Sequence conflict5421Q → H in AAA19118. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P42804 [UniParc].

Last modified April 3, 2002. Version 2.
Checksum: 04A095FEC96CC014

FASTA54359,515
        10         20         30         40         50         60 
MAVSSAFVGC PKLETLLNHH NLSPSSSSSS SVSQTPLGLN GVRVLPKNNR TRRGLIQKAR 

        70         80         90        100        110        120 
CELSASSDSA SNAASISALE QLKNSAADRY TKERSSIVVI GLSIHTAPVE MREKLAIPEA 

       130        140        150        160        170        180 
EWPRAIAELC GLNHIEEAAV LSTCNRMEIY VLALSQHRGV KEVTEWMSKT SGIPVSEICQ 

       190        200        210        220        230        240 
HRFLLYNKDA TQHIFEVSAG LDSLVLGEGQ ILAQVKQVVK VGQGVNGFGR NISGLFKHAI 

       250        260        270        280        290        300 
TVGKRVRTET NIASGAVSVS SAAVELALMK LPQSSNVSAR MCVIGAGKMG KLVIKHLMAK 

       310        320        330        340        350        360 
GCTKVVVVNR SEERVSAIRE EMPGIEIIYR PLDEMLACAS EADVVFTSTA SETPLFLKEH 

       370        380        390        400        410        420 
VENLPQASPE VGGLRHFVDI SVPRNVGSCV GEVETARVYN VDDLKEVVAA NKEDRMRKAM 

       430        440        450        460        470        480 
EAQTIITEES TQFEAWRDSL ETVPTIKKLR AYAERIRVAE LEKCMSKMGD DINKKTTRAV 

       490        500        510        520        530        540 
DDLSRGIVNR FLHGPMQHLR CDGSDSRTLS ETLENMHALN RMYGLEKDIL EEKLKAMAEQ 


QQK 

« Hide

References

« Hide 'large scale' references
[1]"Light regulation of chlorophyll biosynthesis at the level of 5-aminolevulinate formation in Arabidopsis."
Ilag L.L., Kumar A.M., Soell D.
Plant Cell 6:265-275(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
Strain: cv. Columbia.
Tissue: Leaf.
[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]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
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]"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.
[7]"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.
[8]"Concurrent interactions of heme and FLU with Glu tRNA reductase (HEMA1), the target of metabolic feedback inhibition of tetrapyrrole biosynthesis, in dark- and light-grown Arabidopsis plants."
Goslings D., Meskauskiene R., Kim C., Lee K.P., Nater M., Apel K.
Plant J. 40:957-967(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FLU, ENZYME REGULATION, DOMAIN.
Strain: cv. Landsberg erecta.
[9]"PIF3 is a repressor of chloroplast development."
Stephenson P.G., Fankhauser C., Terry M.J.
Proc. Natl. Acad. Sci. U.S.A. 106:7654-7659(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY LIGHT.
[10]"FLU, a negative feedback regulator of tetrapyrrole biosynthesis, is physically linked to the final steps of the Mg(++)-branch of this pathway."
Kauss D., Bischof S., Steiner S., Apel K., Meskauskiene R.
FEBS Lett. 586:211-216(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN THE FLU-CONTAINING CHLOROPLAST MEMBRANE COMPLEX, ENZYME REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U03774 Genomic DNA. Translation: AAA19118.1.
AC008051 Genomic DNA. Translation: AAF82258.1.
CP002684 Genomic DNA. Translation: AEE33532.1.
AY072223 mRNA. Translation: AAL60044.1.
AY096600 mRNA. Translation: AAM20250.1.
AK226332 mRNA. Translation: BAE98482.1.
PIRE96616.
RefSeqNP_176125.1. NM_104609.3.
UniGeneAt.241.

3D structure databases

ProteinModelPortalP42804.
SMRP42804. Positions 95-527.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid27423. 4 interactions.
IntActP42804. 4 interactions.
MINTMINT-8300920.
STRING3702.AT1G58290.1-P.

Proteomic databases

PaxDbP42804.
PRIDEP42804.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G58290.1; AT1G58290.1; AT1G58290.
GeneID842198.
KEGGath:AT1G58290.

Organism-specific databases

TAIRAT1G58290.

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
InParanoidP42804.
KOK02492.
OMARTEIYCA.
PhylomeDBP42804.
ProtClustDBPLN00203.

Enzyme and pathway databases

BioCycARA:AT1G58290-MONOMER.
MetaCyc:AT1G58290-MONOMER.
UniPathwayUPA00251; UER00316.
UPA00668.

Gene expression databases

ArrayExpressP42804.
GenevestigatorP42804.

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]
SUPFAMSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsTIGR01035. hemA. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM11_ARATH
AccessionPrimary (citable) accession number: P42804
Secondary accession number(s): Q0WWL6, Q9LQB9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: April 3, 2002
Last modified: March 19, 2014
This is version 122 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