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P42804

- HEM11_ARATH

UniProt

P42804 - HEM11_ARATH

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Protein

Glutamyl-tRNA reductase 1, chloroplastic

Gene

HEMA1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Enzyme regulationi

Negatively regulated by FLU and heme.2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei144 – 1441NucleophileBy similarity
Sitei193 – 1931Important for activityBy similarity
Binding sitei203 – 2031SubstrateBy similarity
Binding sitei214 – 2141SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi285 – 2906NADPBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. chlorophyll biosynthetic process Source: TAIR
  2. heme biosynthetic process Source: TAIR
  3. 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

BioCyciARA:AT1G58290-MONOMER.
MetaCyc:AT1G58290-MONOMER.
UniPathwayiUPA00251; UER00316.
UPA00668.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase 1, chloroplastic (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:HEMA1
Synonyms:HEMA
Ordered Locus Names:At1g58290
ORF Names:F19C14.9
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G58290.

Subcellular locationi

Plastidchloroplast membrane 2 Publications

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6464ChloroplastSequence AnalysisAdd
BLAST
Chaini65 – 543479Glutamyl-tRNA reductase 1, chloroplasticPRO_0000013307Add
BLAST

Proteomic databases

PaxDbiP42804.
PRIDEiP42804.

Expressioni

Tissue specificityi

Strongly expressed in photosynthetic tissues. Detected in all tissues tested.3 Publications

Inductioni

Circadian-regulation. Up-regulated by light.4 Publications

Gene expression databases

GenevestigatoriP42804.

Interactioni

Subunit structurei

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FLUQ940U63EBI-2319900,EBI-2319882

Protein-protein interaction databases

BioGridi27423. 4 interactions.
IntActiP42804. 4 interactions.
MINTiMINT-8300920.
STRINGi3702.AT1G58290.1-P.

Structurei

Secondary structure

1
543
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi96 – 1038
Turni104 – 1063
Helixi109 – 1157
Helixi119 – 1213
Helixi122 – 13110
Beta strandi135 – 1439
Beta strandi146 – 15510
Helixi156 – 17116
Helixi175 – 1817
Beta strandi183 – 1864
Helixi188 – 19811
Beta strandi202 – 2054
Beta strandi207 – 2093
Helixi211 – 22212
Helixi230 – 24819
Turni252 – 2554
Helixi259 – 27012
Beta strandi273 – 2764
Beta strandi281 – 2844
Helixi288 – 29912
Beta strandi304 – 3107
Helixi312 – 32110
Beta strandi325 – 3317
Helixi332 – 3343
Helixi335 – 3406
Beta strandi343 – 3475
Helixi358 – 3625
Helixi369 – 3713
Beta strandi375 – 3795
Helixi388 – 3925
Beta strandi396 – 4005
Helixi401 – 4077
Turni414 – 4163
Helixi417 – 43923
Helixi440 – 4423
Helixi443 – 46422
Helixi480 – 49213
Turni493 – 4975
Helixi513 – 52311

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4N7RX-ray2.80A/B73-543[»]
ProteinModelPortaliP42804.
SMRiP42804. Positions 94-524.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni143 – 1464Substrate bindingBy similarity
Regioni208 – 2103Substrate bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi23 – 3311Poly-SerAdd
BLAST
Compositional biasi305 – 3084Poly-Val

Domaini

The N-terminus (65-92) is required for heme inhibition, but not for activity.1 Publication

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109651.
InParanoidiP42804.
KOiK02492.
OMAiLAHKLTN.
PhylomeDBiP42804.

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.

P42804-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAVSSAFVGC PKLETLLNHH NLSPSSSSSS SVSQTPLGLN GVRVLPKNNR
60 70 80 90 100
TRRGLIQKAR CELSASSDSA SNAASISALE QLKNSAADRY TKERSSIVVI
110 120 130 140 150
GLSIHTAPVE MREKLAIPEA EWPRAIAELC GLNHIEEAAV LSTCNRMEIY
160 170 180 190 200
VLALSQHRGV KEVTEWMSKT SGIPVSEICQ HRFLLYNKDA TQHIFEVSAG
210 220 230 240 250
LDSLVLGEGQ ILAQVKQVVK VGQGVNGFGR NISGLFKHAI TVGKRVRTET
260 270 280 290 300
NIASGAVSVS SAAVELALMK LPQSSNVSAR MCVIGAGKMG KLVIKHLMAK
310 320 330 340 350
GCTKVVVVNR SEERVSAIRE EMPGIEIIYR PLDEMLACAS EADVVFTSTA
360 370 380 390 400
SETPLFLKEH VENLPQASPE VGGLRHFVDI SVPRNVGSCV GEVETARVYN
410 420 430 440 450
VDDLKEVVAA NKEDRMRKAM EAQTIITEES TQFEAWRDSL ETVPTIKKLR
460 470 480 490 500
AYAERIRVAE LEKCMSKMGD DINKKTTRAV DDLSRGIVNR FLHGPMQHLR
510 520 530 540
CDGSDSRTLS ETLENMHALN RMYGLEKDIL EEKLKAMAEQ QQK
Length:543
Mass (Da):59,515
Last modified:April 3, 2002 - v2
Checksum:i04A095FEC96CC014
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621E → V in AAA19118. (PubMed:7908550)Curated
Sequence conflicti169 – 1691K → N in AAA19118. (PubMed:7908550)Curated
Sequence conflicti291 – 2911K → L in AAA19118. (PubMed:7908550)Curated
Sequence conflicti443 – 4431V → G in BAE98482. 1 PublicationCurated
Sequence conflicti542 – 5421Q → H in AAA19118. (PubMed:7908550)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiE96616.
RefSeqiNP_176125.1. NM_104609.3.
UniGeneiAt.241.

Genome annotation databases

EnsemblPlantsiAT1G58290.1; AT1G58290.1; AT1G58290.
GeneIDi842198.
KEGGiath:AT1G58290.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi E96616.
RefSeqi NP_176125.1. NM_104609.3.
UniGenei At.241.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4N7R X-ray 2.80 A/B 73-543 [» ]
ProteinModelPortali P42804.
SMRi P42804. Positions 94-524.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 27423. 4 interactions.
IntActi P42804. 4 interactions.
MINTi MINT-8300920.
STRINGi 3702.AT1G58290.1-P.

Proteomic databases

PaxDbi P42804.
PRIDEi P42804.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G58290.1 ; AT1G58290.1 ; AT1G58290 .
GeneIDi 842198.
KEGGi ath:AT1G58290.

Organism-specific databases

TAIRi AT1G58290.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
InParanoidi P42804.
KOi K02492.
OMAi LAHKLTN.
PhylomeDBi P42804.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
UPA00668 .
BioCyci ARA:AT1G58290-MONOMER.
MetaCyc:AT1G58290-MONOMER.

Gene expression databases

Genevestigatori P42804.

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. "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.
    , 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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiHEM11_ARATH
AccessioniPrimary (citable) accession number: P42804
Secondary accession number(s): Q0WWL6, Q9LQB9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: April 3, 2002
Last modified: October 29, 2014
This is version 128 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).By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3