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P49294

- HEM12_ARATH

UniProt

P49294 - HEM12_ARATH

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Protein

Glutamyl-tRNA reductase 2, chloroplastic

Gene

HEMA2

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

Functioni

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.3 Publications

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei135 – 1351NucleophileBy similarity
Sitei184 – 1841Important for activityBy similarity
Binding sitei194 – 1941SubstrateBy similarity
Binding sitei205 – 2051SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi277 – 2826NADPBy 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-UniPathway
  2. heme biosynthetic process Source: TAIR
  3. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
  4. response to oxidative stress Source: TAIR
  5. tetrapyrrole biosynthetic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Chlorophyll biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciARA:AT1G09940-MONOMER.
MetaCyc:AT1G09940-MONOMER.
UniPathwayiUPA00251; UER00316.
UPA00668.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase 2, chloroplastic (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:HEMA2
Ordered Locus Names:At1g09940
ORF Names:F21M12.33
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G09940.

Subcellular locationi

Plastidchloroplast By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Disruption phenotypei

No visible phenotype, but decreased heme content in roots.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6464ChloroplastSequence AnalysisAdd
BLAST
Chaini65 – 530466Glutamyl-tRNA reductase 2, chloroplasticPRO_0000013308Add
BLAST

Proteomic databases

PRIDEiP49294.

Expressioni

Tissue specificityi

Expressed in roots and flowers. Detected in leaves, hypocotyls and cotyledons.4 Publications

Inductioni

Not regulated by light. Up-regulated localy by wounding and reactive oxygen species. Not regulated by methyl jasmonate.3 Publications

Gene expression databases

GenevestigatoriP49294.

Structurei

3D structure databases

ProteinModelPortaliP49294.
SMRiP49294. Positions 85-513.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109651.
InParanoidiP49294.
KOiK02492.
OMAiAITCGKK.
PhylomeDBiP49294.

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]
PIRSFiPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
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.

P49294-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAVSSAFVVT PKLEKLLANH HNPTYSSSPA PLDVIGIRAL PMNNRNKRGL
60 70 80 90 100
IQRARCEISP SNKAASISAL EQLKTSAIDR YTKERSSIVV IGLSIHTAPV
110 120 130 140 150
EMREKLAIPE AEWPRAIAEL CGLNHIEEAA VLSTCNRMEI YVLALSQHRG
160 170 180 190 200
VKEVTEWMSK TSGIPVSEIC QHRFLLYNKD VTQHIFEVSA GLDSLVLGEG
210 220 230 240 250
QILAQVKQVV KVGQGVNGFG RNISGLFKHA ITVGKRVRTE TNIAAGAVSV
260 270 280 290 300
SSAAVELALM KLPESSHASS ARMLVVGAGK MGKLVIKHLV AKGCTKMVVV
310 320 330 340 350
NRSEEKVAAV RNEMPPGVEI IYKPLDEMLS CAAEADVVFT STASETPLFL
360 370 380 390 400
KEQVETLPPV RDARLFVDIS VPRNVGSCVA EIDGTRVFNV DDLKEVVAAN
410 420 430 440 450
KEDRVRKAMD AQAIITDESK HFEAWRDSLE TVPTIKKLRG YTERIIAAEI
460 470 480 490 500
EKSLPKMGID MNKKMRKTVD DLIRGIVNKL LHGPMQHLRC DGNDSRTLSE
510 520 530
TLDNMQALNR MYGLDAEILE EKIRAKVEKK
Length:530
Mass (Da):58,292
Last modified:July 24, 2007 - v2
Checksum:i0C0224296BA3D0A8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti245 – 2451A → G in BAF00558. 1 PublicationCurated
Sequence conflicti410 – 4101D → E in AAB01674. (PubMed:8605295)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiG86233.
S65773.
RefSeqiNP_172465.1. NM_100868.2.
UniGeneiAt.27711.

Genome annotation databases

EnsemblPlantsiAT1G09940.1; AT1G09940.1; AT1G09940.
GeneIDi837528.
KEGGiath:AT1G09940.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi G86233.
S65773.
RefSeqi NP_172465.1. NM_100868.2.
UniGenei At.27711.

3D structure databases

ProteinModelPortali P49294.
SMRi P49294. Positions 85-513.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P49294.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G09940.1 ; AT1G09940.1 ; AT1G09940 .
GeneIDi 837528.
KEGGi ath:AT1G09940.

Organism-specific databases

TAIRi AT1G09940.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
InParanoidi P49294.
KOi K02492.
OMAi AITCGKK.
PhylomeDBi P49294.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
UPA00668 .
BioCyci ARA:AT1G09940-MONOMER.
MetaCyc:AT1G09940-MONOMER.

Gene expression databases

Genevestigatori P49294.

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 ]
PIRSFi PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
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. "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.
    , 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.
    , 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.

Entry informationi

Entry nameiHEM12_ARATH
AccessioniPrimary (citable) accession number: P49294
Secondary accession number(s): O04950, Q0WQP1, Q4V3B7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: July 24, 2007
Last modified: October 29, 2014
This is version 124 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

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3