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P48077

- HEM1_CYAPA

UniProt

P48077 - HEM1_CYAPA

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Cyanophora paradoxa
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).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 sitei50 – 501NucleophileUniRule annotation
Sitei99 – 991Important for activityUniRule annotation
Binding sitei109 – 1091SubstrateUniRule annotation
Binding sitei120 – 1201SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi189 – 1946NADPUniRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. chlorophyll biosynthetic process Source: UniProtKB-HAMAP
  2. 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

UniPathwayiUPA00251; UER00316.
UPA00668.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTRUniRule annotation
Gene namesi
Name:hemAUniRule annotation
Encoded oniPlastid; Cyanelle
OrganismiCyanophora paradoxa
Taxonomic identifieri2762 [NCBI]
Taxonomic lineageiEukaryotaGlaucocystophyceaeCyanophoraceaeCyanophora

Subcellular locationi

GO - Cellular componenti

  1. cyanelle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cyanelle, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432Glutamyl-tRNA reductasePRO_0000114096Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliP48077.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni114 – 1163Substrate bindingUniRule annotation

Domaini

Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.UniRule annotation

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.UniRule annotation

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.

P48077-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNIIVVGLSH KTAPVDFREK LSIPKVRIGE AIRELCNYPH IEEVAILSTC
60 70 80 90 100
NRLEIYLLTS DTYQGIREAT QFLADSSDLS LPELRQHLFI LLHQDAVMHL
110 120 130 140 150
MRVTAGLDSL IIGEGQILSQ VKQCYQLGQQ YQGIGPVLNN IFKQAISAGK
160 170 180 190 200
RVRTETQIST GAVSISSAAV ELAQIKKQDL RTANITILGA GKMSRLLVQH
210 220 230 240 250
LLSKRVKDIN IVNRSVERAK LLVDQFKEAN INIYNLSELK TILQNSDIVF
260 270 280 290 300
TGTSSQEPII TPELINDCDN LPSELMLFDI AVPRNVDPNV SQFDNIKVFN
310 320 330 340 350
VDDLKVVVSQ NQQTRRKMAK AAEILLEEEL SAFNIWWGSL EAIPTINKLR
360 370 380 390 400
EKAEIIRVKE LEKAISRLGN EFVSDHQEIV ESLTRGIVNK ILHDPMVQLR
410 420 430
AQQDIEIRGR ALKILQTLFN LDTIKNGMSP TL
Length:432
Mass (Da):48,542
Last modified:February 1, 1996 - v1
Checksum:iF14378FC72FFD05B
GO

Sequence cautioni

The sequence CAC35456.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U30821 Genomic DNA. Translation: AAA81194.1.
X17063 Genomic DNA. Translation: CAC35456.1. Different initiation.
PIRiT06851.
RefSeqiNP_043163.1. NC_001675.1.

Genome annotation databases

GeneIDi801525.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U30821 Genomic DNA. Translation: AAA81194.1 .
X17063 Genomic DNA. Translation: CAC35456.1 . Different initiation.
PIRi T06851.
RefSeqi NP_043163.1. NC_001675.1.

3D structure databases

ProteinModelPortali P48077.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 801525.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
UPA00668 .

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. "Nucleotide sequence of the cyanelle DNA from Cyanophora paradoxa."
    Stirewalt V.L., Michalowski C.B., Loeffelhardt W., Bohnert H.J., Bryant D.A.
    Plant Mol. Biol. Rep. 13:327-332(1995)
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: UTEX LB 555 / Pringsheim.
  2. "The complete sequence of the cyanelle genome of Cyanophora paradoxa: the genetic complexity of a primitive plastid."
    Loeffelhardt W., Stirewalt V.L., Michalowski C.B., Annarella M., Farley J.Y., Schluchter W.M., Chung S., Newmann-Spallart C., Steiner J.M., Jakowitsch J., Bohnert H.J., Bryant D.A.
    (In) Schenk H.E.A., Herrmann R., Jeon K.W., Mueller N.E., Schwemmler W. (eds.); Eukaryotism and symbiosis, pp.40-48, Springer-Verlag, Heidelberg (1997)
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: UTEX LB 555 / Pringsheim.
  3. "The cyanelle genome of Cyanophora paradoxa encodes ribosomal proteins not encoded by the chloroplasts genomes of higher plants."
    Bryant D.A., Stirewalt V.L.
    FEBS Lett. 259:273-280(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 407-432.
    Strain: UTEX LB 555 / Pringsheim.

Entry informationi

Entry nameiHEM1_CYAPA
AccessioniPrimary (citable) accession number: P48077
Secondary accession number(s): Q9BA13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: October 29, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

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.UniRule annotation

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3