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P48077 (HEM1_CYAPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Short name=GluTR
EC=1.2.1.70
Gene names
Name:hemA
Encoded onPlastid; Cyanelle
OrganismCyanophora paradoxa
Taxonomic identifier2762 [NCBI]
Taxonomic lineageEukaryotaGlaucocystophyceaeCyanophoraceaeCyanophora

Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA) By similarity. HAMAP-Rule MF_00087

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

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00087

Subcellular location

Plastidcyanelle HAMAP-Rule MF_00087.

Domain

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 By similarity. HAMAP-Rule MF_00087

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 caution

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

Ontologies

Keywords
   Biological processChlorophyll biosynthesis
Porphyrin biosynthesis
   Cellular componentCyanelle
Plastid
   LigandNADP
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological_processchlorophyll biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

protoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcyanelle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionNADP binding

Inferred from electronic annotation. Source: InterPro

glutamyl-tRNA reductase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 432432Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000114096

Regions

Nucleotide binding189 – 1946NADP By similarity
Region49 – 524Substrate binding By similarity
Region114 – 1163Substrate binding By similarity

Sites

Active site501Nucleophile By similarity
Binding site1091Substrate By similarity
Binding site1201Substrate By similarity
Site991Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P48077 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: F14378FC72FFD05B

FASTA43248,542
        10         20         30         40         50         60 
MNIIVVGLSH KTAPVDFREK LSIPKVRIGE AIRELCNYPH IEEVAILSTC NRLEIYLLTS 

        70         80         90        100        110        120 
DTYQGIREAT QFLADSSDLS LPELRQHLFI LLHQDAVMHL MRVTAGLDSL IIGEGQILSQ 

       130        140        150        160        170        180 
VKQCYQLGQQ YQGIGPVLNN IFKQAISAGK RVRTETQIST GAVSISSAAV ELAQIKKQDL 

       190        200        210        220        230        240 
RTANITILGA GKMSRLLVQH LLSKRVKDIN IVNRSVERAK LLVDQFKEAN INIYNLSELK 

       250        260        270        280        290        300 
TILQNSDIVF TGTSSQEPII TPELINDCDN LPSELMLFDI AVPRNVDPNV SQFDNIKVFN 

       310        320        330        340        350        360 
VDDLKVVVSQ NQQTRRKMAK AAEILLEEEL SAFNIWWGSL EAIPTINKLR EKAEIIRVKE 

       370        380        390        400        410        420 
LEKAISRLGN EFVSDHQEIV ESLTRGIVNK ILHDPMVQLR AQQDIEIRGR ALKILQTLFN 

       430 
LDTIKNGMSP TL 

« Hide

References

« Hide 'large scale' references
[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U30821 Genomic DNA. Translation: AAA81194.1.
X17063 Genomic DNA. Translation: CAC35456.1. Different initiation.
PIRT06851.
RefSeqNP_043163.1. NC_001675.1.

3D structure databases

ProteinModelPortalP48077.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID801525.

Enzyme and pathway databases

UniPathwayUPA00251; UER00316.
UPA00668.

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 nameHEM1_CYAPA
AccessionPrimary (citable) accession number: P48077
Secondary accession number(s): Q9BA13
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: February 19, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways