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P28463 (HEM1_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. 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·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
Ordered Locus Names:slr1808
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis

Protein attributes

Sequence length427 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) Probable. Ref.1

Catalytic activity

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. HAMAP-Rule MF_00087

Enzyme regulation

Feedback inhibition by heme. 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

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 BAA17738.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 427427Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000114079

Regions

Nucleotide binding188 – 1936NADP 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
P28463 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 5F5D9D744A900D7D

FASTA42747,526
        10         20         30         40         50         60 
MNIAVVGLSH KTAPVEIREK LSIQEAKLEE ALTHLRSYPH IEEVTVISTC NRLEIYAVVT 

        70         80         90        100        110        120 
DTEKGVVEIT QFLSETGNIP LATLRRYLFT LLHEDAVRHL MRVAAGLESL VLGEGQILAQ 

       130        140        150        160        170        180 
VRTTHKLGQK YKGVGRLLDR LFKQAITAGR RVRTETDIGT GAVSISSAAV ELVHRQVDLS 

       190        200        210        220        230        240 
SQKTVIIGAG KMACLLVKHL LAKGATDITI VNRSQRRSQD LANQFPQAQL TLCPLTDMFT 

       250        260        270        280        290        300 
AIAAGDIVFT STGATEPILN CENLTGCVIN RKSLMLVDIS VPRNVAADVH AMEQVRAFNV 

       310        320        330        340        350        360 
DDLKEVVAQN QASRRQMARQ AEALLEEEIA AFDLWWRSLE TVPTISSLRS KVEDIREQEL 

       370        380        390        400        410        420 
EKALSRLGSE FAEKHQEVIE ALTRGIVNKI LHEPMVQLRA QQDIEARKQC LRSLKMLFDL 


EVEEQFG 

« Hide

References

« Hide 'large scale' references
[1]"Glutamyl-tRNA reductase from Escherichia coli and Synechocystis 6803. Gene structure and expression."
Verkamp E., Jahn M., Jahn D., Kumar A.M., Soell D.
J. Biol. Chem. 267:8275-8280(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]"Identification of a hemA gene from Synechocystis by complementation of an E. coli hemA mutant."
Grimm B.
Hereditas 117:195-197(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 6803 / Kazusa.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M84218 Genomic DNA. Translation: AAA27289.1.
X65963 Genomic DNA. Translation: CAA46779.1.
BA000022 Genomic DNA. Translation: BAA17738.1. Different initiation.
PIRS77180.
RefSeqYP_007450940.1. NC_020286.1.

3D structure databases

ProteinModelPortalP28463.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING1148.slr1808.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA17738; BAA17738; BAA17738.
KEGGsyz:MYO_111720.
PATRIC23839406. VBISynSp132158_1267.

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OMAAITCGKK.
PhylomeDBP28463.

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_SYNY3
AccessionPrimary (citable) accession number: P28463
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: July 9, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways