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Q9UXR8 (HEM1_METKA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 113. 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:MK0200
OrganismMethanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938) [Reference proteome] [HAMAP]
Taxonomic identifier190192 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanopyriMethanopyralesMethanopyraceaeMethanopyrus

Protein attributes

Sequence length404 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). In the absence of NADPH, exhibits substrate esterase activity, leading to the release of glutamate from tRNA. Ref.1

Catalytic activity

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

Enzyme regulation

Inhibited by heavy metal compounds, Zn2+, and heme. Also competitively inhibited by glutamycin. 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

Subunit structure

Homotetramer. Ref.3

Sequence similarities

Belongs to the glutamyl-tRNA reductase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 8.1. HAMAP-Rule MF_00087

Temperature dependence:

Optimum temperature is 90 degrees Celsius.

Mass spectrometry

Molecular mass is 45436±30 Da from positions 1 - 404. Determined by ESI. Ref.1

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   LigandNADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processprotoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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 – 404404Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000114102

Regions

Nucleotide binding174 – 1796NADP Probable
Region47 – 504Substrate binding HAMAP-Rule MF_00087
Region99 – 1013Substrate binding HAMAP-Rule MF_00087

Sites

Active site481Nucleophile
Binding site941Substrate
Binding site1051Substrate
Site841Important for activity

Experimental info

Mutagenesis481C → S: Complete loss of activity. Ref.1
Mutagenesis841H → A: Complete loss of activity. Ref.1
Mutagenesis841H → N: 30% of wild-type reductase activity. 15% of wild-type esterase activity. Ref.1

Secondary structure

........................................................ 404
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9UXR8 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 8B6DBE436EA073B3

FASTA40445,444
        10         20         30         40         50         60 
MEDLVCVGIT HKEAEVEELE KARFESDEAV RDIVESFGLS GCVLLQTCNR VEVYASGARD 

        70         80         90        100        110        120 
RAEELGDLIH DDAWVKRGSE AVRHLFRVAC GLESMMVGEQ EILRQVKKAY DRAARLGTLD 

       130        140        150        160        170        180 
EALKIVFRRA INLGKRAREE TRISEGAVSI GSAAVELAER ELGSLHDKTV LVVGAGEMGK 

       190        200        210        220        230        240 
TVAKSLVDRG VRAVLVANRT YERAVELARD LGGEAVRFDE LVDHLARSDV VVSATAAPHP 

       250        260        270        280        290        300 
VIHVDDVREA LRKRDRRSPI LIIDIANPRD VEEGVENIED VEVRTIDDLR VIARENLERR 

       310        320        330        340        350        360 
RKEIPKVEKL IEEELSTVEE ELEKLKERRL VADVAKSLHE IKDRELERAL RRLKTGDPEN 

       370        380        390        400 
VLQDFAEAYT KRLINVLTSA IMELPDEYRR AACRALRRAS ELNG 

« Hide

References

« Hide 'large scale' references
[1]"Methanopyrus kandleri glutamyl-tRNA reductase."
Moser J., Lorenz S., Hubschwerlen C., Rompf A., Jahn D.
J. Biol. Chem. 274:30679-30685(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-30, FUNCTION, MASS SPECTROMETRY, CATALYTIC MECHANISM, MUTAGENESIS OF CYS-48 AND HIS-84.
[2]"The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens."
Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A.
Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.
[3]"V-shaped structure of glutamyl-tRNA reductase, the first enzyme of tRNA-dependent tetrapyrrole biosynthesis."
Moser J., Schubert W.-D., Beier V., Bringemeier I., Jahn D., Heinz D.W.
EMBO J. 20:6583-6590(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG, SUBUNIT, CATALYTIC MECHANISM, DOMAIN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ131561 Genomic DNA. Translation: CAB59204.1.
AE009439 Genomic DNA. Translation: AAM01417.1.
PIRT45026.
RefSeqNP_613487.1. NC_003551.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GPJX-ray1.95A1-404[»]
ProteinModelPortalQ9UXR8.
SMRQ9UXR8. Positions 1-404.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING190192.MK0200.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM01417; AAM01417; MK0200.
GeneID1477503.
KEGGmka:MK0200.

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OMAMANLVIK.

Enzyme and pathway databases

BRENDA1.2.1.70. 3274.
UniPathwayUPA00251; UER00316.

Family and domain databases

Gene3D1.10.1200.70. 1 hit.
3.40.50.720. 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...

Other

EvolutionaryTraceQ9UXR8.

Entry information

Entry nameHEM1_METKA
AccessionPrimary (citable) accession number: Q9UXR8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: May 1, 2000
Last modified: February 19, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways