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B2GL19 (HEM1_KOCRD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 52. 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
Ordered Locus Names:KRH_08480
OrganismKocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201) [Complete proteome] [HAMAP]
Taxonomic identifier378753 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeKocuria

Protein attributes

Sequence length437 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

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.

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete 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 – 437437Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000190532

Regions

Nucleotide binding192 – 1976NADP By similarity
Region46 – 494Substrate binding By similarity
Region116 – 1183Substrate binding By similarity

Sites

Active site471Nucleophile By similarity
Binding site1111Substrate By similarity
Binding site1221Substrate By similarity
Site1011Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
B2GL19 [UniParc].

Last modified June 10, 2008. Version 1.
Checksum: 5C9A0BA85B99378A

FASTA43746,442
        10         20         30         40         50         60 
MVLFCLVASH RTVDLNTVAR LSTGALGVAE DAVSRGALAG AITLSTCNRL ELYGELPEHA 

        70         80         90        100        110        120 
SVDVPGAQQQ LAERIARRAG LDERFVLETM DAYEGPEVPR HLFTVVSGLE SAVVGEREIT 

       130        140        150        160        170        180 
GQVRRALAGA QQSGTASPHL VQLFEAAART AREVGASTGL GERGRSIVSV ALDLADDITS 

       190        200        210        220        230        240 
GDWPERHALV FGTGAYAGAT MAALRDRGCA DIEVYSGSGR AQQFTDQRGG SPVTDESLPG 

       250        260        270        280        290        300 
ALRRADVIIG CSGGSAPMPA SRFPAGPRTV VDLALARDFD PAVADLPNVE LITLESVRVA 

       310        320        330        340        350        360 
APEETRESVA AAREIVERAA RDFENARTAR SMDQAIVALR KHTMAVLDAE LDKVRTHHGC 

       370        380        390        400        410        420 
TGAEEQIEMA MRRMVRSLLH TPTVRARQLA AEGRADEYIT GLEALYGLEV AVPDVPEETA 

       430 
PSTRQDPSDT PRPRAVG 

« Hide

References

[1]"Complete genome sequence of the soil actinomycete Kocuria rhizophila."
Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S., Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.
J. Bacteriol. 190:4139-4146(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9341 / DSM 348 / NBRC 103217 / DC2201.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009152 Genomic DNA. Translation: BAG29195.1.
RefSeqYP_001854701.1. NC_010617.1.

3D structure databases

ProteinModelPortalB2GL19.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING378753.KRH_08480.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG29195; BAG29195; KRH_08480.
GeneID6238180.
KEGGkrh:KRH_08480.
PATRIC22181910. VBIKocRhi5258_0824.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109649.
KOK02492.
OMAKCVLINT.
OrthoDBEOG6MWNBM.
ProtClustDBPRK00045.

Enzyme and pathway databases

BioCycKRHI378753:GJ8F-864-MONOMER.
UniPathwayUPA00251; UER00316.

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.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM1_KOCRD
AccessionPrimary (citable) accession number: B2GL19
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 10, 2008
Last modified: February 19, 2014
This is version 52 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

PATHWAY comments

Index of metabolic and biosynthesis pathways