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C5CB93 (HEM1_MICLC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 40. 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:Mlut_15240
OrganismMicrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus) [Complete proteome] [HAMAP]
Taxonomic identifier465515 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeMicrococcus

Protein attributes

Sequence length450 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 – 450450Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000202638

Regions

Nucleotide binding196 – 2016NADP By similarity
Region45 – 484Substrate binding By similarity
Region112 – 1143Substrate binding By similarity

Sites

Active site461Nucleophile By similarity
Binding site1071Substrate By similarity
Binding site1181Substrate By similarity
Site971Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
C5CB93 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: F15E233FC31F3069

FASTA45046,363
        10         20         30         40         50         60 
MTVFSLVASH HDLDLDTVAR LSAGATGVGP ALPGSGAAGA VVLATCNRVE IYAEADGAGV 

        70         80         90        100        110        120 
EAARAGLLSA VAASTSLPDE DVHAAFRTLD ADATARHLFE VGVGLDSAVV GEREIAGQVR 

       130        140        150        160        170        180 
RALTAAQEAG TASGPLVRLF ESATRTAKDV GSHTALGAAG RSVVSVALDL AEELRGLTDA 

       190        200        210        220        230        240 
AAQRDFWAGA TILLIGTGAY AGTTLAQLAD RGATTVGVHS ASGRAEQFVA DRGGWALALG 

       250        260        270        280        290        300 
GEAVAGAVAE ADVIIGSSGG ERQISPERLQ ELREGGRRPL TVVDLALSRD FDPAVADLPD 

       310        320        330        340        350        360 
VDLITLESVR LAAPEQAQVA VAEARALVDD AVEEYRAAQR GRSADAAIKA LRRHTLGVLD 

       370        380        390        400        410        420 
RELERVRARH GCTAAAEEVE FALRRMVNQL LHEPSVRAKR LAAEGRLDRY EDALEAVFGI 

       430        440        450 
EAPGRPASEV GTVEAACPAH EDEGGAARIA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001628 Genomic DNA. Translation: ACS31016.1.
RefSeqYP_002957570.1. NC_012803.1.

3D structure databases

ProteinModelPortalC5CB93.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING465515.Mlut_15240.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS31016; ACS31016; Mlut_15240.
GeneID7986020.
KEGGmlu:Mlut_15240.
PATRIC22623682. VBIMicLut29563_1460.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109649.
KOK02492.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycMLUT465515:GHH6-1521-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.
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.
ProtoNetSearch...

Entry information

Entry nameHEM1_MICLC
AccessionPrimary (citable) accession number: C5CB93
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: May 14, 2014
This is version 40 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