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A9FDP5 (HEM1_SORC5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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:sce1624
OrganismSorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So ce56)) [Complete proteome] [HAMAP]
Taxonomic identifier448385 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesSorangiineaePolyangiaceaeSorangium

Protein attributes

Sequence length529 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 – 529529Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000335074

Regions

Nucleotide binding205 – 2106NADP By similarity
Region47 – 504Substrate binding By similarity
Region130 – 1323Substrate binding By similarity

Sites

Active site481Nucleophile By similarity
Binding site1251Substrate By similarity
Binding site1361Substrate By similarity
Site1151Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A9FDP5 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: C115B5E9345DF6EF

FASTA52955,293
        10         20         30         40         50         60 
MIFVGLSHKT APIEVRERLA IGRDRLPEVL ARLTAHPAIG EALVLSTCNR VEIYASPRQQ 

        70         80         90        100        110        120 
APAPPRPGSA PPPSDEELSR NNEALRAAVA TLVGLGGDAV RGHLAGRVGS DAVLHLFRVA 

       130        140        150        160        170        180 
ASLDSMVVGE PQILGQMKEA IEVARGAKTL GVRLGRAAHR AIKVGKRVRT ETAIGAGQVS 

       190        200        210        220        230        240 
VSSVAIDLAR QIFADLAGHT ALLIGAGDMA EAASKLLVRA GARLIVVNRS PDRAAALARE 

       250        260        270        280        290        300 
VGGEPRPWAD LERSVIDADI VISSTSSPNY VVTPDLVRRA RKARKGRSLF LIDIAVPRDI 

       310        320        330        340        350        360 
DPAVNKLDSV YLYDVDDLSQ IVAESVEGRA AEAARAEAIV ADEAQAFEAW TLERALTPTI 

       370        380        390        400        410        420 
VGLRARTRSI LVAEVERSLS GKLRHLGVAE RQALAMMIDA ATNKLLHVPT TRLRAMASDP 

       430        440        450        460        470        480 
RVAEHVDSLR ELFDIDGAPP ENAAASALAE GELRGAVDGP PTPRSARGAA PPASGARGGG 

       490        500        510        520 
SPRHADPRPQ AAEDNGVYAR QPGGRPAEAG VMAVANPAAA VSAAGLKGA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM746676 Genomic DNA. Translation: CAN91782.1.
RefSeqYP_001612262.1. NC_010162.1.

3D structure databases

ProteinModelPortalA9FDP5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING448385.sce1624.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAN91782; CAN91782; sce1624.
GeneID5807028.
KEGGscl:sce1624.
PATRIC23661093. VBISorCel80414_1772.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OMARTEIYCA.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycSCEL448385:GJ75-1683-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. 2 hits.
TIGRFAMsTIGR01035. hemA. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM1_SORC5
AccessionPrimary (citable) accession number: A9FDP5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: February 19, 2014
This is version 54 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