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A6VND5 (HEM1_ACTSZ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:Asuc_1116
OrganismActinobacillus succinogenes (strain ATCC 55618 / 130Z) [Complete proteome] [HAMAP]
Taxonomic identifier339671 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeActinobacillus

Protein attributes

Sequence length435 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 – 435435Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000071245

Regions

Nucleotide binding204 – 2096NADP By similarity
Region49 – 524Substrate binding By similarity
Region119 – 1213Substrate binding By similarity

Sites

Active site501Nucleophile By similarity
Binding site1141Substrate By similarity
Binding site1251Substrate By similarity
Site1041Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A6VND5 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: F6A876382802D60B

FASTA43549,073
        10         20         30         40         50         60 
MTILVLGINH KTATVALREK VAFSEEKRLS ALNQIEQLKL AQSTVILSTC NRTEVYLHNK 

        70         80         90        100        110        120 
FIQPEQNSAW IDECVAWFAA IHQIQLTDLQ DCLYFYQNQQ AVTHLMRVAC GLDSLILGEP 

       130        140        150        160        170        180 
QILGQVKQAY QLAEEYYQRA HGLGKSAVIS SELSRLFQKT FSTAKRVRTE TNIGESAVSV 

       190        200        210        220        230        240 
AYAACSLGRQ IFESLQELTI LLVGAGETIE LAARHLLRHG VKKLMIANRT RARAEALVAK 

       250        260        270        280        290        300 
LESPFIEILS LSELQDGLNQ ADIVISSTGS PTTLISYEMM KQAQIQRRYR PVLIVDIAVP 

       310        320        330        340        350        360 
RDVEESIVKL DSVYHYTVDD LQNIINHNLS EREKASEQAE EIIAEECAAF FEWLKVRQAS 

       370        380        390        400        410        420 
NLIRTYRESA DEIRQELLEK AQFSLSQGES ADKILDEFST KLMNKLLHSP TLVMQTMVKQ 

       430 
GDSRGLQNFL SVIKK 

« Hide

References

[1]"Complete sequence of Actinobacillus succinogenes 130Z."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Vieille C., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 55618 / 130Z.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000746 Genomic DNA. Translation: ABR74482.1.
RefSeqYP_001344417.1. NC_009655.1.

3D structure databases

ProteinModelPortalA6VND5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING339671.Asuc_1116.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR74482; ABR74482; Asuc_1116.
GeneID5348066.
KEGGasu:Asuc_1116.
PATRIC20760606. VBIActSuc117883_1182.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109650.
KOK02492.
OMALAHKLTN.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycASUC339671:GHDX-1180-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.
TIGRFAMsTIGR01035. hemA. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM1_ACTSZ
AccessionPrimary (citable) accession number: A6VND5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: August 21, 2007
Last modified: May 14, 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