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B0RUA4 (HEM1_XANCB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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:xcc-b100_3481
OrganismXanthomonas campestris pv. campestris (strain B100) [Complete proteome] [HAMAP]
Taxonomic identifier509169 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length432 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 – 432432Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000335081

Regions

Nucleotide binding181 – 1866NADP By similarity
Region49 – 524Substrate binding By similarity
Region106 – 1083Substrate binding By similarity

Sites

Active site501Nucleophile By similarity
Binding site1011Substrate By similarity
Binding site1121Substrate By similarity
Site911Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
B0RUA4 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 0A247EA86CBA35EF

FASTA43247,365
        10         20         30         40         50         60 
MTLWVLGLNH QTAPVDLRER AAFAGDALPR ALDSLRTLPQ VREAALLSTC NRTELYAMAD 

        70         80         90        100        110        120 
DPQTLVAWLD MHAPGLSGYL YQHRDAEAVR HLFRVATGLD SMVLGEPQIL GQVKDAWAVA 

       130        140        150        160        170        180 
RAHGALGSGL DRLFQQTFSV AKRARTDTRV GANPVSVAST AVRLAQESFA RLNESTVLLV 

       190        200        210        220        230        240 
GAGETIELAA KHLSEGRVRR LLIANRTLAH AQTLATQHGG VALPLTELDR HLAEADVVFS 

       250        260        270        280        290        300 
ATAAREPVVT RVQVEQALRT RKRKPMLLFD LAVPRDIEAS VAELSDAYLY TVDDLERAVE 

       310        320        330        340        350        360 
DNRRSRREAA DQAEAIIDLQ VARYVETLQA NERQAPLKRL RAFGDSTRDE LLAKARQQLS 

       370        380        390        400        410        420 
NGKPADEVLE QLAHALTNRL LHPPTAALRD AALNNDLDLT SAADRLFPEK PGYRHPPVAT 

       430 
PIVRTDDANP AP 

« Hide

References

[1]"The genome of Xanthomonas campestris pv. campestris B100 and its use for the reconstruction of metabolic pathways involved in xanthan biosynthesis."
Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T., Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K., Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K., Puehler A.
J. Biotechnol. 134:33-45(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM920689 Genomic DNA. Translation: CAP52846.1.
RefSeqYP_001904886.1. NC_010688.1.

3D structure databases

ProteinModelPortalB0RUA4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING509169.xccb100_3481.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAP52846; CAP52846; xcc-b100_3481.
GeneID6323376.
KEGGxca:xccb100_3481.
PATRIC24086896. VBIXanCam108527_3509.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
KOK02492.
OMALAHKLTN.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycXCAM509169:GHW4-3564-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_XANCB
AccessionPrimary (citable) accession number: B0RUA4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 8, 2008
Last modified: May 14, 2014
This is version 50 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