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Q7WQF0 (HEM1_BORBR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 80. 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:BB0383
OrganismBordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP]
Taxonomic identifier257310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length424 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 – 424424Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000113997

Regions

Nucleotide binding191 – 1966NADP By similarity
Region53 – 564Substrate binding By similarity
Region116 – 1183Substrate binding By similarity

Sites

Active site541Nucleophile By similarity
Binding site1111Substrate By similarity
Binding site1221Substrate By similarity
Site1011Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7WQF0 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 3E9540D9435A8A27

FASTA42446,736
        10         20         30         40         50         60 
MSVAVLAFGL NHTSAPVSVR ERVSMPVDLV KPALEGLRAT FGGAVREAAI LSTCNRTELY 

        70         80         90        100        110        120 
CAAEGQVAEH LPAWLAEHNR LEAAALRPHL YRHQHDDAVR HAFRVASGLD SMVLGEPQIL 

       130        140        150        160        170        180 
GQMKDAVRAA NEAGALGTLL HQLFQRTFSV AKEVRSQTAI GAHSVSMAAA AVRLAERVFG 

       190        200        210        220        230        240 
QLEDARTLFI GAGEMIELCA THFAAQRPRS MVVANRTIER AETLAGRFSA QTMKLADLTE 

       250        260        270        280        290        300 
RLAEFDVIVS CTASSLPILG LGMVERATRQ RRHRPMVMID LAVPRDIEPE VGRLDDVYLY 

       310        320        330        340        350        360 
SVDDLGRLVQ SGTDARRAAV VQAEAIIETR VQGFMHWMQS REVVPVIRDL HQAADDVRAA 

       370        380        390        400        410        420 
ELERARRMLA RGESPEAVLE QLAHGLTQKY LHGPLAALNR SEGDERRQLL AWVPRLFPGR 


DSRR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX640438 Genomic DNA. Translation: CAE30881.1.
RefSeqNP_886932.1. NC_002927.3.

3D structure databases

ProteinModelPortalQ7WQF0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257310.BB0383.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE30881; CAE30881; BB0383.
GeneID2663607.
KEGGbbr:BB0383.
PATRIC21133972. VBIBorBro124907_0386.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG317931.
HOGENOMHOG000010227.
KOK02492.
OMAKMLHGTM.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycBBRO257310:BB0383-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_BORBR
AccessionPrimary (citable) accession number: Q7WQF0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 80 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