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P42807 (HEM1_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. 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:PA4666
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length422 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.

Sequence caution

The sequence CAA57574.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference 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 – 422422Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000114058

Regions

Nucleotide binding187 – 1926NADP By similarity
Region49 – 524Substrate binding By similarity
Region112 – 1143Substrate binding By similarity

Sites

Active site501Nucleophile By similarity
Binding site1071Substrate By similarity
Binding site1181Substrate By similarity
Site971Important for activity By similarity

Experimental info

Sequence conflict591I → V in CAA57574. Ref.1
Sequence conflict153 – 1553DTA → ETD in CAA57574. Ref.1
Sequence conflict3141G → A in CAA57574. Ref.1
Sequence conflict3431L → V in CAA57574. Ref.1
Sequence conflict4181G → C in CAA57574. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P42807 [UniParc].

Last modified December 8, 2000. Version 3.
Checksum: 33EA54A65BA94787

FASTA42246,124
        10         20         30         40         50         60 
MAFIALGINH KTASVAVRER VAFTPEQMVE ALQQLCRLTT SREAAILSTC NRSELYLEID 

        70         80         90        100        110        120 
HPTADDVLAW LADYHRLTLD ELRACAYVHQ DEDAVRHMMR VASGLDSMVL GEPQILGQMK 

       130        140        150        160        170        180 
SAYAVAREAG TVGPLLGRLF QATFSTAKTV RTDTAIGENP VSVAFAAVSL AKQIFSDLHR 

       190        200        210        220        230        240 
SQALLIGAGE TITLVARHLF EQGVKRIVVA NRTLERASLL AEQFGAHAVL LSEIPEELAN 

       250        260        270        280        290        300 
SDIVISSTAS QLPILGKGAV ERALKQRKHK PMFMVDIAVP RDIEPEVGEL DDVYLYSVDD 

       310        320        330        340        350        360 
LHEVVAENLK SRQGAAQAAE ELVGSGVAEF MQRLRELAAV DVLRAYRQQA ERLRDEELGK 

       370        380        390        400        410        420 
AQRQLANGAD PAEVMAQLAR GLTNKLLHAP SVQMKKMSAE GRIDALALAQ ELFALDEGAP 


RH 

« Hide

References

« Hide 'large scale' references
[1]"Regulation of the hemA gene during 5-aminolevulinic acid formation in Pseudomonas aeruginosa."
Hungerer C., Troup B., Roemling U., Jahn D.
J. Bacteriol. 177:1435-1443(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[2]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X82071 Genomic DNA. Translation: CAA57574.1. Different initiation.
AE004091 Genomic DNA. Translation: AAG08053.1.
PIRC83063.
RefSeqNP_253355.1. NC_002516.2.

3D structure databases

ProteinModelPortalP42807.
SMRP42807. Positions 3-400.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA4666.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID881361.
KEGGpae:PA4666.
PATRIC19844093. VBIPseAer58763_4888.

Organism-specific databases

PseudoCAPPA4666.

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109650.
KOK02492.
OMARTEIYCA.
OrthoDBEOG6MWNBM.
ProtClustDBPRK00045.

Enzyme and pathway databases

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_PSEAE
AccessionPrimary (citable) accession number: P42807
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: December 8, 2000
Last modified: April 16, 2014
This is version 111 of the entry and version 3 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