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P42807

- HEM1_PSEAE

UniProt

P42807 - HEM1_PSEAE

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).UniRule annotation

Catalytic activityi

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei50 – 501NucleophileUniRule annotation
Sitei97 – 971Important for activityUniRule annotation
Binding sitei107 – 1071SubstrateUniRule annotation
Binding sitei118 – 1181SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi187 – 1926NADPUniRule annotation

GO - Molecular functioni

  1. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
  2. NADP binding Source: InterPro

GO - Biological processi

  1. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTRUniRule annotation
Gene namesi
Name:hemAUniRule annotation
Ordered Locus Names:PA4666
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438: Chromosome

Organism-specific databases

PseudoCAPiPA4666.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 422422Glutamyl-tRNA reductasePRO_0000114058Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi208964.PA4666.

Structurei

3D structure databases

ProteinModelPortaliP42807.
SMRiP42807. Positions 2-390.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni112 – 1143Substrate bindingUniRule annotation

Domaini

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.UniRule annotation

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109650.
InParanoidiP42807.
KOiK02492.
OMAiLAHKLTN.
OrthoDBiEOG6MWNBM.
PhylomeDBiP42807.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFiPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMiSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42807-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAFIALGINH KTASVAVRER VAFTPEQMVE ALQQLCRLTT SREAAILSTC
60 70 80 90 100
NRSELYLEID HPTADDVLAW LADYHRLTLD ELRACAYVHQ DEDAVRHMMR
110 120 130 140 150
VASGLDSMVL GEPQILGQMK SAYAVAREAG TVGPLLGRLF QATFSTAKTV
160 170 180 190 200
RTDTAIGENP VSVAFAAVSL AKQIFSDLHR SQALLIGAGE TITLVARHLF
210 220 230 240 250
EQGVKRIVVA NRTLERASLL AEQFGAHAVL LSEIPEELAN SDIVISSTAS
260 270 280 290 300
QLPILGKGAV ERALKQRKHK PMFMVDIAVP RDIEPEVGEL DDVYLYSVDD
310 320 330 340 350
LHEVVAENLK SRQGAAQAAE ELVGSGVAEF MQRLRELAAV DVLRAYRQQA
360 370 380 390 400
ERLRDEELGK AQRQLANGAD PAEVMAQLAR GLTNKLLHAP SVQMKKMSAE
410 420
GRIDALALAQ ELFALDEGAP RH
Length:422
Mass (Da):46,124
Last modified:December 8, 2000 - v3
Checksum:i33EA54A65BA94787
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti59 – 591I → V in CAA57574. (PubMed:7883699)Curated
Sequence conflicti153 – 1553DTA → ETD in CAA57574. (PubMed:7883699)Curated
Sequence conflicti314 – 3141G → A in CAA57574. (PubMed:7883699)Curated
Sequence conflicti343 – 3431L → V in CAA57574. (PubMed:7883699)Curated
Sequence conflicti418 – 4181G → C in CAA57574. (PubMed:7883699)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82071 Genomic DNA. Translation: CAA57574.1. Different initiation.
AE004091 Genomic DNA. Translation: AAG08053.1.
PIRiC83063.
RefSeqiNP_253355.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG08053; AAG08053; PA4666.
GeneIDi881361.
KEGGipae:PA4666.
PATRICi19844093. VBIPseAer58763_4888.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82071 Genomic DNA. Translation: CAA57574.1 . Different initiation.
AE004091 Genomic DNA. Translation: AAG08053.1 .
PIRi C83063.
RefSeqi NP_253355.1. NC_002516.2.

3D structure databases

ProteinModelPortali P42807.
SMRi P42807. Positions 2-390.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 208964.PA4666.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG08053 ; AAG08053 ; PA4666 .
GeneIDi 881361.
KEGGi pae:PA4666.
PATRICi 19844093. VBIPseAer58763_4888.

Organism-specific databases

PseudoCAPi PA4666.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109650.
InParanoidi P42807.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.
PhylomeDBi P42807.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_00087. Glu_tRNA_reductase.
InterProi IPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view ]
Pfami PF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMi SSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsi TIGR01035. hemA. 1 hit.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Entry informationi

Entry nameiHEM1_PSEAE
AccessioniPrimary (citable) accession number: P42807
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: December 8, 2000
Last modified: October 29, 2014
This is version 117 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3