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P0A6X1

- HEM1_ECOLI

UniProt

P0A6X1 - HEM1_ECOLI

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). In the absence of NADPH, exhibits substrate esterase activity, leading to the release of glutamate from tRNA.2 Publications

Catalytic activityi

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

Enzyme regulationi

Activated by Mg2+ ions. Inhibited by metal-chelating agents such as EDTA, EGTA, 1,10-phenanthroline, 2,2'-dipyridyl, and by PtCl4 and KPdCl4 as well as Ni2+ and Co2+. Also inhibited by iodoacetamide, N-tosyl-L-phenylalanine chloromethyl ketone, and 5,5'-dithiobis(2-nitrobenzoic acid), as well as glutamycin.1 Publication

Kineticsi

  1. KM=24 µM for L-glutamyl-tRNA(Glu)1 Publication
  2. KM=39 µM for NADPH1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei50 – 501Nucleophile
Sitei99 – 991Important for activity
Binding sitei109 – 1091SubstrateCurated
Binding sitei120 – 1201SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi189 – 1946NADPCurated

GO - Molecular functioni

  1. glutamyl-tRNA reductase activity Source: EcoCyc
  2. identical protein binding Source: EcoCyc
  3. NADP binding Source: InterPro

GO - Biological processi

  1. protoporphyrinogen IX biosynthetic process from glutamate Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciEcoCyc:GLUTRNAREDUCT-MONOMER.
ECOL316407:JW1201-MONOMER.
MetaCyc:GLUTRNAREDUCT-MONOMER.
SABIO-RKP0A6X1.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:hemA
Ordered Locus Names:b1210, JW1201
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10427. hemA.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi7 – 71G → D: Loss of activity. 1 Publication
Mutagenesisi49 – 491T → V: 10% and 5% of wild-type reductase and esterase activity, respectively. 1 Publication
Mutagenesisi50 – 501C → S: Loss of activity. 1 Publication
Mutagenesisi52 – 521R → K: 5% and 4% of wild-type reductase and esterase activity, respectively. 1 Publication
Mutagenesisi52 – 521R → Q: Loss of activity. 1 Publication
Mutagenesisi54 – 541E → K: 6% and 2% of wild-type reductase and esterase activity, respectively. 1 Publication
Mutagenesisi74 – 741C → S: No effect. 1 Publication
Mutagenesisi99 – 991H → N: 5% and 4% of wild-type reductase and esterase activity, respectively. 1 Publication
Mutagenesisi106 – 1061G → N: Loss of activity. 1 Publication
Mutagenesisi109 – 1091S → A: 28% and 25% of wild-type reductase and esterase activity, respectively. 1 Publication
Mutagenesisi114 – 1141E → K: Loss of activity. 1 Publication
Mutagenesisi116 – 1161Q → L: Loss of reductase activity. 30% of wild-type esterase activity. 1 Publication
Mutagenesisi145 – 1451S → F: Loss of activity. 1 Publication
Mutagenesisi170 – 1701C → S: No effect. 1 Publication
Mutagenesisi191 – 1911G → D: Loss of reductase activity. Retains esterase activity. 1 Publication
Mutagenesisi314 – 3141R → C: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 418418Glutamyl-tRNA reductasePRO_0000114023Add
BLAST

Proteomic databases

PaxDbiP0A6X1.
PRIDEiP0A6X1.

Expressioni

Gene expression databases

GenevestigatoriP0A6X1.

Interactioni

Subunit structurei

Homodimer. Interacts with glutamate-1-semialdehyde 2,1-aminomutase (GSA-AM), which forms a metabolic channeling between both enzymes to protect the reactive aldehyde species GSA.2 Publications

Protein-protein interaction databases

DIPiDIP-9877N.
IntActiP0A6X1. 1 interaction.
STRINGi511145.b1210.

Structurei

3D structure databases

ProteinModelPortaliP0A6X1.
SMRiP0A6X1. Positions 3-398.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingCurated
Regioni114 – 1163Substrate bindingCurated

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 (By similarity).By similarity

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.Curated

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109650.
InParanoidiP0A6X1.
KOiK02492.
OMAiLAHKLTN.
OrthoDBiEOG6MWNBM.
PhylomeDBiP0A6X1.

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.

P0A6X1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTLLALGINH KTAPVSLRER VSFSPDKLDQ ALDSLLAQPM VQGGVVLSTC
60 70 80 90 100
NRTELYLSVE EQDNLQEALI RWLCDYHNLN EEDLRKSLYW HQDNDAVSHL
110 120 130 140 150
MRVASGLDSL VLGEPQILGQ VKKAFADSQK GHMKASELER MFQKSFSVAK
160 170 180 190 200
RVRTETDIGA SAVSVAFAAC TLARQIFESL STVTVLLVGA GETIELVARH
210 220 230 240 250
LREHKVQKMI IANRTRERAQ ILADEVGAEV IALSDIDERL READIIISST
260 270 280 290 300
ASPLPIIGKG MVERALKSRR NQPMLLVDIA VPRDVEPEVG KLANAYLYSV
310 320 330 340 350
DDLQSIISHN LAQRKAAAVE AETIVAQETS EFMAWLRAQS ASETIREYRS
360 370 380 390 400
QAEQVRDELT AKALAALEQG GDAQAIMQDL AWKLTNRLIH APTKSLQQAA
410
RDGDNERLNI LRDSLGLE
Length:418
Mass (Da):46,307
Last modified:March 29, 2005 - v1
Checksum:i3CEE59AC53610A88
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti151 – 16818RVRTE…SVAFA → PFALKQISVPALCLSLLP in CAA35476. (PubMed:2664455)CuratedAdd
BLAST
Sequence conflicti172 – 1721L → V in CAA35476. (PubMed:2664455)Curated
Sequence conflicti240 – 2401L → M in CAA35476. (PubMed:2664455)Curated
Sequence conflicti243 – 2431A → R(PubMed:2684779)Curated
Sequence conflicti243 – 2431A → R(PubMed:7543480)Curated
Sequence conflicti365 – 3651A → R in CAA35476. (PubMed:2664455)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M30785 Genomic DNA. Translation: AAA23953.1.
M25323 Genomic DNA. Translation: AAA23954.1.
X17434 Genomic DNA. Translation: CAA35476.1.
U18555 Genomic DNA. Translation: AAC43436.1.
U00096 Genomic DNA. Translation: AAC74294.1.
AP009048 Genomic DNA. Translation: BAA36068.1.
D10264 Genomic DNA. Translation: BAA20969.1.
PIRiA45918. BVECHA.
RefSeqiNP_415728.1. NC_000913.3.
YP_489477.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74294; AAC74294; b1210.
BAA36068; BAA36068; BAA36068.
GeneIDi12931822.
945777.
KEGGiecj:Y75_p1182.
eco:b1210.
PATRICi32117672. VBIEscCol129921_1258.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M30785 Genomic DNA. Translation: AAA23953.1 .
M25323 Genomic DNA. Translation: AAA23954.1 .
X17434 Genomic DNA. Translation: CAA35476.1 .
U18555 Genomic DNA. Translation: AAC43436.1 .
U00096 Genomic DNA. Translation: AAC74294.1 .
AP009048 Genomic DNA. Translation: BAA36068.1 .
D10264 Genomic DNA. Translation: BAA20969.1 .
PIRi A45918. BVECHA.
RefSeqi NP_415728.1. NC_000913.3.
YP_489477.1. NC_007779.1.

3D structure databases

ProteinModelPortali P0A6X1.
SMRi P0A6X1. Positions 3-398.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9877N.
IntActi P0A6X1. 1 interaction.
STRINGi 511145.b1210.

Proteomic databases

PaxDbi P0A6X1.
PRIDEi P0A6X1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74294 ; AAC74294 ; b1210 .
BAA36068 ; BAA36068 ; BAA36068 .
GeneIDi 12931822.
945777.
KEGGi ecj:Y75_p1182.
eco:b1210.
PATRICi 32117672. VBIEscCol129921_1258.

Organism-specific databases

EchoBASEi EB0422.
EcoGenei EG10427. hemA.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109650.
InParanoidi P0A6X1.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.
PhylomeDBi P0A6X1.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci EcoCyc:GLUTRNAREDUCT-MONOMER.
ECOL316407:JW1201-MONOMER.
MetaCyc:GLUTRNAREDUCT-MONOMER.
SABIO-RK P0A6X1.

Miscellaneous databases

PROi P0A6X1.

Gene expression databases

Genevestigatori P0A6X1.

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. "Cloning and structure of the hem A gene of Escherichia coli K-12."
    Li J.-M., Russell C.S., Cosloy S.D.
    Gene 82:209-217(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. "Isolation, nucleotide sequence, and preliminary characterization of the Escherichia coli K-12 hemA gene."
    Verkamp E., Chelm B.K.
    J. Bacteriol. 171:4728-4735(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  3. "Isolation and nucleotide sequence of the hemA gene of Escherichia coli K12."
    Drolet M., Peloquin L., Echelard Y., Cousineau L., Sasarman A.
    Mol. Gen. Genet. 216:347-352(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  4. "Expression of genes kdsA and kdsB involved in 3-deoxy-D-manno-octulosonic acid metabolism and biosynthesis of enterobacterial lipopolysaccharide is growth phase regulated primarily at the transcriptional level in Escherichia coli K-12."
    Strohmaier H., Remler P., Renner W., Hoegenauer G.
    J. Bacteriol. 177:4488-4500(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  7. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  8. "Cloning and characterization of genes involved in the biosynthesis of delta-aminolevulinic acid in Escherichia coli."
    Ikemi M., Murakami K., Hashimoto M., Murooka Y.
    Gene 121:127-132(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49.
  9. Cited for: PROTEIN SEQUENCE OF 1-15, FUNCTION, CATALYTIC ACTIVITY, CHARACTERIZATION, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, KINETIC PARAMETERS, CATALYTIC MECHANISM, MUTAGENESIS OF GLY-7; CYS-50; CYS-74; GLY-106; GLU-114; SER-145; CYS-170; GLY-191 AND ARG-314.
  10. "Glutamyl-tRNA reductase from Escherichia coli and Synechocystis 6803. Gene structure and expression."
    Verkamp E., Jahn M., Jahn D., Kumar A.M., Soell D.
    J. Biol. Chem. 267:8275-8280(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Complex formation between glutamyl-tRNA reductase and glutamate-1-semialdehyde 2,1-aminomutase in Escherichia coli during the initial reactions of porphyrin biosynthesis."
    Lueer C., Schauer S., Moebius K., Schulze J., Schubert W.-D., Heinz D.W., Jahn D., Moser J.
    J. Biol. Chem. 280:18568-18572(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GSA-AM.
  12. "Glutamate recognition and hydride transfer by Escherichia coli glutamyl-tRNA reductase."
    Lueer C., Schauer S., Virus S., Schubert W.-D., Heinz D.W., Moser J., Jahn D.
    FEBS J. 274:4609-4614(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF THR-49; ARG-52; GLU-54; HIS-99; SER-109 AND GLN-116.

Entry informationi

Entry nameiHEM1_ECOLI
AccessioniPrimary (citable) accession number: P0A6X1
Secondary accession number(s): P13580, Q59405
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: October 29, 2014
This is version 94 of the entry and version 1 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.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3