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P0A6X2

- HEM1_ECO57

UniProt

P0A6X2 - HEM1_ECO57

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Escherichia coli O157:H7
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
Sitei99 – 991Important for activityUniRule annotation
Binding sitei109 – 1091SubstrateUniRule annotation
Binding sitei120 – 1201SubstrateUniRule annotation

Regions

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

BioCyciECOL386585:GJFA-1696-MONOMER.
ECOO157:HEMA-MONOMER.
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:Z1981, ECs1715
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 418418Glutamyl-tRNA reductasePRO_0000114024Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi155864.Z1981.

Structurei

3D structure databases

ProteinModelPortaliP0A6X2.
SMRiP0A6X2. Positions 3-398.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni114 – 1163Substrate 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.
KOiK02492.
OMAiLAHKLTN.
OrthoDBiEOG6MWNBM.

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.

P0A6X2-1 [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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG56068.1.
BA000007 Genomic DNA. Translation: BAB35138.1.
PIRiC90843.
RefSeqiNP_287456.1. NC_002655.2.
NP_309742.1. NC_002695.1.

Genome annotation databases

EnsemblBacteriaiAAG56068; AAG56068; Z1981.
BAB35138; BAB35138; BAB35138.
GeneIDi913148.
960460.
KEGGiece:Z1981.
ecs:ECs1715.
PATRICi18352682. VBIEscCol44059_1566.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG56068.1 .
BA000007 Genomic DNA. Translation: BAB35138.1 .
PIRi C90843.
RefSeqi NP_287456.1. NC_002655.2.
NP_309742.1. NC_002695.1.

3D structure databases

ProteinModelPortali P0A6X2.
SMRi P0A6X2. Positions 3-398.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 155864.Z1981.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG56068 ; AAG56068 ; Z1981 .
BAB35138 ; BAB35138 ; BAB35138 .
GeneIDi 913148.
960460.
KEGGi ece:Z1981.
ecs:ECs1715.
PATRICi 18352682. VBIEscCol44059_1566.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109650.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci ECOL386585:GJFA-1696-MONOMER.
ECOO157:HEMA-MONOMER.

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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Entry informationi

Entry nameiHEM1_ECO57
AccessioniPrimary (citable) accession number: P0A6X2
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 1, 2014
This is version 74 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.UniRule annotation

Keywords - Technical termi

Complete proteome

Documents

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

External Data

Dasty 3