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Q8Y6X4

- HEM1_LISMO

UniProt

Q8Y6X4 - HEM1_LISMO

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Protein
Glutamyl-tRNA reductase
Gene
hemA, lmo1557
Organism
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
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) By similarity.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 – 501Nucleophile By similarity
Sitei99 – 991Important for activity By similarity
Binding sitei109 – 1091Substrate By similarity
Binding sitei120 – 1201Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi189 – 1946NADP By similarity

GO - Molecular functioni

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

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

BioCyciLMON169963:LMO1557-MONOMER.
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:lmo1557
OrganismiListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Taxonomic identifieri169963 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
ProteomesiUP000000817: Chromosome

Organism-specific databases

GenoListiLMO1557.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 435435Glutamyl-tRNA reductaseUniRule annotation
PRO_0000114037Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi169963.lmo1557.

Structurei

3D structure databases

ProteinModelPortaliQ8Y6X4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate binding By similarity
Regioni114 – 1163Substrate binding By similarity

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.UniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0373.
HOGENOMiHOG000109651.
KOiK02492.
OMAiLAHKLTN.
OrthoDBiEOG6MWNBM.
PhylomeDBiQ8Y6X4.

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.

Q8Y6X4-1 [UniParc]FASTAAdd to Basket

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MFILTMGLNH HTAPIDIREK LVFKETEEEM ALVTLQQEKS ILENVIISTC    50
NRTEIVAVVD QIHTGRYYLK RFMANWFQMD MEKIEPYLFF HEETEAVNHL 100
YKVTAGLDSL VLGETQILGQ VKHAFEIAKQ TETTGTLLNK LFREVVTFAK 150
KVHHHTKINE NAVSVSYAAV EVAKKLYGSL DNKKIVLVGA GEMSELALQN 200
LAGSGIADIT IINRTKSNAE LLANQFQAKV GAYENMNEHL MLADIVLVST 250
SATEPIIKQA AMQDLMEQKA SSMLVIDIGL PRNVEHDCSY IPNFHLYDID 300
DLAGVVSANS LERQRIVLEL ENTIEVEVRN FFEWEKQLGV VPVIRALREK 350
ALDMQEVAMT SLENKLPGLT EREYIQIGKH MKSIINQMLK QPISELKEMS 400
VEEDATTSIE HFKRIFGLSE TDVTVIEKEQ AETRS 435
Length:435
Mass (Da):49,250
Last modified:March 1, 2002 - v1
Checksum:iABA0CCFDF7DE1C01
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL591979 Genomic DNA. Translation: CAC99635.1.
PIRiAE1269.
RefSeqiNP_465082.1. NC_003210.1.

Genome annotation databases

EnsemblBacteriaiCAC99635; CAC99635; CAC99635.
GeneIDi986920.
KEGGilmo:lmo1557.
PATRICi20312243. VBILisMon69206_1598.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL591979 Genomic DNA. Translation: CAC99635.1 .
PIRi AE1269.
RefSeqi NP_465082.1. NC_003210.1.

3D structure databases

ProteinModelPortali Q8Y6X4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 169963.lmo1557.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAC99635 ; CAC99635 ; CAC99635 .
GeneIDi 986920.
KEGGi lmo:lmo1557.
PATRICi 20312243. VBILisMon69206_1598.

Organism-specific databases

GenoListi LMO1557.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.
PhylomeDBi Q8Y6X4.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci LMON169963:LMO1557-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: ATCC BAA-679 / EGD-e.

Entry informationi

Entry nameiHEM1_LISMO
AccessioniPrimary (citable) accession number: Q8Y6X4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: March 1, 2002
Last modified: September 3, 2014
This is version 92 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 By similarity.

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

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