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B8DHJ1

- HEM1_LISMH

UniProt

B8DHJ1 - HEM1_LISMH

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Protein
Glutamyl-tRNA reductase
Gene
hemA, LMHCC_1012
Organism
Listeria monocytogenes serotype 4a (strain HCC23)
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

BioCyciLMON552536:GIW4-1048-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:LMHCC_1012
OrganismiListeria monocytogenes serotype 4a (strain HCC23)
Taxonomic identifieri552536 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
ProteomesiUP000000743: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 435435Glutamyl-tRNA reductaseUniRule annotation
PRO_1000190533Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi552536.LMHCC_1012.

Structurei

3D structure databases

ProteinModelPortaliB8DHJ1.

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.
OMAiAITCGKK.
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.

B8DHJ1-1 [UniParc]FASTAAdd to Basket

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MFILTMGLNH HTAPIDIREK LVFKETEEEM ALVTLQQEKS ILENVIISTC    50
NRTEIVAVVD QIHTGRYYLK RFMANWFQMD MEKIEPYLFF HEESEAVNHL 100
YKVTAGLDSL VLGETQILGQ VKHAFEIAKQ TATTGTLLNK LFREVVTFAK 150
KVHHHTKINE NAVSVSYAAV EVAKKLYGSL DNKKIVLIGA GEMSELALQN 200
LAGSGMTDIT IINRTKTNAE LLANQFQAKV GAYENMNEHL LLADIVLVST 250
SAAEPIIKQA AMQELMEQKA SSMLVIDIGL PRNVEHDCSY IPNFHLYDID 300
DLAGVVTANS IERQQIVLEL EDTIESEVRN FFEWEKQLGV VPVIRALREK 350
ALDMQEVTMT SLENKLPGLT EREYIQIGKH MKSIINQMLK QPISELKEMS 400
VEEDATTSIE HFKRIFGLTK TDVTIIEKEQ AETRS 435
Length:435
Mass (Da):49,252
Last modified:March 3, 2009 - v1
Checksum:i3ECA6621C50CD6B2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001175 Genomic DNA. Translation: ACK39360.1.
RefSeqiYP_002349974.1. NC_011660.1.

Genome annotation databases

EnsemblBacteriaiACK39360; ACK39360; LMHCC_1012.
GeneIDi7080193.
KEGGilmh:LMHCC_1012.
PATRICi20317141. VBILisMon86872_1001.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001175 Genomic DNA. Translation: ACK39360.1 .
RefSeqi YP_002349974.1. NC_011660.1.

3D structure databases

ProteinModelPortali B8DHJ1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 552536.LMHCC_1012.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACK39360 ; ACK39360 ; LMHCC_1012 .
GeneIDi 7080193.
KEGGi lmh:LMHCC_1012.
PATRICi 20317141. VBILisMon86872_1001.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
KOi K02492.
OMAi AITCGKK.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci LMON552536:GIW4-1048-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. "Genome sequence of lineage III Listeria monocytogenes strain HCC23."
    Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T., Bridges S.M., Lawrence M.L.
    J. Bacteriol. 193:3679-3680(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HCC23.

Entry informationi

Entry nameiHEM1_LISMH
AccessioniPrimary (citable) accession number: B8DHJ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: September 3, 2014
This is version 46 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

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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