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C1KVK4

- HEM1_LISMC

UniProt

C1KVK4 - HEM1_LISMC

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Protein

Glutamyl-tRNA reductase

Gene
hemA, Lm4b_01568
Organism
Listeria monocytogenes serotype 4b (strain CLIP80459)
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. 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

BioCyciLMON568819:GJF9-2313-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:Lm4b_01568
OrganismiListeria monocytogenes serotype 4b (strain CLIP80459)
Taxonomic identifieri568819 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
ProteomesiUP000002203: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 435435Glutamyl-tRNA reductaseUniRule annotationPRO_1000202637Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi634178.Lm4b_01568.

Structurei

3D structure databases

ProteinModelPortaliC1KVK4.

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

HOGENOMiHOG000109651.
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.

C1KVK4-1 [UniParc]FASTAAdd to Basket

« Hide

MFILTMGLNH HTAPIDIREK LVFKESEEEM ALVTLQQEKS ILENVIISTC    50
NRTEIIAVVD QIHTGRYYLK RFMANWFQMD MEKIEPYLFF HEESDAVNHL 100
YKVTAGLDSL VLGETQILGQ VKHAFEIAKQ TATTGTLLNK LFREVVTFAK 150
KVHHHTKINE NAVSVSYAAV EVAKKLYGSL DNKKIVLVGA GEMSELALQN 200
LAGSGIADIT IINRTKSNAE LLANQFQAKV GAYENMNEHL MLADIVLVST 250
SAAEPIIKQA AMQDLMEQKA SSMLVIDIGL PRNVEHDCSY IPNFHLYDID 300
DLAGVVSANS LERQRIVLEL EKTIEAEVRN FFEWEKQLGV VPVIRALREK 350
ALDMQEVTMT SLENKLPGLT EREYIQIGKH MKSIINQMLK QPISELKEMS 400
VEEDATTSIE HFKRIFGLSE TDVTVIEKEQ AETRS 435
Length:435
Mass (Da):49,150
Last modified:May 26, 2009 - v1
Checksum:iFF9A6C21960E7993
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FM242711 Genomic DNA. Translation: CAS05329.1.
RefSeqiYP_002758265.1. NC_012488.1.

Genome annotation databases

EnsemblBacteriaiCAS05329; CAS05329; Lm4b_01568.
GeneIDi7702959.
KEGGilmc:Lm4b_01568.
PATRICi20306303. VBILisMon88360_1578.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
FM242711 Genomic DNA. Translation: CAS05329.1 .
RefSeqi YP_002758265.1. NC_012488.1.

3D structure databases

ProteinModelPortali C1KVK4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 634178.Lm4b_01568.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAS05329 ; CAS05329 ; Lm4b_01568 .
GeneIDi 7702959.
KEGGi lmc:Lm4b_01568.
PATRICi 20306303. VBILisMon88360_1578.

Phylogenomic databases

HOGENOMi HOG000109651.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci LMON568819:GJF9-2313-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: CLIP80459.

Entry informationi

Entry nameiHEM1_LISMC
AccessioniPrimary (citable) accession number: C1KVK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 26, 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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