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B1HVD8

- HEM1_LYSSC

UniProt

B1HVD8 - HEM1_LYSSC

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Protein
Glutamyl-tRNA reductase
Gene
hemA, Bsph_3972
Organism
Lysinibacillus sphaericus (strain C3-41)
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
Complete GO annotation...

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

BioCyciLSPH444177:GJEL-3945-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:Bsph_3972
OrganismiLysinibacillus sphaericus (strain C3-41)
Taxonomic identifieri444177 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeLysinibacillus
ProteomesiUP000002164: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 454454Glutamyl-tRNA reductaseUniRule annotation
PRO_1000093149Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi444177.Bsph_3972.

Structurei

3D structure databases

ProteinModelPortaliB1HVD8.

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.

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.

B1HVD8-1 [UniParc]FASTAAdd to Basket

« Hide

MHTIVVGLNY KTAPVEIREK LSFIESELPQ AMEALQKQKS ILENVIVSTC    50
NRTEIYAVVD QLHTGRHFVK QFLADWFDLP VETFSSYLTI REEDEAVEHL 100
FKVTAGIDSM VLGETQILGQ VKKSFLSGQE IGTTGTVYNQ LFKQAVTFAK 150
RAHNETAIGE NAVSVSYAAV ELAKKIFGSL QRKHVAILGA GKMGELAIEN 200
LYGSGVGKVT VINRTFEKAE SLAAKFHGQA KSMKELQCSL LEADILITST 250
GATDYVIDYE LMQFVERLRK GKPLFMVDIA VPRDIDPRVG DLPNVFLYDI 300
DDLQGIVEAN LAERERAAAD ITDMIGHEVI QFKDWVSTLG VVPVISALRK 350
KANRIQEETM TSIENKMPDL TERERKILSK HTKSIINQLL KEPILQAKEM 400
ANSPKANEQL RLFQQIFGIE EAVEAEVQEM TKQELERKER AQATQTSAEP 450
KYSF 454
Length:454
Mass (Da):50,925
Last modified:April 29, 2008 - v1
Checksum:iED4A1768750B7EAC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000817 Genomic DNA. Translation: ACA41440.1.
RefSeqiYP_001699570.1. NC_010382.1.

Genome annotation databases

EnsemblBacteriaiACA41440; ACA41440; Bsph_3972.
GeneIDi6025001.
KEGGilsp:Bsph_3972.
PATRICi22420379. VBILysSph89750_4047.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000817 Genomic DNA. Translation: ACA41440.1 .
RefSeqi YP_001699570.1. NC_010382.1.

3D structure databases

ProteinModelPortali B1HVD8.
ModBasei Search...

Protein-protein interaction databases

STRINGi 444177.Bsph_3972.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACA41440 ; ACA41440 ; Bsph_3972 .
GeneIDi 6025001.
KEGGi lsp:Bsph_3972.
PATRICi 22420379. VBILysSph89750_4047.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci LSPH444177:GJEL-3945-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. "Complete genome sequence of the mosquitocidal bacterium Bacillus sphaericus C3-41 and comparison with those of closely related Bacillus species."
    Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M., Berry C., Yuan Z.
    J. Bacteriol. 190:2892-2902(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C3-41.

Entry informationi

Entry nameiHEM1_LYSSC
AccessioniPrimary (citable) accession number: B1HVD8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: September 3, 2014
This is version 51 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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