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C5C5B0

- HEM1_BEUC1

UniProt

C5C5B0 - HEM1_BEUC1

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Protein
Glutamyl-tRNA reductase
Gene
hemA, Bcav_4009
Organism
Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432)
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 sitei49 – 491Nucleophile By similarity
Sitei114 – 1141Important for activity By similarity
Binding sitei124 – 1241Substrate By similarity
Binding sitei135 – 1351Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi204 – 2096NADP 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

BioCyciBCAV471853:GI1Z-4062-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:Bcav_4009
OrganismiBeutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432)
Taxonomic identifieri471853 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeBeutenbergiaceaeBeutenbergia
ProteomesiUP000007962: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 441441Glutamyl-tRNA reductaseUniRule annotation
PRO_1000202630Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi471853.Bcav_4009.

Structurei

3D structure databases

ProteinModelPortaliC5C5B0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 514Substrate binding By similarity
Regioni129 – 1313Substrate 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.
HOGENOMiHOG000109649.
KOiK02492.
OMAiPYLYVHY.
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. 2 hits.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

C5C5B0-1 [UniParc]FASTAAdd to Basket

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MLLSVSASHR DADLADLERL SSGVGRVWAD APLVAHGLDG AGVVLLATCN    50
RFEVYLDVAD GTDPQRALAV VRDLVRTVPE SPLAAPGADD DAAGPGPDPS 100
AALRVRVGDD AARHLFGVAS GLDSIVVGER EIAGQVRRAI AAARRAGTTT 150
GALERLFAQA QRTSRAVEAG TGLAAAGRSV VGVALDLAAR SAPPWPLARV 200
VLIGTGSYAG ASLAALRARG CTDVRVHSES GRAEEFARAR EAEAVPPGEL 250
LTAIADADVV VSCRGSVRPV LDAAAVAGAR AAAERRAEER AGHAVGTAVQ 300
PRPLVVVDLA LHRDVDPAVG SVDGVELLDL GTIRAHAPAA ATRDVERARE 350
IVDDAVAQHA LVRAAREMDP AITRLRGRVR EVLDAEVGRL PVGPVSREDA 400
ERALHRLAAT LAHAPTEAAR EAARAGRGEE YVEALRLLFP D 441
Length:441
Mass (Da):45,703
Last modified:July 28, 2009 - v1
Checksum:i0AF8243E92066449
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001618 Genomic DNA. Translation: ACQ82250.1.
RefSeqiYP_002884012.1. NC_012669.1.

Genome annotation databases

EnsemblBacteriaiACQ82250; ACQ82250; Bcav_4009.
GeneIDi7861107.
KEGGibcv:Bcav_4009.
PATRICi21098740. VBIBeuCav91323_4061.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001618 Genomic DNA. Translation: ACQ82250.1 .
RefSeqi YP_002884012.1. NC_012669.1.

3D structure databases

ProteinModelPortali C5C5B0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 471853.Bcav_4009.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACQ82250 ; ACQ82250 ; Bcav_4009 .
GeneIDi 7861107.
KEGGi bcv:Bcav_4009.
PATRICi 21098740. VBIBeuCav91323_4061.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109649.
KOi K02492.
OMAi PYLYVHY.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci BCAV471853:GI1Z-4062-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. 2 hits.
PROSITEi PS00747. GLUTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-8 / DSM 12333 / NBRC 16432.

Entry informationi

Entry nameiHEM1_BEUC1
AccessioniPrimary (citable) accession number: C5C5B0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: September 3, 2014
This is version 42 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