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C5C5B0

- HEM1_BEUC1

UniProt

C5C5B0 - HEM1_BEUC1

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Protein

Glutamyl-tRNA reductase

Gene

hemA

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).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 – 491NucleophileUniRule annotation
Sitei114 – 1141Important for activityUniRule annotation
Binding sitei124 – 1241SubstrateUniRule annotation
Binding sitei135 – 1351SubstrateUniRule annotation

Regions

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

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

BioCyciBCAV471853:GI1Z-4062-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTRUniRule annotation
Gene namesi
Name:hemAUniRule annotation
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 reductasePRO_1000202630Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi471853.Bcav_4009.

Structurei

3D structure databases

ProteinModelPortaliC5C5B0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 514Substrate bindingUniRule annotation
Regioni129 – 1313Substrate bindingUniRule annotation

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.UniRule annotation

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.UniRule annotation

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

« Hide

        10         20         30         40         50
MLLSVSASHR DADLADLERL SSGVGRVWAD APLVAHGLDG AGVVLLATCN
60 70 80 90 100
RFEVYLDVAD GTDPQRALAV VRDLVRTVPE SPLAAPGADD DAAGPGPDPS
110 120 130 140 150
AALRVRVGDD AARHLFGVAS GLDSIVVGER EIAGQVRRAI AAARRAGTTT
160 170 180 190 200
GALERLFAQA QRTSRAVEAG TGLAAAGRSV VGVALDLAAR SAPPWPLARV
210 220 230 240 250
VLIGTGSYAG ASLAALRARG CTDVRVHSES GRAEEFARAR EAEAVPPGEL
260 270 280 290 300
LTAIADADVV VSCRGSVRPV LDAAAVAGAR AAAERRAEER AGHAVGTAVQ
310 320 330 340 350
PRPLVVVDLA LHRDVDPAVG SVDGVELLDL GTIRAHAPAA ATRDVERARE
360 370 380 390 400
IVDDAVAQHA LVRAAREMDP AITRLRGRVR EVLDAEVGRL PVGPVSREDA
410 420 430 440
ERALHRLAAT LAHAPTEAAR EAARAGRGEE YVEALRLLFP D
Length:441
Mass (Da):45,703
Last modified:July 28, 2009 - v1
Checksum:i0AF8243E92066449
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001618 Genomic DNA. Translation: ACQ82250.1.
RefSeqiWP_015884487.1. NC_012669.1.
YP_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:
EMBLi
GenBanki
DDBJi
Links Updated
CP001618 Genomic DNA. Translation: ACQ82250.1 .
RefSeqi WP_015884487.1. NC_012669.1.
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: October 29, 2014
This is version 44 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.UniRule annotation

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