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B3QWI0

- HEM1_CHLT3

UniProt

B3QWI0 - HEM1_CHLT3

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Chloroherpeton thalassium (strain ATCC 35110 / GB-78)
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 sitei50 – 501NucleophileUniRule annotation
Sitei99 – 991Important for activityUniRule annotation
Binding sitei109 – 1091SubstrateUniRule annotation
Binding sitei120 – 1201SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi189 – 1946NADPUniRule annotation

GO - Molecular functioni

  1. glutamyl-tRNA reductase activity Source: UniProtKB-HAMAP
  2. NADP binding Source: InterPro

GO - Biological processi

  1. chlorophyll biosynthetic process Source: UniProtKB-HAMAP
  2. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Chlorophyll biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciCTHA517418:GHTO-2331-MONOMER.
UniPathwayiUPA00251; UER00316.
UPA00668.

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:Ctha_2289
OrganismiChloroherpeton thalassium (strain ATCC 35110 / GB-78)
Taxonomic identifieri517418 [NCBI]
Taxonomic lineageiBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChloroherpeton
ProteomesiUP000001208: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 437437Glutamyl-tRNA reductasePRO_1000093125Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi517418.Ctha_2289.

Structurei

3D structure databases

ProteinModelPortaliB3QWI0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni114 – 1163Substrate 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.
HOGENOMiHOG000109651.
KOiK02492.
OMAiHVEILPP.
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.

B3QWI0-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MNLIAVGVNH NTAPIELREK ISLTDSMARS LLTELIDSKL ASEALVLSTC
60 70 80 90 100
NRTELYVVPA MPEVTANYLK DYLIAHKGVR KEVTRDHFFN YFACGAARHF
110 120 130 140 150
YNVACAIDSL ILGEVQIIGQ VKTAYNRAVE MKTVGPILNK MCHTGFGLAN
160 170 180 190 200
RVRSKTKLTA GAVSVSYAAV ELTQKIYSDV STKNILLVGA GDTAKLAAKN
210 220 230 240 250
LLDKRVRDFY ITNRTYEKAE LLAQELGTGK ILPLEEMTER LHEFDIVVTA
260 270 280 290 300
VGGNDHIIKK EHVAAAMQKR HRDPILILDL GLPRNVAPEV GQVNNVFLKD
310 320 330 340 350
IDDLKMIIDS NLEKRRAEIP KVKHFIQKEL IEYARWYFSL EVKPTIVDLQ
360 370 380 390 400
EKFFEIKALE LARIKNKVSA EEYERMEQLS DRIIKKLLHF PITTLKQQTA
410 420 430
DTTDPVSFIR NIFDLKEQEE EFPGLTFPIN LKEQNNN
Length:437
Mass (Da):49,497
Last modified:September 2, 2008 - v1
Checksum:i20C5230775AC0FBB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001100 Genomic DNA. Translation: ACF14740.1.
RefSeqiWP_012500823.1. NC_011026.1.
YP_001997187.1. NC_011026.1.

Genome annotation databases

EnsemblBacteriaiACF14740; ACF14740; Ctha_2289.
GeneIDi6423371.
KEGGicts:Ctha_2289.
PATRICi21433767. VBIChlTha99257_2675.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001100 Genomic DNA. Translation: ACF14740.1 .
RefSeqi WP_012500823.1. NC_011026.1.
YP_001997187.1. NC_011026.1.

3D structure databases

ProteinModelPortali B3QWI0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 517418.Ctha_2289.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACF14740 ; ACF14740 ; Ctha_2289 .
GeneIDi 6423371.
KEGGi cts:Ctha_2289.
PATRICi 21433767. VBIChlTha99257_2675.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
UPA00668 .
BioCyci CTHA517418:GHTO-2331-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 sequence of Chloroherpeton thalassium ATCC 35110."
    US DOE Joint Genome Institute
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F.
    , Overmann J., Bryant D.A., Richardson P.
    Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35110 / GB-78.

Entry informationi

Entry nameiHEM1_CHLT3
AccessioniPrimary (citable) accession number: B3QWI0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 2, 2008
Last modified: October 29, 2014
This is version 49 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