SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

B3QWI0

- HEM1_CHLT3

UniProt

B3QWI0 - HEM1_CHLT3

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glutamyl-tRNA reductase

Gene
hemA, Ctha_2289
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) 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. 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 reductase (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:hemA
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 reductaseUniRule annotationPRO_1000093125Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi517418.Ctha_2289.

Structurei

3D structure databases

ProteinModelPortaliB3QWI0.

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.
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

« Hide

MNLIAVGVNH NTAPIELREK ISLTDSMARS LLTELIDSKL ASEALVLSTC    50
NRTELYVVPA MPEVTANYLK DYLIAHKGVR KEVTRDHFFN YFACGAARHF 100
YNVACAIDSL ILGEVQIIGQ VKTAYNRAVE MKTVGPILNK MCHTGFGLAN 150
RVRSKTKLTA GAVSVSYAAV ELTQKIYSDV STKNILLVGA GDTAKLAAKN 200
LLDKRVRDFY ITNRTYEKAE LLAQELGTGK ILPLEEMTER LHEFDIVVTA 250
VGGNDHIIKK EHVAAAMQKR HRDPILILDL GLPRNVAPEV GQVNNVFLKD 300
IDDLKMIIDS NLEKRRAEIP KVKHFIQKEL IEYARWYFSL EVKPTIVDLQ 350
EKFFEIKALE LARIKNKVSA EEYERMEQLS DRIIKKLLHF PITTLKQQTA 400
DTTDPVSFIR NIFDLKEQEE EFPGLTFPIN LKEQNNN 437
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.
RefSeqiYP_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 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: September 3, 2014
This is version 47 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

Similar proteinsi