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Q7UKZ2

- HEM1_RHOBA

UniProt

Q7UKZ2 - HEM1_RHOBA

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Rhodopirellula baltica (strain SH1)
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
Sitei100 – 1001Important for activityUniRule annotation
Binding sitei110 – 1101SubstrateUniRule annotation
Binding sitei121 – 1211SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi191 – 1966NADPUniRule 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

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:RB9848
OrganismiRhodopirellula baltica (strain SH1)
Taxonomic identifieri243090 [NCBI]
Taxonomic lineageiBacteriaPlanctomycetesPlanctomycetiaPlanctomycetalesPlanctomycetaceaeRhodopirellula
ProteomesiUP000001025: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 426426Glutamyl-tRNA reductasePRO_0000114062Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi243090.RB9848.

Structurei

3D structure databases

ProteinModelPortaliQ7UKZ2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni115 – 1173Substrate 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.
InParanoidiQ7UKZ2.
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.

Q7UKZ2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTLKMIGCSH HDAAVEIREQ LSFTENEINR TFELFGQRFA DAELVLLSTC
60 70 80 90 100
NRVELYGAGS NPASLQSDDL IDLVADCLNQ SRDFVANHMI IREGREAVEH
110 120 130 140 150
LFLVAASLDS MVVGEAQILS QVKQSYDLAN DADRTGPITH GVFQAANRTA
160 170 180 190 200
KRVQTETSIH RRRLSVPSVA IGEVVPEVFN RLQGKRVVLC GAGEMAEETL
210 220 230 240 250
RYLKNGGANN LCVVNRSLDR AQKLADEFGA DAESMDSLHD QIVQADLLIG
260 270 280 290 300
TTSAEEPIVD ASTFAALNAK RGGRIMLVLD LAVPRDFDPV IGDEPGVYLY
310 320 330 340 350
QIDDLQAACN RNRREREKQW PKAKKIIDEE VDGFFQSLQQ RATGPVIRRL
360 370 380 390 400
RERADKVKAE ELQRLFGKLN GSTDTAMQKE IEKSFDRLTN KLLHPPMASL
410 420
RDDAADGHSR GLLEALRHLF NLGEDS
Length:426
Mass (Da):47,322
Last modified:October 1, 2003 - v1
Checksum:i5326218BA63D1947
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX294150 Genomic DNA. Translation: CAD76488.1.
RefSeqiNP_869102.1. NC_005027.1.

Genome annotation databases

EnsemblBacteriaiCAD76488; CAD76488; RB9848.
GeneIDi1796251.
KEGGirba:RB9848.
PATRICi23250957. VBIRhoBal59814_4739.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX294150 Genomic DNA. Translation: CAD76488.1 .
RefSeqi NP_869102.1. NC_005027.1.

3D structure databases

ProteinModelPortali Q7UKZ2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243090.RB9848.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAD76488 ; CAD76488 ; RB9848 .
GeneIDi 1796251.
KEGGi rba:RB9848.
PATRICi 23250957. VBIRhoBal59814_4739.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109651.
InParanoidi Q7UKZ2.
KOi K02492.
OMAi LAHKLTN.
OrthoDBi EOG6MWNBM.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SH1.

Entry informationi

Entry nameiHEM1_RHOBA
AccessioniPrimary (citable) accession number: Q7UKZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: October 29, 2014
This is version 86 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