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Q1AUK2

- HEM1_RUBXD

UniProt

Q1AUK2 - HEM1_RUBXD

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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129)
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
Sitei98 – 981Important for activityUniRule annotation
Binding sitei108 – 1081SubstrateUniRule annotation
Binding sitei119 – 1191SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi188 – 1936NADPUniRule 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

BioCyciRXYL266117:GH8O-2014-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:Rxyl_1979
OrganismiRubrobacter xylanophilus (strain DSM 9941 / NBRC 16129)
Taxonomic identifieri266117 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaRubrobacteridaeRubrobacteralesRubrobacterineaeRubrobacteraceaeRubrobacter
ProteomesiUP000006637: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 429429Glutamyl-tRNA reductasePRO_0000335068Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi266117.Rxyl_1979.

Structurei

3D structure databases

ProteinModelPortaliQ1AUK2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 524Substrate bindingUniRule annotation
Regioni113 – 1153Substrate 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.
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.

Q1AUK2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLIAVAGMSH RSAPVEARER VAFAPCAARS FLRRLREEDG VPEAVLLSTC
60 70 80 90 100
NRTELYVVAE AEPARDRLLG LLAEDRGVEP GSLYRDTYWH TDAEAVRHLY
110 120 130 140 150
RVSASLDSMV VGEAQILGQV RDAYRMATEE RCTGPVLNRL FHTALRVGKR
160 170 180 190 200
VRAETGIGDS SLSVPHVAAK LAGEVFGSLE GRRALVLGAG EMSELLVRHL
210 220 230 240 250
RDRGVAEIRI ANRTRERAER LAALFGGRAA DLGDLPRELA RADIVVSSTG
260 270 280 290 300
SGEWVIRGPE VAAALESREE PLFLIDIAVP RDVDPVVQSI EGAFLYDIDD
310 320 330 340 350
LQAVVERNAE DRQEAAAAAE EMIGPAVVEF MSWLSTLHVA PLIKELRDGA
360 370 380 390 400
ERIRRHEVSR ALRKMDLSPE QEEAVERMSR SIVNKLLHGP ISEIKARAGA
410 420
GDPLDSAEVR RRLLSLRGPG VELHPSREP
Length:429
Mass (Da):47,130
Last modified:May 20, 2008 - v2
Checksum:iB2D5C9F964D81ABC
GO

Sequence cautioni

The sequence ABG04926.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000386 Genomic DNA. Translation: ABG04926.1. Different initiation.
RefSeqiYP_644738.1. NC_008148.1.

Genome annotation databases

EnsemblBacteriaiABG04926; ABG04926; Rxyl_1979.
GeneIDi4115732.
KEGGirxy:Rxyl_1979.
PATRICi23370762. VBIRubXyl52678_1971.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000386 Genomic DNA. Translation: ABG04926.1 . Different initiation.
RefSeqi YP_644738.1. NC_008148.1.

3D structure databases

ProteinModelPortali Q1AUK2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 266117.Rxyl_1979.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABG04926 ; ABG04926 ; Rxyl_1979 .
GeneIDi 4115732.
KEGGi rxy:Rxyl_1979.
PATRICi 23370762. VBIRubXyl52678_1971.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci RXYL266117:GH8O-2014-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 9941 / NBRC 16129.

Entry informationi

Entry nameiHEM1_RUBXD
AccessioniPrimary (citable) accession number: Q1AUK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: October 1, 2014
This is version 70 of the entry and version 2 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