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Q63QF1

- HEM1_BURPS

UniProt

Q63QF1 - HEM1_BURPS

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Protein

Glutamyl-tRNA reductase

Gene
hemA, BPSL3072
Organism
Burkholderia pseudomallei (strain K96243)
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 sitei65 – 651Nucleophile By similarity
Sitei113 – 1131Important for activity By similarity
Binding sitei123 – 1231Substrate By similarity
Binding sitei134 – 1341Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi203 – 2086NADP By similarity

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

BioCyciBPSE272560:GJNI-3156-MONOMER.
UniPathwayiUPA00251; UER00316.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:hemA
Ordered Locus Names:BPSL3072
OrganismiBurkholderia pseudomallei (strain K96243)
Taxonomic identifieri272560 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
ProteomesiUP000000605: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 441441Glutamyl-tRNA reductaseUniRule annotationPRO_0000114001Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi272560.BPSL3072.

Structurei

3D structure databases

ProteinModelPortaliQ63QF1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni64 – 674Substrate binding By similarity
Regioni128 – 1303Substrate 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.
HOGENOMiHOG000109650.
KOiK02492.
OMAiKMLHGTM.
OrthoDBiEOG6C2WN5.

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.

Q63QF1-1 [UniParc]FASTAAdd to Basket

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MGLNDSLLDM QLLTIGINHH TAPVALRERV AFPLEQIKPA LSTFKSVFLG    50
HPAPNAPEAA ILSTCNRTEL YCATNDRAAR DAAIRWMSDY HRIPADELAP 100
HVYALPQSEA VRHAFRVASG LDSMVLGETQ ILGQMKNAVR TASEAGSLGT 150
YLNQLFQRTF AVAKEVRGTT EIGAQSVSMA AAAVRLAQRI FEQVAQQRVL 200
FIGAGEMIEL CATHFAAQGP RELVVANRTA ERGAKLAERF GGRAMPLADL 250
PARMHEFDII VSCTASTLPI IGLGAVERAV KARRHRPIFM VDLAVPRDIE 300
PEVGKLKDVF LYTVDDLGAI VREGNASRQA AVAQAEAIIE TRVQNFMQWL 350
DARSIVPVIR HMHTQADALR RAEVERARKM LARGDDPDAV LDALSQALTN 400
KLIHGPTSAL NRANGADRDS LIDLMRGFYQ HAPRSSDTSD R 441
Length:441
Mass (Da):48,258
Last modified:October 25, 2004 - v1
Checksum:i06D2A7C3C3F1D032
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX571965 Genomic DNA. Translation: CAH37083.1.
RefSeqiYP_109667.2. NC_006350.1.

Genome annotation databases

EnsemblBacteriaiCAH37083; CAH37083; BPSL3072.
GeneIDi3094369.
KEGGibps:BPSL3072.
PATRICi19266651. VBIBurPse99623_3515.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX571965 Genomic DNA. Translation: CAH37083.1 .
RefSeqi YP_109667.2. NC_006350.1.

3D structure databases

ProteinModelPortali Q63QF1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272560.BPSL3072.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAH37083 ; CAH37083 ; BPSL3072 .
GeneIDi 3094369.
KEGGi bps:BPSL3072.
PATRICi 19266651. VBIBurPse99623_3515.

Phylogenomic databases

eggNOGi COG0373.
HOGENOMi HOG000109650.
KOi K02492.
OMAi KMLHGTM.
OrthoDBi EOG6C2WN5.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci BPSE272560:GJNI-3156-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: K96243.

Entry informationi

Entry nameiHEM1_BURPS
AccessioniPrimary (citable) accession number: Q63QF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: October 25, 2004
Last modified: September 3, 2014
This is version 76 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, 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

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