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Q2SUG3

- HEM1_BURTA

UniProt

Q2SUG3 - HEM1_BURTA

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Protein

Glutamyl-tRNA reductase

Gene
hemA, BTH_I2929
Organism
Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
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 sitei56 – 561Nucleophile By similarity
Sitei104 – 1041Important for activity By similarity
Binding sitei114 – 1141Substrate By similarity
Binding sitei125 – 1251Substrate By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi194 – 1996NADP 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

BioCyciBTHA271848:GJMY-2930-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:BTH_I2929
OrganismiBurkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
Taxonomic identifieri271848 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
ProteomesiUP000001930: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432Glutamyl-tRNA reductaseUniRule annotationPRO_0000335019Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi271848.BTH_I2929.

Structurei

3D structure databases

ProteinModelPortaliQ2SUG3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni55 – 584Substrate binding By similarity
Regioni119 – 1213Substrate 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.
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.

Q2SUG3-1 [UniParc]FASTAAdd to Basket

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MQLLTIGINH HTAPVALRER VAFPLEQIKP ALSTFKSVFL GHPAPNAPEA    50
AILSTCNRTE LYCATDDRAA RDAAIRWMSD YHRIPADELA PHVYALPQSE 100
AVRHAFRVAS GLDSMVLGET QILGQMKNAV RTASEAGSLG TYLNQLFQRT 150
FAVAKEVRGT TEIGAQSVSM AAAAVRLAQR IFEQVAQQRV LFIGAGEMIE 200
LCATHFAAQG PRELVVANRT AERGAKLAER FGGRAMPLSD LPARMHEFDI 250
IVSCTASTLP IIGLGAVERA VKARRHRPIF MVDLAVPRDI EPEVGKLKDV 300
FLYTVDDLGA IVREGNASRQ AAVAQAEAII ETRVQNFMQW LDARSIVPVI 350
RHMHTQADAL RRAELERARK MLARGDDPAA VLDALSQALT NKLIHGPTSA 400
LNRANGADRD SLIDLMRGFY QHAPRSSDTS DH 432
Length:432
Mass (Da):47,267
Last modified:May 20, 2008 - v2
Checksum:i7FF007D754BF1F56
GO

Sequence cautioni

The sequence ABC36831.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000086 Genomic DNA. Translation: ABC36831.1. Different initiation.
RefSeqiYP_443436.2. NC_007651.1.

Genome annotation databases

EnsemblBacteriaiABC36831; ABC36831; BTH_I2929.
GeneIDi3848347.
KEGGibte:BTH_I2929.
PATRICi19309080. VBIBurTha36512_5813.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000086 Genomic DNA. Translation: ABC36831.1 . Different initiation.
RefSeqi YP_443436.2. NC_007651.1.

3D structure databases

ProteinModelPortali Q2SUG3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 271848.BTH_I2929.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABC36831 ; ABC36831 ; BTH_I2929 .
GeneIDi 3848347.
KEGGi bte:BTH_I2929.
PATRICi 19309080. VBIBurTha36512_5813.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00316 .
BioCyci BTHA271848:GJMY-2930-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. "Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies."
    Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., DeShazer D.
    BMC Genomics 6:174-174(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301.

Entry informationi

Entry nameiHEM1_BURTA
AccessioniPrimary (citable) accession number: Q2SUG3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: September 3, 2014
This is version 71 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 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

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