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Protein

L-glutamine:2-deoxy-scyllo-inosose aminotransferase

Gene

btrR

Organism
Bacillus circulans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the PLP-dependent transamination of 2-deoxy-scyllo-inosose (2-DOI) to form 2-deoxy-scyllo-inosamine (2-DOIA) using L-glutamine as the amino donor. Also catalyzes the transamination of 3-amino-2,3-dideoxy-scyllo-inosose (keto-2-DOIA) into 2-deoxystreptamine (2-DOS).3 Publications

Catalytic activityi

L-glutamine + 2-deoxy-scyllo-inosose = 2-oxoglutaramate + 2-deoxy-scyllo-inosamine.3 Publications
L-glutamine + 3-amino-2,3-dideoxy-scyllo-inosose = 2-oxoglutaramate + 2-deoxystreptamine.3 Publications

Cofactori

Pathwayi: 2-deoxystreptamine biosynthesis

This protein is involved in step 2 and 4 of the subpathway that synthesizes 2-deoxystreptamine from D-glucose 6-phosphate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. 2-deoxy-scyllo-inosose synthase (btrC)
  2. L-glutamine:2-deoxy-scyllo-inosose aminotransferase (btrR)
  3. no protein annotated in this organism
  4. L-glutamine:2-deoxy-scyllo-inosose aminotransferase (btrR)
This subpathway is part of the pathway 2-deoxystreptamine biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 2-deoxystreptamine from D-glucose 6-phosphate, the pathway 2-deoxystreptamine biosynthesis and in Metabolic intermediate biosynthesis.

Pathwayi: butirosin biosynthesis

This protein is involved in the pathway butirosin biosynthesis, which is part of Antibiotic biosynthesis.
View all proteins of this organism that are known to be involved in the pathway butirosin biosynthesis and in Antibiotic biosynthesis.

GO - Molecular functioni

GO - Biological processi

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Antibiotic biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17229.
BRENDAi2.6.1.100. 649.
2.6.1.101. 649.
UniPathwayiUPA00907; UER00922.
UPA00907; UER00924.
UPA00964.

Names & Taxonomyi

Protein namesi
Recommended name:
L-glutamine:2-deoxy-scyllo-inosose aminotransferase (EC:2.6.1.1003 Publications)
Short name:
L-glutamine:DOI aminotransferase
Alternative name(s):
L-glutamine:3-amino-2,3-dideoxy-scyllo-inosose aminotransferase (EC:2.6.1.1013 Publications)
Short name:
L-glutamine:amino-DOI aminotransferase
Gene namesi
Name:btrR
Synonyms:btrS
OrganismiBacillus circulans
Taxonomic identifieri1397 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 418418L-glutamine:2-deoxy-scyllo-inosose aminotransferasePRO_0000233016Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei192 – 1921N6-(pyridoxal phosphate)lysineBy similarity

Structurei

Secondary structure

1
418
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 2813Combined sources
Helixi43 – 5513Combined sources
Beta strandi58 – 647Combined sources
Helixi66 – 7611Combined sources
Beta strandi84 – 918Combined sources
Helixi94 – 1018Combined sources
Beta strandi105 – 1095Combined sources
Turni113 – 1153Combined sources
Helixi120 – 1234Combined sources
Helixi124 – 1263Combined sources
Beta strandi131 – 1344Combined sources
Helixi146 – 15510Combined sources
Beta strandi159 – 1635Combined sources
Beta strandi179 – 1879Combined sources
Beta strandi192 – 1943Combined sources
Beta strandi196 – 1983Combined sources
Beta strandi200 – 2056Combined sources
Helixi207 – 21711Combined sources
Beta strandi221 – 2233Combined sources
Helixi227 – 2293Combined sources
Beta strandi235 – 2395Combined sources
Helixi252 – 26211Combined sources
Helixi265 – 28319Combined sources
Beta strandi289 – 2913Combined sources
Beta strandi298 – 3003Combined sources
Beta strandi304 – 3107Combined sources
Helixi312 – 3143Combined sources
Turni315 – 3173Combined sources
Helixi320 – 33112Combined sources
Turni335 – 3373Combined sources
Helixi345 – 3473Combined sources
Helixi353 – 3553Combined sources
Helixi361 – 3644Combined sources
Helixi367 – 3715Combined sources
Helixi376 – 3849Combined sources
Beta strandi385 – 3895Combined sources
Helixi390 – 3945Combined sources
Helixi397 – 41216Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C7TX-ray2.10A1-418[»]
2C81X-ray1.70A1-418[»]
ProteinModelPortaliQ8G8Y2.
SMRiQ8G8Y2. Positions 6-416.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8G8Y2.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

KOiK13547.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR000653. DegT/StrS_aminotransferase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF01041. DegT_DnrJ_EryC1. 1 hit.
[Graphical view]
PIRSFiPIRSF000390. PLP_StrS. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8G8Y2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTIPFDHWPE WPQHSDRTRR KIEEVFQSNR WAISGYWTGE ESMERKFAKA
60 70 80 90 100
FADFNGVPYC VPTTSGSTAL MLALEALGIG EGDEVIVPSL TWIATATAVL
110 120 130 140 150
NVNALPVFVD VEADTYCIDP QLIKSAITDK TKAIIPVHLF GSMANMDEIN
160 170 180 190 200
EIAQEHNLFV IEDCAQSHGS VWNNQRAGTI GDIGAFSCQQ GKVLTAGEGG
210 220 230 240 250
IIVTKNPRLF ELIQQLRADS RVYCDDSSEL MHGDMQLVKK GDIQGSNYCL
260 270 280 290 300
SEFQSAILLD QLQELDDKNA IREKNAMFLN DALSKIDGIK VMKRPPQVSR
310 320 330 340 350
QTYYGYVFRF DPVKFGGLNA DQFCEILREK LNMGTFYLHP PYLPVHKNPL
360 370 380 390 400
FCPWTKNRYL KSVRKTEAYW RGLHYPVSER ASGQSIVIHH AILLAEPSHL
410
SLLVDAVAEL ARKFCVTH
Length:418
Mass (Da):47,032
Last modified:March 1, 2003 - v1
Checksum:i41E7C1102D36D289
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ494863 Genomic DNA. Translation: CAD41947.1.
AB097196 Genomic DNA. Translation: BAE07061.1.

Genome annotation databases

KEGGiag:BAE07061.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ494863 Genomic DNA. Translation: CAD41947.1.
AB097196 Genomic DNA. Translation: BAE07061.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C7TX-ray2.10A1-418[»]
2C81X-ray1.70A1-418[»]
ProteinModelPortaliQ8G8Y2.
SMRiQ8G8Y2. Positions 6-416.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:BAE07061.

Phylogenomic databases

KOiK13547.

Enzyme and pathway databases

UniPathwayiUPA00907; UER00922.
UPA00907; UER00924.
UPA00964.
BioCyciMetaCyc:MONOMER-17229.
BRENDAi2.6.1.100. 649.
2.6.1.101. 649.

Miscellaneous databases

EvolutionaryTraceiQ8G8Y2.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR000653. DegT/StrS_aminotransferase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF01041. DegT_DnrJ_EryC1. 1 hit.
[Graphical view]
PIRSFiPIRSF000390. PLP_StrS. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Biosynthesis of aminoglycoside antibiotics: cloning, expression and characterisation of an aminotransferase involved in the pathway to 2-deoxystreptamine."
    Huang F., Li Y., Yu J., Spencer J.B.
    Chem. Commun. (Camb.) 23:2860-2861(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY.
  2. "Identification of L-glutamine: 2-deoxy-scyllo-inosose aminotransferase required for the biosynthesis of butirosin in Bacillus circulans."
    Tamegai H., Nango E., Kuwahara M., Yamamoto H., Ota Y., Kuriki H., Eguchi T., Kakinuma K.
    J. Antibiot. 55:707-714(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY.
    Strain: SANK 72073.
  3. "Stereochemical recognition of doubly functional aminotransferase in 2-deoxystreptamine biosynthesis."
    Yokoyama K., Kudo F., Kuwahara M., Inomata K., Tamegai H., Eguchi T., Kakinuma K.
    J. Am. Chem. Soc. 127:5869-5874(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, REACTION STEREOCHEMISTRY.
    Strain: SANK 72073.

Entry informationi

Entry nameiGLDSA_BACCI
AccessioniPrimary (citable) accession number: Q8G8Y2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: March 1, 2003
Last modified: April 13, 2016
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.