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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)DescriptionActionsGraphical viewLength
ChainiPRO_00002330161 – 418L-glutamine:2-deoxy-scyllo-inosose aminotransferaseAdd BLAST418

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei192N6-(pyridoxal phosphate)lysineBy similarity1

Structurei

Secondary structure

1418
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi16 – 28Combined sources13
Helixi43 – 55Combined sources13
Beta strandi58 – 64Combined sources7
Helixi66 – 76Combined sources11
Beta strandi84 – 91Combined sources8
Helixi94 – 101Combined sources8
Beta strandi105 – 109Combined sources5
Turni113 – 115Combined sources3
Helixi120 – 123Combined sources4
Helixi124 – 126Combined sources3
Beta strandi131 – 134Combined sources4
Helixi146 – 155Combined sources10
Beta strandi159 – 163Combined sources5
Beta strandi179 – 187Combined sources9
Beta strandi192 – 194Combined sources3
Beta strandi196 – 198Combined sources3
Beta strandi200 – 205Combined sources6
Helixi207 – 217Combined sources11
Beta strandi221 – 223Combined sources3
Helixi227 – 229Combined sources3
Beta strandi235 – 239Combined sources5
Helixi252 – 262Combined sources11
Helixi265 – 283Combined sources19
Beta strandi289 – 291Combined sources3
Beta strandi298 – 300Combined sources3
Beta strandi304 – 310Combined sources7
Helixi312 – 314Combined sources3
Turni315 – 317Combined sources3
Helixi320 – 331Combined sources12
Turni335 – 337Combined sources3
Helixi345 – 347Combined sources3
Helixi353 – 355Combined sources3
Helixi361 – 364Combined sources4
Helixi367 – 371Combined sources5
Helixi376 – 384Combined sources9
Beta strandi385 – 389Combined sources5
Helixi390 – 394Combined sources5
Helixi397 – 412Combined sources16

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ8G8Y2.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

KOiK13547.

Family and domain databases

CDDicd00616. AHBA_syn. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2C7TX-ray2.10A1-418[»]
2C81X-ray1.70A1-418[»]
ProteinModelPortaliQ8G8Y2.
SMRiQ8G8Y2.
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

CDDicd00616. AHBA_syn. 1 hit.
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...

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: November 2, 2016
This is version 59 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.