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Protein

Branched-chain-amino-acid aminotransferase

Gene

DR_1626

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-isoleucine + 2-oxoglutarate = (S)-3-methyl-2-oxopentanoate + L-glutamate.UniRule annotation
L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate.UniRule annotation
L-valine + 2-oxoglutarate = 3-methyl-2-oxobutanoate + L-glutamate.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei100 – 1001N6-(pyridoxal phosphate)lysineCombined sources
Binding sitei202 – 2021N6-(pyridoxal phosphate)lysineCombined sources
Binding sitei207 – 2071N6-(pyridoxal phosphate)lysineCombined sources
Binding sitei304 – 3041N6-(pyridoxal phosphate)lysineCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

AminotransferaseUniRule annotationImported, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesisUniRule annotation

Keywords - Ligandi

Pyridoxal phosphateUniRule annotation

Enzyme and pathway databases

BioCyciDRAD243230:GH46-1656-MONOMER.
BRENDAi2.6.1.42. 1856.

Names & Taxonomyi

Protein namesi
Recommended name:
Branched-chain-amino-acid aminotransferaseUniRule annotation (EC:2.6.1.42UniRule annotation)
Gene namesi
Ordered Locus Names:DR_1626Imported
OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)Imported
Taxonomic identifieri243230 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
ProteomesiUP000002524 Componenti: Chromosome I

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei202 – 2021N6-(pyridoxal phosphate)lysineUniRule annotation

Interactioni

Protein-protein interaction databases

STRINGi243230.DR_1626.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UYYX-ray2.50A/B1-358[»]
3UZBX-ray3.00A/B/C/D1-358[»]
3UZOX-ray2.00A/B1-358[»]
ProteinModelPortaliQ9RTX5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni238 – 2425N6-(pyridoxal phosphate)lysine bindingCombined sources
Regioni265 – 2673N6-(pyridoxal phosphate)lysine bindingCombined sources

Sequence similaritiesi

Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000276704.
InParanoidiQ9RTX5.
KOiK00826.
OMAiSPVLHYG.
OrthoDBiEOG67MF3R.

Family and domain databases

InterProiIPR001544. Aminotrans_IV.
IPR018300. Aminotrans_IV_CS.
IPR005786. B_amino_transII.
[Graphical view]
PANTHERiPTHR11825. PTHR11825. 1 hit.
PfamiPF01063. Aminotran_4. 1 hit.
[Graphical view]
PIRSFiPIRSF006468. BCAT1. 1 hit.
SUPFAMiSSF56752. SSF56752. 1 hit.
TIGRFAMsiTIGR01123. ilvE_II. 1 hit.
PROSITEiPS00770. AA_TRANSFER_CLASS_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9RTX5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLTILGMTA HDSRPEQAKK LADIDWSTLG FSYIRTDLRY LAHWKDGEWD
60 70 80 90 100
AGTLTEDNQI HLAEGSTALH YGQQCFEGLK AYRCADGSIN LFRPDQNAAR
110 120 130 140 150
MRMSCRRLLM PELSDEQFID ACLQVVRANE HFLPPYGTGG SLYLRPFVIG
160 170 180 190 200
VGDNIGVRTA PEFIFSVFCV PVGPYFKGGL TPTNFITSDY DRAAPHGTGA
210 220 230 240 250
AKVGGNYAAS LLPGYEAKKR DFADVIYLDP ATHTTIEEAG AANFFAITQD
260 270 280 290 300
GQKFVTPQSP SILPSITKYS LLWLAEHRLG LEVEEGDIRI DELGKFSEAG
310 320 330 340 350
ACGTAAVITP IGGIQHGDDF HVFYSESEPG PVTRRLYDEL VGIQYGDKEA

PEGWIVKV
Length:358
Mass (Da):39,423
Last modified:May 1, 2000 - v1
Checksum:i30DB1E8C80ABBA99
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF11184.1.
PIRiC75375.
RefSeqiNP_295349.1. NC_001263.1.
WP_010888263.1. NC_001263.1.

Genome annotation databases

EnsemblBacteriaiAAF11184; AAF11184; DR_1626.
GeneIDi1797839.
KEGGidra:DR_1626.
PATRICi21630872. VBIDeiRad64572_1832.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF11184.1.
PIRiC75375.
RefSeqiNP_295349.1. NC_001263.1.
WP_010888263.1. NC_001263.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UYYX-ray2.50A/B1-358[»]
3UZBX-ray3.00A/B/C/D1-358[»]
3UZOX-ray2.00A/B1-358[»]
ProteinModelPortaliQ9RTX5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243230.DR_1626.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF11184; AAF11184; DR_1626.
GeneIDi1797839.
KEGGidra:DR_1626.
PATRICi21630872. VBIDeiRad64572_1832.

Phylogenomic databases

HOGENOMiHOG000276704.
InParanoidiQ9RTX5.
KOiK00826.
OMAiSPVLHYG.
OrthoDBiEOG67MF3R.

Enzyme and pathway databases

BioCyciDRAD243230:GH46-1656-MONOMER.
BRENDAi2.6.1.42. 1856.

Family and domain databases

InterProiIPR001544. Aminotrans_IV.
IPR018300. Aminotrans_IV_CS.
IPR005786. B_amino_transII.
[Graphical view]
PANTHERiPTHR11825. PTHR11825. 1 hit.
PfamiPF01063. Aminotran_4. 1 hit.
[Graphical view]
PIRSFiPIRSF006468. BCAT1. 1 hit.
SUPFAMiSSF56752. SSF56752. 1 hit.
TIGRFAMsiTIGR01123. ilvE_II. 1 hit.
PROSITEiPS00770. AA_TRANSFER_CLASS_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422Imported.
  2. "Crystal structures of complexes of the branched-chain aminotransferase from Deinococcus radiodurans with alpha-ketoisocaproate and L-glutamate suggest the radiation resistance of this enzyme for catalysis."
    Chen C.D., Lin C.H., Chuankhayan P., Huang Y.C., Hsieh Y.C., Huang T.F., Guan H.H., Liu M.Y., Chang W.C., Chen C.J.
    J. Bacteriol. 194:6206-6216(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH N6-(PYRIDOXAL PHOSPHATE)LYSINE.

Entry informationi

Entry nameiQ9RTX5_DEIRA
AccessioniPrimary (citable) accession number: Q9RTX5
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 2000
Last sequence update: May 1, 2000
Last modified: June 24, 2015
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

External Data

Dasty 3

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 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.