Q9RTX5 (Q9RTX5_DEIRA) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Branched-chain-amino-acid aminotransferase RuleBase RU004517
EC=2.6.1.42 RuleBase RU004517

Gene names

Ordered Locus Names:

DR_1626 EMBL AAF11184.1

Organism

Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) [Reference proteome] [HAMAP] EMBL AAF11184.1

Taxonomic identifier

243230 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus › Deinococcus radiodurans

Protein attributes

Sequence length	358 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	L-isoleucine + 2-oxoglutarate = (S)-3-methyl-2-oxopentanoate + L-glutamate. RuleBase RU004517 L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate. L-valine + 2-oxoglutarate = 3-methyl-2-oxobutanoate + L-glutamate. RuleBase RU004517
Cofactor	Pyridoxal phosphate By similarity. RuleBase RU004516
Sequence similarities	Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. RuleBase RU004106

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis RuleBase RU004518
Ligand	Pyridoxal phosphate RuleBase RU004516
Molecular function	Aminotransferase RuleBase RU004517 EMBL AAF11184.1 Transferase
Technical term	3D-structure PDB 3UZB PDB 3UYY PDB 3UZO Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	branched-chain amino acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	L-isoleucine transaminase activity Inferred from electronic annotation. Source: EC L-leucine transaminase activity Inferred from electronic annotation. Source: EC L-valine transaminase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Amino acid modifications
	Modified residue	202	1	N6-(pyridoxal phosphate)lysine By similarity PIRSR PIRSR006468-1

Sequences

	Sequence		Length	Mass (Da)
	Q9RTX5 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 30DB1E8C80ABBA99	FASTA	358	39,423
	10 20 30 40 50 60 MRLTILGMTA HDSRPEQAKK LADIDWSTLG FSYIRTDLRY LAHWKDGEWD AGTLTEDNQI 70 80 90 100 110 120 HLAEGSTALH YGQQCFEGLK AYRCADGSIN LFRPDQNAAR MRMSCRRLLM PELSDEQFID 130 140 150 160 170 180 ACLQVVRANE HFLPPYGTGG SLYLRPFVIG VGDNIGVRTA PEFIFSVFCV PVGPYFKGGL 190 200 210 220 230 240 TPTNFITSDY DRAAPHGTGA AKVGGNYAAS LLPGYEAKKR DFADVIYLDP ATHTTIEEAG 250 260 270 280 290 300 AANFFAITQD GQKFVTPQSP SILPSITKYS LLWLAEHRLG LEVEEGDIRI DELGKFSEAG 310 320 330 340 350 ACGTAAVITP IGGIQHGDDF HVFYSESEPG PVTRRLYDEL VGIQYGDKEA PEGWIVKV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1." White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., Vamathevan J.J., Lam P. , McDonald L.A., Utterback T.R., Zalewski C., Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M. Science 286:1571-1577(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
[2]	"Crystal structures of complexes of the branched-chain aminotransferase from Deinococcus radiodurans with ?-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).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000513 Genomic DNA. Translation: AAF11184.1.

PIR

C75375.

RefSeq

NP_295349.1. NC_001263.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3UYY	X-ray	2.50	A/B	1-358	[»]
3UZB	X-ray	3.00	A/B/C/D	1-358	[»]
3UZO	X-ray	2.00	A/B	1-358	[»]

HSSP

HSSP built from PDB template 1I1K based on UniProtKB P00510.

ProteinModelPortal

Q9RTX5.

ModBase

Search...

Protein-protein interaction databases

STRING

243230.DR_1626.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAF11184; AAF11184; DR_1626.

GeneID

1797839.

KEGG

dra:DR_1626.

PATRIC

21630872. VBIDeiRad64572_1832.

Phylogenomic databases

HOGENOM

HOG000276704.

KO

K00826.

OMA

SPIGGVQ.

ProtClustDB

PRK13357.

Enzyme and pathway databases

BioCyc

DRAD243230:GH46-1995-MONOMER.

Family and domain databases

InterPro

IPR001544. Aminotrans_IV.
IPR018300. Aminotrans_IV_CS.
IPR005786. B_amino_transII.
[Graphical view]

PANTHER

PTHR11825. PTHR11825. 1 hit.
PTHR11825:SF2. PTHR11825:SF2. 1 hit.

Pfam

PF01063. Aminotran_4. 1 hit.
[Graphical view]

PIRSF

PIRSF006468. BCAT1. 1 hit.

SUPFAM

SSF56752. Aminotrans_IV. 1 hit.

TIGRFAMs

TIGR01123. ilvE_II. 1 hit.

PROSITE

PS00770. AA_TRANSFER_CLASS_4. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q9RTX5_DEIRA

Accession

Primary (citable) accession number: Q9RTX5

Entry history

Integrated into UniProtKB/TrEMBL:	May 1, 2000
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)