NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.

Comments

CATALYTIC ACTIVITY: (R)-2,3-dihydroxy-3-methylbutanoate + NADP⁺ = (S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH.
CATALYTIC ACTIVITY: (2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP⁺ = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH.
PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4 .
PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4 .
SIMILARITY: Belongs to the ketol-acid reductoisomerase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CP000512; ABM33674.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_971448.1; -.

3D structure databases

SMR

A1TRT6; 1-327.

ModBase

A1TRT6.

Ontologies

GO:0004455;	Molecular function: ketol-acid reductoisomerase activity (inferred from electronic annotation from HAMAP).
GO:0009097;	Biological process: isoleucine biosynthetic process (inferred from electronic annotation from HAMAP).
GO:0009099;	Biological process: valine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00435; -; 1.
PBIL [Tree]

InterPro

IPR013023; AcH_isomrdctse.
IPR000506; AcH_isomrdctse_C.
IPR013116; IlvN.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

PANTHER

PTHR21371; AcH_isomrdctse; 1.

Pfam

PF01450; IlvC; 1.
PF07991; IlvN; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00465; ilvC; 1.

BLOCKS

A1TRT6.

Genome annotation databases

GeneID

4665217; -.

GenomeReviews

CP000512_GR; Aave_3110.

KEGG

aav:Aave_3110; -.

NMPDR

fig|397945.5.peg.2650; -.

CMR

A1TRT6; Aave_3110.

Other

ProtoNet

A1TRT6.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Complete proteome; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 338`	`338`	`Ketol-acid reductoisomerase.`	`PRO_1000050470`
`ACT_SITE`	`107 107`		`Potential.`

Sequence information

Length: 338 AA [This is the length of the unprocessed precursor]

Molecular weight: 36861 Da [This is the MW of the unprocessed precursor]

CRC64: 60BE893F2FDFE59E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKVFYDKDCD LSLIKGKTVA IIGYGSQGHA HAQNLNDSGV KVVVGLRKGG ASWDKVGKAG 

        70         80         90        100        110        120 
LTVLEVNEAV KSADVVMILL PDEQIAEVYK NNVEPNIKQG ASLAFAHGFN VHYNQVVPRA 

       130        140        150        160        170        180 
DLDVWMVAPK APGHTVRSTY SQGGGVPHLV AVHQDKSGKA RDLALSYAMA NGGGKAGIIE 

       190        200        210        220        230        240 
TNFKEETETD LFGEQAVLCG GAVELIKMGF ETLVEAGYAP EMAYFECLHE LKLIVDLIYE 

       250        260        270        280        290        300 
GGIANMNYSI SNNAEFGEYV TGPEVINEQS RAAMRNALKR IQNGDYAKMF IQEGRLNYPS 

       310        320        330 
MTARRRNTAD HKIEVVGAQL RAMMPWIAKN KLVDQSRN

A1TRT6 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools