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:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.

TIGR00465; ilvC; 1.

Genome annotation databases

GeneID

881483; -.

GenomeReviews

AE004091_GR; PA4694.

KEGG

pae:PA4694; -.

Phylogenomic databases

HOGENOM

Q9HVA2; -.

Genome annotation databases

CMR

Q9HVA2; PA4694.

Other

UniRef

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

Keywords

3D-structure; 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_0000151342`
`ACT_SITE`	`107 107`		`Potential.`
`HELIX`	`6 8`	`3`
`HELIX`	`11 15`	`5`
`STRAND`	`19 22`	`4`
`HELIX`	`26 37`	`12`
`STRAND`	`42 45`	`4`
`HELIX`	`51 58`	`8`
`STRAND`	`62 64`	`3`
`HELIX`	`66 71`	`6`
`STRAND`	`74 78`	`5`
`HELIX`	`82 92`	`11`
`HELIX`	`94 96`	`3`
`STRAND`	`102 106`	`5`
`HELIX`	`109 112`	`4`
`STRAND`	`123 131`	`9`
`HELIX`	`134 141`	`8`
`STRAND`	`148 154`	`7`
`STRAND`	`156 158`	`3`
`HELIX`	`160 170`	`11`
`HELIX`	`173 176`	`4`
`STRAND`	`178 180`	`3`
`HELIX`	`183 196`	`14`
`TURN`	`197 199`	`3`
`HELIX`	`200 215`	`16`
`HELIX`	`220 227`	`8`
`TURN`	`228 230`	`3`
`HELIX`	`231 249`	`19`
`HELIX`	`252 265`	`14`
`HELIX`	`268 282`	`15`
`HELIX`	`285 295`	`11`
`HELIX`	`299 310`	`12`
`HELIX`	`312 321`	`10`

Sequence information

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

Molecular weight: 36425 Da [This is the MW of the unprocessed precursor]

CRC64: 93CF5F7DA9F61B0A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRVFYDKDCD LSIIQGKKVA IIGYGSQGHA HACNLKDSGV DVTVGLRSGS ATVAKAEAHG 

        70         80         90        100        110        120 
LKVADVKTAV AAADVVMILT PDEFQGRLYK EEIEPNLKKG ATLAFAHGFS IHYNQVVPRA 

       130        140        150        160        170        180 
DLDVIMIAPK APGHTVRSEF VKGGGIPDLI AIYQDASGNA KNVALSYACG VGGGRTGIIE 

       190        200        210        220        230        240 
TTFKDETETD LFGEQAVLCG GCVELVKAGF ETLVEAGYAP EMAYFECLHE LKLIVDLMYE 

       250        260        270        280        290        300 
GGIANMNYSI SNNAEYGEYV TGPEVINAES RAAMRNALKR IQDGEYAKMF ITEGAANYPS 

       310        320        330 
MTAYRRNNAA HPIEQIGEKL RAMMPWIAAN KIVDKSKN

Q9HVA2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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