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Protein

Probable ketol-acid reductoisomerase, mitochondrial

Gene

ilv5

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalytic activityi

(2R)-2,3-dihydroxy-3-methylbutanoate + NADP+ = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH.
(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP+ = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH.

Cofactori

Mg2+By similarityNote: Binds 2 magnesium ions per subunit.By similarity

Pathwayi: L-isoleucine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase, mitochondrial (ilv1), Probable acetolactate synthase small subunit (SPBC14C8.04)
  2. Probable ketol-acid reductoisomerase, mitochondrial (ilv5)
  3. Putative dihydroxy-acid dehydratase, mitochondrial (SPAC17G8.06c)
  4. no protein annotated in this organism
This subpathway is part of the pathway L-isoleucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-isoleucine from 2-oxobutanoate, the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-valine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-valine from pyruvate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase, mitochondrial (ilv1), Probable acetolactate synthase small subunit (SPBC14C8.04)
  2. Probable ketol-acid reductoisomerase, mitochondrial (ilv5)
  3. Putative dihydroxy-acid dehydratase, mitochondrial (SPAC17G8.06c)
  4. no protein annotated in this organism
This subpathway is part of the pathway L-valine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-valine from pyruvate, the pathway L-valine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei178Sequence analysis1
Metal bindingi262Magnesium 1PROSITE-ProRule annotation1
Metal bindingi262Magnesium 2PROSITE-ProRule annotation1
Metal bindingi266Magnesium 1PROSITE-ProRule annotation1
Metal bindingi298Magnesium 2PROSITE-ProRule annotation1
Metal bindingi302Magnesium 2PROSITE-ProRule annotation1
Binding sitei324SubstratePROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi91 – 100NADPSequence analysis10
Nucleotide bindingi115 – 120NADPBy similarity6
Nucleotide bindingi153 – 157NADPBy similarity5

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processAmino-acid biosynthesis, Branched-chain amino acid biosynthesis
LigandMagnesium, Metal-binding, NADP

Enzyme and pathway databases

UniPathwayiUPA00047; UER00056
UPA00049; UER00060

Names & Taxonomyi

Protein namesi
Recommended name:
Probable ketol-acid reductoisomerase, mitochondrial (EC:1.1.1.86)
Alternative name(s):
Acetohydroxy-acid reductoisomerase
Alpha-keto-beta-hydroxylacyl reductoisomerase
Gene namesi
Name:ilv5
ORF Names:SPBC56F2.12
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC56F2.12
PomBaseiSPBC56F2.12 ilv5

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000015633? – 404Probable ketol-acid reductoisomerase, mitochondrial
Transit peptidei1 – ?MitochondrionSequence analysis

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei261Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP78827
PaxDbiP78827
PRIDEiP78827

PTM databases

iPTMnetiP78827

Interactioni

Protein-protein interaction databases

STRINGi4896.SPBC56F2.12.1

Structurei

3D structure databases

ProteinModelPortaliP78827
SMRiP78827
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini63 – 253KARI N-terminal RossmannPROSITE-ProRule annotationAdd BLAST191
Domaini254 – 401KARI C-terminal knottedPROSITE-ProRule annotationAdd BLAST148

Sequence similaritiesi

Belongs to the ketol-acid reductoisomerase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000016231
InParanoidiP78827
KOiK00053
OMAiRAMFSWL
OrthoDBiEOG092C2OSA
PhylomeDBiP78827

Family and domain databases

Gene3Di1.10.1040.10, 3 hits
InterProiView protein in InterPro
IPR008927 6-PGluconate_DH-like_C_sf
IPR013328 6PGD_dom2
IPR013023 KARI
IPR000506 KARI_C
IPR013116 KARI_N
IPR016207 KetolA_reductoisomerase_fun
IPR036291 NAD(P)-bd_dom_sf
PANTHERiPTHR21371 PTHR21371, 1 hit
PfamiView protein in Pfam
PF01450 IlvC, 1 hit
PF07991 IlvN, 1 hit
PIRSFiPIRSF000119 Ilv5_fungal, 1 hit
SUPFAMiSSF48179 SSF48179, 1 hit
SSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR00465 ilvC, 1 hit
PROSITEiView protein in PROSITE
PS51851 KARI_C, 1 hit
PS51850 KARI_N, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P78827-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFRNSSRMA MKALRTMGSR RLATRSMSVM ARTIAAPSMR FAPRMTAPLM
60 70 80 90 100
QTRGMRVMDF AGTKENVWER SDWPREKLVD YFKNDTLAII GYGSQGHGQG
110 120 130 140 150
LNARDQGLNV IVGVRKDGAS WKQAIEDGWV PGKTLFPVEE AIKKGSIIMN
160 170 180 190 200
LLSDAAQTET WPKIAPLITK GKTLYFSHGF SVIFKDQTKI HPPKDVDVIL
210 220 230 240 250
VAPKGSGRTV RTLFKEGRGI NSSFAVYQDV TGKAQEKAIG LAVAVGSGFI
260 270 280 290 300
YQTTFKKEVI SDLVGERGCL MGGINGLFLA QYQVLRERGH SPAEAFNETV
310 320 330 340 350
EEATQSLYPL IGKYGLDYMF AACSTTARRG AIDWTPRFLE ANKKVLNELY
360 370 380 390 400
DNVENGNEAK RSLEYNSAPN YRELYDKELE EIRNLEIWKA GEVVRSLRPE

HNKH
Length:404
Mass (Da):45,189
Last modified:January 11, 2001 - v2
Checksum:i9AB3674C71AD6FEB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti38S → R in BAA13837 (PubMed:9501991).Curated1
Sequence conflicti92Y → S in BAA13837 (PubMed:9501991).Curated1
Sequence conflicti275N → P in BAA13837 (PubMed:9501991).Curated1
Sequence conflicti297N → P in BAA13837 (PubMed:9501991).Curated1
Sequence conflicti394V → G in BAA13837 (PubMed:9501991).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89175 mRNA Translation: BAA13837.1
CU329671 Genomic DNA Translation: CAA18891.1
AB009603 mRNA Translation: BAA24000.1
PIRiT40532
RefSeqiNP_001018845.2, NM_001022630.3

Genome annotation databases

EnsemblFungiiSPBC56F2.12.1; SPBC56F2.12.1:pep; SPBC56F2.12
GeneIDi3361354
KEGGispo:SPBC56F2.12

Similar proteinsi

Entry informationi

Entry nameiILV5_SCHPO
AccessioniPrimary (citable) accession number: P78827
Secondary accession number(s): O42619
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 11, 2001
Last modified: May 23, 2018
This is version 138 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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