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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: Annotation score: 4 out of 5-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 1By similarity1
Metal bindingi262Magnesium 2By similarity1
Metal bindingi266Magnesium 1By similarity1

Regions

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis

Keywords - Ligandi

Magnesium, 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

GO - Cellular componenti

  • mitochondrion Source: PomBase
Complete GO annotation...

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.
PRIDEiP78827.

PTM databases

iPTMnetiP78827.

Interactioni

Protein-protein interaction databases

MINTiMINT-4691399.

Structurei

3D structure databases

ProteinModelPortaliP78827.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ketol-acid reductoisomerase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000016231.
InParanoidiP78827.
KOiK00053.
OMAiFATAYSA.
OrthoDBiEOG092C2OSA.
PhylomeDBiP78827.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR000506. AcH_isomrdctse_C.
IPR013116. IlvN.
IPR013023. Ketol-acid_reductoisomrdctse.
IPR016207. KetolA_reductoisomerase_fun.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR21371. PTHR21371. 1 hit.
PfamiPF01450. IlvC. 1 hit.
PF07991. IlvN. 1 hit.
[Graphical view]
PIRSFiPIRSF000119. Ilv5_fungal. 1 hit.
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00465. ilvC. 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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP78827.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4691399.

PTM databases

iPTMnetiP78827.

Proteomic databases

MaxQBiP78827.
PRIDEiP78827.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:SPBC56F2.12.
PomBaseiSPBC56F2.12. ilv5.

Phylogenomic databases

HOGENOMiHOG000016231.
InParanoidiP78827.
KOiK00053.
OMAiFATAYSA.
OrthoDBiEOG092C2OSA.
PhylomeDBiP78827.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00056.
UPA00049; UER00060.

Miscellaneous databases

PROiP78827.

Family and domain databases

Gene3Di1.10.1040.10. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR000506. AcH_isomrdctse_C.
IPR013116. IlvN.
IPR013023. Ketol-acid_reductoisomrdctse.
IPR016207. KetolA_reductoisomerase_fun.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR21371. PTHR21371. 1 hit.
PfamiPF01450. IlvC. 1 hit.
PF07991. IlvN. 1 hit.
[Graphical view]
PIRSFiPIRSF000119. Ilv5_fungal. 1 hit.
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00465. ilvC. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiILV5_SCHPO
AccessioniPrimary (citable) accession number: P78827
Secondary accession number(s): O42619
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 11, 2001
Last modified: October 5, 2016
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.