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Protein

Putative dihydroxy-acid dehydratase, mitochondrial

Gene

SPAC17G8.06c

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O.

Cofactori

[4Fe-4S] clusterCuratedNote: Binds 1 [4Fe-4S] cluster.Curated

Pathwayi: L-isoleucine biosynthesis

This protein is involved in step 3 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 3 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
Metal bindingi157Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi232Iron-sulfur (4Fe-4S)By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00047; UER00057.
UPA00049; UER00061.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative dihydroxy-acid dehydratase, mitochondrial (EC:4.2.1.9)
Short name:
DAD
Alternative name(s):
2,3-dihydroxy acid hydrolyase
Gene namesi
ORF Names:SPAC17G8.06c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC17G8.06c.
PomBaseiSPAC17G8.06c.

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_0000015635? – 598Putative dihydroxy-acid dehydratase, mitochondrial
Transit peptidei1 – ?MitochondrionSequence analysis

Proteomic databases

MaxQBiQ10318.
PRIDEiQ10318.

Interactioni

Protein-protein interaction databases

BioGridi278631. 2 interactors.
MINTiMINT-4698699.

Structurei

3D structure databases

ProteinModelPortaliQ10318.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the IlvD/Edd family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000173155.
InParanoidiQ10318.
KOiK01687.
OMAiGYEGNPC.
OrthoDBiEOG092C1HK3.
PhylomeDBiQ10318.

Family and domain databases

HAMAPiMF_00012. IlvD. 1 hit.
InterProiIPR015928. Aconitase/3IPM_dehydase_swvl.
IPR004404. DihydroxyA_deHydtase.
IPR000581. DiOHA_6PGluconate_deHydtase.
IPR020558. DiOHA_6PGluconate_deHydtase_CS.
[Graphical view]
PANTHERiPTHR21000. PTHR21000. 1 hit.
PfamiPF00920. ILVD_EDD. 1 hit.
[Graphical view]
SUPFAMiSSF52016. SSF52016. 1 hit.
TIGRFAMsiTIGR00110. ilvD. 1 hit.
PROSITEiPS00886. ILVD_EDD_1. 1 hit.
PS00887. ILVD_EDD_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q10318-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMFCKLLRCQ NGIASKRAAL SLKGFKTSSI NLVEKKLNKY SETITGPKSQ
60 70 80 90 100
GASQAMLYAT GLNEEDMKKP QVGIASCWYE GNPCNMHLLD LGRRVKEGVK
110 120 130 140 150
KAGLTGFQFN TIGVSDGISM GTTGMRYSLQ SREIIADSIE TVMQGQWYDA
160 170 180 190 200
NVSIPGCDKN MPGCLIAMGR FNRPSIMVYG GSIRAGHSPC QNNAPIDIVS
210 220 230 240 250
AFQSYGEFIT GKIDEPTRHD IIRHACPGGG ACGGMYTANT MASCAEAMGM
260 270 280 290 300
TLPGSSSYLA GSPEKFAECE AAGSAIKRLL VDDIKPRDIM TRSAFENAMV
310 320 330 340 350
LTMTLGGSTN SVLHLIAIAK SVGITLTLDD FQAVSNRTPF IADMKPSGKY
360 370 380 390 400
VMEDLFAIGG IPSVLKYLHA EGLIDGSNIT VTGKTLAENL RGFKDLAEGQ
410 420 430 440 450
KIIRPLSNPI KTEGHLRVLR GSLAPEGSVA KITGKEGLNF TGKARVFDAE
460 470 480 490 500
NDFIAALERG EFKKGEKTVV IIRFEGPKGG PGMPEMLKPS SAIMGAGLGK
510 520 530 540 550
DVALLTDGRF SGGSHGFLIG HVDPEAQVGG PIALVQDGDV IEINAVKNTL
560 570 580 590
DLMVDEKEMA RRRSVWKAPP LKYQQGTLLK YARNVSTASK GAVTDSLE
Length:598
Mass (Da):63,927
Last modified:October 1, 1996 - v1
Checksum:iDF9E5544F0B87393
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti196I → V in BAA13915 (PubMed:9501991).Curated1
Sequence conflicti205Y → F in BAA13915 (PubMed:9501991).Curated1
Sequence conflicti270E → A in BAA13915 (PubMed:9501991).Curated1
Sequence conflicti285K → E in BAA13915 (PubMed:9501991).Curated1
Sequence conflicti290M → L in BAA13915 (PubMed:9501991).Curated1
Sequence conflicti293S → F in BAA13915 (PubMed:9501991).Curated1
Sequence conflicti318I → T in BAA13915 (PubMed:9501991).Curated1
Sequence conflicti399G → D in BAA13915 (PubMed:9501991).Curated1
Sequence conflicti552L → V in BAA13915 (PubMed:9501991).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA93689.1.
D89254 mRNA. Translation: BAA13915.1.
PIRiT37858.
T43179.
RefSeqiNP_593729.1. NM_001019160.2.

Genome annotation databases

EnsemblFungiiSPAC17G8.06c.1; SPAC17G8.06c.1:pep; SPAC17G8.06c.
GeneIDi2542155.
KEGGispo:SPAC17G8.06c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA93689.1.
D89254 mRNA. Translation: BAA13915.1.
PIRiT37858.
T43179.
RefSeqiNP_593729.1. NM_001019160.2.

3D structure databases

ProteinModelPortaliQ10318.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278631. 2 interactors.
MINTiMINT-4698699.

Proteomic databases

MaxQBiQ10318.
PRIDEiQ10318.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC17G8.06c.1; SPAC17G8.06c.1:pep; SPAC17G8.06c.
GeneIDi2542155.
KEGGispo:SPAC17G8.06c.

Organism-specific databases

EuPathDBiFungiDB:SPAC17G8.06c.
PomBaseiSPAC17G8.06c.

Phylogenomic databases

HOGENOMiHOG000173155.
InParanoidiQ10318.
KOiK01687.
OMAiGYEGNPC.
OrthoDBiEOG092C1HK3.
PhylomeDBiQ10318.

Enzyme and pathway databases

UniPathwayiUPA00047; UER00057.
UPA00049; UER00061.

Miscellaneous databases

PROiQ10318.

Family and domain databases

HAMAPiMF_00012. IlvD. 1 hit.
InterProiIPR015928. Aconitase/3IPM_dehydase_swvl.
IPR004404. DihydroxyA_deHydtase.
IPR000581. DiOHA_6PGluconate_deHydtase.
IPR020558. DiOHA_6PGluconate_deHydtase_CS.
[Graphical view]
PANTHERiPTHR21000. PTHR21000. 1 hit.
PfamiPF00920. ILVD_EDD. 1 hit.
[Graphical view]
SUPFAMiSSF52016. SSF52016. 1 hit.
TIGRFAMsiTIGR00110. ilvD. 1 hit.
PROSITEiPS00886. ILVD_EDD_1. 1 hit.
PS00887. ILVD_EDD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiILV3_SCHPO
AccessioniPrimary (citable) accession number: Q10318
Secondary accession number(s): P78903
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 5, 2016
This is version 121 of the entry and version 1 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.