Q10318 (ILV3_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative dihydroxy-acid dehydratase, mitochondrial
Short name=DAD
EC=4.2.1.9

Alternative name(s):
2,3-dihydroxy acid hydrolyase

Gene names

ORF Names:

SPAC17G8.06c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	598 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O.
Cofactor	Binds 1 4Fe-4S cluster Potential.
Pathway	Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 3/4. Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 3/4.
Subcellular location	Mitochondrion Potential.
Sequence similarities	Belongs to the IlvD/Edd family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	isoleucine biosynthetic process Inferred from sequence or structural similarity. Source: GeneDB_Spombe leucine metabolic process Inferred from sequence or structural similarity. Source: GeneDB_Spombe valine biosynthetic process Inferred from sequence or structural similarity. Source: GeneDB_Spombe
Cellular component	mitochondrion Inferred from direct assay. Source: GeneDB_Spombe
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW dihydroxy-acid dehydratase activity Inferred from sequence or structural similarity. Source: GeneDB_Spombe metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 598		Putative dihydroxy-acid dehydratase, mitochondrial		PRO_0000015635
Sites
	Metal binding	157	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	232	1	Iron-sulfur (4Fe-4S) By similarity
Experimental info
	Sequence conflict	196	1	I → V in BAA13915. Ref.2
	Sequence conflict	205	1	Y → F in BAA13915. Ref.2
	Sequence conflict	270	1	E → A in BAA13915. Ref.2
	Sequence conflict	285	1	K → E in BAA13915. Ref.2
	Sequence conflict	290	1	M → L in BAA13915. Ref.2
	Sequence conflict	293	1	S → F in BAA13915. Ref.2
	Sequence conflict	318	1	I → T in BAA13915. Ref.2
	Sequence conflict	399	1	G → D in BAA13915. Ref.2
	Sequence conflict	552	1	L → V in BAA13915. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q10318 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: DF9E5544F0B87393	FASTA	598	63,927
	10 20 30 40 50 60 MMFCKLLRCQ NGIASKRAAL SLKGFKTSSI NLVEKKLNKY SETITGPKSQ GASQAMLYAT 70 80 90 100 110 120 GLNEEDMKKP QVGIASCWYE GNPCNMHLLD LGRRVKEGVK KAGLTGFQFN TIGVSDGISM 130 140 150 160 170 180 GTTGMRYSLQ SREIIADSIE TVMQGQWYDA NVSIPGCDKN MPGCLIAMGR FNRPSIMVYG 190 200 210 220 230 240 GSIRAGHSPC QNNAPIDIVS AFQSYGEFIT GKIDEPTRHD IIRHACPGGG ACGGMYTANT 250 260 270 280 290 300 MASCAEAMGM TLPGSSSYLA GSPEKFAECE AAGSAIKRLL VDDIKPRDIM TRSAFENAMV 310 320 330 340 350 360 LTMTLGGSTN SVLHLIAIAK SVGITLTLDD FQAVSNRTPF IADMKPSGKY VMEDLFAIGG 370 380 390 400 410 420 IPSVLKYLHA EGLIDGSNIT VTGKTLAENL RGFKDLAEGQ KIIRPLSNPI KTEGHLRVLR 430 440 450 460 470 480 GSLAPEGSVA KITGKEGLNF TGKARVFDAE NDFIAALERG EFKKGEKTVV IIRFEGPKGG 490 500 510 520 530 540 PGMPEMLKPS SAIMGAGLGK DVALLTDGRF SGGSHGFLIG HVDPEAQVGG PIALVQDGDV 550 560 570 580 590 IEINAVKNTL DLMVDEKEMA RRRSVWKAPP LKYQQGTLLK YARNVSTASK GAVTDSLE

References

[1]

"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.

[2]

"Identification of open reading frames in Schizosaccharomyces pombe cDNAs." Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H. DNA Res. 4:363-369(1997) [PubMed: 9501991] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 86-598. Strain: PR745.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAA93689.1. D89254 mRNA. Translation: BAA13915.1.
PIR	T37858. T43179.
RefSeq	NP_593729.1. NM_001019160.1.
3D structure databases
ProteinModelPortal	Q10318.
ModBase	Search...
Protein-protein interaction databases
STRING	Q10318.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC17G8.06c.1; SPAC17G8.06c.1:pep; SPAC17G8.06c.
GeneID	2542155.
KEGG	spo:SPAC17G8.06c.
NMPDR	fig|4896.1.peg.3699.
Organism-specific databases
GeneDB_Spombe	SPAC17G8.06c.
Phylogenomic databases
eggNOG	fuNOG06287.
GeneTree	EFGT00050000003650.
HOGENOM	HBG671001.
OMA	GIDETEG.
OrthoDB	EOG4VDT6Q.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-001391-MONOMER.
Gene expression databases
ArrayExpress	Q10318.
Family and domain databases
InterPro	IPR015928. Aconitase/3IPM_dehydase_swvl. IPR004404. DihydroxyA_deHydtase. IPR000581. DiOHA_6PGluconate_deHydtase. IPR020558. DiOHA_6PGluconate_deHydtase_CS. [Graphical view]
KO	K01687.
PANTHER	PTHR21000. ILVD_EDD_family. 1 hit.
Pfam	PF00920. ILVD_EDD. 1 hit. [Graphical view]
SUPFAM	SSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit.
TIGRFAMs	TIGR00110. IlvD. 1 hit.
PROSITE	PS00886. ILVD_EDD_1. 1 hit. PS00887. ILVD_EDD_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ILV3_SCHPO

Accession

Primary (citable) accession number: Q10318
Secondary accession number(s): P78903

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	December 14, 2011
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program