UniProtKB - P07342 (ILVB_YEAST)

BLAST

>sp|P07342|ILVB_YEAST Acetolactate synthase catalytic subunit, mitochondrial OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=ILV2 PE=1 SV=1
MIRQSTLKNFAIKRCFQHIAYRNTPAMRSVALAQRFYSSSSRYYSASPLPASKRPEPAPS
FNVDPLEQPAEPSKLAKKLRAEPDMDTSFVGLTGGQIFNEMMSRQNVDTVFGYPGGAILP
VYDAIHNSDKFNFVLPKHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVVTPMADAFAD
GIPMVVFTGQVPTSAIGTDAFQEADVVGISRSCTKWNVMVKSVEELPLRINEAFEIATSG
RPGPVLVDLPKDVTAAILRNPIPTKTTLPSNALNQLTSRAQDEFVMQSINKAADLINLAK
KPVLYVGAGILNHADGPRLLKELSDRAQIPVTTTLQGLGSFDQEDPKSLDMLGMHGCATA
NLAVQNADLIIAVGARFDDRVTGNISKFAPEARRAAAEGRGGIIHFEVSPKNINKVVQTQ
IAVEGDATTNLGKMMSKIFPVKERSEWFAQINKWKKEYPYAYMEETPGSKIKPQTVIKKL
SKVANDTGRHVIVTTGVGQHQMWAAQHWTWRNPHTFITSGGLGTMGYGLPAAIGAQVAKP
ESLVIDIDGDASFNMTLTELSSAVQAGTPVKILILNNEEQGMVTQWQSLFYEHRYSHTHQ
LNPDFIKLAEAMGLKGLRVKKQEELDAKLKEFVSTKGPVLLEVEVDKKVPVLPMVAGGSG
LDEFINFDPEVERQQTELRHKRTGGKH

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History
Entry version 206 (07 Nov 2018)
Sequence version 1 (01 Apr 1988)
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Protein

Acetolactate synthase catalytic subunit, mitochondrial

Gene

ILV2

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Miscellaneous

Contains 1 molecule of FAD per monomer. The role of this cofactor is not clear considering that the reaction does not involve redox chemistry.

Present with 31900 molecules/cell in log phase SD medium.1 Publication

Catalytic activityⁱ

2 pyruvate = 2-acetolactate + CO₂.

Cofactorⁱ

Protein has several cofactor binding sites:

Mg²⁺By similarityNote: Binds 1 Mg²⁺ ion per subunit.By similarity
thiamine diphosphateBy similarityNote: Binds 1 thiamine pyrophosphate per subunit.By similarity

Activity regulationⁱ

The regulatory subunit ILV6 stimulates enzymatic activity seven- to tenfold and confers sensitivity to inhibition by valine and activation by ATP.1 Publication

Pathwayⁱ: L-isoleucine biosynthesis

This protein is involved in step 1 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:

Acetolactate synthase catalytic subunit, mitochondrial (ILV2), Acetolactate synthase small subunit, mitochondrial (ILV6)
Ketol-acid reductoisomerase, mitochondrial (ILV5)
Dihydroxy-acid dehydratase, mitochondrial (ILV3)
Branched-chain-amino-acid aminotransferase, mitochondrial (BAT1), Branched-chain-amino-acid aminotransferase, cytosolic (BAT2)

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 1 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:

Acetolactate synthase catalytic subunit, mitochondrial (ILV2), Acetolactate synthase small subunit, mitochondrial (ILV6)
Ketol-acid reductoisomerase, mitochondrial (ILV5)
Dihydroxy-acid dehydratase, mitochondrial (ILV3)
Branched-chain-amino-acid aminotransferase, mitochondrial (BAT1), Branched-chain-amino-acid aminotransferase, cytosolic (BAT2)

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 key	Position(s)	DescriptionActions	Length
Binding siteⁱ	139	Thiamine pyrophosphate	1
Binding siteⁱ	241	FAD1 Publication	1
Metal bindingⁱ	550	Magnesium	1
Metal bindingⁱ	577	Magnesium	1
Metal bindingⁱ	579	Magnesium; via carbonyl oxygen	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	355 – 376	FAD1 PublicationAdd BLAST		22
Nucleotide bindingⁱ	407 – 426	FAD1 PublicationAdd BLAST		20

GO - Molecular functionⁱ

acetolactate synthase activity
Source: SGD
Inferred from direct assayⁱ
- 10213630
flavin adenine dinucleotide binding
Source: SGD
Inferred from direct assayⁱ
- 15709745
magnesium ion binding Source: InterPro
thiamine pyrophosphate binding Source: InterPro

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

branched-chain amino acid biosynthetic process
Source: SGD
Inferred from direct assayⁱ
- 2406721
isoleucine biosynthetic process Source: UniProtKB-UniPathway
valine biosynthetic process Source: UniProtKB-UniPathway

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Transferase
Biological process	Amino-acid biosynthesis, Branched-chain amino acid biosynthesis
Ligand	Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCycⁱ	YEAST:MONOMER3O-29
BRENDAⁱ	2.2.1.6 984
UniPathwayⁱ	UPA00047;UER00055 UPA00049;UER00059

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Acetolactate synthase catalytic subunit, mitochondrial (EC:2.2.1.6) Alternative name(s): Acetohydroxy-acid synthase catalytic subunit Short name: AHAS Short name: ALS
Gene namesⁱ	Name:ILV2 Synonyms:SMR1 Ordered Locus Names:YMR108W ORF Names:YM9718.07
Organismⁱ	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifierⁱ	559292 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae
Proteomesⁱ	UP000002311 Componentⁱ: Chromosome XIII

Organism-specific databases

Saccharomyces Genome Database More...SGDⁱ	S000004714 ILV2

SGDⁱ

S000004714 ILV2

Keywords - Cellular componentⁱ

Mitochondrion

Pathology & Biotechⁱ

Chemistry databases

ChEMBLⁱ	CHEMBL1075095

ChEMBLⁱ

CHEMBL1075095

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Transit peptideⁱ	1 – 90	MitochondrionSequence analysisAdd BLAST		90
ChainⁱPRO_0000035664	91 – 687	Acetolactate synthase catalytic subunit, mitochondrialAdd BLAST		597

Proteomic databases

MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P07342
PaxDbⁱ	P07342
PRIDEⁱ	P07342

PTM databases

CarbonylDBⁱ	P07342
iPTMnetⁱ	P07342

Interactionⁱ

Subunit structureⁱ

Homodimer. The acetolactate synthase complex contains the catalytic regulatory subunit ILV2 and the regulatory small subunit ILV6.1 Publication

Protein-protein interaction databases

BioGridⁱ	35284, 43 interactors
ComplexPortalⁱ	CPX-3034 Acetolactate synthase complex
Database of interacting proteins More...DIPⁱ	DIP-1104N
IntActⁱ	P07342, 73 interactors
Molecular INTeraction database More...MINTⁱ	P07342
STRINGⁱ	4932.YMR108W

Chemistry databases

BindingDBⁱ

P07342

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Turnⁱ	88 – 91	Combined sources	4
Helixⁱ	94 – 104	Combined sources	11
Beta strandⁱ	109 – 112	Combined sources	4
Helixⁱ	116 – 118	Combined sources	3
Helixⁱ	119 – 127	Combined sources	9
Beta strandⁱ	132 – 134	Combined sources	3
Helixⁱ	139 – 153	Combined sources	15
Beta strandⁱ	157 – 161	Combined sources	5
Helixⁱ	165 – 168	Combined sources	4
Helixⁱ	171 – 180	Combined sources	10
Beta strandⁱ	184 – 190	Combined sources	7
Helixⁱ	193 – 195	Combined sources	3
Turnⁱ	196 – 199	Combined sources	4
Helixⁱ	206 – 209	Combined sources	4
Helixⁱ	211 – 213	Combined sources	3
Beta strandⁱ	214 – 219	Combined sources	6
Helixⁱ	223 – 225	Combined sources	3
Helixⁱ	226 – 237	Combined sources	12
Beta strandⁱ	239 – 241	Combined sources	3
Beta strandⁱ	244 – 250	Combined sources	7
Helixⁱ	251 – 255	Combined sources	5
Helixⁱ	264 – 267	Combined sources	4
Beta strandⁱ	272 – 275	Combined sources	4
Helixⁱ	281 – 298	Combined sources	18
Beta strandⁱ	300 – 306	Combined sources	7
Helixⁱ	308 – 312	Combined sources	5
Helixⁱ	316 – 327	Combined sources	12
Beta strandⁱ	331 – 333	Combined sources	3
Helixⁱ	335 – 337	Combined sources	3
Beta strandⁱ	348 – 351	Combined sources	4
Helixⁱ	358 – 366	Combined sources	9
Beta strandⁱ	368 – 374	Combined sources	7
Helixⁱ	379 – 382	Combined sources	4
Helixⁱ	385 – 387	Combined sources	3
Helixⁱ	390 – 397	Combined sources	8
Beta strandⁱ	402 – 408	Combined sources	7
Helixⁱ	410 – 412	Combined sources	3
Beta strandⁱ	415 – 417	Combined sources	3
Beta strandⁱ	420 – 425	Combined sources	6
Helixⁱ	427 – 435	Combined sources	9
Helixⁱ	445 – 457	Combined sources	13
Beta strandⁱ	467 – 469	Combined sources	3
Helixⁱ	473 – 486	Combined sources	14
Beta strandⁱ	491 – 495	Combined sources	5
Helixⁱ	499 – 507	Combined sources	9
Beta strandⁱ	512 – 514	Combined sources	3
Helixⁱ	528 – 538	Combined sources	11
Beta strandⁱ	542 – 549	Combined sources	8
Helixⁱ	550 – 556	Combined sources	7
Helixⁱ	557 – 559	Combined sources	3
Helixⁱ	560 – 566	Combined sources	7
Beta strandⁱ	571 – 576	Combined sources	6
Beta strandⁱ	582 – 587	Combined sources	6
Beta strandⁱ	589 – 591	Combined sources	3
Beta strandⁱ	594 – 596	Combined sources	3
Helixⁱ	605 – 612	Combined sources	8
Beta strandⁱ	614 – 619	Combined sources	6
Helixⁱ	622 – 624	Combined sources	3
Helixⁱ	625 – 634	Combined sources	10
Beta strandⁱ	639 – 645	Combined sources	7
Beta strandⁱ	652 – 654	Combined sources	3
Helixⁱ	669 – 682	Combined sources	14
Turnⁱ	683 – 685	Combined sources	3

Show more details

3D structure databases

Database of protein disorder More...DisProtⁱ	DP00398
ProteinModelPortalⁱ	P07342
SMRⁱ	P07342
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P07342

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	499 – 579	Thiamine pyrophosphate bindingAdd BLAST		81

Sequence similaritiesⁱ

Belongs to the TPP enzyme family.Curated

Keywords - Domainⁱ

Transit peptide

Phylogenomic databases

Ensembl GeneTree More...GeneTreeⁱ	ENSGT00550000075465
HOGENOMⁱ	HOG000258448
InParanoidⁱ	P07342
KEGG Orthology (KO) More...KOⁱ	K01652
OMAⁱ	QGMVRQW
Database of Orthologous Groups More...OrthoDBⁱ	EOG092C14MZ

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd02015 TPP_AHAS, 1 hit
InterProⁱ	View protein in InterPro IPR012846 Acetolactate_synth_lsu IPR039368 AHAS_TPP IPR029035 DHS-like_NAD/FAD-binding_dom IPR029061 THDP-binding IPR012000 Thiamin_PyroP_enz_cen_dom IPR012001 Thiamin_PyroP_enz_TPP-bd_dom IPR000399 TPP-bd_CS IPR011766 TPP_enzyme-bd_C
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02775 TPP_enzyme_C, 1 hit PF00205 TPP_enzyme_M, 1 hit PF02776 TPP_enzyme_N, 1 hit
SUPFAMⁱ	SSF52467 SSF52467, 1 hit SSF52518 SSF52518, 2 hits
TIGRFAMsⁱ	TIGR00118 acolac_lg, 1 hit
PROSITEⁱ	View protein in PROSITE PS00187 TPP_ENZYMES, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P07342-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MIRQSTLKNF AIKRCFQHIA YRNTPAMRSV ALAQRFYSSS SRYYSASPLP 
        60         70         80         90        100
ASKRPEPAPS FNVDPLEQPA EPSKLAKKLR AEPDMDTSFV GLTGGQIFNE 
       110        120        130        140        150
MMSRQNVDTV FGYPGGAILP VYDAIHNSDK FNFVLPKHEQ GAGHMAEGYA 
       160        170        180        190        200
RASGKPGVVL VTSGPGATNV VTPMADAFAD GIPMVVFTGQ VPTSAIGTDA 
       210        220        230        240        250
FQEADVVGIS RSCTKWNVMV KSVEELPLRI NEAFEIATSG RPGPVLVDLP 
       260        270        280        290        300
KDVTAAILRN PIPTKTTLPS NALNQLTSRA QDEFVMQSIN KAADLINLAK 
       310        320        330        340        350
KPVLYVGAGI LNHADGPRLL KELSDRAQIP VTTTLQGLGS FDQEDPKSLD 
       360        370        380        390        400
MLGMHGCATA NLAVQNADLI IAVGARFDDR VTGNISKFAP EARRAAAEGR 
       410        420        430        440        450
GGIIHFEVSP KNINKVVQTQ IAVEGDATTN LGKMMSKIFP VKERSEWFAQ 
       460        470        480        490        500
INKWKKEYPY AYMEETPGSK IKPQTVIKKL SKVANDTGRH VIVTTGVGQH 
       510        520        530        540        550
QMWAAQHWTW RNPHTFITSG GLGTMGYGLP AAIGAQVAKP ESLVIDIDGD 
       560        570        580        590        600
ASFNMTLTEL SSAVQAGTPV KILILNNEEQ GMVTQWQSLF YEHRYSHTHQ 
       610        620        630        640        650
LNPDFIKLAE AMGLKGLRVK KQEELDAKLK EFVSTKGPVL LEVEVDKKVP 
       660        670        680 
VLPMVAGGSG LDEFINFDPE VERQQTELRH KRTGGKH

Length:687

Mass (Da):74,937

Last modified:April 1, 1988 - v1

Checksum:ⁱB03C4D0F38AA1362

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X02549 Genomic DNA Translation: CAA26400.1 Z49702 Genomic DNA Translation: CAA89744.1 AY692995 Genomic DNA Translation: AAT93014.1 BK006946 Genomic DNA Translation: DAA10005.1
PIRⁱ	A23808 YCBYI
NCBI Reference Sequences More...RefSeqⁱ	NP_013826.1, NM_001182608.1

Genome annotation databases

EnsemblFungiⁱ	YMR108W; YMR108W; YMR108W
GeneIDⁱ	855135
KEGGⁱ	sce:YMR108W

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P07342	Acetolactate synthase		YEAS8		687	UniRef100_P07342
Acetolactate synthase		YEASO		687
Acetolactate synthase		YEASC		687
Acetolactate synthase		YEAS6		687
Acetolactate synthase		YEAS2		687
+3

Protein	Similar proteins		Species	Score	Length	Source
P07342	Acetolactate synthase		YEAS8		687	UniRef90_P07342
Acetolactate synthase		YEASO		687
Acetolactate synthase		YEASC		687
Acetolactate synthase		YEAS6		687
Acetolactate synthase		YEAS2		687
+14

Protein	Similar proteins		Species	Score	Length	Source
P07342	Acetolactate synthase, mitochondrial		SCHPO		669	UniRef50_P07342
Acetolactate synthase, mitochondrial		CRYNH		718
Acetolactate synthase, mitochondrial		CRYNJ		718
Acetolactate synthase		YEAS8		687
Acetolactate synthase		YEASO		687
+340

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X02549 Genomic DNA Translation: CAA26400.1 Z49702 Genomic DNA Translation: CAA89744.1 AY692995 Genomic DNA Translation: AAT93014.1 BK006946 Genomic DNA Translation: DAA10005.1
PIRⁱ	A23808 YCBYI
RefSeqⁱ	NP_013826.1, NM_001182608.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1JSC	X-ray	2.60	A/B	58-687	[»]
	1N0H	X-ray	2.80	A/B	58-687	[»]
	1T9A	X-ray	2.59	A/B	58-687	[»]
	1T9B	X-ray	2.20	A/B	58-687	[»]
	1T9C	X-ray	2.34	A/B	58-687	[»]
	1T9D	X-ray	2.30	A/B/C/D	58-687	[»]
	5FEM	X-ray	2.17	A/B	58-687	[»]
	5IMS	X-ray	1.98	A/B	58-687	[»]
	5WKC	X-ray	2.33	A/B/D/E	58-687	[»]
	6BD3	X-ray	2.28	A/B	58-687	[»]
	6BD9	X-ray	1.98	A/B	58-687	[»]
DisProtⁱ	DP00398
ProteinModelPortalⁱ	P07342
SMRⁱ	P07342
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	35284, 43 interactors
ComplexPortalⁱ	CPX-3034 Acetolactate synthase complex
DIPⁱ	DIP-1104N
IntActⁱ	P07342, 73 interactors
MINTⁱ	P07342
STRINGⁱ	4932.YMR108W

Chemistry databases

BindingDBⁱ	P07342
ChEMBLⁱ	CHEMBL1075095

PTM databases

CarbonylDBⁱ	P07342
iPTMnetⁱ	P07342

Proteomic databases

MaxQBⁱ	P07342
PaxDbⁱ	P07342
PRIDEⁱ	P07342

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblFungiⁱ	YMR108W; YMR108W; YMR108W
GeneIDⁱ	855135
KEGGⁱ	sce:YMR108W

Organism-specific databases

SGDⁱ	S000004714 ILV2

Phylogenomic databases

GeneTreeⁱ	ENSGT00550000075465
HOGENOMⁱ	HOG000258448
InParanoidⁱ	P07342
KOⁱ	K01652
OMAⁱ	QGMVRQW
OrthoDBⁱ	EOG092C14MZ

Enzyme and pathway databases

UniPathwayⁱ	UPA00047;UER00055 UPA00049;UER00059
BioCycⁱ	YEAST:MONOMER3O-29
BRENDAⁱ	2.2.1.6 984

Miscellaneous databases

EvolutionaryTraceⁱ	P07342
Protein Ontology More...PROⁱ	PR:P07342

Family and domain databases

CDDⁱ	cd02015 TPP_AHAS, 1 hit
InterProⁱ	View protein in InterPro IPR012846 Acetolactate_synth_lsu IPR039368 AHAS_TPP IPR029035 DHS-like_NAD/FAD-binding_dom IPR029061 THDP-binding IPR012000 Thiamin_PyroP_enz_cen_dom IPR012001 Thiamin_PyroP_enz_TPP-bd_dom IPR000399 TPP-bd_CS IPR011766 TPP_enzyme-bd_C
Pfamⁱ	View protein in Pfam PF02775 TPP_enzyme_C, 1 hit PF00205 TPP_enzyme_M, 1 hit PF02776 TPP_enzyme_N, 1 hit
SUPFAMⁱ	SSF52467 SSF52467, 1 hit SSF52518 SSF52518, 2 hits
TIGRFAMsⁱ	TIGR00118 acolac_lg, 1 hit
PROSITEⁱ	View protein in PROSITE PS00187 TPP_ENZYMES, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ILVB_YEAST
Accessionⁱ	P07342Primary (citable) accession number: P07342 Secondary accession number(s): D6VZT1
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
	Last sequence update:	April 1, 1988
	Last modified:	November 7, 2018
	This is version 206 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Fungal Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Yeast chromosome XIII
Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names
PATHWAY comments
Index of metabolic and biosynthesis pathways
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

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UniProtKB - P07342 (ILVB_YEAST)

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Acetolactate synthase catalytic subunit, mitochondrial

ILV2

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-isoleucine biosynthesis

Pathwayi: L-valine biosynthesis

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Mitochondrion

Mitochondrion

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Pathwayⁱ: L-isoleucine biosynthesis

Pathwayⁱ: L-valine biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ