Reviewed, UniProtKB/Swiss-Prot Q00955 (ACAC_YEAST)

Names and origin

Protein names

Recommended name:
    Acetyl-CoA carboxylase
      Short name=ACC
    EC=6.4.1.2
Including the following 1 domains:
    1- Recommended name:
            Biotin carboxylase
              EC=6.3.4.14

Gene names

Name:	FAS3
Synonyms:	ACC1
Ordered Locus Names:	YNR016C
ORF Names:	N3175

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	2233 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.
Catalytic activity	ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate + malonyl-CoA. ATP + biotin-carboxyl-carrier protein + CO(2) = ADP + phosphate + carboxybiotin-carboxyl-carrier protein.
Cofactor	Biotin By similarity. Binds 2 manganese ions per subunit By similarity.
Enzyme regulation	By phosphorylation.
Pathway	Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. Context: Fatty acid biosynthesis.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Miscellaneous	Present with 20200 molecules/cell in log phase SD medium.
Sequence similarities	Contains 1 ATP-grasp domain. Contains 1 biotin carboxylation domain. Contains 1 biotinyl-binding domain. Contains 1 carboxyltransferase domain.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Biotin Manganese Metal-binding Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological process	nuclear membrane organization and biogenesis Traceable author statement. Source: SGD protein import into nucleus Inferred from mutant phenotype. Source: SGD
Cellular component	endoplasmic reticulum membrane Inferred from direct assay. Source: SGD mitochondrion Inferred from direct assay. Source: SGD
Molecular function	acetyl-CoA carboxylase activity Inferred from mutant phenotype. Source: SGD biotin carboxylase activity Inferred from mutant phenotype. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Chain

1 – 2233

2233

Acetyl-CoA carboxylase

Regions

Domain

58 – 567

510

Biotin carboxylation

Domain

216 – 408

193

ATP-grasp

Domain

701 – 767

67

Biotinyl-binding

Domain

1603 – 2101

499

Carboxyltransferase

Nucleotide binding

256 – 261

6

ATP By similarity

Region

1627 – 1629

3

Acetyl-CoA binding

Sites

Active site

383

1

By similarity

Metal binding

365

1

Manganese 1 By similarity

Metal binding

379

1

Manganese 1 By similarity

Metal binding

379

1

Manganese 2 By similarity

Metal binding

381

1

Manganese 2 By similarity

Binding site

735

1

Biotin (covalent) By similarity

Binding site

1731

1

Coenzyme A

Binding site

1998

1

Acetyl-CoA; via amide nitrogen

Binding site

2034

1

Coenzyme A

Binding site

2036

1

Coenzyme A

Amino acid modifications

Modified residue

10

1

Phosphoserine

Modified residue

233

1

Phosphothreonine

Modified residue

430

1

Phosphoserine

Modified residue

1114

1

Phosphothreonine

Modified residue

1145

1

Phosphothreonine

Modified residue

1148

1

Phosphoserine

Modified residue

1157

1

Phosphoserine

Modified residue

1159

1

Phosphoserine

Modified residue

1162

1

Phosphoserine

Modified residue

1163

1

Phosphotyrosine

Modified residue

1169

1

Phosphoserine

Experimental info

Mutagenesis

1705

1

L → I: Raises KM for malonyl-CoA by a factor of 20

Mutagenesis

1731

1

R → S: Raises KM for malonyl-CoA by a factor of 15

Mutagenesis

1738

1

Y → F: No effect

Mutagenesis

1954

1

R → S: Raises KM for malonyl-CoA by a factor of 70

Mutagenesis

1994

1

E → Q: Lowers activity 10-fold

Sequence conflict

1523

1

W → G in AAA20073. Ref.1

Sequence conflict

1755

1

I → IWYRCL in AAA20073. Ref.1

Sequence conflict

1761 – 1766

6

AINKML → ESTNA in AAA20073. Ref.1

Secondary structure

1

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2233

Helix Strand Turn

Details...

Helix

22 – 27

6

Helix

30 – 32

3

Beta strand

35 – 37

3

Helix

38 – 40

3

Helix

45 – 52

8

Beta strand

61 – 64

4

Helix

68 – 86

19

Beta strand

91 – 98

8

Helix

100 – 104

5

Helix

108 – 112

5

Beta strand

113 – 118

6

Helix

124 – 126

3

Turn

127 – 129

3

Helix

131 – 140

10

Beta strand

144 – 147

4

Turn

152 – 155

4

Helix

158 – 165

8

Beta strand

171 – 174

4

Helix

177 – 182

6

Helix

186 – 195

10

Turn

204 – 207

4

Turn

215 – 217

3

Helix

224 – 227

4

Helix

228 – 230

3

Helix

235 – 245

11

Beta strand

247 – 253

7

Turn

258 – 261

4

Beta strand

262 – 265

4