Q00955 (ACAC_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetyl-CoA carboxylase
Short name=ACC
EC=6.4.1.2

Alternative name(s):
Fatty acid synthetase 3
mRNA transport-defective protein 7

Including the following 1 domains:

1. Biotin carboxylase
   EC=6.3.4.14

Gene names

Name:	ACC1
Synonyms:	ABP2, FAS3, MTR7
Ordered Locus Names:	YNR016C
ORF Names:	N3175

Organism

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

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	2233 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase. Involved in the synthesis of very-long-chain fatty acid synthesis which is required to maintain a functional nuclear envelope. Required for acylation and vacuolar membrane association of VAC8 which is necessary to maintain a normal morphology of the vacuole. Ref.4 Ref.5 Ref.10 Ref.12 Ref.14
Catalytic activity	ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA. ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].
Cofactor	Biotin By similarity. Binds 2 manganese ions per subunit By similarity.
Enzyme regulation	By phosphorylation. The catalytic activity is inhibited by soraphen A, a polyketide isolated from the myxobacterium Sorangium cellulosum and a potent inhibitor of fungal growth. Ref.8
Pathway	Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Subunit structure	Homodimer. Ref.20 Ref.21 Ref.22
Subcellular location	Cytoplasm. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Ref.10 Ref.11.
Induction	Repressed in presence of fatty acids. Repressed 3-fold by lipid precursors, inositol and choline, and also controlled by regulatory factors INO2, INO4 and OPI1. Ref.6 Ref.7 Ref.8 Ref.9
Miscellaneous	Present with 20200 molecules/cell in log phase SD medium. Ref.15
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 Endoplasmic reticulum Membrane
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 Reference proteome
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW nuclear envelope organization Traceable author statement. Source: SGD protein import into nucleus Inferred from mutant phenotype Ref.14. Source: SGD
Cellular component	endoplasmic reticulum membrane Inferred from direct assay Ref.11. Source: SGD mitochondrion Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acetyl-CoA carboxylase activity Inferred from mutant phenotype Ref.7. Source: SGD biotin carboxylase activity Inferred from mutant phenotype Ref.4. Source: SGD 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

Chain

1 – 2233

2233

Acetyl-CoA carboxylase

PRO_0000146770

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

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 Ref.19

Modified residue

233

1

Phosphothreonine Ref.19

Modified residue

430

1

Phosphoserine Ref.19

Modified residue

735

1

N6-biotinyllysine By similarity

Modified residue

1114

1

Phosphothreonine Ref.19

Modified residue

1145

1

Phosphothreonine Ref.19

Modified residue

1148

1

Phosphoserine Ref.18 Ref.19

Modified residue

1157

1

Phosphoserine Ref.13 Ref.16 Ref.17 Ref.19

Modified residue

1159

1

Phosphoserine Ref.19

Modified residue

1162

1

Phosphoserine Ref.19

Modified residue

1163

1

Phosphotyrosine Ref.19

Modified residue

1169

1

Phosphoserine Ref.19

Experimental info

Mutagenesis

1705

1

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

Mutagenesis

1731

1

R → S: Raises KM for malonyl-CoA by a factor of 15. Ref.20

Mutagenesis

1738

1

Y → F: No effect. Ref.20

Mutagenesis

1954

1

R → S: Raises KM for malonyl-CoA by a factor of 70. Ref.20

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

Helix

268 – 281

14

Beta strand

287 – 291

5

Beta strand

297 – 305

9

Beta strand

311 – 323

13

Beta strand

326 – 333

8

Helix

339 – 356

18

Beta strand

360 – 368

9

Turn

370 – 372

3

Beta strand

375 – 381

7

Helix

388 – 395

8

Helix

399 – 407

9

Helix

412 – 414

3

Helix

416 – 421

6

Helix

439 – 444

6

Beta strand

452 – 462

11

Beta strand

472 – 478

7

Beta strand

484 – 492

9

Beta strand

503 – 515

13

Helix

516 – 530

15

Helix

541 – 547

7

Helix

550 – 553

4

Helix

561 – 565

5

Helix

1490 – 1493

4

Helix

1495 – 1502

8

Helix

1508 – 1510

3

Helix

1511 – 1524

14

Beta strand

1537 – 1544

8

Beta strand

1546 – 1548

3

Beta strand

1550 – 1553

4

Beta strand

1561 – 1573

13

Beta strand

1576 – 1587

12

Helix

1591 – 1594

4

Helix

1598 – 1614

17

Beta strand

1618 – 1622

5

Turn

1633 – 1635

3

Helix

1636 – 1638

3

Beta strand

1640 – 1645

6

Helix

1649 – 1651

3

Beta strand

1653 – 1658

6

Helix

1660 – 1665

6

Helix

1667 – 1669

3

Beta strand

1683 – 1686

4

Beta strand

1691 – 1693

3

Beta strand

1696 – 1698

3

Helix

1702 – 1718

17

Turn

1719 – 1721

3

Beta strand

1724 – 1730

7

Helix

1735 – 1742

8

Beta strand

1746 – 1749

4

Beta strand

1754 – 1757

4

Helix

1759 – 1765

7

Helix

1775 – 1778

4

Helix

1780 – 1783

4

Turn

1784 – 1787

4

Beta strand

1788 – 1795

8

Helix

1796 – 1807

12

Beta strand

1827 – 1829

3

Beta strand

1837 – 1839

3

Helix

1843 – 1848

6

Beta strand

1849 – 1852

4

Beta strand

1855 – 1858

4

Beta strand

1867 – 1870

4

Beta strand

1877 – 1884

8

Beta strand

1887 – 1894

8

Beta strand

1899 – 1903

5

Beta strand

1915 – 1919

5

Helix

1926 – 1941

16

Beta strand

1947 – 1949

3

Helix

1960 – 1964

5

Helix

1967 – 1980

14

Beta strand

1985 – 1989

5

Beta strand

1994 – 1996

3

Helix

1997 – 2001

5

Helix

2005 – 2008

4

Turn

2009 – 2011

3

Beta strand

2012 – 2017

6

Beta strand

2021 – 2025

5

Helix

2027 – 2034

8

Helix

2037 – 2047

11

Helix

2049 – 2059

11

Helix

2065 – 2094

30

Turn

2095 – 2097

3

Helix

2100 – 2105

6

Beta strand

2109 – 2113

5

Helix

2115 – 2117

3

Helix

2118 – 2138

21

Beta strand

2141 – 2144

4

Helix

2148 – 2156

9

Helix

2168 – 2177

10

Helix

2179 – 2193

15

Helix

2196 – 2199

4

Turn

2203 – 2205

3

Helix

2206 – 2214

9

Sequences

	Sequence		Length	Mass (Da)
	Q00955 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 0A335AAD9B1F8308	FASTA	2,233	250,353
	10 20 30 40 50 60 MSEESLFESS PQKMEYEITN YSERHTELPG HFIGLNTVDK LEESPLRDFV KSHGGHTVIS 70 80 90 100 110 120 KILIANNGIA AVKEIRSVRK WAYETFGDDR TVQFVAMATP EDLEANAEYI RMADQYIEVP 130 140 150 160 170 180 GGTNNNNYAN VDLIVDIAER ADVDAVWAGW GHASENPLLP EKLSQSKRKV IFIGPPGNAM 190 200 210 220 230 240 RSLGDKISST IVAQSAKVPC IPWSGTGVDT VHVDEKTGLV SVDDDIYQKG CCTSPEDGLQ 250 260 270 280 290 300 KAKRIGFPVM IKASEGGGGK GIRQVEREED FIALYHQAAN EIPGSPIFIM KLAGRARHLE 310 320 330 340 350 360 VQLLADQYGT NISLFGRDCS VQRRHQKIIE EAPVTIAKAE TFHEMEKAAV RLGKLVGYVS 370 380 390 400 410 420 AGTVEYLYSH DDGKFYFLEL NPRLQVEHPT TEMVSGVNLP AAQLQIAMGI PMHRISDIRT 430 440 450 460 470 480 LYGMNPHSAS EIDFEFKTQD ATKKQRRPIP KGHCTACRIT SEDPNDGFKP SGGTLHELNF 490 500 510 520 530 540 RSSSNVWGYF SVGNNGNIHS FSDSQFGHIF AFGENRQASR KHMVVALKEL SIRGDFRTTV 550 560 570 580 590 600 EYLIKLLETE DFEDNTITTG WLDDLITHKM TAEKPDPTLA VICGAATKAF LASEEARHKY 610 620 630 640 650 660 IESLQKGQVL SKDLLQTMFP VDFIHEGKRY KFTVAKSGND RYTLFINGSK CDIILRQLSD 670 680 690 700 710 720 GGLLIAIGGK SHTIYWKEEV AATRLSVDSM TTLLEVENDP TQLRTPSPGK LVKFLVENGE 730 740 750 760 770 780 HIIKGQPYAE IEVMKMQMPL VSQENGIVQL LKQPGSTIVA GDIMAIMTLD DPSKVKHALP 790 800 810 820 830 840 FEGMLPDFGS PVIEGTKPAY KFKSLVSTLE NILKGYDNQV IMNASLQQLI EVLRNPKLPY 850 860 870 880 890 900 SEWKLHISAL HSRLPAKLDE QMEELVARSL RRGAVFPARQ LSKLIDMAVK NPEYNPDKLL 910 920 930 940 950 960 GAVVEPLADI AHKYSNGLEA HEHSIFVHFL EEYYEVEKLF NGPNVREENI ILKLRDENPK 970 980 990 1000 1010 1020 DLDKVALTVL SHSKVSAKNN LILAILKHYQ PLCKLSSKVS AIFSTPLQHI VELESKATAK 1030 1040 1050 1060 1070 1080 VALQAREILI QGALPSVKER TEQIEHILKS SVVKVAYGSS NPKRSEPDLN ILKDLIDSNY 1090 1100 1110 1120 1130 1140 VVFDVLLQFL THQDPVVTAA AAQVYIRRAY RAYTIGDIRV HEGVTVPIVE WKFQLPSAAF 1150 1160 1170 1180 1190 1200 STFPTVKSKM GMNRAVSVSD LSYVANSQSS PLREGILMAV DHLDDVDEIL SQSLEVIPRH 1210 1220 1230 1240 1250 1260 QSSSNGPAPD RSGSSASLSN VANVCVASTE GFESEEEILV RLREILDLNK QELINASIRR 1270 1280 1290 1300 1310 1320 ITFMFGFKDG SYPKYYTFNG PNYNENETIR HIEPALAFQL ELGRLSNFNI KPIFTDNRNI 1330 1340 1350 1360 1370 1380 HVYEAVSKTS PLDKRFFTRG IIRTGHIRDD ISIQEYLTSE ANRLMSDILD NLEVTDTSNS 1390 1400 1410 1420 1430 1440 DLNHIFINFI AVFDISPEDV EAAFGGFLER FGKRLLRLRV SSAEIRIIIK DPQTGAPVPL 1450 1460 1470 1480 1490 1500 RALINNVSGY VIKTEMYTEV KNAKGEWVFK SLGKPGSMHL RPIATPYPVK EWLQPKRYKA 1510 1520 1530 1540 1550 1560 HLMGTTYVYD FPELFRQASS SQWKNFSADV KLTDDFFISN ELIEDENGEL TEVEREPGAN 1570 1580 1590 1600 1610 1620 AIGMVAFKIT VKTPEYPRGR QFVVVANDIT FKIGSFGPQE DEFFNKVTEY ARKRGIPRIY 1630 1640 1650 1660 1670 1680 LAANSGARIG MAEEIVPLFQ VAWNDAANPD KGFQYLYLTS EGMETLKKFD KENSVLTERT 1690 1700 1710 1720 1730 1740 VINGEERFVI KTIIGSEDGL GVECLRGSGL IAGATSRAYH DIFTITLVTC RSVGIGAYLV 1750 1760 1770 1780 1790 1800 RLGQRAIQVE GQPIILTGAP AINKMLGREV YTSNLQLGGT QIMYNNGVSH LTAVDDLAGV 1810 1820 1830 1840 1850 1860 EKIVEWMSYV PAKRNMPVPI LETKDTWDRP VDFTPTNDET YDVRWMIEGR ETESGFEYGL 1870 1880 1890 1900 1910 1920 FDKGSFFETL SGWAKGVVVG RARLGGIPLG VIGVETRTVE NLIPADPANP NSAETLIQEP 1930 1940 1950 1960 1970 1980 GQVWHPNSAF KTAQAINDFN NGEQLPMMIL ANWRGFSGGQ RDMFNEVLKY GSFIVDALVD 1990 2000 2010 2020 2030 2040 YKQPIIIYIP PTGELRGGSW VVVDPTINAD QMEMYADVNA RAGVLEPQGM VGIKFRREKL 2050 2060 2070 2080 2090 2100 LDTMNRLDDK YRELRSQLSN KSLAPEVHQQ ISKQLADRER ELLPIYGQIS LQFADLHDRS 2110 2120 2130 2140 2150 2160 SRMVAKGVIS KELEWTEARR FFFWRLRRRL NEEYLIKRLS HQVGEASRLE KIARIRSWYP 2170 2180 2190 2200 2210 2220 ASVDHEDDRQ VATWIEENYK TLDDKLKGLK LESFAQDLAK KIRSDHDNAI DGLSEVIKML 2230 STDDKEKLLK TLK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the yeast FAS3 gene and primary structure of yeast acetyl-CoA carboxylase." Al-Feel W., Chirala S.S., Wakil S.J. Proc. Natl. Acad. Sci. U.S.A. 89:4534-4538(1992) [PubMed: 1350093] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2015-2022.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J. Nature 387:93-98(1997) [PubMed: 9169873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Yeast mutants defective in acetyl-coenzyme A carboxylase and biotin: apocarboxylase ligase." Mishina M., Roggenkamp R., Schweizer E. Eur. J. Biochem. 111:79-87(1980) [PubMed: 6108218] [Abstract] Cited for: FUNCTION.
[5]	"Fatty acid-requiring mutant of Saccharomyces cerevisiae defective in acetyl-CoA carboxylase." Roggenkamp R., Numa S., Schweizer E. Proc. Natl. Acad. Sci. U.S.A. 77:1814-1817(1980) [PubMed: 6103540] [Abstract] Cited for: FUNCTION.
[6]	"Coordinated regulation and inositol-mediated and fatty acid-mediated repression of fatty acid synthase genes in Saccharomyces cerevisiae." Chirala S.S. Proc. Natl. Acad. Sci. U.S.A. 89:10232-10236(1992) [PubMed: 1359536] [Abstract] Cited for: INDUCTION.
[7]	"Acetyl-CoA carboxylase from yeast is an essential enzyme and is regulated by factors that control phospholipid metabolism." Hasslacher M., Ivessa A.S., Paltauf F., Kohlwein S.D. J. Biol. Chem. 268:10946-10952(1993) [PubMed: 8098706] [Abstract] Cited for: INDUCTION.
[8]	"Identification of the yeast ACC1 gene product (acetyl-CoA carboxylase) as the target of the polyketide fungicide soraphen A." Vahlensieck H.F., Pridzun L., Reichenbach H., Hinnen A. Curr. Genet. 25:95-100(1994) [PubMed: 7916271] [Abstract] Cited for: ENZYME REGULATION.
[9]	"Analysis of FAS3/ACC regulatory region of Saccharomyces cerevisiae: identification of a functional UASINO and sequences responsible for fatty acid mediated repression." Chirala S.S., Zhong Q., Huang W., al-Feel W. Nucleic Acids Res. 22:412-418(1994) [PubMed: 8127678] [Abstract] Cited for: INDUCTION.
[10]	"A yeast acetyl coenzyme A carboxylase mutant links very-long-chain fatty acid synthesis to the structure and function of the nuclear membrane-pore complex." Schneiter R., Hitomi M., Ivessa A.S., Fasch E.V., Kohlwein S.D., Tartakoff A.M. Mol. Cell. Biol. 16:7161-7172(1996) [PubMed: 8943372] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]	"Yeast acetyl-CoA carboxylase is associated with the cytoplasmic surface of the endoplasmic reticulum." Ivessa A.S., Schneiter R., Kohlwein S.D. Eur. J. Cell Biol. 74:399-406(1997) [PubMed: 9438137] [Abstract] Cited for: SUBCELLULAR LOCATION.
[12]	"A novel cold-sensitive allele of the rate-limiting enzyme of fatty acid synthesis, acetyl coenzyme A carboxylase, affects the morphology of the yeast vacuole through acylation of Vac8p." Schneiter R., Guerra C.E., Lampl M., Tatzer V., Zellnig G., Klein H.L., Kohlwein S.D. Mol. Cell. Biol. 20:2984-2995(2000) [PubMed: 10757783] [Abstract] Cited for: FUNCTION.
[13]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1157, MASS SPECTROMETRY. Strain: 2124.
[14]	"Nuclear accumulation of the small GTPase Gsp1p depends on nucleoporins Nup133p, Rat2p/Nup120p, Nup85p, Nic96p, and the acetyl-CoA carboxylase Acc1p." Gao H., Sumanaweera N., Bailer S.M., Stochaj U. J. Biol. Chem. 278:25331-25340(2003) [PubMed: 12730220] [Abstract] Cited for: FUNCTION.
[15]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[16]	"A proteomics approach to understanding protein ubiquitination." Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P. Nat. Biotechnol. 21:921-926(2003) [PubMed: 12872131] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1157, MASS SPECTROMETRY. Strain: SUB592.
[17]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1157, MASS SPECTROMETRY. Strain: ADR376.
[18]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1148, MASS SPECTROMETRY.
[19]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; THR-233; SER-430; THR-1114; THR-1145; SER-1148; SER-1157; SER-1159; SER-1162; TYR-1163 AND SER-1169, MASS SPECTROMETRY.
[20]	"Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase." Zhang H., Yang Z., Shen Y., Tong L. Science 299:2064-2067(2003) [PubMed: 12663926] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1429-2233 IN COMPLEX WITH COA, MUTAGENESIS OF LEU-1705; ARG-1731; TYR-1738 AND ARG-1954, HOMODIMERIZATION.
[21]	"A mechanism for the potent inhibition of eukaryotic acetyl-coenzyme A carboxylase by soraphen A, a macrocyclic polyketide natural product." Shen Y., Volrath S.L., Weatherly S.C., Elich T.D., Tong L. Mol. Cell 16:881-891(2004) [PubMed: 15610732] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 13-566 IN COMPLEX WITH SORAPHEN, SUBUNIT.
[22]	"Molecular basis for the inhibition of the carboxyltransferase domain of acetyl-coenzyme-A carboxylase by haloxyfop and diclofop." Zhang H., Tweel B., Tong L. Proc. Natl. Acad. Sci. U.S.A. 101:5910-5915(2004) [PubMed: 15079078] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1482-2218 IN COMPLEXES WITH THE INHIBITORS HALOXYFOP OR DICLOFOP, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M92156 Genomic DNA. Translation: AAA20073.1.
Z71631 Genomic DNA. Translation: CAA96294.1.
BK006947 Genomic DNA. Translation: DAA10557.1.

PIR

S63347.

RefSeq

NP_014413.1. NM_001183193.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OD2	X-ray	2.70	A/B	1429-2233	[»]
1OD4	X-ray	2.70	A/B/C	1429-2233	[»]
1UYR	X-ray	2.50	A/B	1482-2218	[»]
1UYS	X-ray	2.80	A/B/C	1482-2218	[»]
1UYT	X-ray	2.50	A/B/C	1482-2218	[»]
1UYV	X-ray	2.60	A/B/C	1482-2218	[»]
1W2X	X-ray	2.80	A/B/C	1476-2233	[»]
1W93	X-ray	2.50	A	14-566	[»]
1W96	X-ray	1.80	A/B/C	13-566	[»]
3H0J	X-ray	2.80	A/B/C	1476-2233	[»]
3H0Q	X-ray	2.50	A/B/C	1476-2233	[»]
3H0S	X-ray	2.43	A/B/C	1476-2233	[»]
3K8X	X-ray	2.30	A/B/C	1476-2233	[»]
3PGQ	X-ray	2.80	A/B/C	1476-2233	[»]
3TV5	X-ray	2.80	A/B/C	1476-2233	[»]
3TVU	X-ray	2.40	A/B/C	1476-2233	[»]
3TVW	X-ray	2.80	A/B/C	1476-2233	[»]
3TZ3	X-ray	2.70	A/B/C	1476-2233	[»]

ProteinModelPortal

Q00955.

SMR

Q00955. Positions 14-783, 1484-2202.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-975N.

IntAct

Q00955. 32 interactions.

MINT

MINT-636412.

STRING

Q00955.

Proteomic databases

PeptideAtlas

Q00955.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YNR016C; YNR016C; YNR016C.

GeneID

855750.

KEGG

sce:YNR016C.

NMPDR

fig|4932.3.peg.5493.

Organism-specific databases

CYGD

YNR016c.

SGD

S000005299. ACC1.

Phylogenomic databases

eggNOG

fuNOG05453.

GeneTree

EFGT00050000001254.

HOGENOM

HBG320067.

OMA

HTIAVRV.

OrthoDB

EOG4P2T99.

Gene expression databases

ArrayExpress

Q00955.

Genevestigator

Q00955.

GermOnline

YNR016C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR013537. AcCoA_COase_cen.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
IPR005479. CarbamoylP_synth_lsu_ATP-bd.
IPR005481. CarbamoylP_synth_lsu_N.
IPR000022. Carboxyl_trans.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
IPR013817. Pre-ATP_grasp.
IPR016185. PreATP-grasp-like.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view]

Gene3D

G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit.
G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit.
G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.

KO

K11262.

Pfam

PF08326. ACC_central. 1 hit.
PF02785. Biotin_carb_C. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF01039. Carboxyl_trans. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]

SMART

SM00878. Biotin_carb_C. 1 hit.
[Graphical view]

SUPFAM

SSF51230. Hybrid_motif. 1 hit.
SSF52440. PreATP-grasp-like. 1 hit.
SSF51246. Rudmnt_hyb_motif. 1 hit.

PROSITE

PS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00188. BIOTIN. 1 hit.
PS50968. BIOTINYL_LIPOYL. 1 hit.
PS50989. COA_CT_CTER. 1 hit.
PS50980. COA_CT_NTER. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00173. Adenine.

NextBio

980163.

Entry information

Entry name

ACAC_YEAST

Accession

Primary (citable) accession number: Q00955
Secondary accession number(s): D6W1J1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	October 1, 1996
Last modified:	December 14, 2011
This is version 131 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program