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Q00955 (ACAC_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length2233 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.13

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.

Sequence similarities

Contains 1 ATP-grasp domain.

Contains 1 biotin carboxylation domain.

Contains 1 biotinyl-binding domain.

Contains 1 carboxyltransferase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 22332232Acetyl-CoA carboxylase
PRO_0000146770

Regions

Domain58 – 567510Biotin carboxylation
Domain216 – 408193ATP-grasp
Domain701 – 76767Biotinyl-binding
Domain1603 – 2101499Carboxyltransferase
Nucleotide binding256 – 2616ATP By similarity
Region1627 – 16293Acetyl-CoA binding

Sites

Active site3831 By similarity
Metal binding3651Manganese 1 By similarity
Metal binding3791Manganese 1 By similarity
Metal binding3791Manganese 2 By similarity
Metal binding3811Manganese 2 By similarity
Binding site17311Coenzyme A
Binding site19981Acetyl-CoA; via amide nitrogen
Binding site20341Coenzyme A
Binding site20361Coenzyme A

Amino acid modifications

Modified residue21N-acetylserine Ref.15 Ref.19
Modified residue21Phosphoserine Ref.15
Modified residue7351N6-biotinyllysine By similarity
Modified residue7901Phosphoserine Ref.18
Modified residue11481Phosphoserine Ref.15 Ref.17 Ref.18
Modified residue11571Phosphoserine Ref.15 Ref.16 Ref.17 Ref.18
Modified residue11621Phosphoserine Ref.18

Experimental info

Mutagenesis17051L → I: Raises KM for malonyl-CoA by a factor of 20. Ref.20
Mutagenesis17311R → S: Raises KM for malonyl-CoA by a factor of 15. Ref.20
Mutagenesis17381Y → F: No effect. Ref.20
Mutagenesis19541R → S: Raises KM for malonyl-CoA by a factor of 70. Ref.20
Mutagenesis19941E → Q: Lowers activity 10-fold.
Sequence conflict15231W → G in AAA20073. Ref.1
Sequence conflict17551I → IWYRCL in AAA20073. Ref.1
Sequence conflict1761 – 17666AINKML → ESTNA in AAA20073. Ref.1

Secondary structure

....................................................................................................................................................................................................................................... 2233
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q00955 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 0A335AAD9B1F8308

FASTA2,233250,353
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[15]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-1148 AND SER-1157, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Strain: YAL6B.
[16]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1157, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[17]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1148 AND SER-1157, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-790; SER-1148; SER-1157 AND SER-1162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
PIRS63347.
RefSeqNP_014413.1. NM_001183193.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OD2X-ray2.70A/B1429-2233[»]
1OD4X-ray2.70A/B/C1429-2233[»]
1UYRX-ray2.50A/B1482-2218[»]
1UYSX-ray2.80A/B/C1482-2218[»]
1UYTX-ray2.50A/B/C1482-2218[»]
1UYVX-ray2.60A/B/C1482-2218[»]
1W2XX-ray2.80A/B/C1476-2233[»]
1W93X-ray2.50A14-566[»]
1W96X-ray1.80A/B/C13-566[»]
3H0JX-ray2.80A/B/C1476-2233[»]
3H0QX-ray2.50A/B/C1476-2233[»]
3H0SX-ray2.43A/B/C1476-2233[»]
3K8XX-ray2.30A/B/C1476-2233[»]
3PGQX-ray2.80A/B/C1476-2233[»]
3TV5X-ray2.80A/B/C1476-2233[»]
3TVUX-ray2.40A/B/C1476-2233[»]
3TVWX-ray2.80A/B/C1476-2233[»]
3TZ3X-ray2.70A/B/C1476-2233[»]
DisProtDP00557.
ProteinModelPortalQ00955.
SMRQ00955. Positions 14-549, 1484-2202.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35841. 71 interactions.
DIPDIP-975N.
IntActQ00955. 36 interactions.
MINTMINT-636412.
STRING4932.YNR016C.

Chemistry

DrugBankDB00173. Adenine.

Proteomic databases

PaxDbQ00955.
PeptideAtlasQ00955.
PRIDEQ00955.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNR016C; YNR016C; YNR016C.
GeneID855750.
KEGGsce:YNR016C.

Organism-specific databases

CYGDYNR016c.
SGDS000005299. ACC1.

Phylogenomic databases

eggNOGCOG0511.
GeneTreeENSGT00550000074703.
HOGENOMHOG000214115.
KOK11262.
OMAQHITRAQ.
OrthoDBEOG74J9H5.

Enzyme and pathway databases

BioCycYEAST:MONOMER3O-7.
UniPathwayUPA00655; UER00711.

Gene expression databases

GenevestigatorQ00955.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProIPR013537. 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.
IPR005481. CarbamoylP_synth_lsu_N.
IPR000022. Carboxyl_trans.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR011763. COA_CT_C.
IPR011762. COA_CT_N.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF08326. 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]
SMARTSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
PROSITEPS50975. 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]
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Other

EvolutionaryTraceQ00955.
NextBio980163.

Entry information

Entry nameACAC_YEAST
AccessionPrimary (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: March 19, 2014
This is version 154 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways