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Q00955

- ACAC_YEAST

UniProt

Q00955 - ACAC_YEAST

Protein

Acetyl-CoA carboxylase

Gene

ACC1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    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.5 Publications

    Catalytic activityi

    ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.
    ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].

    Cofactori

    Biotin.By similarity
    Binds 2 manganese ions per subunit.By similarity

    Enzyme regulationi

    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.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi365 – 3651Manganese 1By similarity
    Metal bindingi379 – 3791Manganese 1By similarity
    Metal bindingi379 – 3791Manganese 2By similarity
    Metal bindingi381 – 3811Manganese 2By similarity
    Active sitei383 – 3831By similarity
    Binding sitei1731 – 17311Coenzyme A
    Binding sitei1998 – 19981Acetyl-CoA; via amide nitrogen
    Binding sitei2034 – 20341Coenzyme A
    Binding sitei2036 – 20361Coenzyme A

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi256 – 2616ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. acetyl-CoA carboxylase activity Source: SGD
    2. ATP binding Source: UniProtKB-KW
    3. biotin carboxylase activity Source: SGD
    4. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. long-chain fatty acid biosynthetic process Source: SGD
    2. malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway
    3. nuclear envelope organization Source: SGD
    4. protein import into nucleus Source: SGD

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Keywords - Ligandi

    ATP-binding, Biotin, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:MONOMER3O-7.
    ReactomeiREACT_188404. Defective HLCS causes multiple carboxylase deficiency.
    REACT_188774. Biotin transport and metabolism.
    UniPathwayiUPA00655; UER00711.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyl-CoA carboxylase (EC:6.4.1.2)
    Short name:
    ACC
    Alternative name(s):
    Fatty acid synthetase 3
    mRNA transport-defective protein 7
    Including the following 1 domains:
    Biotin carboxylase (EC:6.3.4.14)
    Gene namesi
    Name:ACC1
    Synonyms:ABP2, FAS3, MTR7
    Ordered Locus Names:YNR016C
    ORF Names:N3175
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIV

    Organism-specific databases

    CYGDiYNR016c.
    SGDiS000005299. ACC1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1705 – 17051L → I: Raises KM for malonyl-CoA by a factor of 20. 1 Publication
    Mutagenesisi1731 – 17311R → S: Raises KM for malonyl-CoA by a factor of 15. 1 Publication
    Mutagenesisi1738 – 17381Y → F: No effect. 1 Publication
    Mutagenesisi1954 – 19541R → S: Raises KM for malonyl-CoA by a factor of 70. 1 Publication
    Mutagenesisi1994 – 19941E → Q: Lowers activity 10-fold.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 22332232Acetyl-CoA carboxylasePRO_0000146770Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei2 – 21Phosphoserine1 Publication
    Modified residuei735 – 7351N6-biotinyllysineBy similarity
    Modified residuei790 – 7901Phosphoserine1 Publication
    Modified residuei1148 – 11481Phosphoserine3 Publications
    Modified residuei1157 – 11571Phosphoserine4 Publications
    Modified residuei1162 – 11621Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ00955.
    PaxDbiQ00955.
    PeptideAtlasiQ00955.
    PRIDEiQ00955.

    Expressioni

    Inductioni

    Repressed in presence of fatty acids. Repressed 3-fold by lipid precursors, inositol and choline, and also controlled by regulatory factors INO2, INO4 and OPI1.3 Publications

    Gene expression databases

    GenevestigatoriQ00955.

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Protein-protein interaction databases

    BioGridi35841. 71 interactions.
    DIPiDIP-975N.
    IntActiQ00955. 36 interactions.
    MINTiMINT-636412.
    STRINGi4932.YNR016C.

    Structurei

    Secondary structure

    1
    2233
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi22 – 276
    Helixi30 – 323
    Beta strandi35 – 373
    Helixi38 – 403
    Helixi45 – 528
    Beta strandi61 – 644
    Helixi68 – 8619
    Beta strandi91 – 988
    Helixi100 – 1045
    Helixi108 – 1125
    Beta strandi113 – 1186
    Helixi124 – 1263
    Turni127 – 1293
    Helixi131 – 14010
    Beta strandi144 – 1474
    Turni152 – 1554
    Helixi158 – 1658
    Beta strandi171 – 1744
    Helixi177 – 1826
    Helixi186 – 19510
    Turni204 – 2074
    Turni215 – 2173
    Helixi224 – 2274
    Helixi228 – 2303
    Helixi235 – 24511
    Beta strandi247 – 2537
    Turni258 – 2614
    Beta strandi262 – 2654
    Helixi268 – 28114
    Beta strandi287 – 2915
    Beta strandi297 – 3059
    Turni307 – 3093
    Beta strandi311 – 32313
    Beta strandi326 – 3338
    Helixi339 – 35618
    Beta strandi360 – 3689
    Turni370 – 3723
    Beta strandi375 – 3817
    Helixi388 – 3958
    Helixi399 – 4079
    Helixi412 – 4143
    Helixi416 – 4216
    Helixi439 – 4446
    Beta strandi452 – 46211
    Beta strandi466 – 4683
    Beta strandi472 – 4787
    Beta strandi484 – 4929
    Beta strandi503 – 51513
    Helixi516 – 53015
    Helixi541 – 5477
    Helixi550 – 5534
    Helixi561 – 5655
    Helixi1490 – 14934
    Helixi1495 – 15028
    Helixi1508 – 15103
    Helixi1511 – 152616
    Helixi1534 – 15363
    Beta strandi1537 – 15448
    Beta strandi1546 – 15483
    Beta strandi1550 – 15534
    Beta strandi1561 – 157111
    Beta strandi1580 – 15878
    Helixi1592 – 15943
    Helixi1598 – 161417
    Beta strandi1618 – 16225
    Helixi1633 – 16353
    Turni1636 – 16383
    Beta strandi1640 – 16456
    Helixi1649 – 16513
    Beta strandi1653 – 16586
    Helixi1660 – 16689
    Helixi1672 – 16743
    Beta strandi1675 – 16828
    Beta strandi1685 – 16939
    Beta strandi1696 – 16983
    Helixi1702 – 171918
    Beta strandi1724 – 17285
    Helixi1735 – 17428
    Beta strandi1745 – 17495
    Beta strandi1754 – 17574
    Helixi1759 – 17668
    Helixi1775 – 17784
    Helixi1780 – 17834
    Turni1784 – 17874
    Beta strandi1788 – 17958
    Helixi1796 – 180712
    Beta strandi1827 – 18293
    Beta strandi1837 – 18393
    Helixi1843 – 18486
    Beta strandi1850 – 18523
    Beta strandi1855 – 18573
    Beta strandi1867 – 18704
    Beta strandi1877 – 18848
    Beta strandi1887 – 18948
    Beta strandi1899 – 19035
    Beta strandi1909 – 19113
    Beta strandi1915 – 19195
    Helixi1926 – 194116
    Beta strandi1947 – 19493
    Beta strandi1953 – 19564
    Helixi1960 – 19645
    Helixi1967 – 197913
    Beta strandi1985 – 19895
    Beta strandi1994 – 19963
    Helixi1998 – 20014
    Helixi2005 – 20073
    Turni2009 – 20113
    Beta strandi2012 – 20176
    Beta strandi2021 – 20255
    Helixi2027 – 20348
    Helixi2037 – 204711
    Turni2049 – 20513
    Helixi2083 – 209513
    Helixi2100 – 21067
    Beta strandi2109 – 21135
    Helixi2115 – 21173
    Helixi2118 – 214023
    Beta strandi2142 – 21443
    Helixi2148 – 21569
    Helixi2168 – 219023
    Helixi2196 – 21994
    Turni2203 – 22053
    Helixi2206 – 22149

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    DisProtiDP00557.
    ProteinModelPortaliQ00955.
    SMRiQ00955. Positions 14-549, 1484-2202.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ00955.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini58 – 567510Biotin carboxylationAdd
    BLAST
    Domaini216 – 408193ATP-graspPROSITE-ProRule annotationAdd
    BLAST
    Domaini701 – 76767Biotinyl-bindingAdd
    BLAST
    Domaini1603 – 2101499CarboxyltransferaseAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1627 – 16293Acetyl-CoA binding

    Sequence similaritiesi

    Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
    Contains 1 biotin carboxylation domain.Curated
    Contains 1 biotinyl-binding domain.Curated
    Contains 1 carboxyltransferase domain.Curated

    Phylogenomic databases

    eggNOGiCOG0511.
    GeneTreeiENSGT00550000074703.
    HOGENOMiHOG000214115.
    KOiK11262.
    OMAiQLIAMAT.
    OrthoDBiEOG74J9H5.

    Family and domain databases

    Gene3Di3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    3.90.226.10. 3 hits.
    InterProiIPR013537. 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.
    IPR029045. ClpP/crotonase-like_dom.
    IPR011763. COA_CT_C.
    IPR011762. COA_CT_N.
    IPR016185. PreATP-grasp_dom.
    IPR011054. Rudment_hybrid_motif.
    IPR011053. Single_hybrid_motif.
    [Graphical view]
    PfamiPF08326. 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]
    SMARTiSM00878. Biotin_carb_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF51230. SSF51230. 1 hit.
    SSF51246. SSF51246. 1 hit.
    SSF52096. SSF52096. 2 hits.
    SSF52440. SSF52440. 1 hit.
    PROSITEiPS50975. 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]

    Sequencei

    Sequence statusi: Complete.

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

    Q00955-1 [UniParc]FASTAAdd to Basket

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    MSEESLFESS PQKMEYEITN YSERHTELPG HFIGLNTVDK LEESPLRDFV     50
    KSHGGHTVIS KILIANNGIA AVKEIRSVRK WAYETFGDDR TVQFVAMATP 100
    EDLEANAEYI RMADQYIEVP GGTNNNNYAN VDLIVDIAER ADVDAVWAGW 150
    GHASENPLLP EKLSQSKRKV IFIGPPGNAM RSLGDKISST IVAQSAKVPC 200
    IPWSGTGVDT VHVDEKTGLV SVDDDIYQKG CCTSPEDGLQ KAKRIGFPVM 250
    IKASEGGGGK GIRQVEREED FIALYHQAAN EIPGSPIFIM KLAGRARHLE 300
    VQLLADQYGT NISLFGRDCS VQRRHQKIIE EAPVTIAKAE TFHEMEKAAV 350
    RLGKLVGYVS AGTVEYLYSH DDGKFYFLEL NPRLQVEHPT TEMVSGVNLP 400
    AAQLQIAMGI PMHRISDIRT LYGMNPHSAS EIDFEFKTQD ATKKQRRPIP 450
    KGHCTACRIT SEDPNDGFKP SGGTLHELNF RSSSNVWGYF SVGNNGNIHS 500
    FSDSQFGHIF AFGENRQASR KHMVVALKEL SIRGDFRTTV EYLIKLLETE 550
    DFEDNTITTG WLDDLITHKM TAEKPDPTLA VICGAATKAF LASEEARHKY 600
    IESLQKGQVL SKDLLQTMFP VDFIHEGKRY KFTVAKSGND RYTLFINGSK 650
    CDIILRQLSD GGLLIAIGGK SHTIYWKEEV AATRLSVDSM TTLLEVENDP 700
    TQLRTPSPGK LVKFLVENGE HIIKGQPYAE IEVMKMQMPL VSQENGIVQL 750
    LKQPGSTIVA GDIMAIMTLD DPSKVKHALP FEGMLPDFGS PVIEGTKPAY 800
    KFKSLVSTLE NILKGYDNQV IMNASLQQLI EVLRNPKLPY SEWKLHISAL 850
    HSRLPAKLDE QMEELVARSL RRGAVFPARQ LSKLIDMAVK NPEYNPDKLL 900
    GAVVEPLADI AHKYSNGLEA HEHSIFVHFL EEYYEVEKLF NGPNVREENI 950
    ILKLRDENPK DLDKVALTVL SHSKVSAKNN LILAILKHYQ PLCKLSSKVS 1000
    AIFSTPLQHI VELESKATAK VALQAREILI QGALPSVKER TEQIEHILKS 1050
    SVVKVAYGSS NPKRSEPDLN ILKDLIDSNY VVFDVLLQFL THQDPVVTAA 1100
    AAQVYIRRAY RAYTIGDIRV HEGVTVPIVE WKFQLPSAAF STFPTVKSKM 1150
    GMNRAVSVSD LSYVANSQSS PLREGILMAV DHLDDVDEIL SQSLEVIPRH 1200
    QSSSNGPAPD RSGSSASLSN VANVCVASTE GFESEEEILV RLREILDLNK 1250
    QELINASIRR ITFMFGFKDG SYPKYYTFNG PNYNENETIR HIEPALAFQL 1300
    ELGRLSNFNI KPIFTDNRNI HVYEAVSKTS PLDKRFFTRG IIRTGHIRDD 1350
    ISIQEYLTSE ANRLMSDILD NLEVTDTSNS DLNHIFINFI AVFDISPEDV 1400
    EAAFGGFLER FGKRLLRLRV SSAEIRIIIK DPQTGAPVPL RALINNVSGY 1450
    VIKTEMYTEV KNAKGEWVFK SLGKPGSMHL RPIATPYPVK EWLQPKRYKA 1500
    HLMGTTYVYD FPELFRQASS SQWKNFSADV KLTDDFFISN ELIEDENGEL 1550
    TEVEREPGAN AIGMVAFKIT VKTPEYPRGR QFVVVANDIT FKIGSFGPQE 1600
    DEFFNKVTEY ARKRGIPRIY LAANSGARIG MAEEIVPLFQ VAWNDAANPD 1650
    KGFQYLYLTS EGMETLKKFD KENSVLTERT VINGEERFVI KTIIGSEDGL 1700
    GVECLRGSGL IAGATSRAYH DIFTITLVTC RSVGIGAYLV RLGQRAIQVE 1750
    GQPIILTGAP AINKMLGREV YTSNLQLGGT QIMYNNGVSH LTAVDDLAGV 1800
    EKIVEWMSYV PAKRNMPVPI LETKDTWDRP VDFTPTNDET YDVRWMIEGR 1850
    ETESGFEYGL FDKGSFFETL SGWAKGVVVG RARLGGIPLG VIGVETRTVE 1900
    NLIPADPANP NSAETLIQEP GQVWHPNSAF KTAQAINDFN NGEQLPMMIL 1950
    ANWRGFSGGQ RDMFNEVLKY GSFIVDALVD YKQPIIIYIP PTGELRGGSW 2000
    VVVDPTINAD QMEMYADVNA RAGVLEPQGM VGIKFRREKL LDTMNRLDDK 2050
    YRELRSQLSN KSLAPEVHQQ ISKQLADRER ELLPIYGQIS LQFADLHDRS 2100
    SRMVAKGVIS KELEWTEARR FFFWRLRRRL NEEYLIKRLS HQVGEASRLE 2150
    KIARIRSWYP ASVDHEDDRQ VATWIEENYK TLDDKLKGLK LESFAQDLAK 2200
    KIRSDHDNAI DGLSEVIKML STDDKEKLLK TLK 2233
    Length:2,233
    Mass (Da):250,353
    Last modified:October 1, 1996 - v2
    Checksum:i0A335AAD9B1F8308
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1523 – 15231W → G in AAA20073. (PubMed:1350093)Curated
    Sequence conflicti1755 – 17551I → IWYRCL in AAA20073. (PubMed:1350093)Curated
    Sequence conflicti1761 – 17666AINKML → ESTNA in AAA20073. (PubMed:1350093)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M92156 Genomic DNA. Translation: AAA20073.1.
    Z71631 Genomic DNA. Translation: CAA96294.1.
    BK006947 Genomic DNA. Translation: DAA10557.1.
    PIRiS63347.
    RefSeqiNP_014413.1. NM_001183193.1.

    Genome annotation databases

    EnsemblFungiiYNR016C; YNR016C; YNR016C.
    GeneIDi855750.
    KEGGisce:YNR016C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M92156 Genomic DNA. Translation: AAA20073.1 .
    Z71631 Genomic DNA. Translation: CAA96294.1 .
    BK006947 Genomic DNA. Translation: DAA10557.1 .
    PIRi S63347.
    RefSeqi NP_014413.1. NM_001183193.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    DisProti DP00557.
    ProteinModelPortali Q00955.
    SMRi Q00955. Positions 14-549, 1484-2202.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35841. 71 interactions.
    DIPi DIP-975N.
    IntActi Q00955. 36 interactions.
    MINTi MINT-636412.
    STRINGi 4932.YNR016C.

    Proteomic databases

    MaxQBi Q00955.
    PaxDbi Q00955.
    PeptideAtlasi Q00955.
    PRIDEi Q00955.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YNR016C ; YNR016C ; YNR016C .
    GeneIDi 855750.
    KEGGi sce:YNR016C.

    Organism-specific databases

    CYGDi YNR016c.
    SGDi S000005299. ACC1.

    Phylogenomic databases

    eggNOGi COG0511.
    GeneTreei ENSGT00550000074703.
    HOGENOMi HOG000214115.
    KOi K11262.
    OMAi QLIAMAT.
    OrthoDBi EOG74J9H5.

    Enzyme and pathway databases

    UniPathwayi UPA00655 ; UER00711 .
    BioCyci YEAST:MONOMER3O-7.
    Reactomei REACT_188404. Defective HLCS causes multiple carboxylase deficiency.
    REACT_188774. Biotin transport and metabolism.

    Miscellaneous databases

    EvolutionaryTracei Q00955.
    NextBioi 980163.

    Gene expression databases

    Genevestigatori Q00955.

    Family and domain databases

    Gene3Di 3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    3.90.226.10. 3 hits.
    InterProi 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.
    IPR005481. CarbamoylP_synth_lsu_N.
    IPR000022. Carboxyl_trans.
    IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
    IPR029045. ClpP/crotonase-like_dom.
    IPR011763. COA_CT_C.
    IPR011762. COA_CT_N.
    IPR016185. PreATP-grasp_dom.
    IPR011054. Rudment_hybrid_motif.
    IPR011053. Single_hybrid_motif.
    [Graphical view ]
    Pfami 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 ]
    SMARTi SM00878. Biotin_carb_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51230. SSF51230. 1 hit.
    SSF51246. SSF51246. 1 hit.
    SSF52096. SSF52096. 2 hits.
    SSF52440. SSF52440. 1 hit.
    PROSITEi 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 ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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. 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.

    Entry informationi

    Entry nameiACAC_YEAST
    AccessioniPrimary (citable) accession number: Q00955
    Secondary accession number(s): D6W1J1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 158 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 20200 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

    Documents

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

    External Data

    Dasty 3