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Q00955

- ACAC_YEAST

UniProt

Q00955 - ACAC_YEAST

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Protein

Acetyl-CoA carboxylase

Gene
ACC1, ABP2, FAS3, MTR7, YNR016C, N3175
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 1 By similarity
Metal bindingi379 – 3791Manganese 1 By similarity
Metal bindingi379 – 3791Manganese 2 By similarity
Metal bindingi381 – 3811Manganese 2 By similarity
Active sitei383 – 3831 By 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 – 2616ATP By similarity

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
Complete GO annotation...

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

Cytoplasm. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side 2 Publications

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: SGD
Complete GO annotation...

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 – 11Removed1 Publication
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-biotinyllysine By 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 OPI1.4 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.

Miscellaneous databases

EvolutionaryTraceiQ00955.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini58 – 567510Biotin carboxylationAdd
BLAST
Domaini216 – 408193ATP-graspAdd
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.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1523 – 15231W → G in AAA20073. 1 Publication
Sequence conflicti1755 – 17551I → IWYRCL in AAA20073. 1 Publication
Sequence conflicti1761 – 17666AINKML → ESTNA in AAA20073. 1 Publication

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.

Chemistry

DrugBanki DB00173. Adenine.

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 ]
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Publicationsi

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  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: September 3, 2014
This is version 157 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.

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

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