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Q00955

- ACAC_YEAST

UniProt

Q00955 - ACAC_YEAST

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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

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

Protein has several cofactor binding sites:
  • biotinBy similarityNote: Biotin.By similarity
  • Mn2+By similarityNote: 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
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.
REACT_241476. ChREBP activates metabolic gene expression.
REACT_258513. Fatty Acyl-CoA Biosynthesis.
REACT_260529. Import of palmitoyl-CoA into the mitochondrial matrix.
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
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 – 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 similarityPROSITE-ProRule annotation
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. 72 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 – 276Combined sources
Helixi30 – 323Combined sources
Beta strandi35 – 373Combined sources
Helixi38 – 403Combined sources
Helixi45 – 528Combined sources
Beta strandi61 – 644Combined sources
Helixi68 – 8619Combined sources
Beta strandi91 – 988Combined sources
Helixi100 – 1045Combined sources
Helixi108 – 1125Combined sources
Beta strandi113 – 1186Combined sources
Helixi124 – 1263Combined sources
Turni127 – 1293Combined sources
Helixi131 – 14010Combined sources
Beta strandi144 – 1474Combined sources
Turni152 – 1554Combined sources
Helixi158 – 1658Combined sources
Beta strandi171 – 1744Combined sources
Helixi177 – 1826Combined sources
Helixi186 – 19510Combined sources
Turni204 – 2074Combined sources
Turni215 – 2173Combined sources
Helixi224 – 2274Combined sources
Helixi228 – 2303Combined sources
Helixi235 – 24511Combined sources
Beta strandi247 – 2537Combined sources
Turni258 – 2614Combined sources
Beta strandi262 – 2654Combined sources
Helixi268 – 28114Combined sources
Beta strandi287 – 2915Combined sources
Beta strandi297 – 3059Combined sources
Turni307 – 3093Combined sources
Beta strandi311 – 32313Combined sources
Beta strandi326 – 3338Combined sources
Helixi339 – 35618Combined sources
Beta strandi360 – 3689Combined sources
Turni370 – 3723Combined sources
Beta strandi375 – 3817Combined sources
Helixi388 – 3958Combined sources
Helixi399 – 4079Combined sources
Helixi412 – 4143Combined sources
Helixi416 – 4216Combined sources
Helixi439 – 4446Combined sources
Beta strandi452 – 46211Combined sources
Beta strandi466 – 4683Combined sources
Beta strandi472 – 4787Combined sources
Beta strandi484 – 4929Combined sources
Beta strandi503 – 51513Combined sources
Helixi516 – 53015Combined sources
Helixi541 – 5477Combined sources
Helixi550 – 5534Combined sources
Helixi561 – 5655Combined sources
Helixi1490 – 14934Combined sources
Helixi1495 – 15028Combined sources
Helixi1508 – 15103Combined sources
Helixi1511 – 152616Combined sources
Helixi1534 – 15363Combined sources
Beta strandi1537 – 15448Combined sources
Beta strandi1546 – 15483Combined sources
Beta strandi1550 – 15534Combined sources
Beta strandi1561 – 157111Combined sources
Beta strandi1580 – 15878Combined sources
Helixi1592 – 15943Combined sources
Helixi1598 – 161417Combined sources
Beta strandi1618 – 16225Combined sources
Helixi1633 – 16353Combined sources
Turni1636 – 16383Combined sources
Beta strandi1640 – 16456Combined sources
Helixi1649 – 16513Combined sources
Beta strandi1653 – 16586Combined sources
Helixi1660 – 16689Combined sources
Helixi1672 – 16743Combined sources
Beta strandi1675 – 16828Combined sources
Beta strandi1685 – 16939Combined sources
Beta strandi1696 – 16983Combined sources
Helixi1702 – 171918Combined sources
Beta strandi1724 – 17285Combined sources
Helixi1735 – 17428Combined sources
Beta strandi1745 – 17495Combined sources
Beta strandi1754 – 17574Combined sources
Helixi1759 – 17668Combined sources
Helixi1775 – 17784Combined sources
Helixi1780 – 17834Combined sources
Turni1784 – 17874Combined sources
Beta strandi1788 – 17958Combined sources
Helixi1796 – 180712Combined sources
Beta strandi1827 – 18293Combined sources
Beta strandi1837 – 18393Combined sources
Helixi1843 – 18486Combined sources
Beta strandi1850 – 18523Combined sources
Beta strandi1855 – 18573Combined sources
Beta strandi1867 – 18704Combined sources
Beta strandi1877 – 18848Combined sources
Beta strandi1887 – 18948Combined sources
Beta strandi1899 – 19035Combined sources
Beta strandi1909 – 19113Combined sources
Beta strandi1915 – 19195Combined sources
Helixi1926 – 194116Combined sources
Beta strandi1947 – 19493Combined sources
Beta strandi1953 – 19564Combined sources
Helixi1960 – 19645Combined sources
Helixi1967 – 197913Combined sources
Beta strandi1985 – 19895Combined sources
Beta strandi1994 – 19963Combined sources
Helixi1998 – 20014Combined sources
Helixi2005 – 20073Combined sources
Turni2009 – 20113Combined sources
Beta strandi2012 – 20176Combined sources
Beta strandi2021 – 20255Combined sources
Helixi2027 – 20348Combined sources
Helixi2037 – 204711Combined sources
Turni2049 – 20513Combined sources
Helixi2083 – 209513Combined sources
Helixi2100 – 21067Combined sources
Beta strandi2109 – 21135Combined sources
Helixi2115 – 21173Combined sources
Helixi2118 – 214023Combined sources
Beta strandi2142 – 21443Combined sources
Helixi2148 – 21569Combined sources
Helixi2168 – 219023Combined sources
Helixi2196 – 21994Combined sources
Turni2203 – 22053Combined sources
Helixi2206 – 22149Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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
Domaini694 – 76875Biotinyl-bindingPROSITE-ProRule annotationAdd
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.CuratedPROSITE-ProRule annotation
Contains 1 carboxyltransferase domain.Curated

Phylogenomic databases

eggNOGiCOG0511.
GeneTreeiENSGT00550000074703.
HOGENOMiHOG000214115.
InParanoidiQ00955.
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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        10         20         30         40         50
MSEESLFESS PQKMEYEITN YSERHTELPG HFIGLNTVDK LEESPLRDFV
60 70 80 90 100
KSHGGHTVIS KILIANNGIA AVKEIRSVRK WAYETFGDDR TVQFVAMATP
110 120 130 140 150
EDLEANAEYI RMADQYIEVP GGTNNNNYAN VDLIVDIAER ADVDAVWAGW
160 170 180 190 200
GHASENPLLP EKLSQSKRKV IFIGPPGNAM RSLGDKISST IVAQSAKVPC
210 220 230 240 250
IPWSGTGVDT VHVDEKTGLV SVDDDIYQKG CCTSPEDGLQ KAKRIGFPVM
260 270 280 290 300
IKASEGGGGK GIRQVEREED FIALYHQAAN EIPGSPIFIM KLAGRARHLE
310 320 330 340 350
VQLLADQYGT NISLFGRDCS VQRRHQKIIE EAPVTIAKAE TFHEMEKAAV
360 370 380 390 400
RLGKLVGYVS AGTVEYLYSH DDGKFYFLEL NPRLQVEHPT TEMVSGVNLP
410 420 430 440 450
AAQLQIAMGI PMHRISDIRT LYGMNPHSAS EIDFEFKTQD ATKKQRRPIP
460 470 480 490 500
KGHCTACRIT SEDPNDGFKP SGGTLHELNF RSSSNVWGYF SVGNNGNIHS
510 520 530 540 550
FSDSQFGHIF AFGENRQASR KHMVVALKEL SIRGDFRTTV EYLIKLLETE
560 570 580 590 600
DFEDNTITTG WLDDLITHKM TAEKPDPTLA VICGAATKAF LASEEARHKY
610 620 630 640 650
IESLQKGQVL SKDLLQTMFP VDFIHEGKRY KFTVAKSGND RYTLFINGSK
660 670 680 690 700
CDIILRQLSD GGLLIAIGGK SHTIYWKEEV AATRLSVDSM TTLLEVENDP
710 720 730 740 750
TQLRTPSPGK LVKFLVENGE HIIKGQPYAE IEVMKMQMPL VSQENGIVQL
760 770 780 790 800
LKQPGSTIVA GDIMAIMTLD DPSKVKHALP FEGMLPDFGS PVIEGTKPAY
810 820 830 840 850
KFKSLVSTLE NILKGYDNQV IMNASLQQLI EVLRNPKLPY SEWKLHISAL
860 870 880 890 900
HSRLPAKLDE QMEELVARSL RRGAVFPARQ LSKLIDMAVK NPEYNPDKLL
910 920 930 940 950
GAVVEPLADI AHKYSNGLEA HEHSIFVHFL EEYYEVEKLF NGPNVREENI
960 970 980 990 1000
ILKLRDENPK DLDKVALTVL SHSKVSAKNN LILAILKHYQ PLCKLSSKVS
1010 1020 1030 1040 1050
AIFSTPLQHI VELESKATAK VALQAREILI QGALPSVKER TEQIEHILKS
1060 1070 1080 1090 1100
SVVKVAYGSS NPKRSEPDLN ILKDLIDSNY VVFDVLLQFL THQDPVVTAA
1110 1120 1130 1140 1150
AAQVYIRRAY RAYTIGDIRV HEGVTVPIVE WKFQLPSAAF STFPTVKSKM
1160 1170 1180 1190 1200
GMNRAVSVSD LSYVANSQSS PLREGILMAV DHLDDVDEIL SQSLEVIPRH
1210 1220 1230 1240 1250
QSSSNGPAPD RSGSSASLSN VANVCVASTE GFESEEEILV RLREILDLNK
1260 1270 1280 1290 1300
QELINASIRR ITFMFGFKDG SYPKYYTFNG PNYNENETIR HIEPALAFQL
1310 1320 1330 1340 1350
ELGRLSNFNI KPIFTDNRNI HVYEAVSKTS PLDKRFFTRG IIRTGHIRDD
1360 1370 1380 1390 1400
ISIQEYLTSE ANRLMSDILD NLEVTDTSNS DLNHIFINFI AVFDISPEDV
1410 1420 1430 1440 1450
EAAFGGFLER FGKRLLRLRV SSAEIRIIIK DPQTGAPVPL RALINNVSGY
1460 1470 1480 1490 1500
VIKTEMYTEV KNAKGEWVFK SLGKPGSMHL RPIATPYPVK EWLQPKRYKA
1510 1520 1530 1540 1550
HLMGTTYVYD FPELFRQASS SQWKNFSADV KLTDDFFISN ELIEDENGEL
1560 1570 1580 1590 1600
TEVEREPGAN AIGMVAFKIT VKTPEYPRGR QFVVVANDIT FKIGSFGPQE
1610 1620 1630 1640 1650
DEFFNKVTEY ARKRGIPRIY LAANSGARIG MAEEIVPLFQ VAWNDAANPD
1660 1670 1680 1690 1700
KGFQYLYLTS EGMETLKKFD KENSVLTERT VINGEERFVI KTIIGSEDGL
1710 1720 1730 1740 1750
GVECLRGSGL IAGATSRAYH DIFTITLVTC RSVGIGAYLV RLGQRAIQVE
1760 1770 1780 1790 1800
GQPIILTGAP AINKMLGREV YTSNLQLGGT QIMYNNGVSH LTAVDDLAGV
1810 1820 1830 1840 1850
EKIVEWMSYV PAKRNMPVPI LETKDTWDRP VDFTPTNDET YDVRWMIEGR
1860 1870 1880 1890 1900
ETESGFEYGL FDKGSFFETL SGWAKGVVVG RARLGGIPLG VIGVETRTVE
1910 1920 1930 1940 1950
NLIPADPANP NSAETLIQEP GQVWHPNSAF KTAQAINDFN NGEQLPMMIL
1960 1970 1980 1990 2000
ANWRGFSGGQ RDMFNEVLKY GSFIVDALVD YKQPIIIYIP PTGELRGGSW
2010 2020 2030 2040 2050
VVVDPTINAD QMEMYADVNA RAGVLEPQGM VGIKFRREKL LDTMNRLDDK
2060 2070 2080 2090 2100
YRELRSQLSN KSLAPEVHQQ ISKQLADRER ELLPIYGQIS LQFADLHDRS
2110 2120 2130 2140 2150
SRMVAKGVIS KELEWTEARR FFFWRLRRRL NEEYLIKRLS HQVGEASRLE
2160 2170 2180 2190 2200
KIARIRSWYP ASVDHEDDRQ VATWIEENYK TLDDKLKGLK LESFAQDLAK
2210 2220 2230
KIRSDHDNAI DGLSEVIKML STDDKEKLLK TLK
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 72 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.
InParanoidi Q00955.
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.
REACT_241476. ChREBP activates metabolic gene expression.
REACT_258513. Fatty Acyl-CoA Biosynthesis.
REACT_260529. Import of palmitoyl-CoA into the mitochondrial matrix.

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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 160 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