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Protein

Acetyl-CoA carboxylase

Gene

ACC1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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.2 Publications
ATP + biotin-[carboxyl-carrier-protein] + HCO3- = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].By similarity

Cofactori

Protein has several cofactor binding sites:
  • biotinBy 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: malonyl-CoA biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes malonyl-CoA from acetyl-CoA.
Proteins known to be involved in this subpathway in this organism are:
  1. Acetyl-CoA carboxylase (ACC1), Acetyl-CoA carboxylase, mitochondrial (HFA1)
This subpathway is part of the pathway malonyl-CoA biosynthesis, which is itself part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes malonyl-CoA from acetyl-CoA, the pathway malonyl-CoA biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi365Manganese 1By similarity1
Metal bindingi379Manganese 1By similarity1
Metal bindingi379Manganese 2By similarity1
Metal bindingi381Manganese 2By similarity1
Active sitei383By similarity1
Binding sitei1731Coenzyme A1
Binding sitei1998Acetyl-CoA; via amide nitrogen1
Binding sitei2034Coenzyme A1
Binding sitei2036Coenzyme A1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi256 – 261ATPPROSITE-ProRule annotation6

GO - Molecular functioni

  • acetyl-CoA carboxylase activity Source: SGD
  • ATP binding Source: UniProtKB-KW
  • biotin carboxylase activity Source: SGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • long-chain fatty acid biosynthetic process Source: SGD
  • malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway
  • nuclear envelope organization Source: SGD
  • 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.
BRENDAi6.3.4.14. 984.
6.4.1.2. 984.
ReactomeiR-SCE-163765. ChREBP activates metabolic gene expression.
R-SCE-196780. Biotin transport and metabolism.
R-SCE-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
R-SCE-75105. Fatty Acyl-CoA Biosynthesis.
UniPathwayiUPA00655; UER00711.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA carboxylase (EC:6.4.1.22 Publications)
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
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNR016C.
SGDiS000005299. ACC1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1705L → I: Raises KM for malonyl-CoA by a factor of 20. 1 Publication1
Mutagenesisi1731R → S: Raises KM for malonyl-CoA by a factor of 15. 1 Publication1
Mutagenesisi1738Y → F: No effect. 1 Publication1
Mutagenesisi1954R → S: Raises KM for malonyl-CoA by a factor of 70. 1 Publication1
Mutagenesisi1994E → Q: Lowers activity 10-fold. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001467702 – 2233Acetyl-CoA carboxylaseAdd BLAST2232

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei2PhosphoserineCombined sources1
Modified residuei735N6-biotinyllysinePROSITE-ProRule annotationBy similarity1
Modified residuei790PhosphoserineCombined sources1
Modified residuei1148PhosphoserineCombined sources1
Modified residuei1157PhosphoserineCombined sources1
Modified residuei1162PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ00955.
PRIDEiQ00955.

PTM databases

iPTMnetiQ00955.

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

Interactioni

Subunit structurei

Homodimer.3 Publications

Protein-protein interaction databases

BioGridi35841. 78 interactors.
DIPiDIP-975N.
IntActiQ00955. 36 interactors.
MINTiMINT-636412.

Structurei

Secondary structure

12233
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi22 – 27Combined sources6
Helixi30 – 32Combined sources3
Beta strandi35 – 37Combined sources3
Helixi38 – 40Combined sources3
Helixi45 – 52Combined sources8
Beta strandi61 – 64Combined sources4
Helixi68 – 86Combined sources19
Beta strandi91 – 98Combined sources8
Helixi100 – 104Combined sources5
Helixi108 – 112Combined sources5
Beta strandi113 – 118Combined sources6
Helixi124 – 126Combined sources3
Turni127 – 129Combined sources3
Helixi131 – 140Combined sources10
Beta strandi144 – 147Combined sources4
Turni152 – 155Combined sources4
Helixi158 – 165Combined sources8
Beta strandi171 – 174Combined sources4
Helixi177 – 182Combined sources6
Helixi186 – 195Combined sources10
Turni204 – 207Combined sources4
Turni215 – 217Combined sources3
Helixi224 – 227Combined sources4
Helixi228 – 230Combined sources3
Helixi235 – 245Combined sources11
Beta strandi247 – 253Combined sources7
Turni258 – 261Combined sources4
Beta strandi262 – 265Combined sources4
Helixi268 – 281Combined sources14
Beta strandi287 – 291Combined sources5
Beta strandi297 – 305Combined sources9
Turni307 – 309Combined sources3
Beta strandi311 – 323Combined sources13
Beta strandi326 – 333Combined sources8
Helixi339 – 356Combined sources18
Beta strandi360 – 368Combined sources9
Turni370 – 372Combined sources3
Beta strandi375 – 381Combined sources7
Helixi388 – 395Combined sources8
Helixi399 – 407Combined sources9
Helixi412 – 414Combined sources3
Helixi416 – 421Combined sources6
Helixi439 – 444Combined sources6
Beta strandi452 – 462Combined sources11
Beta strandi466 – 468Combined sources3
Beta strandi472 – 478Combined sources7
Beta strandi484 – 492Combined sources9
Beta strandi503 – 515Combined sources13
Helixi516 – 530Combined sources15
Beta strandi531 – 536Combined sources6
Helixi541 – 547Combined sources7
Helixi550 – 553Combined sources4
Helixi561 – 565Combined sources5
Helixi577 – 605Combined sources29
Helixi612 – 615Combined sources4
Beta strandi618 – 624Combined sources7
Beta strandi626 – 636Combined sources11
Beta strandi638 – 648Combined sources11
Beta strandi650 – 657Combined sources8
Beta strandi659 – 661Combined sources3
Beta strandi663 – 669Combined sources7
Beta strandi671 – 675Combined sources5
Beta strandi682 – 687Combined sources6
Beta strandi690 – 695Combined sources6
Beta strandi702 – 704Combined sources3
Beta strandi709 – 716Combined sources8
Beta strandi727 – 733Combined sources7
Beta strandi736 – 741Combined sources6
Beta strandi746 – 750Combined sources5
Beta strandi763 – 767Combined sources5
Helixi772 – 774Combined sources3
Beta strandi793 – 795Combined sources3
Helixi798 – 813Combined sources16
Helixi818 – 833Combined sources16
Helixi838 – 850Combined sources13
Helixi851 – 853Combined sources3
Helixi856 – 871Combined sources16
Helixi878 – 889Combined sources12
Turni892 – 894Combined sources3
Beta strandi896 – 898Combined sources3
Helixi900 – 913Combined sources14
Turni914 – 916Combined sources3
Helixi918 – 937Combined sources20
Helixi938 – 940Combined sources3
Beta strandi942 – 944Combined sources3
Helixi947 – 957Combined sources11
Helixi962 – 972Combined sources11
Helixi975 – 995Combined sources21
Helixi997 – 1002Combined sources6
Helixi1004 – 1011Combined sources8
Helixi1016 – 1018Combined sources3
Helixi1019 – 1030Combined sources12
Helixi1037 – 1051Combined sources15
Beta strandi1054 – 1056Combined sources3
Beta strandi1057 – 1059Combined sources3
Beta strandi1062 – 1066Combined sources5
Helixi1069 – 1076Combined sources8
Helixi1083 – 1086Combined sources4
Helixi1087 – 1091Combined sources5
Helixi1095 – 1109Combined sources15
Turni1110 – 1112Combined sources3
Beta strandi1113 – 1120Combined sources8
Beta strandi1124 – 1126Combined sources3
Beta strandi1128 – 1134Combined sources7
Helixi1138 – 1140Combined sources3
Beta strandi1155 – 1157Combined sources3
Helixi1158 – 1160Combined sources3
Beta strandi1167 – 1170Combined sources4
Beta strandi1173 – 1182Combined sources10
Helixi1183 – 1185Combined sources3
Helixi1186 – 1193Combined sources8
Helixi1194 – 1196Combined sources3
Beta strandi1220 – 1227Combined sources8
Helixi1235 – 1255Combined sources21
Beta strandi1258 – 1265Combined sources8
Beta strandi1268 – 1270Combined sources3
Beta strandi1274 – 1278Combined sources5
Beta strandi1280 – 1282Combined sources3
Turni1288 – 1291Combined sources4
Helixi1294 – 1300Combined sources7
Helixi1302 – 1305Combined sources4
Beta strandi1308 – 1313Combined sources6
Beta strandi1318 – 1329Combined sources12
Beta strandi1334 – 1342Combined sources9
Beta strandi1349 – 1351Combined sources3
Helixi1353 – 1374Combined sources22
Beta strandi1378 – 1380Combined sources3
Beta strandi1382 – 1393Combined sources12
Helixi1397 – 1403Combined sources7
Turni1404 – 1406Combined sources3
Helixi1407 – 1418Combined sources12
Beta strandi1420 – 1430Combined sources11
Turni1432 – 1434Combined sources3
Beta strandi1437 – 1445Combined sources9
Beta strandi1447 – 1450Combined sources4
Beta strandi1455 – 1458Combined sources4
Beta strandi1463 – 1465Combined sources3
Beta strandi1467 – 1469Combined sources3
Beta strandi1472 – 1474Combined sources3
Turni1477 – 1480Combined sources4
Beta strandi1482 – 1484Combined sources3
Helixi1490 – 1493Combined sources4
Helixi1495 – 1502Combined sources8
Helixi1508 – 1510Combined sources3
Helixi1511 – 1526Combined sources16
Helixi1534 – 1536Combined sources3
Beta strandi1537 – 1544Combined sources8
Beta strandi1546 – 1548Combined sources3
Beta strandi1550 – 1553Combined sources4
Beta strandi1561 – 1571Combined sources11
Beta strandi1580 – 1587Combined sources8
Helixi1592 – 1594Combined sources3
Helixi1598 – 1614Combined sources17
Beta strandi1618 – 1622Combined sources5
Turni1633 – 1638Combined sources6
Beta strandi1640 – 1645Combined sources6
Helixi1649 – 1651Combined sources3
Beta strandi1653 – 1658Combined sources6
Helixi1660 – 1668Combined sources9
Helixi1672 – 1674Combined sources3
Beta strandi1675 – 1682Combined sources8
Beta strandi1685 – 1693Combined sources9
Beta strandi1696 – 1698Combined sources3
Helixi1702 – 1719Combined sources18
Beta strandi1724 – 1728Combined sources5
Helixi1735 – 1742Combined sources8
Beta strandi1745 – 1749Combined sources5
Beta strandi1754 – 1757Combined sources4
Helixi1759 – 1766Combined sources8
Helixi1775 – 1778Combined sources4
Helixi1780 – 1783Combined sources4
Turni1784 – 1787Combined sources4
Beta strandi1788 – 1795Combined sources8
Helixi1796 – 1807Combined sources12
Beta strandi1812 – 1816Combined sources5
Beta strandi1827 – 1829Combined sources3
Beta strandi1837 – 1839Combined sources3
Helixi1843 – 1848Combined sources6
Beta strandi1850 – 1852Combined sources3
Beta strandi1855 – 1857Combined sources3
Beta strandi1867 – 1870Combined sources4
Beta strandi1877 – 1884Combined sources8
Beta strandi1887 – 1894Combined sources8
Beta strandi1899 – 1903Combined sources5
Beta strandi1909 – 1911Combined sources3
Beta strandi1915 – 1919Combined sources5
Helixi1926 – 1940Combined sources15
Turni1941 – 1943Combined sources3
Beta strandi1947 – 1950Combined sources4
Beta strandi1953 – 1956Combined sources4
Helixi1960 – 1964Combined sources5
Helixi1967 – 1979Combined sources13
Beta strandi1985 – 1989Combined sources5
Beta strandi1994 – 1996Combined sources3
Helixi1997 – 2000Combined sources4
Turni2001 – 2003Combined sources3
Helixi2005 – 2008Combined sources4
Turni2009 – 2011Combined sources3
Beta strandi2012 – 2017Combined sources6
Beta strandi2021 – 2025Combined sources5
Helixi2027 – 2034Combined sources8
Helixi2039 – 2047Combined sources9
Helixi2049 – 2058Combined sources10
Helixi2059 – 2063Combined sources5
Helixi2065 – 2072Combined sources8
Helixi2078 – 2095Combined sources18
Helixi2100 – 2106Combined sources7
Beta strandi2108 – 2113Combined sources6
Helixi2115 – 2117Combined sources3
Helixi2118 – 2139Combined sources22
Beta strandi2142 – 2144Combined sources3
Helixi2148 – 2157Combined sources10
Helixi2168 – 2186Combined sources19
Turni2189 – 2191Combined sources3
Turni2196 – 2199Combined sources4
Turni2203 – 2205Combined sources3
Helixi2206 – 2215Combined sources10
Helixi2223 – 2233Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4WYOX-ray2.89B/C1476-2233[»]
4WZ8X-ray2.23B/C1476-2233[»]
5CS0X-ray2.50A/B797-1033[»]
5CS4X-ray3.19A/B1036-1503[»]
5CSAX-ray3.00A/B569-1494[»]
5CSKX-ray3.10A/B22-2233[»]
5CSLX-ray3.20A/B22-2233[»]
5CTBX-ray2.40A/B/C1476-2233[»]
5CTCX-ray2.70A/B/C1476-2233[»]
5CTEX-ray2.34B/C1476-2233[»]
5I6EX-ray3.00A768-1494[»]
DisProtiDP00557.
ProteinModelPortaliQ00955.
SMRiQ00955.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00955.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini58 – 567Biotin carboxylationAdd BLAST510
Domaini216 – 408ATP-graspPROSITE-ProRule annotationAdd BLAST193
Domaini694 – 768Biotinyl-bindingPROSITE-ProRule annotationAdd BLAST75
Domaini1486 – 1822CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST337
Domaini1826 – 2141CoA carboxyltransferase C-terminalPROSITE-ProRule annotationAdd BLAST316

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1486 – 2141CarboxyltransferasePROSITE-ProRule annotationAdd BLAST656
Regioni1627 – 1629Acetyl-CoA binding3

Sequence similaritiesi

Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
Contains 1 biotin carboxylation domain.Curated
Contains 1 biotinyl-binding domain.PROSITE-ProRule annotationCurated
Contains 1 CoA carboxyltransferase C-terminal domain.PROSITE-ProRule annotation
Contains 1 CoA carboxyltransferase N-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000074703.
HOGENOMiHOG000214115.
InParanoidiQ00955.
KOiK11262.
OMAiLEWTEAR.
OrthoDBiEOG092C00TE.

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.
IPR005481. BC-like_N.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
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.
PF00289. Biotin_carb_N. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF01039. Carboxyl_trans. 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

« Hide

        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)DescriptionActionsGraphical viewLength
Sequence conflicti1523W → G in AAA20073 (PubMed:1350093).Curated1
Sequence conflicti1755I → IWYRCL in AAA20073 (PubMed:1350093).Curated1
Sequence conflicti1761 – 1766AINKML → ESTNA in AAA20073 (PubMed:1350093).Curated6

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.
PIRiS63347.
RefSeqiNP_014413.1. NM_001183193.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4WYOX-ray2.89B/C1476-2233[»]
4WZ8X-ray2.23B/C1476-2233[»]
5CS0X-ray2.50A/B797-1033[»]
5CS4X-ray3.19A/B1036-1503[»]
5CSAX-ray3.00A/B569-1494[»]
5CSKX-ray3.10A/B22-2233[»]
5CSLX-ray3.20A/B22-2233[»]
5CTBX-ray2.40A/B/C1476-2233[»]
5CTCX-ray2.70A/B/C1476-2233[»]
5CTEX-ray2.34B/C1476-2233[»]
5I6EX-ray3.00A768-1494[»]
DisProtiDP00557.
ProteinModelPortaliQ00955.
SMRiQ00955.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35841. 78 interactors.
DIPiDIP-975N.
IntActiQ00955. 36 interactors.
MINTiMINT-636412.

PTM databases

iPTMnetiQ00955.

Proteomic databases

MaxQBiQ00955.
PRIDEiQ00955.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YNR016C.
SGDiS000005299. ACC1.

Phylogenomic databases

GeneTreeiENSGT00550000074703.
HOGENOMiHOG000214115.
InParanoidiQ00955.
KOiK11262.
OMAiLEWTEAR.
OrthoDBiEOG092C00TE.

Enzyme and pathway databases

UniPathwayiUPA00655; UER00711.
BioCyciYEAST:MONOMER3O-7.
BRENDAi6.3.4.14. 984.
6.4.1.2. 984.
ReactomeiR-SCE-163765. ChREBP activates metabolic gene expression.
R-SCE-196780. Biotin transport and metabolism.
R-SCE-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
R-SCE-75105. Fatty Acyl-CoA Biosynthesis.

Miscellaneous databases

EvolutionaryTraceiQ00955.
PROiQ00955.

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.
IPR005481. BC-like_N.
IPR001882. Biotin_BS.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR000089. Biotin_lipoyl.
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.
PF00289. Biotin_carb_N. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF01039. Carboxyl_trans. 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]
ProtoNetiSearch...

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 30, 2016
This is version 182 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.