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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)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

  • 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)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 methionineiRemovedCombined sources
Chaini2 – 22332232Acetyl-CoA carboxylasePRO_0000146770Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei2 – 21PhosphoserineCombined sources
Modified residuei735 – 7351N6-biotinyllysinePROSITE-ProRule annotationBy similarity
Modified residuei790 – 7901PhosphoserineCombined sources
Modified residuei1148 – 11481PhosphoserineCombined sources
Modified residuei1157 – 11571PhosphoserineCombined sources
Modified residuei1162 – 11621PhosphoserineCombined sources

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. 77 interactions.
DIPiDIP-975N.
IntActiQ00955. 36 interactions.
MINTiMINT-636412.

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
Beta strandi531 – 5366Combined sources
Helixi541 – 5477Combined sources
Helixi550 – 5534Combined sources
Helixi561 – 5655Combined sources
Helixi577 – 60529Combined sources
Helixi612 – 6154Combined sources
Beta strandi618 – 6247Combined sources
Beta strandi626 – 63611Combined sources
Beta strandi638 – 64811Combined sources
Beta strandi650 – 6578Combined sources
Beta strandi659 – 6613Combined sources
Beta strandi663 – 6697Combined sources
Beta strandi671 – 6755Combined sources
Beta strandi682 – 6876Combined sources
Beta strandi690 – 6956Combined sources
Beta strandi702 – 7043Combined sources
Beta strandi709 – 7168Combined sources
Beta strandi727 – 7337Combined sources
Beta strandi736 – 7416Combined sources
Beta strandi746 – 7505Combined sources
Beta strandi763 – 7675Combined sources
Helixi772 – 7743Combined sources
Beta strandi793 – 7953Combined sources
Helixi798 – 81316Combined sources
Helixi818 – 83316Combined sources
Helixi838 – 85013Combined sources
Helixi851 – 8533Combined sources
Helixi856 – 87116Combined sources
Helixi878 – 88912Combined sources
Turni892 – 8943Combined sources
Beta strandi896 – 8983Combined sources
Helixi900 – 91314Combined sources
Turni914 – 9163Combined sources
Helixi918 – 93720Combined sources
Helixi938 – 9403Combined sources
Beta strandi942 – 9443Combined sources
Helixi947 – 95711Combined sources
Helixi962 – 97211Combined sources
Helixi975 – 99521Combined sources
Helixi997 – 10026Combined sources
Helixi1004 – 10118Combined sources
Helixi1016 – 10183Combined sources
Helixi1019 – 103012Combined sources
Helixi1037 – 105115Combined sources
Beta strandi1054 – 10563Combined sources
Beta strandi1057 – 10593Combined sources
Beta strandi1062 – 10665Combined sources
Helixi1069 – 10768Combined sources
Helixi1083 – 10864Combined sources
Helixi1087 – 10915Combined sources
Helixi1095 – 110915Combined sources
Turni1110 – 11123Combined sources
Beta strandi1113 – 11208Combined sources
Beta strandi1124 – 11263Combined sources
Beta strandi1128 – 11347Combined sources
Helixi1138 – 11403Combined sources
Beta strandi1155 – 11573Combined sources
Helixi1158 – 11603Combined sources
Beta strandi1167 – 11704Combined sources
Beta strandi1173 – 118210Combined sources
Helixi1183 – 11853Combined sources
Helixi1186 – 11938Combined sources
Helixi1194 – 11963Combined sources
Beta strandi1220 – 12278Combined sources
Helixi1235 – 125521Combined sources
Beta strandi1258 – 12658Combined sources
Beta strandi1268 – 12703Combined sources
Beta strandi1274 – 12785Combined sources
Beta strandi1280 – 12823Combined sources
Turni1288 – 12914Combined sources
Helixi1294 – 13007Combined sources
Helixi1302 – 13054Combined sources
Beta strandi1308 – 13136Combined sources
Beta strandi1318 – 132912Combined sources
Beta strandi1334 – 13429Combined sources
Beta strandi1349 – 13513Combined sources
Helixi1353 – 137422Combined sources
Beta strandi1378 – 13803Combined sources
Beta strandi1382 – 139312Combined sources
Helixi1397 – 14037Combined sources
Turni1404 – 14063Combined sources
Helixi1407 – 141812Combined sources
Beta strandi1420 – 143011Combined sources
Turni1432 – 14343Combined sources
Beta strandi1437 – 14459Combined sources
Beta strandi1447 – 14504Combined sources
Beta strandi1455 – 14584Combined sources
Beta strandi1463 – 14653Combined sources
Beta strandi1467 – 14693Combined sources
Beta strandi1472 – 14743Combined sources
Turni1477 – 14804Combined sources
Beta strandi1482 – 14843Combined 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
Turni1633 – 16386Combined 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 strandi1812 – 18165Combined 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 – 194015Combined sources
Turni1941 – 19433Combined sources
Beta strandi1947 – 19504Combined sources
Beta strandi1953 – 19564Combined sources
Helixi1960 – 19645Combined sources
Helixi1967 – 197913Combined sources
Beta strandi1985 – 19895Combined sources
Beta strandi1994 – 19963Combined sources
Helixi1997 – 20004Combined sources
Turni2001 – 20033Combined sources
Helixi2005 – 20084Combined sources
Turni2009 – 20113Combined sources
Beta strandi2012 – 20176Combined sources
Beta strandi2021 – 20255Combined sources
Helixi2027 – 20348Combined sources
Helixi2039 – 20479Combined sources
Helixi2049 – 205810Combined sources
Helixi2059 – 20635Combined sources
Helixi2065 – 20728Combined sources
Helixi2078 – 209518Combined sources
Helixi2100 – 21067Combined sources
Beta strandi2108 – 21136Combined sources
Helixi2115 – 21173Combined sources
Helixi2118 – 213922Combined sources
Beta strandi2142 – 21443Combined sources
Helixi2148 – 215710Combined sources
Helixi2168 – 218619Combined sources
Turni2189 – 21913Combined sources
Turni2196 – 21994Combined sources
Turni2203 – 22053Combined sources
Helixi2206 – 221510Combined sources
Helixi2223 – 223311Combined 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[»]
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. 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.PROSITE-ProRule annotationCurated
Contains 1 carboxyltransferase domain.Curated

Phylogenomic databases

GeneTreeiENSGT00840000130392.
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)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.
PIRiS63347.
RefSeqiNP_014413.1. NM_001183193.1.

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[»]
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. Positions 14-549, 1484-2202.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35841. 77 interactions.
DIPiDIP-975N.
IntActiQ00955. 36 interactions.
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

GeneTreeiENSGT00840000130392.
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: September 7, 2016
This is version 179 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.