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Protein

Acetyl-CoA carboxylase

Gene

ACAC

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.By similarity

Catalytic activityi

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.By similarity
ATP + [biotin carboxyl-carrier protein]-biotin-N6-L-lysine + hydrogencarbonate- = ADP + phosphate + [biotin carboxyl-carrier protein]-carboxybiotin-N6-L-lysine.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.

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 (ACAC)
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 bindingi424Manganese 1By similarity1
Metal bindingi437Manganese 1By similarity1
Metal bindingi437Manganese 2By similarity1
Metal bindingi439Manganese 2By similarity1
Active sitei441By similarity1
Binding sitei1800Coenzyme ABy similarity1
Binding sitei2104Coenzyme ABy similarity1
Binding sitei2106Coenzyme ABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi315 – 320ATPPROSITE-ProRule annotation6

GO - Molecular functioni

  • acetyl-CoA carboxylase activity Source: AgBase
  • ATP binding Source: AgBase
  • biotin binding Source: AgBase
  • biotin carboxylase activity Source: AgBase
  • DBD domain binding Source: AgBase
  • metal ion binding Source: UniProtKB-KW
  • signaling receptor binding Source: AgBase
  • sterol response element binding Source: AgBase
  • thyroid hormone receptor binding Source: AgBase

GO - Biological processi

  • fatty acid biosynthetic process Source: AgBase
  • malonyl-CoA biosynthetic process Source: AgBase
  • positive regulation of gene expression Source: AgBase
  • positive regulation of transcription, DNA-templated Source: AgBase
  • regulation of biological quality Source: AgBase
  • regulation of gene expression, epigenetic Source: AgBase
  • response to carbohydrate Source: AgBase
  • response to fatty acid Source: AgBase
  • response to thyroid hormone Source: AgBase
  • transport Source: AgBase

Keywordsi

Molecular functionLigase, Multifunctional enzyme
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandATP-binding, Biotin, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RKiP11029
UniPathwayiUPA00655; UER00711

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA carboxylase (EC:6.4.1.2)
Short name:
ACC
Including the following 1 domains:
Biotin carboxylase (EC:6.3.4.14)
Gene namesi
Name:ACAC
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001467681 – 2324Acetyl-CoA carboxylaseAdd BLAST2324

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine1 Publication1
Modified residuei78PhosphoserineBy similarity1
Modified residuei80PhosphoserineBy similarity1
Modified residuei786N6-biotinyllysinePROSITE-ProRule annotation1 Publication1
Modified residuei1193PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP11029

Interactioni

GO - Molecular functioni

  • DBD domain binding Source: AgBase
  • signaling receptor binding Source: AgBase
  • thyroid hormone receptor binding Source: AgBase

Protein-protein interaction databases

BioGridi676751, 1 interactor

Structurei

3D structure databases

ProteinModelPortaliP11029
SMRiP11029
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini117 – 618Biotin carboxylationAdd BLAST502
Domaini275 – 466ATP-graspPROSITE-ProRule annotationAdd BLAST192
Domaini745 – 819Biotinyl-bindingPROSITE-ProRule annotationAdd BLAST75
Domaini1553 – 1891CoA carboxyltransferase N-terminalPROSITE-ProRule annotationAdd BLAST339
Domaini1895 – 2211CoA carboxyltransferase C-terminalPROSITE-ProRule annotationAdd BLAST317

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1553 – 2211CarboxyltransferasePROSITE-ProRule annotationAdd BLAST659

Phylogenomic databases

HOVERGENiHBG005371
InParanoidiP11029
KOiK11262
PhylomeDBiP11029

Family and domain databases

Gene3Di3.30.1490.20, 1 hit
InterProiView protein in InterPro
IPR034733 AcCoA_carboxyl
IPR013537 AcCoA_COase_cen
IPR011761 ATP-grasp
IPR013815 ATP_grasp_subdomain_1
IPR005481 BC-like_N
IPR001882 Biotin_BS
IPR011764 Biotin_carboxylation_dom
IPR005482 Biotin_COase_C
IPR000089 Biotin_lipoyl
IPR005479 CbamoylP_synth_lsu-like_ATP-bd
IPR029045 ClpP/crotonase-like_dom_sf
IPR011763 COA_CT_C
IPR011762 COA_CT_N
IPR016185 PreATP-grasp_dom_sf
IPR011054 Rudment_hybrid_motif
IPR011053 Single_hybrid_motif
PfamiView protein in Pfam
PF08326 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
SMARTiView protein in SMART
SM00878 Biotin_carb_C, 1 hit
SUPFAMiSSF51230 SSF51230, 1 hit
SSF51246 SSF51246, 1 hit
SSF52096 SSF52096, 2 hits
SSF52440 SSF52440, 1 hit
PROSITEiView protein in PROSITE
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

Sequencei

Sequence statusi: Complete.

P11029-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEESSQPAKP LEMNPHSRFI IGSVSEDNSE DETSSLVKLD LLEEKERSLS
60 70 80 90 100
PVSVCSDSLS DLGLPSAQDG LANHMRPSMS GLHLVKQGRD RKKVDVQRDF
110 120 130 140 150
TVASPAEFVT RFGGNRVIEK VLIANNGIAA VKCMRSIRRW SYEMFRNERA
160 170 180 190 200
IRFVVMVTPE DLKANAEYIK MADHYVPVPG GPNNNNYANV ELILDIAKRI
210 220 230 240 250
PVQAVWAGWG HASENPKLPE LLHKNGIAFM GPPSQAMWAL GDKIASSIVA
260 270 280 290 300
QTAGIPTLPW NGSGLRVDWQ ENDLQKRILN VPQELYEKGY VKDADDGLRA
310 320 330 340 350
AEEVGYPVMI KASEGGGGKG IRKVNNADDF PNLFRQVQAE VPGSPIFVMR
360 370 380 390 400
LAKQSRHLEV QILADQYGNA ISLFGRDCSV QRRHQKIIEE APASIATSVV
410 420 430 440 450
FEHMEQCAVK LAKMVGYVSA GTVEYLYSQD GSFYFLELNP RLQVEHPCTE
460 470 480 490 500
MVADVNLPAA QLQIAMGIPL HRIKDIRVMY GVSPWGDGSI DFENSAHVPC
510 520 530 540 550
PRGHVIAARI TSENPDEGFK PSSGTVQELN FRSNKNVWGY FSVAAAGGLH
560 570 580 590 600
EFADSQFGHC FSWGENREEA ISNMVVALKE LSIRGDFRTT VEYLIKLLET
610 620 630 640 650
ESFQQNRIDT GWLDRLIAEK VQAERPDTML GVVCGALHVA DVSFRNSVSN
660 670 680 690 700
FLHSLERGQV LPAHTLLNTV DVELIYEGRK YVLKVTRQSP NSYVVIMNSS
710 720 730 740 750
CVEVDVHRLS DGGLLLSYDG SSYTTYMKEE VDRYRITIGN KTCVFEKEND
760 770 780 790 800
PSILRSPSAG KLIQYVVEDG GHVFAGQCFA EIEVMKMVMT LTAGESGCIH
810 820 830 840 850
YVKRPGAVLD PGCVIAKLQL DDPSRVQQAE LHTGTLPQIQ STALRGEKLH
860 870 880 890 900
RIFHYVLDNL VNVMNGYCLP EPYFSSKVKG WVERLMKTLR DPSLPLLELQ
910 920 930 940 950
DIMTSVSGRI PPNVEKSIKK EMAQYASNIT SVLCQFPSQQ IANILDSHAA
960 970 980 990 1000
TLNRKSEREV FFMNTQSIVQ LVQRYRSGIR GHMKAVVMDL LRQYLKVETQ
1010 1020 1030 1040 1050
FQHGHYDKCV FALREENKSD MNAVLNYIFS HAQVTKKNLL VTMLIDQLCG
1060 1070 1080 1090 1100
RDPTLTDELI NILTELTQLS KTTNAKVALR ARQVLIASHL PSYELRHNQV
1110 1120 1130 1140 1150
ESIFLSAIDM YGHQFCIENL QKLILSETSI FDVLPNFFYH SNQVVRMAAL
1160 1170 1180 1190 1200
EVYVRRAYIA YELNSVQHRQ LKDNTCVVEF QFMLPTSHPN RMSFSSNLNH
1210 1220 1230 1240 1250
YGMVHVASVS DVLLDNSFTP PCQRMGGMVS FRTFEDFVRI FDEVMSCFCD
1260 1270 1280 1290 1300
SPPQSPTFPE AGHASLYDED KAAREEPIHI LNVAIKTDGD VDDDGLAAMF
1310 1320 1330 1340 1350
REFTQSKKSV LIEHGIRRLT FLVAQKREFP KFFTFRARDK FEEDRIYRHL
1360 1370 1380 1390 1400
EPALAFQLEL NRMRNFDLTA IPCANHKMHL YLGAAKVEVG TEVTDYRFFV
1410 1420 1430 1440 1450
RAIIRHSDLV TKEASFEYLQ NEGERLLLEA MDELEVAFNN TNVRTDCNHI
1460 1470 1480 1490 1500
FLNFVPTVIM DPSKIEESVR SMVMRYGSRL WKLRVLQAEL KINIRLTPTG
1510 1520 1530 1540 1550
KAIPIRLFLT NESGYYLDIS LYKEVTDSRT GQIMFQAYGD KQGPLHGMLI
1560 1570 1580 1590 1600
NTPYVTKDLL QSKRFQAQSL GTSYVYDIPE MFRQSLIKLW DSMNEHAFLP
1610 1620 1630 1640 1650
TPPLPSDILT YTELVLDDQG QLVHMNRLPG GNEIGMVAWK MTLKTPEYPE
1660 1670 1680 1690 1700
GRDIIVIGND ITYRIGSFGP QEDVLFLRAS ELARTHGIPR IYVAANSGAR
1710 1720 1730 1740 1750
IGLAEEIRHM FHVAWEDPDD PYKGYKYLYL TPQDYKKVSA LNSVHCEHVE
1760 1770 1780 1790 1800
DNGESRYKIT DIIGKEDGLG IENLRGSGMI AGESSLAYES IITINLVTCR
1810 1820 1830 1840 1850
AIGIGAYLVR LGQRTIQVEN SHIILTGCGA LNKVLGREVY TSNNQLGGIQ
1860 1870 1880 1890 1900
IMHNNGVTHG TVCDDFEGVY TILLWLSYMP KSVYSPVPIL KVKDPIDRTI
1910 1920 1930 1940 1950
DFVPTKTPYD PRWMLAGRPN PSQKGQWQSG FFDNGSFLEI MQPWAQTVVV
1960 1970 1980 1990 2000
GRARLGGIPV GVVAVETRTV ELSIPADPAN LDSEAKIIQQ AGQVWFPDSA
2010 2020 2030 2040 2050
FKTAQAINDF NREGLPLMVF ANWRGFSGGM KDMYDQVLKF GAYIVDGLRE
2060 2070 2080 2090 2100
YRQPVLIYIP PQAELRGGSW AVIDPTINPR HMEMYADRES RGGILEPEGT
2110 2120 2130 2140 2150
VEIKFRRKDL VKTMRRVDPV YMRLAERLGT PELSAADRKD LESKLKEREE
2160 2170 2180 2190 2200
FLIPIYHQVA MQFADLHDTP GRMQEKGAIT DILDWKTSRT FFYWRLRRLL
2210 2220 2230 2240 2250
LEDVVKKKIH DANPELTDGQ IQAMLRRWFV EVEGTVKAYL WDSNKDLVEW
2260 2270 2280 2290 2300
LEKQLMEEEG VRSVVDENIK YISRDYILKQ IRSLVQANPE VAMDSIVHMT
2310 2320
QHISPTQRAE IVRILSTMDS PSST
Length:2,324
Mass (Da):262,720
Last modified:July 1, 1989 - v1
Checksum:i3F1C541F01BBBEF6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03541 mRNA Translation: AAA48701.1
X05019 mRNA Translation: CAA28675.1
PIRiA29924
RefSeqiNP_990836.1, NM_205505.1
UniGeneiGga.1480
Gga.6380

Genome annotation databases

GeneIDi396504
KEGGigga:396504

Similar proteinsi

Entry informationi

Entry nameiACAC_CHICK
AccessioniPrimary (citable) accession number: P11029
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: May 23, 2018
This is version 142 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways

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