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P11029

- ACAC_CHICK

UniProt

P11029 - ACAC_CHICK

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Protein

Acetyl-CoA carboxylase

Gene

ACAC

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- 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.

Catalytic activityi

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.
ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].

Cofactori

Biotin.By similarity
Binds 2 manganese ions per subunit.By similarity

Enzyme regulationi

By phosphorylation.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi424 – 4241Manganese 1By similarity
Metal bindingi437 – 4371Manganese 1By similarity
Metal bindingi437 – 4371Manganese 2By similarity
Metal bindingi439 – 4391Manganese 2By similarity
Active sitei441 – 4411By similarity
Binding sitei1800 – 18001Coenzyme ABy similarity
Binding sitei2104 – 21041Coenzyme ABy similarity
Binding sitei2106 – 21061Coenzyme ABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi315 – 3206ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. acetyl-CoA carboxylase activity Source: UniProtKB-EC
  2. ATP binding Source: UniProtKB-KW
  3. biotin carboxylase activity Source: UniProtKB-EC
  4. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-KW
  2. malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway
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

SABIO-RKP11029.
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 23242324Acetyl-CoA carboxylasePRO_0000146768Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei78 – 781PhosphoserineBy similarity
Modified residuei80 – 801PhosphoserineBy similarity
Modified residuei786 – 7861N6-biotinyllysine1 Publication
Modified residuei1193 – 11931PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP11029.
PRIDEiP11029.

Interactioni

Protein-protein interaction databases

BioGridi676751. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP11029.
SMRiP11029. Positions 97-616, 742-834, 1551-2285.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini117 – 618502Biotin carboxylationAdd
BLAST
Domaini275 – 466192ATP-graspPROSITE-ProRule annotationAdd
BLAST
Domaini752 – 81867Biotinyl-bindingAdd
BLAST
Domaini1675 – 2171497CarboxyltransferaseAdd
BLAST

Sequence similaritiesi

Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
Contains 1 biotin carboxylation domain.Curated
Contains 1 biotinyl-binding domain.Curated
Contains 1 carboxyltransferase domain.Curated

Phylogenomic databases

eggNOGiCOG0511.
HOVERGENiHBG005371.
InParanoidiP11029.
KOiK11262.
PhylomeDBiP11029.

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.

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:
EMBL
GenBank
DDBJ
Links Updated
J03541 mRNA. Translation: AAA48701.1.
X05019 mRNA. Translation: CAA28675.1.
PIRiA29924.
RefSeqiNP_990836.1. NM_205505.1.
UniGeneiGga.1480.

Genome annotation databases

GeneIDi396504.
KEGGigga:396504.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03541 mRNA. Translation: AAA48701.1 .
X05019 mRNA. Translation: CAA28675.1 .
PIRi A29924.
RefSeqi NP_990836.1. NM_205505.1.
UniGenei Gga.1480.

3D structure databases

ProteinModelPortali P11029.
SMRi P11029. Positions 97-616, 742-834, 1551-2285.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 676751. 1 interaction.

Proteomic databases

PaxDbi P11029.
PRIDEi P11029.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 396504.
KEGGi gga:396504.

Organism-specific databases

CTDi 31.

Phylogenomic databases

eggNOGi COG0511.
HOVERGENi HBG005371.
InParanoidi P11029.
KOi K11262.
PhylomeDBi P11029.

Enzyme and pathway databases

UniPathwayi UPA00655 ; UER00711 .
SABIO-RK P11029.

Miscellaneous databases

NextBioi 20816543.
PROi P11029.

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

  1. "Primary structure of chicken liver acetyl-CoA carboxylase deduced from cDNA sequence."
    Takai T., Yokoyama C., Wada K., Tanabe T.
    J. Biol. Chem. 263:2651-2657(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, BIOTINYLATION AT LYS-786.
    Tissue: Liver.
  2. "Primary structure of the biotin-binding site of chicken liver acetyl-CoA carboxylase."
    Takai T., Wada K., Tanabe T.
    FEBS Lett. 212:98-102(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 493-820.
    Tissue: Liver.
  3. Bienvenut W.V., Black E.J., Gillespie D.A.
    Submitted (JAN-2007) to UniProtKB
    Tissue: B-cell lymphoma.

Entry informationi

Entry nameiACAC_CHICK
AccessioniPrimary (citable) accession number: P11029
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: October 29, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3