ID   ACAC_DICDI              Reviewed;        2282 AA.
AC   Q54J08;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Acetyl-CoA carboxylase;
DE            EC=6.4.1.2;
DE   AltName: Full=ACC-alpha;
DE   Includes:
DE     RecName: Full=Biotin carboxylase;
DE              EC=6.3.4.14;
GN   Name=accA; ORFNames=DDB_G0288387;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Catalyzes the rate-limiting reaction in the biogenesis of
CC       long-chain fatty acids. Carries out three functions: biotin carboxyl
CC       carrier protein, biotin carboxylase and carboxyltransferase.
CC       {ECO:0000250|UniProtKB:Q13085}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-
CC         CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;
CC         Evidence={ECO:0000250|UniProtKB:Q5SWU9};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] =
CC         ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
CC         Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC         ChEBI:CHEBI:456216; EC=6.3.4.14;
CC         Evidence={ECO:0000250|UniProtKB:Q5SWU9};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000250|UniProtKB:O00763};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC       acetyl-CoA: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; AAFI02000111; EAL63219.1; -; Genomic_DNA.
DR   RefSeq; XP_636722.1; XM_631630.1.
DR   AlphaFoldDB; Q54J08; -.
DR   SMR; Q54J08; -.
DR   STRING; 44689.Q54J08; -.
DR   PaxDb; 44689-DDB0230067; -.
DR   EnsemblProtists; EAL63219; EAL63219; DDB_G0288387.
DR   GeneID; 8626599; -.
DR   KEGG; ddi:DDB_G0288387; -.
DR   dictyBase; DDB_G0288387; accA.
DR   eggNOG; KOG0368; Eukaryota.
DR   HOGENOM; CLU_000395_5_2_1; -.
DR   InParanoid; Q54J08; -.
DR   OMA; PTPKGHC; -.
DR   PhylomeDB; Q54J08; -.
DR   Reactome; R-DDI-163765; ChREBP activates metabolic gene expression.
DR   Reactome; R-DDI-196780; Biotin transport and metabolism.
DR   Reactome; R-DDI-200425; Carnitine metabolism.
DR   Reactome; R-DDI-75105; Fatty acyl-CoA biosynthesis.
DR   UniPathway; UPA00655; UER00711.
DR   PRO; PR:Q54J08; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:dictyBase.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004075; F:biotin carboxylase activity; ISS:dictyBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; HDA:dictyBase.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; ISS:dictyBase.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006606; P:protein import into nucleus; ISS:dictyBase.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 2.40.460.10; Biotin dependent carboxylase carboxyltransferase; 1.
DR   Gene3D; 3.90.1770.10; PreATP-grasp domain; 1.
DR   InterPro; IPR049076; ACCA.
DR   InterPro; IPR049074; ACCA_BT.
DR   InterPro; IPR034733; AcCoA_carboxyl_beta.
DR   InterPro; IPR013537; AcCoA_COase_cen.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR45728:SF3; ACETYL-COA CARBOXYLASE; 1.
DR   PANTHER; PTHR45728; ACETYL-COA CARBOXYLASE, ISOFORM A; 1.
DR   Pfam; PF08326; ACC_central; 1.
DR   Pfam; PF21385; ACCA_BT; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 2.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Biotin; Cytoplasm; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
KW   Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..2282
FT                   /note="Acetyl-CoA carboxylase"
FT                   /id="PRO_0000328220"
FT   DOMAIN          16..515
FT                   /note="Biotin carboxylation"
FT   DOMAIN          170..360
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   DOMAIN          646..720
FT                   /note="Biotinyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   DOMAIN          1495..1851
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT   DOMAIN          1852..2178
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT   REGION          1109..1141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1495..2178
FT                   /note="Carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT   ACT_SITE        335
FT                   /evidence="ECO:0000250"
FT   BINDING         196..253
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         319
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         331
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         331
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         333
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         1761
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         2068
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         2070
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         687
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT                   ProRule:PRU01066"
SQ   SEQUENCE   2282 AA;  256735 MW;  BDBEA99629EE1B2B CRC64;
     MIEINEYIKK LGGDKNIEKI LIANNGIAAV KAIRSVRKWA YTNFGNERAI KFVVMATPED
     MKANAEYIRM ADQILQVPGG SNNNNYANVD IIVDFAERAG VQAVWAGWGH ASENPRLPDL
     LSKTETGIVF IGPPAKAMAD LGDKIASTIV AQSARVACVP WSGSGLKVDY SECNGVPSEI
     YGRACINSVE EARECAQRVG FPAMIKASEG GGGKGIRKVT SMEDLESSFR QVQNEVPGSP
     IFFMKLVSNA RHLEVQIVAD RHGEAISLNG RDCSVQRRHQ KIIEEGPAIA PTPQVWEEME
     RAAVRLVKEV GYVGAGTVEY LFAEGEYYFL ELNPRLQVEH PVTEQITGVN LPATQLQIAM
     GIPLHRIPDI RKLYGRTGDD LYGDSMIDLH DFTKRNPPAG HCIAVRITGE NPDEGFKPTS
     GQIHELTFRS TPNIWGYFSV GAKGGLHEYA DSQFGHIFAN GATREEARKT IILGLKEISI
     RGDIRTPVEY IIHLLESKDF KENHIHTGWL DQLISEKIQT KKPETMIVVL CGAIYKASTI
     FSTKIQEFSN QLSNGQLPSL ELLNNSLPIE LIYNNVKYQF EVSRTGINNY SVCLKNDKSA
     VSIDSSVIML SDSGLLILLN GSTHVCYGRE DVIGLSLMID SKTCVFSQEY DPSILRTSSP
     GKLVRYLVDD GSLVVKGTPF AEIEVMKMYM PLLVPEKGII KFVLTEGSVM APGAIIANLE
     LSDQSSIQKS TVFTGSLTKM SPPTLIGNKP HQLLNYTLGK ISNVLCGYES NDLNQLLNDT
     IKQLSNQKLP LFEFKEQLSI VQSRIPQSLF KLINDELNKF EFNNDDDDED DSELFNSKNL
     QLSISLYLNK LLLENEQLSI AIQLLIKPII LLAEKYNDGV SFAAINIFKN YLEEFIQIET
     NLQNKNIQTV LKSIRPTYKD NISKVVDIAQ SLHPQSKKYK FILLLLNKIQ EQGLVCDFVE
     QFKKLSSLGG NCMEISLKAK HIMVHSQLPS NKQRSNDLIN SLKSILNVNN EQQQQVDEKV
     QDNKDEKISK LSKQTNEISD ILIPMFFNES NNDDDIRKLA MEVYVRHSYR SYYVEDTKVT
     LSNDEGSSGF SFIEWHFYIN LPQQSNLGGS NSGSPTYGSP LIRSISSSGG SSGGSGFQIS
     PRPSMSIFNG LSMLRTDSTD SLTAMEDQTK LRYGMMVFFE NEKKFEEKLP LILTRYNEEN
     NKKSQLSLSP NESTDILSVI ISIYPESISQ ENQAISSFQS ILKGYIKELS IARIRRITFI
     CCGGDEGKPL KYFTFRERHM YMEDPIFRHI EPAMAYHLEV RKLSNFDITH VPTTSQRIHL
     YYAQEKGKKE TDPDADRSFF VRSVIRYSDL YGHSNEIKVD ILLSQIETLL SESIESLEIA
     MSNKKYEKAQ NHSIFLNVMP EVMFDEKMIG YVVQEIGDRL GKRLWKLRVG RVEVRGRIRK
     GDGLIPVRFF VQNPTGYAFQ VQCYYEQQNS IGQMVFAVVP GSSKGSWEGL PVDTPYPIMD
     AVQRNRFKAQ RLDTTYCYDY PDLFREAMQN IWMEFMESNK TNPVKVYPSS RGVLESVELI
     LPSTINTDFP PSIPLDQLPE ESKPKLEETY RPIGYNDIGM VAWRMTFYTP EYPLGRQAIV
     IANDITHQIG SFGPQEDMLF KLASELARKE KIPRIYLSSN SGARIGLADE IKSKFKVTWN
     VPSDPTKGIK NLYLTNNDYQ ALKDSVIAYQ DTTDKDKWII HDIIGQKNGI GVENLSWSGL
     IAGETSQAYN EIFTITLVSG RSVGIGAYLV RLGQRTIQND APIILTGASA LNKVLGKEVY
     ESNQQLGGSQ IMYPNGVSHI IVNDELRGIT NVLQWLSFVP KSGGEMVPII SPIDSPHRDI
     EFDPSNSING KCDTRHLIAG LQSELDPNYW ISGMFDKDSF METLAGWANT VITGRARLGG
     IPVGIIAVET KSVEKIIPAD PANPLSYEQV NTQAGQVWYP DSSFKTAQAI ADFNNGEELP
     LMILANWRGF SGGMRDMFDE ILKFGSMIVD NLRNYKQPVM VYIPPFAELR GGAWVVLDST
     INLDMMEMYC SEEGRGGVLE PNGIAEIKYR DPELIKTMHR LDPKLIEWDK SIPIGVSVNG
     LDQSQKTIKS QIQQREKELL GIYQQIAIKF ADLHDTPGRM KAKGVIKQMV PWKSARSFFY
     DRIKRRLFEE DKLKLIDKSH PGLNRQSKLN LLETWIKQIL GNNQSVDYHQ NDKLISSTIE
     SNSHIINDKI IDLSKQYAIN QILNFVQSDS ESIVDGFQNL LPFISTQQKE FLFESLKKDL
     NK
//