ACAC_DICDI
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 03-AUG-2022, entry version 125.
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 (Slime mold).
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.DDB0230067; -.
DR PaxDb; Q54J08; -.
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; LIQCAMP; -.
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 Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR034733; AcCoA_carboxyl.
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 Pfam; PF08326; ACC_central; 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; SSF51230; SSF51230; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52096; SSF52096; 2.
DR SUPFAM; SSF52440; SSF52440; 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
