GenomeNet

Database: UniProt
Entry: Q54J08
LinkDB: Q54J08
Original site: Q54J08 
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   05-DEC-2018, entry version 112.
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; Mycetozoa; Dictyostelids; 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.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   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.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   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
CC       of long-chain fatty acids. Carries out three functions: biotin
CC       carboxyl carrier protein, biotin carboxylase and
CC       carboxyltransferase. {ECO:0000250|UniProtKB:Q13085}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) +
CC         malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384,
CC         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] +
CC         phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505,
CC         Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144,
CC         ChEBI:CHEBI:83145, 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
CC       from acetyl-CoA: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
DR   EMBL; AAFI02000111; EAL63219.1; -; Genomic_DNA.
DR   RefSeq; XP_636722.1; XM_631630.1.
DR   ProteinModelPortal; Q54J08; -.
DR   SMR; Q54J08; -.
DR   STRING; 44689.DDB0230067; -.
DR   PaxDb; Q54J08; -.
DR   PRIDE; Q54J08; -.
DR   EnsemblProtists; EAL63219; EAL63219; DDB_G0288387.
DR   GeneID; 8626599; -.
DR   KEGG; ddi:DDB_G0288387; -.
DR   dictyBase; DDB_G0288387; accA.
DR   eggNOG; ENOG410ISCY; Eukaryota.
DR   eggNOG; KOG0368; Eukaryota.
DR   eggNOG; COG0439; LUCA.
DR   eggNOG; COG0511; LUCA.
DR   eggNOG; COG4799; LUCA.
DR   InParanoid; Q54J08; -.
DR   KO; K11262; -.
DR   OMA; LPYGEWN; -.
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; Import of palmitoyl-CoA into the mitochondrial matrix.
DR   Reactome; R-DDI-75105; Fatty acyl-CoA biosynthesis.
DR   UniPathway; UPA00655; UER00711.
DR   PRO; PR:Q54J08; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   Proteomes; UP000002195; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:dictyBase.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
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; Complete proteome; Cytoplasm;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Ligase;
KW   Lipid biosynthesis; Lipid metabolism; Manganese; Metal-binding;
KW   Multifunctional enzyme; Nucleotide-binding; Reference proteome.
FT   CHAIN         1   2282       Acetyl-CoA carboxylase.
FT                                /FTId=PRO_0000328220.
FT   DOMAIN       16    515       Biotin carboxylation.
FT   DOMAIN      170    360       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      646    720       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   DOMAIN     1495   1851       CoA carboxyltransferase N-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01136}.
FT   DOMAIN     1852   2178       CoA carboxyltransferase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01137}.
FT   NP_BIND     196    253       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   REGION     1495   2178       Carboxyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01138}.
FT   COMPBIAS     82     85       Poly-Asn.
FT   COMPBIAS    210    215       Poly-Gly.
FT   COMPBIAS    825    831       Poly-Asp.
FT   COMPBIAS    943    946       Poly-Leu.
FT   COMPBIAS   1012   1015       Poly-Gln.
FT   ACT_SITE    335    335       {ECO:0000250}.
FT   METAL       319    319       Manganese 1. {ECO:0000250}.
FT   METAL       331    331       Manganese 1. {ECO:0000250}.
FT   METAL       331    331       Manganese 2. {ECO:0000250}.
FT   METAL       333    333       Manganese 2. {ECO:0000250}.
FT   BINDING    1761   1761       Coenzyme A. {ECO:0000250}.
FT   BINDING    2068   2068       Coenzyme A. {ECO:0000250}.
FT   BINDING    2070   2070       Coenzyme A. {ECO:0000250}.
FT   MOD_RES     687    687       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-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
//
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