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Database: UniProt
Entry: H0WWB9_OTOGA
LinkDB: H0WWB9_OTOGA
Original site: H0WWB9_OTOGA 
ID   H0WWB9_OTOGA            Unreviewed;      2460 AA.
AC   H0WWB9;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=acetyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00013058};
DE            EC=6.4.1.2 {ECO:0000256|ARBA:ARBA00013058};
GN   Name=ACACB {ECO:0000313|Ensembl:ENSOGAP00000006667.2};
OS   Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC   Galagidae; Otolemur.
OX   NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000006667.2, ECO:0000313|Proteomes:UP000005225};
RN   [1] {ECO:0000313|Proteomes:UP000005225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA   Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA   Walker B.J., Sharpe T., Hall G.;
RT   "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSOGAP00000006667.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001448};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11309;
CC         Evidence={ECO:0000256|ARBA:ARBA00001448};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC       acetyl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00004956}.
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DR   EMBL; AAQR03070116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03070117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03070118; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03070119; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03070120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03070121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03070122; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03070123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03070124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03070125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 30611.ENSOGAP00000006667; -.
DR   Ensembl; ENSOGAT00000007455.2; ENSOGAP00000006667.2; ENSOGAG00000007444.2.
DR   eggNOG; KOG0368; Eukaryota.
DR   GeneTree; ENSGT00940000155049; -.
DR   HOGENOM; CLU_000395_5_0_1; -.
DR   InParanoid; H0WWB9; -.
DR   OMA; TEHCKVA; -.
DR   TreeFam; TF300061; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000005225; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:Ensembl.
DR   GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0031999; P:negative regulation of fatty acid beta-oxidation; IEA:Ensembl.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0060421; P:positive regulation of heart growth; IEA:Ensembl.
DR   GO; GO:0010884; P:positive regulation of lipid storage; IEA:Ensembl.
DR   GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
DR   GO; GO:0010906; P:regulation of glucose metabolic process; IEA:Ensembl.
DR   GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
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; 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:SF1; ACETYL-COA CARBOXYLASE 2; 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; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005225}.
FT   DOMAIN          259..761
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          414..609
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          888..962
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          1695..2025
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          2029..2347
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
FT   REGION          29..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          170..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        29..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..144
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2460 AA;  276936 MW;  18BC288188B0035A CRC64;
     MVLLLFVSCL IFSCLTFSWL RIWRKMTDSQ PVTKSKSEVS STQSQEPFPA SDSFGEPPQK
     NGDGSSLPKT PQQAEPVSRR GPKDACQRRN SLPPSHQKPP RNPLSSTDAS PSPGLQSNGA
     ESEGPEAPDT NGLSSLPQPQ GQRARSPSKE DKKQANIKKQ LMTNFILGSF DDYSSDEDPG
     TGSFRESSRK GSRASLGTVT LEVPLTTGEP DTRIPTMRPS MSGLHLVKRG REHKKLDLHR
     DFTVASPAEF VTRFGGDRVI EKVLIANNGI AAVKCMRSIR RWAYEMFRNE RAIRFVVMVT
     PEDLKANAEY IKMADQYVPV PGGPNNNNYA NVELIVDIAK RIPVQAVWAG WGHASENPKL
     PELLCKDGIA FLGPPSEAMW ALGDKIASTI VAQTLQIPTL PWSGSGLTVE WTDDDLQQGK
     RISVPEDVYE KGCVKDVDEG LEAAEKIGFP LMIKASEGGG GKGIRKAESA EDFPILFRQV
     QSEIPGSPVF LMKLAQHARH LEVQILADQY GNAVSLFGRD CSIQRRHQKI IEEAPATIAP
     LAVFEFMEQC AVRLAKTVGY VSAGTVEYLY SQDGSFHFLE LNPRLQVEHP CTEMIADVNL
     PAAQLQIAMG VPLHRLKDIR LLYGESPWGV MPISFETPAN PPLARGHVIA ARITSENPDE
     GFKPSSGTVQ ELNFRSSKNV WGYFSVAATG GLHEFADSQF GHCFSWGENR EEAISNMVVA
     LKELSIRGDF RTTVEYLINL LETDSFQNND IDTGWLDHLI AEKVQAEKPD IMLGVVCGAL
     NVADAMFRTC MTDFLHSLER GQVLPADSLL NIVDVELIYG GIKYILKVAR QSLTMFVLIM
     NGCHIEIDAH RLNDGGLLLS YNGNSYTTYM KEEVDSYRIT IGNKTCVFEK ENDPTVLRSP
     SAGKLTQYTV EDGGHVEAGS SYAEMEVMKM IMTLNVQESG RVKYIKRPGA VLEAGCMVAR
     LELDDPSKVH PAEPFMGELP SQQTLPILGE KLHQVFHNVL ENLTNVMSGY CLPEPIFSIK
     LKEWVQKLMV TLRHPSLPLL ELQEIMTSVS GRIPTPVEKA VQRVMAQYAS NITSVLCQFP
     SQQIATILDC HAATLQRKAD REVFFMNTQS IVQLVQRYRS GTRGYMKTVV LDLLRRYLHV
     EHHFQQAHYD KCVINLREKF KPDMSQVLDC IFSHAQVAKK NQLVIMLIDE LCGPDPSLSD
     ELTSILNELT QLSKSEHCKV ALRARQVLIA SHLPSYELRH NQVESIFLSA IDMYGHQFCP
     ENLKKLILSE TTIFDVLPSF FYHTNKVVCM ASLEVYVRRG YIAYELNSLQ HRQLPDGTCV
     VEFQFMLPSS HPNRMAMPIS ITNPDLLRHS TELFMDSGFS PLCQRMGAMV AFERFEDFTR
     NFDEVISCFA NVPKDTPLFS KARTSLYSDD DCKSLREEPI HILNVAIQCA DRLEDEALVQ
     TLRTFVQSKK NILVDYGLRR ITFLIAQEKE FPKFFTFRAR DEFAEDRIYR HLEPALAFQL
     ELSRMRNFDL TAVPCANHKM HLYLGAAKVK EGAEVTDHRF FIRAIIRHSD LITKEASFEY
     LQNEGERLLL EAMDELEVAF NNTSVRTDCN HIFLNFVPTV IMDPSKIEES VRSMVMRYGS
     RLWKLRVLQA EVKINIRQTT TGSAVPIRLF ITNESGYYLD ISLYKELTDP RSGNIMFHSF
     GNKQGPQHGM LINTPYVTKD LLQAKRFQAQ SLGTTYIYDF PEMFRQALFK LWGSPDKYPK
     DILTYTELVL DSQGQLVEMN RLPGGNEVGM VAFKMRFKTQ EYPEGRDVIV IGNDITFRIG
     SFGPREDLLY LRASEMARAE GIPKIYLAAN SGARIGMAEE IKHMFQVAWV DPEDPQKGFK
     YLYLTPQDFT KISSLNSVHC KHIEEGGESR YVITDIIGKD DGLGVENLKG SGTIAGESSL
     AYEEIVTISL VTCRALGIGA YLVRLGQRVI QVENSHIILT GASALNKVLG REVYTSNNQL
     GGVQIMHYNG VSHITVPDDF EGVYTILEWL SYMPKDNLSP VPIITPTDPI DREIEFLPSR
     APYDPRWMLA GRPHPTLKGT WQSGFFDHGS FKEIMAPWAQ TVVTGRARLP LGGIPIGVIA
     VETRTVELVV PADPANLDSE AKIIQQAGQV WFPDSAYKTA QAIEDFRREK LPLLIFANWR
     GFSGGMKDMY DQVLKFGAYI VDGLRKYTQP ILIYIPPYAE LRGGSWVVVD ATINPLCIEM
     YADKESRGGV LEPEGTVEIK FRKKDLIKSM RRLDPVYKKL VEQLGAPELS EKERKDLDSR
     LKAREDMLFP IYHQVAVQFA DLHDTPGRML EKGVISDILE WKTARTFLYW RLRRLLLEDQ
     VRQEILRASG QLSHVHIQSM LRRWFVESEG AVKAYLWDNN QVVVQWLEQH WQAEDGPHST
     ISENIRCLKH DSVLKTIRGL VQENPEVAMD CVMYLSQHIS PAERAQVAHL LSTLESPAST
//
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