ID C1ML75_MICPC Unreviewed; 2145 AA.
AC C1ML75;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Acetyl-coa carboxylase {ECO:0000313|EMBL:EEH59502.1};
GN ORFNames=MICPUCDRAFT_31755 {ECO:0000313|EMBL:EEH59502.1};
OS Micromonas pusilla (strain CCMP1545) (Picoplanktonic green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Mamiellaceae; Micromonas.
OX NCBI_TaxID=564608 {ECO:0000313|Proteomes:UP000001876};
RN [1] {ECO:0000313|EMBL:EEH59502.1, ECO:0000313|Proteomes:UP000001876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1545 {ECO:0000313|EMBL:EEH59502.1,
RC ECO:0000313|Proteomes:UP000001876};
RX PubMed=19359590; DOI=10.1126/science.1167222;
RA Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W., Gready J.E.,
RA John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F., Moreau H.,
RA Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I., Piegu B.,
RA Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T., Zelensky A.,
RA Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W., Van de Peer Y.,
RA Grigoriev I.V.;
RT "Green evolution and dynamic adaptations revealed by genomes of the marine
RT picoeukaryotes Micromonas.";
RL Science 324:268-272(2009).
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:0000256|ARBA:ARBA00000861};
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:ARBA00001455};
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; GG663736; EEH59502.1; -; Genomic_DNA.
DR RefSeq; XP_003056126.1; XM_003056080.1.
DR SMR; C1ML75; -.
DR STRING; 564608.C1ML75; -.
DR GeneID; 9681766; -.
DR KEGG; mpp:MICPUCDRAFT_31755; -.
DR eggNOG; KOG0368; Eukaryota.
DR OMA; PTPKGHC; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000001876; Unassembled WGS sequence.
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:0046872; F:metal ion binding; IEA:InterPro.
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 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: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; 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 Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000001876}.
FT DOMAIN 109..604
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 259..453
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1420..1758
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1762..2058
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 1762..1784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2145 AA; 236970 MW; 27C58E120185009D CRC64;
MHALSAAANW WPVHKAHAST SSSNRRHIAQ LLRLNKHGNY FNLRPQGNSA RVPAPAITFK
PCRIELQHDT SPGDVCTCAS VSAPADTSAD TTTTEALARY VAAHGGKRVI RKVLIANNGM
AATKSIISMR RWAYTELGDE NAIEFIAMAT PEDLNANAEF IRFADDFVEV PGGSNKNNYA
NVNLIVDIAE REGVDAVWPG WGHASENPKL PTSLKERGIQ FIGPTAPVMS VLGDKIAANI
LAQTAKVPSI PWSGEGLEAE LTEEGTIPDD IFNKAMVTTV EESLVAANRI GYPVMLKASE
GGGGKGIRMS ANDEELRVNF EMVKAEVPGS PMFMMQLCSQ ARHLEVQIVG DEYGNAVALS
GRDCSTQRRF QKIFEEAPPT IADPTIFREM EKAAQRLTRN IGYVGAGTVE YLYNATTKKY
YFLELNPRLQ VEHPVTEGIT GVNLPATQLQ VAMGIPLSRI PDIRRFYGRD PETDTNIDFM
EEDYVLPERH VIAARITAEN PDEGFKPTSG GIERVSFQST PTVWGYFSVG ANGGVHEFAD
SQFGHIFATG STREESRKSL VLALKGMVVR GEIRTAVEYL VQLLETDDFK NNNIDTSWLD
GIIKAKSIAM KEDPHTIVAS AALYRAFRIV QAEESAFKEF WQKGQTATQG IERLTEFPMD
ITYQDVKYSF TIHRRGPDSL VLSLKGEDLI NARIRERSDG VLLGIWGGQT HEIDGLEEPL
GLRMVLDGQT WLLPNQFDPS ELRTDVTGKL IRFLQDDGGE VIAGKPYAEV EAMKMVMPLI
ATESGTISHA KSGGAVIEAG DLLGSLTLKD PNKVKKISPF GGEFRCSSIE GQEAPPSASE
ALEEAISSTN LLLDGYVLPV EETVNNLLET LCDPALPEAD GGRWQRACSI LNCIVDRYLS
VESLFAGKKG DSVMREQTQK NSGDMDALLR MVVAHARIKQ STQMVISLLK QAPTLPQRVM
GGPIGWADDH SPISDDFRAS IERLSNLRGA DYGELALTAS NILLEKRLPS IDKRLDELRS
ILLGGMGLKR PWGTSEAGDL KSLIESPTLA VDLLPSLFVD SDADVADAAL EVYTKRVYRA
HNVISSEIVR ENDLDSMNFK FQFNTYPEES PLRFGVMVVT TTLEQAKAQM PAILDRLAHH
IDDAAKDTPF HVLHIALSCQ TEETTLADRC AAVLSEHRGR MAELGVKFVN VISYVPPNLP
HYYTFTAANG YQEDPLYRGE RPTVAHLLEL ARLENYNLTR LPTVNRDLHV YVGESKQGFG
KRGLQKHILL RRISHSRDAA EGGIERVLGK AVEALDLARL DPRTKGASSG RIYINFLPAQ
TNSPFDTIVT SLKTKVLEFI SRKSTELLAQ QVDEIEIRFR IAESPGSSVQ VPVRIMATSM
SGQWLKVDVY REYLDPQTGK ATQFCMLGKD GVEEACFMEP YPMPGTLQQK RSIARAIGTT
YIYDFLGLIE KAMVLEWRQF IADNGEGTVP VDMFRAEELI LNADDRSLSK AETSRIAGSN
DIGMVAWQCF MKTPEYPEGR EIVLVGNDCT FMSGSFGVKE DDFYYAVSQY ARRKGVPRVY
IASNSGARIG LVEELKPYFK VAWNDVSNPS LGFRYLYLSP DDYAAFPEGT VNATEVVDDG
EKRMQLDDII GQIHGIGVEN LRGSGMIAGE QSAAYSDAFT LSYITGRSVG IGAYLCRLGQ
RNIQMTNGPL ILTGYLALNK LLGREVYTSQ DQLGGPQVMM PNGVSHMQVE DDQEGVKAIL
RWLSYVPSNC FTRAPALPSA DPTSRKIAFK PTKTPYDPRH MISGTESSDG SWIGGFFDRG
SWTETLADWG KSVVCGRARL GGIPMGVIAV ETRLMEQRIP ADPANPDSRE SVLAQAGQVW
FPDSAHKTAT AIRDFNNAEN LPLIIFANWR GFSGGTRDMY GEILKFGAMI VDELRVYRHP
VFVYIPPNGE LRGGAWVVVD PTINEAQMEM YADEESRGGI LEPPGICEVK FRDKDQKAVM
HRLDPVLLEL DQDPEENQVE ISSREAQLLP MYTQVAHEFA DLHDRSGRML AKGVIRDVVK
WEDARAYFHA RLQRRLAMDD LAMEAGTDRT VVEEHLEKLA VEANINWSSD AAVTGWLQTE
ADHIRNIISS LGRDAAVEDA VESLSSLDEE ALKMVLQMLK AQGKQ
//
