ID Q8IKE1_PLAF7 Unreviewed; 3367 AA.
AC Q8IKE1;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 2.
DT 27-MAR-2024, entry version 147.
DE SubName: Full=Acetyl-CoA carboxylase {ECO:0000313|EMBL:CZU00393.1};
DE EC=6.4.1.2 {ECO:0000313|EMBL:CZU00393.1};
GN ORFNames=PF3D7_1469600 {ECO:0000313|EMBL:CZU00393.1};
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329 {ECO:0000313|EMBL:CZU00393.1, ECO:0000313|Proteomes:UP000001450};
RN [1] {ECO:0000313|EMBL:CZU00393.1, ECO:0000313|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450};
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.,
RA Eisen J.A., Rutherford K., Salzberg S.L., Craig A., Kyes S., Chan M.S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
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; LN999946; CZU00393.1; -; Genomic_DNA.
DR RefSeq; XP_001348838.2; XM_001348802.2.
DR SMR; Q8IKE1; -.
DR STRING; 36329.Q8IKE1; -.
DR PaxDb; 5833-PF14_0664; -.
DR EnsemblProtists; CZU00393; CZU00393; PF3D7_1469600.
DR GeneID; 812246; -.
DR KEGG; pfa:PF3D7_1469600; -.
DR VEuPathDB; PlasmoDB:PF3D7_1469600; -.
DR HOGENOM; CLU_000395_5_1_1; -.
DR InParanoid; Q8IKE1; -.
DR OMA; PTPKGHC; -.
DR OrthoDB; 911at2759; -.
DR PhylomeDB; Q8IKE1; -.
DR Reactome; R-PFA-163765; ChREBP activates metabolic gene expression.
DR Reactome; R-PFA-196780; Biotin transport and metabolism.
DR Reactome; R-PFA-200425; Carnitine metabolism.
DR Reactome; R-PFA-75105; Fatty acyl-CoA biosynthesis.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000001450; Chromosome 14.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; ISS:GeneDB.
DR GO; GO:0020011; C:apicoplast; IDA:GeneDB.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; ISS:GeneDB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009374; F:biotin binding; ISS:GeneDB.
DR GO; GO:0004075; F:biotin carboxylase activity; ISS:GeneDB.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; ISS:GeneDB.
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; 2.
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; IPR034733; AcCoA_carboxyl_beta.
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; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF01039; Carboxyl_trans; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CZU00393.1};
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:UP000001450};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..3367
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030176274"
FT DOMAIN 499..1141
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 651..843
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1295..1369
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 2600..2857
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 2970..3289
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 110..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1607..1648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1764..1794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2404..2426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 3280..3307
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 3367 AA; 394881 MW; 0D60042DDFCD22C8 CRC64;
MINFFLSLLL FVLFFENLVV SIKYRNIHYI HMPNNAHNKN FNEKENREIY HNVNISGGNT
IYEEPKNKYI TLFLSNGKKI LHSIFRNNNN NNITICNENT GKNSNINLKN NSENNTKSNS
KNYSRGSSSC LNIQNVSNTY YDKRRIKKDI MNKKVEENLI HDENENNIIN DKICCDEKQD
LDKEIHVDEQ NEKKSNSTLN NESFISILSN DNSEKKKDME ESNNYSNNFY LNSLEENIIY
PTQHVDCDFN GKWKSHVDDI LENDSYYSNM NDNSNKSCIS DYELLKTSIL LNNTKDDFPL
YENSRKNILT TSGKINKNKN LKERKKKNLN RLFYTLKLTN NFSFKNSKNR RKYTNSYNSG
SSTHSRYVMD NKEYIIYHNN NNNNNNNYNS YSNNCNNMYI QGNKKKYNRL YCKKSANSQE
KDYDKDINLI ASDKINSELS QDDLKYNSQI INMPNDHFNI ITSDEKENIK KNAYKNYVNY
INERRYGYFD LLEKKNEKII RKLLIANNGM AALKCILSLK DWLFKKFYDE NLIKIIVMAT
DEDIKSNAKY ISLADKVIKV PGGKNIHNYA NVPLIVELAK SENVDAVWPG WGHSSENPLL
STLLEKENII FIGPTGNVME ALGDKISANI LAQSVEVPVV KWSGDNIRID KFENNKINDE
LYNNATIHSL DDCIKECKRI GFPVMIKASQ GGGGKGIRKV ENEYEIKKAY EQVQNELPNS
PIFLMKVCNN VRHIEIQVVG DMYGNVCSLS GRDCTTQRRF QKIFEEGPPS VVPYPIFREM
EKSSIRLTKM IKYRGAGTIE YLYDQINKKY FFLELNPRLQ VEHPVSEGIT NCNLISIQLQ
VAMGIPLQNI DDIRNLYQID KIEKIKKKDE QKKEFELTDN LCNDTINKDN INNDNIYKDN
INNDNIYKDN IYKDNINNDN IYKDNIYKDN INNDNIYKDN IYKDNIYNDN IYKDNINNDN
IHHIDNTTNE QNNKNLLHYN NYRNQNLCNN NSIKSLLNYD TNENVNRKYN LLNEHFDFYN
NKPYIKNHVI AARITAENSN DSFKPTSGNV RRINFQNWKD VWGYFSINDG FVHEFSDSQI
GHIFAKGETR EVARKNLILA LRKLHIDGDI KTGTKYLAKI LESKAFIDNN ITTNWLDIII
EKKKHVFYNT CHIILLCATI FKLLIYFMNE KGKVEENLDR DDIAIKRDKN YGNVINKNNN
HSGNINNNGE HMCKMKSAYI FDMIFQNIKY PFKGYNIGEN LYQLEINGQE IEISAEYDKN
NNKVFSTFNN QTYIYACSED TLGIHMQLEK DNIFIPNVRN PYHLISNTNG KIVKYLINDG
EEVKKNDDYI EVEAMKMIMT FKSTESGILR HKLSEGTIIK IGDLLGIIEK KDNDKKHIKQ
DNEIQYFNGH LDLSNKYTYE LIDNRTIFPN ILDDNYNKSC DNSYAFTDNM SLQNSEEHYL
VKDEQKKKKK KNISSILNNN MVSIKTVSND LTDNINVLRA ETLSEEGLKD EIYHGQMCDD
RMCDDQMCDD QMCDDENVVK KNDKEQNKSH KNLKENNMDE CTYEDDNYIY MKENQKKKLF
MKQNRKKIFR LFSNDNEKIT TALNYLNDKF HCVKNYLSNL NFSSANSVSD SSNSSYQNNK
NNNNNNDNNN NNYNNNNNNN SKNKKKNNSV QYNYSNAKYS NVNMIHKYDK KPFDKSYLMN
EVNSNNVNVL MMKNKNNSTF PLIENLENNI STEIMSSRNT SNEKILHNNI SKDNTISEPI
FNNNSSDESN INNITFFNNL SNNGSIRKRN NNNNSSSSNN NNNNNNNNKN NNFKHSYYMD
YNNDNIYWNH VKNEKSKYLL DIPIMKRIEF LLKGYEQDYE KCFDELINKK DIKNVSNWSA
YIINNINDIL DTFIQYNILF SKKEFISEID LYDILYNNIR DKKKQYEIIH AYTYNDLSIK
FIEKILKYIL NNINSNLAFD IILDKLKILA EFKGKIFRNI IVLSRHILFL LEGLELIEYI
KIALNYNDNK NMKNGGKLSN NMLLLSNYMK KNNLDFSKMI EYKNNKNDIE IVNMFFKGHS
SNIHMFVPSL IKSNKNSMFL KFYLNNLYKY CNIKSIMVTN NIIKFSINNS EYTNLLIWNE
NDTIDINKIL ESDIKINNDR YLNTVHIINT NNELCLHPSH SFEGNIIKNK ILQKCKKLYI
YNYANNKYGD IYEWKNEDLS KGLVGKYSKD GSINNILPYE EYIFGNEKEI LEYYELKNIN
QAIYEKTKIF FGIYKNNKND NNIRNNVNNN YTSLFGHRVI DFNEIKNTSN EYNNFEEHNY
QDDKFIFNKD IHNILLELKE SLNDISRGRL NTLIRDNKIS SCIIYHIIVD DMMDIETIKE
AYKVFMIKYN EMILENYVNN IFIKIYRTNK KSCTENAPQI QLERMFKLNV LLNKGGVKKE
RTDRYNVEDD NNKKDNDNKY NCNNNNNDDN KYDCNNNFYY DNKYDCNNNF YHDNKFNCNN
NYYHNYHFVE EINQFPSFQI DTLYMKRKRA REVDTLYAYD FINLINISLN RSNKNRESHK
ICNYINSIKE FKLKSDMICY NSNSDNLKNH AMNIKSAHIP LEKKEEYLFE HFDNLSNYEI
KIRKSLYLSD KLDIGQNKRS VVGLLLNIRT DEYEEGRDVI FIINDISTQG GSFSIFEDEL
FYGISSYARE KKIPRIYISC NSGARIGLYN FLMDKIRIEW KDEQKKELGY KYIYITQDVK
EQIDKEDIIF LTEIIENNEK RYIIDAIVGN LKNPVGVENL RGSGLIAGET SKAYEEIFTL
SYVTGRSVGI GAYLVRLGKR TIQKKGSSLL LTGFNALNKI LGENVYVSNE QLGGVNIMMR
NGISQVQVES DQEGMDKIIQ WLSYVPRTSN DYYDLIQNIY KENNRKFLQN NNFLITNKQK
TMNTYNNLFI HNNKNVSNSV DIKDNIKNQI DTNINTETNI NVQDLNIIKK NGINTKSKQD
ENVYEKKDKV EEIYKDQNTY STNNSKTSKP NDNSMSSYNF ELLHINDMDY DHIDDSNIID
LIKGTQEEQG FLDKNTYFEY MNEWGKGIIT GRGKLGSIPV GFIAVNKNLV TQSIPCDPAL
KTKAQKLIQA PCVFFPDNSF KTAQSIEDFN KENLPLFIFA NWRGFSGGSM DMFYGILKFG
SMIVNQLVNY KHPVFVYIPI SAELRGGSWV VVDETLNSQI IEMYADVNSK GGILEPPGIV
EVKFRYPDIR KLMHSIDTTI IALNEKMARC ENDEEKNNIK KDIEIKEKEL LPYYLQVCHK
YADLHDMSTC MKAKGVIRKI VPWNKARSFF YYRLMRRLLI NILSRKYDNA LIKNEEIENI
LNDLNNSEDD DYIVCNRVFN NNILRNLKYD TKDIIYNKTL NDFLKIFKML SQEQRTEFLN
KINSYEN
//
