ID A0A0B2UZ26_TOXCA Unreviewed; 2150 AA.
AC A0A0B2UZ26;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Acetyl-CoA carboxylase {ECO:0000313|EMBL:KHN74327.1};
GN Name=ACAC {ECO:0000313|EMBL:KHN74327.1};
GN ORFNames=Tcan_13723 {ECO:0000313|EMBL:KHN74327.1};
OS Toxocara canis (Canine roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN74327.1, ECO:0000313|Proteomes:UP000031036};
RN [1] {ECO:0000313|EMBL:KHN74327.1, ECO:0000313|Proteomes:UP000031036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN74327.1};
RA Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA Gasser R.B.;
RT "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHN74327.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPKZ01002923; KHN74327.1; -; Genomic_DNA.
DR STRING; 6265.A0A0B2UZ26; -.
DR OMA; PTPKGHC; -.
DR Proteomes; UP000031036; Unassembled WGS sequence.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:InterPro.
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:InterPro.
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; 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; 2.
DR Pfam; PF21385; ACCA_BT; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 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 Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000031036}.
FT DOMAIN 48..550
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 206..400
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1417..1750
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 1754..2062
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 2150 AA; 243010 MW; 7015AC3335E74E8C CRC64;
MPTPPLLTHN NREFVDFEKS NEVDQRAETF ATVEEFLGRY ADPKVARPIK TLLIANNGMA
AFKCVMSIRR WAQETFKDDR LFKFINLTTE QEIASNPEYL KMIDNFVFSQ SGGNESNYAN
VDEILKHATG NNVDAVWAGW GHASENPDLP NRLKANNILF MGPPGPAMFT LGDKIASTIL
AQSARVPVVP WSGSDLYLPK EECENGRCDI EVSNELRMAA CVNDHEEAIR IMKEKNIPYP
VMIKASEGGG GKGIRQVRCE AEFEVNFRRV QAEIPGGHIF LMHCLEGARH IEVQLLGDLY
GQVIALRTRD CSVQRRCQKI IEEAPAIAAP LAVQRSMEAD AVRLAKMVGY VSAGTVEYLY
LPSTNEYFFL ELNPRLQVEH PLSEMLTNVN LPAAQLQIAM GVPLHCISEV RLYCGKSRYG
TDKIPFDELH MSSDKHIVSV RITSEDPEEN FRPASGEITN LNFRSTQFVW GYFSHVGAGS
LHEYADSQFG HLFASGSTRH AAISNMLNAL QELQLQSKFP VTVPYLISLF KDSDFEQNEI
NTSWLDRRIA SKKHTIEQPP LPMAVAYGAM LIAHSRITEA FSAFNNAISR GQILQPSDLT
ETHQVELIYN NVKYSVTATR TSNIEYTVKL NGCSTRVEYR ELRNGTLLLK YNERSHPCYV
DEEAERYKIH IGRTQITFEK ENDPTVLRSS CAGKLLTYEA EDGDILKPGQ LFASMESMKV
VLDMRTKKVG GRFKRVAQVG QVLHPGTLVA RLEAQAGVEV TKPVDFEGTF EEWAHTSTTT
SPINIHFSEI VQEVRNVFDG YCKAEPTFAQ YADSLVASLF TVLSERSLPY EQMRQILAVL
KSRIKATMLQ KLHAFVDCKS GTLPQFPAKA IRNAVNASEY LEPMDPQRLS VERLNFAPIL
AICDKFANGE EGHTSLVLKE LFGYYLQGEQ YFQFLQYDKC VSNLLAEVKD TERCVRTIYS
HTRINEKNLL AMKLLKRMSN NRRLILSQAA ILEKMAGFMK SENIELAHMA RALLIDAETP
TYTEIKLRGS SPSPSNLEKY EILFETFNSS FDSVQKYVTI CCGVPESSLM RLEDGHPNDV
RFPIRVQKIA HGLGLPNDVV EEHSVDLRIV GDVLDITISL PEAAAKVVKP GSTLFVVSHS
RTPKYTPDSE AKLAAMIKET MMGLRSDCMS QLVVMVAPSE SYPLYFYYDM NTREELVSRR
NVDFAHLPKL GLRRLEENYN VEKVRSPYSS GHLYRAQGKQ DRTELRFFYR AVVRVVDSYT
ASEVTCSLKK ALKRAAGEIA VGLYRSNTID RNHVFLFIDR TPSSNKIQMS PADWRNVVYK
AYRDCKEYLW RSRVNQVEVD FVLFGETRSY EQATKILITD DTGFTPCIRF LRAEATNGNS
APSRWVHVDA GMDGFEHGLE IMVEGNRNPD WNPFIDPYLG RSEIDKRRLK AHAAKTTYVY
DYPLLFQRAL IVEWTTAPSS TKRRERLLPQ DLCEFRELVY DESSKKLLVR EDAGSLSKIG
MVAWRVRLIV PEYPEGREVI IIANDISHQI GSFSMREHNL YNAASKLSRD EGLPRIYIAA
NSGARIGLSS DLKRLFRVMW KKEGSPEQGF DGLYLTDDAL TEVKDLVDVE RVGEYNQLMG
IIGKERDLGV ENLVGSGLIA GETSRAYDDV VTYCLVTGRT VGIGAYVARL SRRICQVENA
DIILTGAPAL NSLLGRPVYT SNGQLGGTQI MTRNGVSHSS VANDFDGVCQ LLRWLSHTRK
TTKAPFNQQK FVDPIDRPVC YVPSANKEND PRYMLTGHQD MTTLEYLDGL FDRNSFEEVK
PGWGKTVITG RARLAGISVG VIAVETRSVV TEIPADPAAP DSQVKYIQQA GQVWYPDSAY
KTAEAIVDFN KESLPLFILA NWRGFSGGQK DMFEMVLKFG AYIVDELCRY AHPVFVYIPP
FGELRGGAWA VVDKTINPMC MHMYADPRSR GSILEPEGTV QVKMRKDFVP LMYRLDAQMQ
QLAARQEAGE DVKEELEARI EFLMPTYRNI CINFADLHDT PVRMKAVGAI EGVVRWEESR
SFFARRLLRL CIERDIYREC GEVKSVEDIR KSHASMLDYF AKSRGEQFCW EQLDDEQAVA
ILTRERPNIV AHITHNELAI IGQRYGVPIN KLNEFARKCD QLIREIRGQM
//
