ID U6LW93_9EIME Unreviewed; 2503 AA.
AC U6LW93;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Acetyl-CoA carboxylase, putative {ECO:0000313|EMBL:CDJ53523.1};
GN ORFNames=EBH_0007810 {ECO:0000313|EMBL:CDJ53523.1};
OS Eimeria brunetti.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=51314 {ECO:0000313|EMBL:CDJ53523.1};
RN [1] {ECO:0000313|EMBL:CDJ53523.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ53523.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ53523.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ53523.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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; HG713352; CDJ53523.1; -; Genomic_DNA.
DR EnsemblProtists; CDJ53523; CDJ53523; EBH_0007810.
DR VEuPathDB; ToxoDB:EBH_0007810; -.
DR OrthoDB; 911at2759; -.
DR UniPathway; UPA00655; UER00711.
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; -; 2.
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; 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; 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 PANTHER; PTHR45728:SF3; ACETYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR45728; ACETYL-COA CARBOXYLASE, ISOFORM A; 1.
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; 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; 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; 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 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}.
FT DOMAIN 227..752
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 406..601
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 870..944
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 1722..2068
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 2100..2418
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 176..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1555..1589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1609..1648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1663..1700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2100..2128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1165..1192
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1271..1302
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2329..2358
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 811..826
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1621..1648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1669..1696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2503 AA; 269663 MW; ECB726C263C852C1 CRC64;
MKLKGEERQI SMGIVRFLLG GYQSAFLSLP LLLPRLLLLL LLLLLTPASA WAFTDLAGVP
GGALLPPQLQ QQQQLQQGLH LPLLPPLQQQ QQQQLPPAFL VSLGNPQPSG LSCRLNRTQG
QALECRSLLF SSRRHTSAAP AAAAAVATAA AAEYQPRTGA AAATALAAAA EAAAAAAPTM
QPTPEGPPPL SGPQKAQAEE VKRQSGPWME AADPLSAYVK LHGGDRPIRR ILIANNGMAA
TKAIASMRQW TFETFGDPNV SPAPTAAAAA VPELVLLPRH MLEQGELCLL LTFVAMASPE
DLEANSEYLK KADEIVPVPG GPSRENYGNV PLICDIAVKQ KVDAVWPGWG HASERPELPA
RLKALGLAFL GPRAPVMAAL GDKIAANILA QTARVPAIPW SGTGLTAKLD RDGNIPPDVF
KAATISSLDQ CRAAAERVGF PVLLKASGGG GGKGIRLCMN AADLETALVQ VEAEVQGSPI
FLMKLCEKAR HIEVQIAGDK HGNAVALSGR DCTTQRRFQK IFEEAPPTVV PPETFKEMER
AAQRLTQSLG YEGLGTVEYL YSPSSNSFFF LELNPRLQVE HPVTEAVTAQ NLPALQLQIA
MGIPLYRVPS IRTFFNKNPT GTDKIDFLTE DYRPLNMHVI AARITAENPS EGFRPTSGRV
RSLDFAPPEK VWGYFSVSAN GALHAHADSQ FGHIFAAGDT RNEARKRLIW GLQQLQIRGD
IRTPIDFLQR LLQQPAFVNH TLNTEWLDGI IKAKGLLPAP KTADVVFASA AFRAIQALEV
SAHPAAAAAN GDDGGAAADD TAAAVDDGPI VDDPAADDED GLSEDNAVAD DPAAASVAAA
LLLLLNVLAG FATEEPLGLR LELGSSSLMV LDQRDPSELR SDVNGRLVRY LIQDGETVKK
GQPFAEVEAM KMILTLTAGE SGVLIHRKSA GSLIQQGELL ASLRLADPSK VVRLLPFEGS
LDLSPPPLSP PAETAAAVGA AAEAAAAAGA DAAPAAPKAE QEAAEAAAAA ESRLELLLSG
FVQMQAAQQL LQQLIGGPCG TSISTFVSFV ERCLTRFLET EELFAGKGNA DAAAAVAAAA
TDTEGQFRMY VSHYALKNKA EVLLLLLKEL TARLAAPGAG SFDSTRLEDL LRRVGALKGV
AYNVLALASQ RLLKQLLLPP VADRVDTLRS QLQQLQQQQQ QEQQQVLRDE LLQLPEELGG
YGLLAHLFKD PQVGRAAQEM TLRRQLLGLD LQLQQQQQQQ QNAIPFTWRR SLEEGAAVTE
NGGLFAAVSS VEELQQKMGP LLQQLQQQQK TLKQEAKGLL LVSLPPSNIQ QGTGGAQTAA
TEAAAAAAAA AAAAAAKSPE AAAALRSLHS LRLLLPTANG DAQQVALLLQ QDQQQLKEDP
LQRGLSLSQF VFGEIEMMQS VGTVRRLPSA AAAAAVPPAA STDLLMHAVS PKPPAPAAGA
AAPLRTPPQR ETVFVHRIIP KADVLLQQQG LQQLLQHLLQ QLEAAFRDPH VHPTSNSTVV
VQLLQRESAA RQTALQKCFF EALQRLKAEH GDRLLRLNVE KVELRVPQDA TTATATAAGA
AEATGNTAGE SGAGAGAVGA AAPPQQQHVV RASSRGGCWL EPEEVSPGYE GGCDLHAPAG
SRLKQQQQQQ QQHPLAPEAS TAESSAAPSP LLSELFTPES VSFQEGEGDA LAASSSSSSV
ASSSSHRSSS LTNERLPFSW GRGGTAAAAA EAERTAPLVP LRGITDAQLA AKRAAAQRAG
STYIYDFLGL INAELQEQWR RSQEALAAAG DTRPLSVPHK LLEAREFHMG PDGKLQLHRE
WRVGDNRVGM VAFLLLLRTP EYPQGREVVL IGNDVTYQGG SFGVEEHEVY RQASAFSRQH
KIPRLYIACN SGARIGVYEQ LKEKLQVEWN DPQNPWLGFK HLYIREEDMK ELPEGAVVGH
WSTSPAVQGQ RVFVLEAVIG EGGQHLGVEN LRGSGKIAGE TSQAYDEVFT LSLVSGRSVG
IGAYVVRLAQ RCIQQKQSPL VLTGYQALNK LLGRDVYISQ EQLGGPEVMG PNGVTHLQVA
SDKEGIAEAV RWLEFVPPTA DAVHTPHRIT DPIHRNVDFQ PSSTPYDPRH MLAGHWVEET
PDKQQQQQQQ PQQQQQQQQQ QQQPQQQQQQ QQRWVSGFCD KDSFKEVLGP WGAGVVVGRA
RLGGQPIGVI AVDTRTTTAS SPADPANPDS ARVDTPQAGQ VWFPSSAYKT AQAIADFNRG
ENLPLIIFAN WRGFSGGTRD MFNEVLKFGS MIVDALRVYR HPVFVYIPPY GELRGGSWVV
IDPTINSSQM ELYADERARG GVLEPPGICE IKFKEAERIK LMHLNDHAMQ QLHKDLQAAK
TEEEVAKIKE NIKKRESLLM PVYTQVAHVY ADLHDRAPRM AARGGVRKIL NWQRAREFFY
WRVRRRLAAN SVVKKLMAAD LSLTWDEALS LLNSDIPQIA DTVEDAEAVA FLESNEGREK
VGALLRRTEG AAARRELLQL VGRLSAAEKK DVLSEVQSLL SQQ
//
