ID U6GMY8_EIMAC Unreviewed; 2052 AA.
AC U6GMY8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Polyketide synthase, related {ECO:0000313|EMBL:CDI81520.1};
DE Flags: Fragment;
GN ORFNames=EAH_00061600 {ECO:0000313|EMBL:CDI81520.1};
OS Eimeria acervulina (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5801 {ECO:0000313|EMBL:CDI81520.1};
RN [1] {ECO:0000313|EMBL:CDI81520.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI81520.1};
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:CDI81520.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI81520.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; HG671674; CDI81520.1; -; Genomic_DNA.
DR RefSeq; XP_013248779.1; XM_013393325.1.
DR EnsemblProtists; CDI81520; CDI81520; EAH_00061600.
DR GeneID; 25274230; -.
DR VEuPathDB; ToxoDB:EAH_00061600; -.
DR OMA; GWKEHCK; -.
DR OrthoDB; 5491581at2759; -.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.11460; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 382..458
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 480..905
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 1569..1620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1569..1594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CDI81520.1"
FT NON_TER 2052
FT /evidence="ECO:0000313|EMBL:CDI81520.1"
SQ SEQUENCE 2052 AA; 221640 MW; 7B3831643A6C2364 CRC64;
KLLGPNGRFM ELGKRGIWTH EQMKEARPDV YYETIAVDTM MEEDPAWFGG MLDRIRERVE
SGEIISLPLK VFDMEDPVEG GVAAFRFLQR AQHIGKVVVK FASAIEPVED GAIVITGGLG
ALGLVVAGWL AEEGARNIVL IARRDAPPAP GNVPEWDWLS NINCKVSFFS CDVSNYESVR
GVFKKIQKTV APIKGIFHAA GALADSLLDS QSLEGLRRVY NGKVIGAWNI HRVCEEQGID
KDLQFFVLFS SISSLIGNVA QANYASANAC LDALARWRRR KGLCCQSIQW GPWIEQGMAV
EMRQQLARNG MKGITNELGF RTLHDVLLHP ECPPVLACQA FKWRAFFIRY VTVPPLFEGV
PQEAADLPES SGMTMKHLSA AERKEFIKAQ VAAAARQVLG SSSAPSFDKP LQDLGVDSLG
AVEFRNLLSK KLGMKLSATT LFDYPTLNAI TEYVFEATGE EKGPADGSAG LQLGRVAVVH
DGLAVVSVAC RLPGRSNSPE AVWQMLLDRT DCMMDIPLSR WSVYEMYNDD FDFPGKAYVK
RAAFIDNVEY FDNTLFNITP PEVKAMDPQQ RILLEVSYET FISSGFTKTS LHNANIGVFV
GVCNHDWIYL MSDDTISSFS GTGSAGCIIA NRLSYVYGLK GPSVAVDTAC SSSLVAVDVA
FEKVFRGDCK SALVAGANLM LTPHLFIAFC KARMLSPDGK CKTFDASADG YARGEGVAAA
LLVPLSEAQE AKMEVLAVIR STACNHVGRS ASLIAPNGPS QADVVRSAIA RAGIKPDDIC
YVETHGTGTA LGDPIEVHAL KGVFANGRPK DAPLVLGAVK TNIGHLEGSS GIAGLIKAIL
VLQNRTVPPN IHFKKLNEHI NVSDFPVQFP TDTVQLKASG PSKRLLAGVS SFGFGGANAH
VVLEEVPPSL RSVRRPVSRQ KICFMFTGQG SQYVNMGKVL YEENETFRSS LLKASDIVVG
ILGVSIIDIL YPSPQKESEA RELLAGNTIS QLALFAFEYA LAELWMSKSV FPDMVLGHSL
GEYVAACVAG VFTLEDALQL VAARAKIMGD TPSKDGVMAA VRATEEQGEK AISAYYGEKK
RESSVAVVNG LKSIVLAGPR KDVSAILDQM EASSRAKFLS VSHAFHSPLV ESTCSPFKKI
VEQVHLNAPH VEMISTVTGE LCDEALRQPD YWAEHIIKKV RFCDAVQQCV ANGATLLVEI
GPRPTLTLMG KGWAIIQATV EPSTQLPIGI LVEWSLSIVS FQMLCAARGA TPASVVFNRK
YFPWRDICHP LLGRKETRED GRVDFVGGLG EEAELLFADH VVKAQPMLPA TSMLELMAVA
SREVLDKGAA ASPPCLSQLV FEKPLTFQPE SKVSISVSVD SYGQVRLMST SEADEGEERI
HAHAQILTSA IELPDVDNKG ILKACPDEVD MATAYAEFQK VGLSYGPRFR TIKRAFKGEN
AVVGLLQAVS PKNFERGFRM HPAVMDGALQ LSAILLSEKG QRRAMIPFSI ESVTMLSASA
DKEVWARVSL LSRTSTAATV DAQLFTADGK VIADFGGVTF RQIDMEPSAA VPRDLLWYTE
WIPASKLEAQ TTAETESESI GQLSPLSNKV QTPLTPEPAD EDNANPQSDD IEPCSTDTCS
TAEPTRPTVI FLDCTGDHEA LRSDFSDCEE TTVVWLTQPT AETIANTLSM PDASSAIASE
KMLFVLALTS TSTPQDTLSS VLEIAKIMAS QKAAQFYPMW ILTCGTQGPT YDCVHPQNAG
IWGLVRSVRL ELDASGVSHF IGCADIEEGL DIARAVNEIM DQHLVHPQES EMLVRSADLG
SGLQVLFPRL SRSGLVVRGP LELYLPDRGA VTNLVLRPQA HVQPGSLEPG QCRIRVRAVG
LNFRDVLNVM GLYPGDPGQP GADCAGTVVA VGDKVSGLKI GDSVFGIAQG CLKTFVTASS
DLLRPMPATC SFEEAAALPV VAATVEYALG QLAEVKAGDK VLIHTATGGV GLIAIQHCQK
VGATVYATCS GGVKEEHLKS AGIQYITTSR DSKTFAKEMR EFLGPDGHID VVLNTLVEDY
IPESLKLLGP NG
//
