PKS22_DICDI
ID PKS22_DICDI Reviewed; 2499 AA.
AC Q54QD3;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Probable polyketide synthase 22;
DE Short=dipks22;
DE EC=2.3.1.-;
GN Name=pks22; ORFNames=DDB_G0284001;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP IDENTIFICATION.
RX PubMed=17660200; DOI=10.1093/bioinformatics/btm381;
RA Zucko J., Skunca N., Curk T., Zupan B., Long P.F., Cullum J., Kessin R.H.,
RA Hranueli D.;
RT "Polyketide synthase genes and the natural products potential of
RT Dictyostelium discoideum.";
RL Bioinformatics 23:2543-2549(2007).
CC -!- FUNCTION: Probable polyketide synthase. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000250};
CC Note=Binds 1 phosphopantetheine covalently. {ECO:0000250};
CC -!- DOMAIN: Modular protein that is responsible for the completion of one
CC condensation-processing cycle. The beta-ketoacyl synthase region is
CC responsible for the actual condensation reaction while the acyl/malonyl
CC transferase region is responsible for incorporating carboxylic acids
CC units onto an acyl carrier protein (ACP) domain (By similarity).
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Encoded by one of the numerous copies of polyketide
CC synthase genes and clustered as a pair pks22/pks23 in chromosome 4.
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; AAFI02000058; EAL65488.1; -; Genomic_DNA.
DR RefSeq; XP_638811.1; XM_633719.1.
DR AlphaFoldDB; Q54QD3; -.
DR SMR; Q54QD3; -.
DR STRING; 44689.DDB0230076; -.
DR PaxDb; Q54QD3; -.
DR EnsemblProtists; EAL65488; EAL65488; DDB_G0284001.
DR GeneID; 8624335; -.
DR KEGG; ddi:DDB_G0284001; -.
DR dictyBase; DDB_G0284001; pks22.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_5_1; -.
DR InParanoid; Q54QD3; -.
DR OMA; NWIRANI; -.
DR PhylomeDB; Q54QD3; -.
DR PRO; PR:Q54QD3; -.
DR Proteomes; UP000002195; Chromosome 4.
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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.150; -; 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; IPR013154; ADH_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; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
KW Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..2499
FT /note="Probable polyketide synthase 22"
FT /id="PRO_0000371385"
FT DOMAIN 2414..2491
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 158..211
FT /note="Beta-ketoacyl synthase"
FT REGION 623..656
FT /note="Acyl/malonyl transferases"
FT ACT_SITE 177
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 633
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2451
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2499 AA; 282695 MW; DD7EEADA0AEF8D3A CRC64;
MIEGNIEKNN DNQVAIVGLG LRLPGNSGSP SEFWKNLLGG FDGIVDSNER WSDTFHSMGE
ISNKNAGLID LEENWHSFEP LFFGINPTDA KQIDPQIKLM LKLTWEAFED ASIDPLKLRG
TNTSVFVGAA NTDYSFINFE QNEAPINVFN GTLSAFANRI SYCFDLRGTS LTLDTACSSS
LNAVHLGYES IVNGKSNYSV VAGCNILLNP YITRSFHSIN ITGKSGRCNS FDESADGFVR
SEGVVVLILK RLSLAIQDGD QIYCVMKGSS SNVDGTFKKT NFFAPSKNAQ STNIKNAFLS
SNGAMKYQDI DFFELHSTGT QVGDPIEVEA VADIFKNVKQ EPLLIGSVKS NIGHLEPASG
VASLAKVCLM FKHRQFVKNI HFNNPNPNIK FKEWNVKVCT ETTAFPDRQV SMAINSFGIT
GSNACVLLSE YIKPSELKNQ TSMKLNEKSK LLIPISTNSK KSLEQFKSKL LEEIDTYSES
LTFEEFAMFQ VYSKTTKLSQ RSVLIGNDWN DLKIDINEII STKNNKSGNI IKSNDINPPL
VFSFCGQGPQ YSKMGLNLYE NEPIYKQSMD ILDSILFKYF GYSIIQKLRS INDDPILINE
PILAQPSIFM IQISLYKLYL HWGITPSIIV GHSLGEVASA FCSGMIDLET ACFVIYKRAT
IQNKTNGSGR LLAISLNLEE FNNQFSKEYP EIEISCFNSP SSIVVCGNEL DILNISKSLK
DKQIFNSLLG TSSAFHSSKQ DIIKDEIIES TNHIQSRPPS ITTFSTVTSN KFDKNTPYNS
SYIFDNLRKP VLFQQTIENI FKHIESNDLG NSVIFLELSP HPTLNHYVKE MIPKNSNYFL
NKDSISVLSS LNKKKEDINE IQSTISQLYC FGYNVDFSAQ FKSEITSNSF KKCSYLIPHY
QWDESLFWRE GISSLNNRKN GAPINQLGNK NESSPHISYT SYIDIKEEPF RFLKDHQFRG
KSLFPGVGYL DIILKLFPNQ DLTIPLLEFK SQFVLTEGVK KTLTTNLYKS AKNEYRATFN
FKDQTSGKWI QSANSRILMK SLDVTVKKVD VQSIRDQCNW STLKREQLYD LIKNYANISL
LEPFQRIEEA SYGDNRCLCK VSLDPTSSYD NESFLNICII DTCIHPCIFF DNPASSVFER
IEHLKIYSSS VPLTAEDRVK QQYVYCYAEL IKQFSDFIYF KTTCFLKDGT VLLHSPLVTI
ASTLSTKSET DLECPNNQLF SQCLQPKDSI LQSPLILKEH FNQQLQLQQS NIISISTLST
YLFSILKKRL NNLTVDEFQN NSLEQLIEKY SYVLDEVEVG TIRSNLILLT INFLLTHHKH
IDQNQVSNFL LNNIPNELLV VDTIVSNKGI SHIGIYQHQL ILDIISKSII PIVNEKIVFR
ILEIGCGVGE LTKLINDNLE SILNDNPSYN IDIEFVFSDY TDSKVLLIKE RLFNSKKSCF
FKIIDLNKQL QEQSFSPSYY DLIILSNTTN QIKDIKTSIS FINEILTPNG HLLILDTNFI
QTSIDEDYYL ENYKQWLSFN YLNSGSGAMK LNQWNQLLIN DLKFNNFICS TGEIEPYLIQ
VQKPNLSNSI NSVSKEHTSE YDQIIIFGTC DEINIGSSFC GSGGVVPIAI NSIDKFKEHA
KLQPLTDKSL ILFIESVNLL TVDNFNQVSM NYIEINQHLL KNEISGCKHI LISRNINFET
SNLFGSSLIG SFRYFCEFNQ LNIYSFEFEG NNILSGGDKL FNIIQELSNS NKHSQNEFSI
RSDGKIYYER IKLESNLKLK YKSKSYIENK NELVSRLKPD LTFALEAVLP LNPNFVEVKV
MASGVNFKDF LVYRQLINMA NSNENGDPSK PQFGYELSGI VTKVGKNVTK FKVGDHVMGV
TFHTFSSSVH VDQDRIELKP SNISWFEASI SLVYLTSYCS LFELGRLGLH GSTETVLIHS
GSGGIGLSCI DLLQVYGFKG FLFVTVGSEE KKQFLKDRYG NFITEIYSTK NTDYEYLIKE
KLIELKAPSQ EYGGFSMICV DLIINTLSAD YMDANFNCLS QGGRIIDLSI THMTTTDTTD
FYKFKNHIGY MTYESVIAGF RKHKHVLKII VDLLASGKLK TIPFNVYPVT KIKEAIESLG
DRKHIGKNIV NFNDPEGIDL IDCPEFSNNH NFIHRSSNYK IHQDTLGQTI LITGQAGLSD
TIIKWIREKR SDSIESIIVL SKSPIKFELE RAIGRIRSTN LKIYFKQVDI SDEKLLLKTI
NQLFEENKDI KPIESIFHNA FSPAECEPLE IDMNHLISSH SAKSMGAYNL HKLSLNWPIK
QFVLSSSVTS ILGSQRQCGY VASNCFIDAL SRHRKSLNLP CISINWGLLG GGGFAARNDA
VFKLFELQGL VGISKDLVWG SLDLLLQNQN ESTNKMVASF EFHATCKTYK NHKLSYKLDY
FLNPIISKES VTDEKEFSIR QDIVDKFASL LSTDQSKLNL DIKVIDYGAD SLLVVEVKNW
ADNKFTRNIL SMPEIQNSTI NQIINIVTTK VSNLPSKKK