PKS25_DICDI
ID PKS25_DICDI Reviewed; 2380 AA.
AC Q54KU3;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Probable polyketide synthase 25;
DE Short=dipks25;
DE EC=2.3.1.-;
GN Name=pks25; ORFNames=DDB_G0287095;
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 pks24/pks25 in chromosome 4.
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DR EMBL; AAFI02000096; EAL63912.1; -; Genomic_DNA.
DR RefSeq; XP_637427.1; XM_632335.1.
DR AlphaFoldDB; Q54KU3; -.
DR SMR; Q54KU3; -.
DR STRING; 44689.DDB0230080; -.
DR PaxDb; Q54KU3; -.
DR PRIDE; Q54KU3; -.
DR EnsemblProtists; EAL63912; EAL63912; DDB_G0287095.
DR GeneID; 8625960; -.
DR KEGG; ddi:DDB_G0287095; -.
DR dictyBase; DDB_G0287095; pks25.
DR eggNOG; KOG1202; Eukaryota.
DR HOGENOM; CLU_000022_31_0_1; -.
DR InParanoid; Q54KU3; -.
DR PhylomeDB; Q54KU3; -.
DR PRO; PR:Q54KU3; -.
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; 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; 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; 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; 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 SUPFAM; SSF55048; SSF55048; 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..2380
FT /note="Probable polyketide synthase 25"
FT /id="PRO_0000371387"
FT DOMAIN 2299..2376
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..232
FT /note="Beta-ketoacyl synthase"
FT REGION 649..682
FT /note="Acyl/malonyl transferase"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 198
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 659
FT /note="For acyl/malonyl transferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 2336
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2380 AA; 269876 MW; 28E19C43818B1035 CRC64;
MDNSYLNNPQ FDINNGNKEV TDDDNNKNNQ DNLVAIVGVG FRLPSGENER NNTPQALWNN
LINGFDGVVK TSERFNDNFF KNHEIANNYS GLLPLDEVKS FDPLFFGITP NEAQTIDPHQ
RLLLKCTWEA LEDSLIDPIS IKGTDTSVFI GSSTNDYLTL NRNEVKSNVF GSMAHSIANR
VSYCYDLHGN SITLDTACSS SLNAIALGYD SIKNKKSKMS IVGGVNILLD PYPYKAFSIL
NMLSKSNGRC KSFDASADGF VRGECIGVVI LKNLKDAIKD GNRIYCTING ASANVDGIGY
SDKSNFYSPS SISQSENLKN AIQSTNGTVK PSDIDYVEAH GTGTPNGDPV ETEGISKVFK
DTRSTDTPLL IGSFKSNIGH CEAASGIASL IKCCLMYKNK CFAPNIHFKT PNPAIKFKEW
NLKVVTEPIP FNENKNTSMI INNFGVTGSN CCLVLSQFNN TNKQKQQMKT KINNYLIPFS
ANSVESLKKY QSLIINSKEN ELKYSFEEFV KNQVFIKPTS LYQRSVIVAK DWNDFNNVEN
QVKYQTSSST SSNITITNKN NNPITVFVFC GQGSQYNTMA LELYKNEKVF RNSMDMLDNK
MKNYFGYSIL EKLRAIQDSD KRSVHEQTMA QPSTVIIQVS LYELYKHWGI KASFMLGHSL
GEVTTAYCSG MIDIDQLCYL IYHRSTLQIR TNGLGKMLSI NISSDEYKTN YMSRYPTIEI
ACYNSPSSIV IAGNEQILNE ISKELKEKEI FSAMLGSLSS FHTSSQNIIK DDILNLNIQS
SQPVIPTFST VTSNLFNEST IFDSEYFFDN ISKPVSFTQT ISNLYKHIED NQIGSNIVFI
EIAPHPTLSF YLKQMIPKQS QYFRNGESIS VYSTLHKKKN DVEEFQKSIS QLFCDDAYDI
NFKCQFNNIN SNIEAISNFN LPLYQWDDQH YWLNKSIEHK NNLIGPPISI LGNSMQDSNP
FIKSYQTIID TGKDAFKYLK GHNVSDKCYF PGAGYIDNLL KLYPNQDLTI NSIEFKTPLI
LSDDNGQFLQ TNVYQTGKSD YRAQFHFKDN RTNVWVQTCT ANFQLYNNGK VDKLNLEEIK
STKCNLSSIP WDKFYPHIKN RTGLNYKDKF QNTIECYLGD NCSLTEISLE LPENFHDQES
FFNTPILDIC FHGSIVLIKD NCKLVLDKID GFKLYTSNIP KNRFDHLSIF VYTTMKSTKS
NSYNSTYTVM LEDGTVILEV ENLICTSLTP VKDPLLIEIP TDMYYTPYLQ SKDSQIQSPL
EFKSIYQNNQ DNDSLLIPNV VLETIKPLIN EQMEFRILEF GGNNLSNSTL LLNSINSLLE
ENPHYEIDIE YTWSDNNSSI LKDAKLELSK VDKGYLSILY RSLGLDVDNS LLEKQKLNPS
YYDLIIVSNI SNLTKDIKYS LNQIYQILTP NGNLIINEQQ PNNENNENNE DSLKNLLVNC
NFNSDIMMKS SSVSDSDIKS IIIQAQKPSL KLQPKTINTF DQVILYCNQD EQFQQQQQLI
NKFESHYNNN CKIIKVSTIE EFYKLSTTIT NNSIIYFIKS IEQLTLENFK SITFEYVQIN
QKLYEFKSKC THVLITYDSQ SSNYLSSSIL GAARYFDEIP TLQLFTFDFD KDSLINLDIS
VIDHLIDPKQ NTLIEFFIKK NGKVYFERFK KGLKKNSFKS ESYHQITNEQ EILISKLDEN
LDYQLKSKDS ILKPYDIEVE IKATGLNYKD YLVYSGLIKL KGDSVDFGLD FSGRVSRVGI
KSSKEFKVGD EVYGIGQSTS SSHIIIDSMH ACHKPSKITH VQAASIPAVY ATSIHSLYNI
GNLREGESIL IHSGSGGVGL SALEILKSNN HSSPIFVTVG SEEKKQYLIN TYGNLITGIY
STRDTNYQKQ IKNKLIELGY ETHGVDLIIN TLSSEFMDSN FKCLNPEGRI VDLTITHLNP
NEFIDNNKFK YNFGYHNIEL YYCEKPTIKK LLQSISKSIE NNTLNYLIPI TEFSNSNIKK
AIEYINERKH VGKIVISHDT DITNKLIENQ PKIDYSLLKS NYKIKNLGKN VLVTGQTGLI
LDIINWIMKY NSTVENIIIL SKSSMKWEME FLINNNKTKI KFYYKRCDIG GDSDSINKTF
DKLFTENPTI TNIDSIFHFA VVQITRKVKD IDMKSLNISH DAKTIGAINL HNQSIKRDWK
LSNFILASSI LSKVGSLDQC GYVSACCVLD SFSKYRLSIG LPALSINIGA MGGSGMVARS
ELVETVLNGQ GYNLTSTNQL LGTIDLLIQN PGQESNNLMV GNFNFPVFNN FKQKIHQKFD
FIFNALDSNS ENGDGSNIKN STNIKDKFLN KVSEFLSIDS SKINNDIKLM NYGADSLITV
QLKNWVDKEW SPNLITIHQI QSNSIGMVCQ IINDNFEKKK
