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PKS24_DICDI
ID   PKS24_DICDI             Reviewed;        2471 AA.
AC   Q54KU5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Probable polyketide synthase 24;
DE            Short=dipks24;
DE            EC=2.3.1.-;
GN   Name=pks24; ORFNames=DDB_G0287119;
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; EAL63924.1; -; Genomic_DNA.
DR   RefSeq; XP_637425.1; XM_632333.1.
DR   AlphaFoldDB; Q54KU5; -.
DR   SMR; Q54KU5; -.
DR   STRING; 44689.DDB0230081; -.
DR   PaxDb; Q54KU5; -.
DR   PRIDE; Q54KU5; -.
DR   EnsemblProtists; EAL63924; EAL63924; DDB_G0287119.
DR   GeneID; 8625958; -.
DR   KEGG; ddi:DDB_G0287119; -.
DR   dictyBase; DDB_G0287119; pks24.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_0_1; -.
DR   InParanoid; Q54KU5; -.
DR   PhylomeDB; Q54KU5; -.
DR   PRO; PR:Q54KU5; -.
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; 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; 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; 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   SUPFAM; SSF55048; SSF55048; 1.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW   Transferase.
FT   CHAIN           1..2471
FT                   /note="Probable polyketide synthase 24"
FT                   /id="PRO_0000367830"
FT   DOMAIN          2336..2413
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          171..224
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          654..687
FT                   /note="Acyl/malonyl transferase"
FT   COILED          1426..1469
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        190
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        664
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2373
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2471 AA;  280910 MW;  C78993A055394DB1 CRC64;
     MKQNKINKAE ILQVDDKHVE ENLVAIVGVG FRLPSGSIEN ERNNTPQTLW NNLINGFDGV
     VKTSERFNDN FFKNHEIANN YSGLLPLDEV KSFDPLFFGI NPNEAPTIDP IQRLLLKCTW
     EALEDSLIDP ISIKGTDTSV FIGCTESDYH NINKNEVKSN VFSSLNHAIS NRISYCYDLH
     GNSITLDTAC SSSLNAIALG YDSIKNKKSK MSIVGGVNIL LDSYFFKAYS SLNILSKSNG
     RCKSFDASAD GYVRSECIGV VVLKNLKDAI KDGNRIYCTI NGASANVDGI GYSDKSNFYS
     PSSISQSENL KNAIQSTNGT VKPSDIDYVE AHGTGTPTGD PIEVEGISKV FKDTRSTDTP
     LLIGSFKSNI GHCEAASGIA SLIKCCLMYK NKCFAPNIHF KTPNPAIKFK EWNLKVVTEP
     IPFNKFKNTS MVVNNFGATG SNCCLVLSQF NYNTINNNIN NHNNNHNHNH NHNNIKINNY
     LIPFSANSVE SLKKYQSLII ENKEYESQYS FEEFVKNQIY NKSTSLYQRS VIVAKDWNDF
     NNVENQVKYQ TSSSTSSNIT ITNKNNNPIT VFVFCGQGSQ YNTMALELYK NEKVFRNSMD
     MLDNKMKNYF GYSILEKLRA IQDSDKCSVH EQTMAQPSTV IIQVSLYELY KHWGIKASFM
     LGHSLGEVTT AYCSGMIDID QLCYLIYHRS TLQIRTNGSG KMLSINISSD EYKTNYMSRY
     PTIEIACYNS PSSIVIAGNE QILNEISKEL KEKEIFSAML GSLSSFHTSS QNIIKDDILN
     LNIQSSQPVI PTFSTVTSNL FNESTIFDSE YFFDNISKPV SFTQTISNLY KHIEDNQIGS
     NIVFIEIAPH PTLSFYLKQM IPKQSQYFRN GESISVYSTL HKKKNDVEEF QKSISQLFCD
     DAYDINFKCQ FNNINSNIEA ISNFNLPLYQ WDDQHYWLNK SIEHKNNLIG PPISILGNSM
     QDSNPFIKSY QTIIDTGKDA FKYLKGHNVS DKCYFPGTGY IDNIFKLYPN QDLTINSIEF
     KVPFVLTDGI GQCLQTNVYQ TGKSEYRAQF HLKDEMNNQW INTSNSNFHL NSNDNYHEEK
     QKLDIQDIKQ TKCNLSSIPW DEFYSLMKTQ LGANFYGIFS KVVECYIGDN CSLTEISLEL
     PENFHDEQSF FNCPLIDACF HGTVILYIQK NCKIVTDKVE GLRYYASNIP KNRDEHSSIF
     IYSTLKSSPS DDLLSSSIVV MLEDGTVIIE VDNLVVKSLT PVKDPLLIET PSDFIYTPYL
     QSKDSQIQSP LEFKSIYQNN QVDDGLLIPN VVIETIKPLI NRKMEFRILE FGGNNLSKST
     LLLNEINSLL EENPHYEIDI EYTWSDNNSS ILKDAKLELS KVDKGYLSIL YRSLGLDVDN
     SLLEKQKLNP SYYDLIIVSN ISNLTKDIEY SLNQIYQILT PNGYLIINEQ QQQQQQQQQQ
     QQQQQQQQQQ LLNNENNKES LKNLLVNCNF NSDIMIKSSS ISDSDIKSII IQAQKPSLKL
     QPKTINTFDQ VILYCYQDEQ LQQQQLINKF ENHYNNCKII KVSTIEEFYK LSTTITNNSI
     IYFIKSIEQL TLENFKSVTF EYVQINQKLY ELKSKCTHVL ITCDSQSSNY LSSSVLGAAR
     YFDEIPTLQL FTLDFDKDSL TNDLDLFKTI DYLINPKNNI QREFYIKNSG TVYFEMYKKE
     LKNLKNSYKS ESYHDLSKQQ DQLVSKLDEH FEYQLNSKQI DLEPYEIEVK VKATGINYKD
     YLKYNEMIKV NEAGIGFDFS GVVSRVGIKS SKEFKVGDQV YGIAYETSSS HIIIDSLLAC
     HKPSKITHVQ AASIPAVYST SLYCLYDVGN LRDEESVLIH SGSGGVGLSG LEILKSNNHS
     SPIFVTVGSE EKKQYLINTY GDLITGIYST RDTNYQKQIK NKLIELGYET HGVDLIINTL
     SSEFMDTNFK CLNPKGRIVD LTTTHLNPNE FIDNSRYRYN IGYNSIEILK VGKSTIKKLL
     QSISKSIENE TLNALIPITE FSNSNIKKSI ESIKERKHVG KIVISHDTDI IDKLIEKESM
     IDYSILKSDY KIKNLGKNVL VTGQTGLILE VLKWITKYNS TVENIIILSK SSLKWELEFL
     MNYNNNNNNN NNNNKIKYHF KKCDISNWNL INKTIDQVLK DNPTITNIDS IFHFAALQIN
     KKLKDIDMNS LNVSHSAKTF GAVNLHNLSI KRDWKIINFI LASSVVSVLG SFDQCSYVSA
     CCVVDSLSQY RKSIGLPSFT INIGGVSDRG YLSRHKLVEA VLGGQGVELI SPNQLLGTLD
     LQIQNPNMPT NAFVNNFNWP LFKSFKQKLH QKFDFILNPI NVDNSISMEN DTNQSSSSTN
     VKNKFLNKVS ELLSIDPSKI NTNIKMINYG ADSLITVQLK NWVDKEWSPH LITIQQIQSN
     SIGMVYQIIN DSLDKKKKEM DEKLLPITAK TTTTTKNDPN DKTEYKYIAG GDCCREFSIK
     FHYSSVVNFI I
 
 
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