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PKS16_DICDI
ID   PKS16_DICDI             Reviewed;        2603 AA.
AC   Q869W9; Q554C7;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Probable polyketide synthase 16;
DE            Short=dipks16;
DE            EC=2.3.1.-;
GN   Name=pks16; ORFNames=DDB_G0275069;
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=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2]
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   [3]
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).
RN   [4]
RP   INDUCTION [LARGE SCALE ANALYSIS].
RX   PubMed=18590548; DOI=10.1186/1471-2180-8-109;
RA   Carilla-Latorre S., Calvo-Garrido J., Bloomfield G., Skelton J., Kay R.R.,
RA   Ivens A., Martinez J.L., Escalante R.;
RT   "Dictyostelium transcriptional responses to Pseudomonas aeruginosa: common
RT   and specific effects from PAO1 and PA14 strains.";
RL   BMC Microbiol. 8:109-109(2008).
RN   [5]
RP   INDUCTION [LARGE SCALE ANALYSIS].
RX   PubMed=18559084; DOI=10.1186/1471-2164-9-291;
RA   Sillo A., Bloomfield G., Balest A., Balbo A., Pergolizzi B., Peracino B.,
RA   Skelton J., Ivens A., Bozzaro S.;
RT   "Genome-wide transcriptional changes induced by phagocytosis or growth on
RT   bacteria in Dictyostelium.";
RL   BMC Genomics 9:291-291(2008).
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   -!- INDUCTION: Up-regulated by P.aeruginosa, PAO1 strain and PA14 strain
CC       infection and down-regulated by phagocytic stimuli and growth on
CC       bacteria. {ECO:0000269|PubMed:18559084, ECO:0000269|PubMed:18590548}.
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 pks16/pks17 in chromosome 2.
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DR   EMBL; AAFI02000013; EAL69815.1; -; Genomic_DNA.
DR   RefSeq; XP_643784.1; XM_638692.1.
DR   AlphaFoldDB; Q869W9; -.
DR   SMR; Q869W9; -.
DR   STRING; 44689.DDB0230068; -.
DR   PaxDb; Q869W9; -.
DR   PRIDE; Q869W9; -.
DR   EnsemblProtists; EAL69815; EAL69815; DDB_G0275069.
DR   GeneID; 8619829; -.
DR   KEGG; ddi:DDB_G0275069; -.
DR   dictyBase; DDB_G0275069; pks16.
DR   eggNOG; KOG1202; Eukaryota.
DR   HOGENOM; CLU_000022_31_5_1; -.
DR   InParanoid; Q869W9; -.
DR   OMA; YVAMVGE; -.
DR   PhylomeDB; Q869W9; -.
DR   Reactome; R-DDI-163765; ChREBP activates metabolic gene expression.
DR   Reactome; R-DDI-199220; Vitamin B5 (pantothenate) metabolism.
DR   Reactome; R-DDI-75105; Fatty acyl-CoA biosynthesis.
DR   PRO; PR:Q869W9; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0019953; P:sexual reproduction; IEP:dictyBase.
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; 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; 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; PF00550; PP-binding; 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   2: Evidence at transcript level;
KW   Phosphopantetheine; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..2603
FT                   /note="Probable polyketide synthase 16"
FT                   /id="PRO_0000371381"
FT   DOMAIN          2506..2583
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          160..213
FT                   /note="Beta-ketoacyl synthase"
FT   REGION          631..664
FT                   /note="Acyl/malonyl transferases"
FT   REGION          1358..1407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2580..2603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1360..1407
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        179
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        641
FT                   /note="For acyl/malonyl transferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   MOD_RES         2543
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   2603 AA;  290905 MW;  8FE8316C8505F63D CRC64;
     MTFNNIKDEN NDDIAIIGMG FRFPGGGNNP DQFWNQLSNK MDGISKISQE KWSRSFYEQK
     YINNEYGGVL KDEEWKNFDP LFFGISPKEA PTIDPQQRLL MTTLWEAFED ANIKPSTLRG
     SDTAVFIGMM NLDYQRCQFR DISYINPYTV TGSAGSFVSN RLSFSFDLRG PSMTLDTACS
     SSLNAVYLGC QAIATGDSKM AIVGGVNGIF DPSISMTFSG LNMLGHKGQC RSFDAGADGY
     IRSEGGGVCI LKKYSDAIKD GDRIYCVIKG GSSNVDGYNA KTNITQPSMK AQGENIEIAL
     KKSGVNPSDI YYIEAHGTGT PVGDPIEIEA ISRIFKDNHT PDAPLYIGSV KSNIGHLESA
     AGIASLIKVA LSLKNRSLVP NIHFEKPNPL IKFEDWNIRV VTDEIQFPTN KLINMGINCF
     GLSGSNCHMI LSEAPINYDE LLKTTNNNST SSSSNDDKKE YLIPFSANCN ISLDKYIEKL
     ISNQSIYKDT ILFKDFVKHQ TISKSNLIKR KVITASDWDD FLNKRNETTS TSSLTSTISA
     PASSTPVIYV FTGQGPQWRD MGKALYETES VFKDAIDHCD KLLANYFGYS ILQKLRSLES
     DDSPEIHHPI LAQPSIFLIQ VGLVALYKSF GISPSIVVGH SFGEVSSALF SGVISLETAV
     KIVYYRGLAQ NLTMGTGRLL SIGIGADAYL EKCALLYPEI EIACYNDPNS IVITGSEQDL
     LGAKSTLSAE GVFCAFLGTP CSFHSSKQEM IKEKIFKDLS DLPESNVPCV PFFSTITGSQ
     LSHKGFYNVQ YIYDNLRMPV EFTKAISNIF NFIEENESYK NAIFLEIGPH PTLGFYIPKC
     KPSNSTITSK PIIVSPLHKK KEELTQFKLA ISTLYCNGVE IDFASGQQLL PTSSSSGGGD
     ISSFKESTNK LPRYQWDFEE YWDEPNQSKM VKRGPSNNLL GHDQFAGNTL MELFIDINKS
     AHQYLKGHKI KGKYLFPGSG YIDNILRQFN GQDITIFNLE FSNPFFLKDG VQHHLQTSIT
     PTTKGEFKVE FFIKDNRNST KWTKTSNGRI GLFKHNPKNN KLDIEKLKSQ CSFTTLTKSE
     VYNKLLLLSL PYGPTFQRVE SCSIGDGCSF FKLSMSPCSE FDKDFLNPSI IDCAFHGLLV
     LSEGPQEIVF DRLQDMKFYS SNVPSTRPQF IYAFAKFDKI VGNSTHGSLD IMLEDGTLLI
     SIKNVKCTSL IRLKKQSIKY PSQNVYSHHW QSKDSPLTLI ENQLIEEKSS ESKINFEKLL
     NDKLFNDYLI RLLNQSIKSE FIEFDYKTST VDTLEIDSNN TKLLEKIQSI LKTIDSLDQS
     IDLASLKQVI IEKSSSFKKE INLIEKSIKR IVSLLKGGES EHFSPSNPSS PNDTPRYNSN
     NCSSKSNNTS SGADDDTNNE ETINQLNNEP FNFSNSQFIS NQNQLISKTI VNSFDRLINS
     IEIGEKKLIK IIDLSSIYQN NQLSKLLLLQ LNQLLINLSN NNNIEIEYTI PSNTKNIDSI
     KEETKSISNL LNIKYRSFDL QDDLESNGYL NSNYDLIITS LLLVSTNSID SNEVLSKLYK
     LLLPKGQLIL MEPPKDVLSF NLLFANDFKQ SLEIKSEQEI KSLIRYCGFT KIETNNITQD
     DEEEQQQPPS ILIVQTEKRD IESMSLTFSS DPESLNSSYS NCIFIVSKEQ KENPTSYIQE
     YFDITEVFCD NTTIIEAGDS ELLTKTIESG IGKNDIIFFL VSLEELTIEN YKQVTMQYTL
     VNQILLRNNL STRFALLTYD SQNGGKNYLG SSLIGTFRYF LEFPSLNTFS IDVDKDSIDN
     LTLFLRLVDL STIGDRETIV RNNKIFVQKI FKEPKLLSPS NNYEKDTNNL YLNTNSNLDF
     SFQCKEKLPH GSVEIKVMST GINYKDNLFY RGLLPQEIFT KGDIYSPPFG LECAGYITRV
     APSGVTRFKV GDQVVGFASH SLSSLAITHQ DKIVLKPENI SFNEAAAVCV VYATSYYSIF
     HIGAFMADKE SILVHSATGG VGLATLNLLK WKRNQLKKHG NSEISNDASI YATVGSKEKV
     DYLQEKYGDL ITAIYNSRDT EYCDEIKQQS AQGGVDLILN TLSGDYLSAN FRSLSQVGRI
     MDLSVTQLVE NDSLDFSNFK YHVTYSTIDL ERATTYNSKI VRDILTEVFD AISDGSLENI
     PVKVFPATQV KTAIEYINER VHIGKIVVDF ENFEQDILKP ALQEKENPIQ LNKVKKLEHT
     CDTLNNTILI TGQTGIAVHI LKWIISGSVL NSNKSQQQVT DFIILSRSSL KWELENLINQ
     TKHKYGDRFR FHYKSVNIAD LNSTRTAIDQ VYSSCKNVSP IKSVLHFATV YEYILPEDIT
     QTVIDNTHNP KAVGAINLHN LSIEKDWKLE NFILFSSIGA IIGGSKQCAY SSANLVLDSL
     SNYRKSIGLA STSINWGGLD AGGVAATDKS VASFLEGQGI LLVSLSKILG CLDSVFQPSN
     SHLSNFMLSS FNIDNLLSSA PQMKRKMGHH LTNYKTSSAS SDDSLGDSSS TQAKVISTIS
     ELLSIHPSKL NLDTRLKDYG IDSLLTVQLK NWIDKEFTKN LFTHLQLSSS SINSIIQRIS
     SKSTSTSTPN PTNTTKQTAT TKT
 
 
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