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Protein

Probable polyketide synthase 16

Gene

pks16

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Probable polyketide synthase.By similarity

Cofactori

pantetheine 4'-phosphateBy similarityNote: Binds 1 phosphopantetheine covalently.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei179 – 1791For beta-ketoacyl synthase activityPROSITE-ProRule annotation
Active sitei641 – 6411For acyl/malonyl transferase activityPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • sexual reproduction Source: dictyBase
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

ReactomeiR-DDI-163765. ChREBP activates metabolic gene expression.
R-DDI-199220. Vitamin B5 (pantothenate) metabolism.
R-DDI-75105. Fatty Acyl-CoA Biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable polyketide synthase 16 (EC:2.3.1.-)
Short name:
dipks16
Gene namesi
Name:pks16
ORF Names:DDB_G0275069
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
Proteomesi
  • UP000002195 Componentsi: Chromosome 2, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0275069. pks16.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 26032603Probable polyketide synthase 16PRO_0000371381Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2543 – 25431O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PaxDbiQ869W9.
PRIDEiQ869W9.

Expressioni

Inductioni

Up-regulated by P.aeruginosa, PAO1 strain and PA14 strain infection and down-regulated by phagocytic stimuli and growth on bacteria.2 Publications

Interactioni

Protein-protein interaction databases

STRINGi44689.DDB0230068.

Structurei

3D structure databases

ProteinModelPortaliQ869W9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2511 – 258070Acyl carrierPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni160 – 21354Beta-ketoacyl synthaseAdd
BLAST
Regioni631 – 66434Acyl/malonyl transferasesAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi449 – 4546Poly-Ser
Compositional biasi893 – 8964Poly-Ser
Compositional biasi1085 – 10906Poly-Leu
Compositional biasi1466 – 14716Poly-Leu
Compositional biasi1480 – 14834Poly-Asn
Compositional biasi2568 – 25714Poly-Ser

Domaini

Modular protein that is responsible for the completion of one condensation-processing cycle. The beta-ketoacyl synthase region is responsible for the actual condensation reaction while the acyl/malonyl transferase region is responsible for incorporating carboxylic acids units onto an acyl carrier protein (ACP) domain (By similarity).By similarity

Sequence similaritiesi

Contains 1 acyl carrier domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1202. Eukaryota.
COG3321. LUCA.
InParanoidiQ869W9.
OMAiRCYTFDE.
PhylomeDBiQ869W9.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
3.40.366.10. 2 hits.
3.40.47.10. 2 hits.
3.40.50.150. 1 hit.
3.40.50.720. 2 hits.
3.90.180.10. 1 hit.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR011032. GroES-like.
IPR032821. KAsynt_C_assoc.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR016040. NAD(P)-bd_dom.
IPR020801. PKS_acyl_transferase.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR020807. PKS_dehydratase.
IPR020843. PKS_ER.
IPR013968. PKS_KR.
IPR009081. PP-bd_ACP.
IPR029063. SAM-dependent_MTases.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
PF16197. KAsynt_C_assoc. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF08659. KR. 1 hit.
PF00550. PP-binding. 1 hit.
PF14765. PS-DH. 1 hit.
[Graphical view]
SMARTiSM00827. PKS_AT. 1 hit.
SM00829. PKS_ER. 1 hit.
SM00825. PKS_KS. 1 hit.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 1 hit.
SSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 2 hits.
SSF52151. SSF52151. 2 hits.
SSF53335. SSF53335. 1 hit.
SSF53901. SSF53901. 1 hit.
SSF55048. SSF55048. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q869W9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTFNNIKDEN NDDIAIIGMG FRFPGGGNNP DQFWNQLSNK MDGISKISQE
60 70 80 90 100
KWSRSFYEQK YINNEYGGVL KDEEWKNFDP LFFGISPKEA PTIDPQQRLL
110 120 130 140 150
MTTLWEAFED ANIKPSTLRG SDTAVFIGMM NLDYQRCQFR DISYINPYTV
160 170 180 190 200
TGSAGSFVSN RLSFSFDLRG PSMTLDTACS SSLNAVYLGC QAIATGDSKM
210 220 230 240 250
AIVGGVNGIF DPSISMTFSG LNMLGHKGQC RSFDAGADGY IRSEGGGVCI
260 270 280 290 300
LKKYSDAIKD GDRIYCVIKG GSSNVDGYNA KTNITQPSMK AQGENIEIAL
310 320 330 340 350
KKSGVNPSDI YYIEAHGTGT PVGDPIEIEA ISRIFKDNHT PDAPLYIGSV
360 370 380 390 400
KSNIGHLESA AGIASLIKVA LSLKNRSLVP NIHFEKPNPL IKFEDWNIRV
410 420 430 440 450
VTDEIQFPTN KLINMGINCF GLSGSNCHMI LSEAPINYDE LLKTTNNNST
460 470 480 490 500
SSSSNDDKKE YLIPFSANCN ISLDKYIEKL ISNQSIYKDT ILFKDFVKHQ
510 520 530 540 550
TISKSNLIKR KVITASDWDD FLNKRNETTS TSSLTSTISA PASSTPVIYV
560 570 580 590 600
FTGQGPQWRD MGKALYETES VFKDAIDHCD KLLANYFGYS ILQKLRSLES
610 620 630 640 650
DDSPEIHHPI LAQPSIFLIQ VGLVALYKSF GISPSIVVGH SFGEVSSALF
660 670 680 690 700
SGVISLETAV KIVYYRGLAQ NLTMGTGRLL SIGIGADAYL EKCALLYPEI
710 720 730 740 750
EIACYNDPNS IVITGSEQDL LGAKSTLSAE GVFCAFLGTP CSFHSSKQEM
760 770 780 790 800
IKEKIFKDLS DLPESNVPCV PFFSTITGSQ LSHKGFYNVQ YIYDNLRMPV
810 820 830 840 850
EFTKAISNIF NFIEENESYK NAIFLEIGPH PTLGFYIPKC KPSNSTITSK
860 870 880 890 900
PIIVSPLHKK KEELTQFKLA ISTLYCNGVE IDFASGQQLL PTSSSSGGGD
910 920 930 940 950
ISSFKESTNK LPRYQWDFEE YWDEPNQSKM VKRGPSNNLL GHDQFAGNTL
960 970 980 990 1000
MELFIDINKS AHQYLKGHKI KGKYLFPGSG YIDNILRQFN GQDITIFNLE
1010 1020 1030 1040 1050
FSNPFFLKDG VQHHLQTSIT PTTKGEFKVE FFIKDNRNST KWTKTSNGRI
1060 1070 1080 1090 1100
GLFKHNPKNN KLDIEKLKSQ CSFTTLTKSE VYNKLLLLSL PYGPTFQRVE
1110 1120 1130 1140 1150
SCSIGDGCSF FKLSMSPCSE FDKDFLNPSI IDCAFHGLLV LSEGPQEIVF
1160 1170 1180 1190 1200
DRLQDMKFYS SNVPSTRPQF IYAFAKFDKI VGNSTHGSLD IMLEDGTLLI
1210 1220 1230 1240 1250
SIKNVKCTSL IRLKKQSIKY PSQNVYSHHW QSKDSPLTLI ENQLIEEKSS
1260 1270 1280 1290 1300
ESKINFEKLL NDKLFNDYLI RLLNQSIKSE FIEFDYKTST VDTLEIDSNN
1310 1320 1330 1340 1350
TKLLEKIQSI LKTIDSLDQS IDLASLKQVI IEKSSSFKKE INLIEKSIKR
1360 1370 1380 1390 1400
IVSLLKGGES EHFSPSNPSS PNDTPRYNSN NCSSKSNNTS SGADDDTNNE
1410 1420 1430 1440 1450
ETINQLNNEP FNFSNSQFIS NQNQLISKTI VNSFDRLINS IEIGEKKLIK
1460 1470 1480 1490 1500
IIDLSSIYQN NQLSKLLLLQ LNQLLINLSN NNNIEIEYTI PSNTKNIDSI
1510 1520 1530 1540 1550
KEETKSISNL LNIKYRSFDL QDDLESNGYL NSNYDLIITS LLLVSTNSID
1560 1570 1580 1590 1600
SNEVLSKLYK LLLPKGQLIL MEPPKDVLSF NLLFANDFKQ SLEIKSEQEI
1610 1620 1630 1640 1650
KSLIRYCGFT KIETNNITQD DEEEQQQPPS ILIVQTEKRD IESMSLTFSS
1660 1670 1680 1690 1700
DPESLNSSYS NCIFIVSKEQ KENPTSYIQE YFDITEVFCD NTTIIEAGDS
1710 1720 1730 1740 1750
ELLTKTIESG IGKNDIIFFL VSLEELTIEN YKQVTMQYTL VNQILLRNNL
1760 1770 1780 1790 1800
STRFALLTYD SQNGGKNYLG SSLIGTFRYF LEFPSLNTFS IDVDKDSIDN
1810 1820 1830 1840 1850
LTLFLRLVDL STIGDRETIV RNNKIFVQKI FKEPKLLSPS NNYEKDTNNL
1860 1870 1880 1890 1900
YLNTNSNLDF SFQCKEKLPH GSVEIKVMST GINYKDNLFY RGLLPQEIFT
1910 1920 1930 1940 1950
KGDIYSPPFG LECAGYITRV APSGVTRFKV GDQVVGFASH SLSSLAITHQ
1960 1970 1980 1990 2000
DKIVLKPENI SFNEAAAVCV VYATSYYSIF HIGAFMADKE SILVHSATGG
2010 2020 2030 2040 2050
VGLATLNLLK WKRNQLKKHG NSEISNDASI YATVGSKEKV DYLQEKYGDL
2060 2070 2080 2090 2100
ITAIYNSRDT EYCDEIKQQS AQGGVDLILN TLSGDYLSAN FRSLSQVGRI
2110 2120 2130 2140 2150
MDLSVTQLVE NDSLDFSNFK YHVTYSTIDL ERATTYNSKI VRDILTEVFD
2160 2170 2180 2190 2200
AISDGSLENI PVKVFPATQV KTAIEYINER VHIGKIVVDF ENFEQDILKP
2210 2220 2230 2240 2250
ALQEKENPIQ LNKVKKLEHT CDTLNNTILI TGQTGIAVHI LKWIISGSVL
2260 2270 2280 2290 2300
NSNKSQQQVT DFIILSRSSL KWELENLINQ TKHKYGDRFR FHYKSVNIAD
2310 2320 2330 2340 2350
LNSTRTAIDQ VYSSCKNVSP IKSVLHFATV YEYILPEDIT QTVIDNTHNP
2360 2370 2380 2390 2400
KAVGAINLHN LSIEKDWKLE NFILFSSIGA IIGGSKQCAY SSANLVLDSL
2410 2420 2430 2440 2450
SNYRKSIGLA STSINWGGLD AGGVAATDKS VASFLEGQGI LLVSLSKILG
2460 2470 2480 2490 2500
CLDSVFQPSN SHLSNFMLSS FNIDNLLSSA PQMKRKMGHH LTNYKTSSAS
2510 2520 2530 2540 2550
SDDSLGDSSS TQAKVISTIS ELLSIHPSKL NLDTRLKDYG IDSLLTVQLK
2560 2570 2580 2590 2600
NWIDKEFTKN LFTHLQLSSS SINSIIQRIS SKSTSTSTPN PTNTTKQTAT

TKT
Length:2,603
Mass (Da):290,905
Last modified:June 1, 2003 - v1
Checksum:i8FE8316C8505F63D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000013 Genomic DNA. Translation: EAL69815.1.
RefSeqiXP_643784.1. XM_638692.1.

Genome annotation databases

EnsemblProtistsiDDB0230068; DDB0230068; DDB_G0275069.
GeneIDi8619829.
KEGGiddi:DDB_G0275069.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000013 Genomic DNA. Translation: EAL69815.1.
RefSeqiXP_643784.1. XM_638692.1.

3D structure databases

ProteinModelPortaliQ869W9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi44689.DDB0230068.

Proteomic databases

PaxDbiQ869W9.
PRIDEiQ869W9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiDDB0230068; DDB0230068; DDB_G0275069.
GeneIDi8619829.
KEGGiddi:DDB_G0275069.

Organism-specific databases

dictyBaseiDDB_G0275069. pks16.

Phylogenomic databases

eggNOGiKOG1202. Eukaryota.
COG3321. LUCA.
InParanoidiQ869W9.
OMAiRCYTFDE.
PhylomeDBiQ869W9.

Enzyme and pathway databases

ReactomeiR-DDI-163765. ChREBP activates metabolic gene expression.
R-DDI-199220. Vitamin B5 (pantothenate) metabolism.
R-DDI-75105. Fatty Acyl-CoA Biosynthesis.

Miscellaneous databases

PROiQ869W9.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
3.40.366.10. 2 hits.
3.40.47.10. 2 hits.
3.40.50.150. 1 hit.
3.40.50.720. 2 hits.
3.90.180.10. 1 hit.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR011032. GroES-like.
IPR032821. KAsynt_C_assoc.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR016040. NAD(P)-bd_dom.
IPR020801. PKS_acyl_transferase.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR020807. PKS_dehydratase.
IPR020843. PKS_ER.
IPR013968. PKS_KR.
IPR009081. PP-bd_ACP.
IPR029063. SAM-dependent_MTases.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
PF16197. KAsynt_C_assoc. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF08659. KR. 1 hit.
PF00550. PP-binding. 1 hit.
PF14765. PS-DH. 1 hit.
[Graphical view]
SMARTiSM00827. PKS_AT. 1 hit.
SM00829. PKS_ER. 1 hit.
SM00825. PKS_KS. 1 hit.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 1 hit.
SSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 2 hits.
SSF52151. SSF52151. 2 hits.
SSF53335. SSF53335. 1 hit.
SSF53901. SSF53901. 1 hit.
SSF55048. SSF55048. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPKS16_DICDI
AccessioniPrimary (citable) accession number: Q869W9
Secondary accession number(s): Q554C7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: June 1, 2003
Last modified: May 11, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

Encoded by one of the numerous copies of polyketide synthase genes and clustered as a pair pks16/pks17 in chromosome 2.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.