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Protein

Probable polyketide synthase 30

Gene

pks30

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Probable polyketide synthase (By similarity). May be involved in the process of cell migration.By similarity1 Publication

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei198 – 1981For beta-ketoacyl synthase activityPROSITE-ProRule annotation
Active sitei673 – 6731For acyl/malonyl transferase activityPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • cell motility Source: dictyBase
  • oxidation-reduction process Source: InterPro
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 30 (EC:2.3.1.-)
Short name:
dipks30
Gene namesi
Name:pks30
ORF Names:DDB_G0290701
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
Proteomesi
  • UP000002195 Componentsi: Chromosome 5, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0290701. pks30.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 30753075Probable polyketide synthase 30PRO_0000371390Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2570 – 25701O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PaxDbiQ54FQ2.
PRIDEiQ54FQ2.

Interactioni

Protein-protein interaction databases

STRINGi44689.DDB0235263.

Structurei

3D structure databases

ProteinModelPortaliQ54FQ2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2538 – 260770Acyl carrierPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni179 – 23254Beta-ketoacyl synthaseAdd
BLAST
Regioni663 – 69634Acyl/malonyl transferaseAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi199 – 2024Poly-Ser
Compositional biasi881 – 93858Asn-richAdd
BLAST
Compositional biasi1160 – 11656Poly-Asn
Compositional biasi1207 – 12148Poly-Asn
Compositional biasi1683 – 16886Poly-Asn
Compositional biasi2525 – 25284Poly-Ser
Compositional biasi2612 – 262413Poly-AsnAdd
BLAST
Compositional biasi2659 – 26635Poly-Asn

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.
InParanoidiQ54FQ2.
OMAiNENINER.
PhylomeDBiQ54FQ2.

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. 4 hits.
3.90.180.10. 1 hit.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013154. ADH_N.
IPR011032. GroES-like.
IPR032821. KAsynt_C_assoc.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR013120. Male_sterile_NAD-bd.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR013217. Methyltransf_12.
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.
PF08240. ADH_N. 1 hit.
PF16197. KAsynt_C_assoc. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF08659. KR. 1 hit.
PF08242. Methyltransf_12. 1 hit.
PF07993. NAD_binding_4. 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. 4 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.

Q54FQ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVQNTDNNTY NQLIRDINDY DDAGSSGDVA VIGIGLRFPS GSLKESISKP
60 70 80 90 100
NQLFNELLNG LDGIVTTSER WSDNYFLNGE IASKFAGLLP LDEWKQFDPI
110 120 130 140 150
FFAINPSNDN VSSIDPQQRF LLKCVWEALE DSGIDPISLR GTNTSTFIGS
160 170 180 190 200
STIDYNNLQK SSFETQNNIF GSSTHSVANR IGYCFDFRGE NLTIDTACSS
210 220 230 240 250
SSNAINCGYN SIKSNKSNVS IVGGVNFILD PHISKSFTQL GLLSPTGRCH
260 270 280 290 300
TFSSDADGYV RSEGVGIVVL KKLKDAIKDS NNIYCVIKGS SSNIDGNFDK
310 320 330 340 350
LNFYSPSKSS QYENIKLAIK STNGQINESD IDYCETHGTG TPTGDPIELE
360 370 380 390 400
GISRVFNKAP ATTNNNHKQV LIGSIKSNIG HTEACSGVAS LIKCCLMFKN
410 420 430 440 450
KLFLQNINFK EPNPLINFKE WGLKVVTEPI KFNENKSTVM LINNFGVTGS
460 470 480 490 500
NVCLILSEFK NNLSRYGNGN GYHKMEIDNN LNEKKKYLIP LSSNSSTSLN
510 520 530 540 550
NYKSSIIKHS NSNSSPTTTS FKEFVYNQIK FKSTSLIQKS VIIASDWNEF
560 570 580 590 600
QDESNQIKLN NSDNLISNIT VEKKKSPITV MVLCGQGSQY NKMALSLYDN
610 620 630 640 650
EPIFRESVNR FDKELFKYYG YSVLDKLRSI DDKDLISIHQ PILAQPANVI
660 670 680 690 700
IQVSLYELYK HWGVSADIII GHSLGEVSSP YCSGMIDFQT LCYLTYHRSV
710 720 730 740 750
AQNRTTGTGR MLSVNISSDE FINKYQSTTK YKSLEIACYN SPTSIVIAGN
760 770 780 790 800
EDLLNEITNE FKSNDIFCSM LGSLSSFHTS SQQMIKDEVC SLNISSKQPS
810 820 830 840 850
IAVFSTVTTN LFNHQTSPFN ANYVFDNIIQ PVYFTQTITN LYKHIESNDM
860 870 880 890 900
GNEITFIEVS PHPTLQYYLN QMKSTQSSYF NNGKNITIYS PLNKKKNDYN
910 920 930 940 950
EFLKTISLLY VNNNFDINFK SQLINDNNNI SNTTKLNNLP LYQWDDKEYF
960 970 980 990 1000
KLNSSLEKIK SEGPSINNLG NNTDSPYLSY QTFIDIKKSP FQWLKGHQVS
1010 1020 1030 1040 1050
DKFYYPGMGY VHNLLSIYPN QDITISSLEF KSPLVLTEGN NQCLQTIIAP
1060 1070 1080 1090 1100
LSKNEFNIKS HYKDQKTNQW ILSSLGNFSL TKHNSITSNK LINIQSLKDK
1110 1120 1130 1140 1150
CNFTSMSKQD FYETIRIKTN LTYKGLFQGV KQCYIGNNCS LAIVSLNEIY
1160 1170 1180 1190 1200
NQKEYNHLIN NNNMNTFFNA AILDTCLHGS LVAVTQPVVL DKIEAFKFYS
1210 1220 1230 1240 1250
SNIPLLNKNN NNNNSDDDSI KELYVFSDIK PRTNSQTYSV SVKVILPNGT
1260 1270 1280 1290 1300
LLVDISNVVC ALVSLGSNPD STIICKPPSN DIYTPYLQLK DSIINKPEQF
1310 1320 1330 1340 1350
KHLYSVDEFS VKEEDNQFIS NELLLSLFYK HINNRSPSIN LESLTTLEYN
1360 1370 1380 1390 1400
QFKQLYYNSL ANENLFKFIF ENLKRYSNIL NHDNNHSNIK SKHEELYIRT
1410 1420 1430 1440 1450
TKIMAKQLFP LKDDDSITDT PQSLFESGFL DDFYKNSRVV QPLNNLLSEI
1460 1470 1480 1490 1500
IVETLKPILN EPIVFRILEA GGGTGSLSLL ILEKICKLLN DNSTTSIINI
1510 1520 1530 1540 1550
EFTWSDVSAS FFAEIKEKFS SFTNHNNLNI IYRVLDLEKP LLDQDLKASY
1560 1570 1580 1590 1600
YDFIVMSNVM HVVKKLKPTL NEIHNILTPN GQLLYIEPPY KSFYYDSIFG
1610 1620 1630 1640 1650
CFSQWWPSSD SDIELRPDRC CMKQEKWINL LNQCNYRDTI MSGNDNLLFL
1660 1670 1680 1690 1700
IQTRKPTINE IISEQSISLD QLNSFNNIIL FCNNNNSNDK NRNSCSSSIL
1710 1720 1730 1740 1750
DLIRSNQELK HKIININNYN EFQSWITNNQ NKDDCNKTLI IFLKSIESTM
1760 1770 1780 1790 1800
NTFNFKEITF EYIQINQLIL KLELSNNFKH LLLSLNSSTD NYLSSSIIGA
1810 1820 1830 1840 1850
ARYFVEFPQL DLYILNYDNV SIENNQQLSL INYLINPNNN IQKEFTINNN
1860 1870 1880 1890 1900
KVYYERYCRR SNNIKSIFQS ESFETNKDNL YIQLNSNLEY QLYSKKAELN
1910 1920 1930 1940 1950
SNEVEIEVKA NGINYKDYLM YIGMIGTDLD IKYGKEYEIE NGIGIDNPNI
1960 1970 1980 1990 2000
GNDFSGIITR LGSNVKKFKV GDQVCGIGSK TNSSHVIIDF NFIYYKPLNY
2010 2020 2030 2040 2050
NHSVSASIPS IYITSLHSIY SIGNLKSNES ILIHSAAGGV GISSLDLLKS
2060 2070 2080 2090 2100
KQHQGYIFLT VGSKDKEEYL TKKYGSLITA IYSSRNKDYV YEIKNKLIEL
2110 2120 2130 2140 2150
GVVEQNQQGV DIILNTLSSE YMDSNFQCLN MSGCIVDLSI THLTPNDYMT
2160 2170 2180 2190 2200
NNHYKFNMGY NNVEVVDFPS KLIKSYLKKI IKMINSNELE LSVPIIEYSN
2210 2220 2230 2240 2250
NQFKDAIEYI NQRKHIGKII VNHNQDEFNR VYNNYQSNNN QIIMKHSYDI
2260 2270 2280 2290 2300
SKLNIGKNIL LTGQTGIVLE ILKYLVKYSN HSIENIIILS KSKLKWELEL
2310 2320 2330 2340 2350
LINQSKFKKD NNIKFHFNQI DIEDSNKVNQ VLNQLELNEN ITNIDSIIHF
2360 2370 2380 2390 2400
AFMNDIGDVQ QVDMNRLNNA HGAKTIGAIN LHNQSINRSW NIKQFIMASS
2410 2420 2430 2440 2450
IVSIFGSDQQ CCYVSACSVI DSLSKYRHSI GLPSLAINLG AISSTGFISR
2460 2470 2480 2490 2500
NNAIETMFKS SILKLFSPQL VISSLDLFIQ NQHQYPNYCL SDFNFEVLPS
2510 2520 2530 2540 2550
TLTNHFLTKF DYQINISKKL SQIKSSSSGN GGDNNEIIRS TILNKICELL
2560 2570 2580 2590 2600
SIDESKINED LQLTQYGMDS LVIVQLKNFI DNQIGHNLIT IQQLQNNKIN
2610 2620 2630 2640 2650
QSIEIIKSAH INNNKNKNNN NNNNLVKKEQ QSLDEFIKNE IKLNESIISR
2660 2670 2680 2690 2700
PYSIKNILNN NNNKSIFLTG STGFLGAYLL TELIKMDNIS KIYCLIRNNS
2710 2720 2730 2740 2750
KLTNPIDVII NNLKKHQLID MNKESPNQRL TKIINRTGNM SNDKLNSNIE
2760 2770 2780 2790 2800
NSENNNKQIS EDQLIKIIPM IGDVSKDKFG LTEQDYLKLS NECDIIINSA
2810 2820 2830 2840 2850
ADLNLKSNYE ESKTVNVDSI NQVIKLSVSN NSSQKLIVHF SSIAVFINHQ
2860 2870 2880 2890 2900
LKDGETFEET NILPNFYTTP IGYIQCKVIS EKLLTNAAES RGIPSIIIRP
2910 2920 2930 2940 2950
PDIFSNPITG IGHSNDFVSL LLKVSKEIGY YPNIHKPIFT TPITTIAKTT
2960 2970 2980 2990 3000
IDLIFNENSW NQNKSKPISI YSLNGNSIEM KSIYEFLENK FNCKEIDYQE
3010 3020 3030 3040 3050
WIKLVSKSNG KSSKRYSAFH IHDNQNLLIS TFKINSLFKM SNSTKELLIS
3060 3070
IGSYNHQDWE INESIILNNI NSNSN
Length:3,075
Mass (Da):349,549
Last modified:May 24, 2005 - v1
Checksum:i034D04EA30186AD2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000167 Genomic DNA. Translation: EAL62085.1.
RefSeqiXP_635589.1. XM_630497.1.

Genome annotation databases

EnsemblProtistsiDDB0235263; DDB0235263; DDB_G0290701.
GeneIDi8627786.
KEGGiddi:DDB_G0290701.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000167 Genomic DNA. Translation: EAL62085.1.
RefSeqiXP_635589.1. XM_630497.1.

3D structure databases

ProteinModelPortaliQ54FQ2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi44689.DDB0235263.

Proteomic databases

PaxDbiQ54FQ2.
PRIDEiQ54FQ2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiDDB0235263; DDB0235263; DDB_G0290701.
GeneIDi8627786.
KEGGiddi:DDB_G0290701.

Organism-specific databases

dictyBaseiDDB_G0290701. pks30.

Phylogenomic databases

eggNOGiKOG1202. Eukaryota.
COG3321. LUCA.
InParanoidiQ54FQ2.
OMAiNENINER.
PhylomeDBiQ54FQ2.

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

PROiQ54FQ2.

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. 4 hits.
3.90.180.10. 1 hit.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013154. ADH_N.
IPR011032. GroES-like.
IPR032821. KAsynt_C_assoc.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR013120. Male_sterile_NAD-bd.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR013217. Methyltransf_12.
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.
PF08240. ADH_N. 1 hit.
PF16197. KAsynt_C_assoc. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF08659. KR. 1 hit.
PF08242. Methyltransf_12. 1 hit.
PF07993. NAD_binding_4. 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. 4 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...

Publicationsi

« Hide 'large scale' publications
  1. "The genome of the social amoeba Dictyostelium discoideum."
    Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
    , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
    Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AX4.
  2. "Polyketide synthase genes and the natural products potential of Dictyostelium discoideum."
    Zucko J., Skunca N., Curk T., Zupan B., Long P.F., Cullum J., Kessin R.H., Hranueli D.
    Bioinformatics 23:2543-2549(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  3. "Screening of genes involved in cell migration in Dictyostelium."
    Nagasaki A., Uyeda T.Q.P.
    Exp. Cell Res. 314:1136-1146(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiPKS30_DICDI
AccessioniPrimary (citable) accession number: Q54FQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 24, 2005
Last modified: May 11, 2016
This is version 78 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 quartet pks29/pks30/pks31/pks32 in chromosome 5.

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.