Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Probable polyketide synthase 40

Gene

pks40

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

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 sitei639 – 6391For acyl/malonyl transferase activityPROSITE-ProRule annotation

GO - Molecular functioni

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 40 (EC:2.3.1.-)
Short name:
dipks40
Gene namesi
Name:pks40
ORF Names:DDB_G0291614
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
Proteomesi
  • UP000002195 Componentsi: Chromosome 6, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0291614. pks40.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 25522552Probable polyketide synthase 40PRO_0000371397Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2505 – 25051O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PaxDbiQ54ED7.

Interactioni

Protein-protein interaction databases

STRINGi44689.DDB0235302.

Structurei

3D structure databases

ProteinModelPortaliQ54ED7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2473 – 254068Acyl carrierPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni160 – 21354Beta-ketoacyl synthaseAdd
BLAST
Regioni629 – 66234Acyl/malonyl transferaseAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi180 – 1834Poly-Ser
Compositional biasi450 – 4545Poly-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.
ENOG410XNPJ. LUCA.
InParanoidiQ54ED7.
OMAiISARSTW.
PhylomeDBiQ54ED7.

Family and domain databases

Gene3Di3.40.366.10. 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.
IPR013149. ADH_C.
IPR013154. ADH_N.
IPR011032. GroES-like.
IPR032821. KAsynt_C_assoc.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
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.
PF00107. ADH_zinc_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.
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.

Q54ED7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDYKNKYQSN ENCNKVAIIG IGFRFPNLKG DLTPNGLWSQ LLNKYDGIVK
60 70 80 90 100
NDRWNESFYK TGDIPTKYAG LIPFEELKSF DPLFFGINPS EVIHMCPQQR
110 120 130 140 150
ILLKCTWEAL EDSGIDPIEI RDSNTSVFLG CSNFDYQNLN KNNNKIQQNI
160 170 180 190 200
FASSSHSVSN RISYCFDLHG ESMTIDTACS SSSNAIRRGY KSIIDGSSNI
210 220 230 240 250
SVVGGINILL DPNTSKSYSQ LNMLGKDGKC KTFDADADGY VRSESAGIAI
260 270 280 290 300
LKNLNDAIKD GNNIYCVIDG SASNVDGNGF SDKSNFYSPS KSSQVECIRL
310 320 330 340 350
ALESTNGGVN ENDIVYFEAH GTGTPTGDPI ELESVSIALK TSENRSSNNP
360 370 380 390 400
LLIGSFKPNI GHSECASGIS SLIKCCLILK NQCFVPNINY NKPNPNIKFN
410 420 430 440 450
QWNLKVVTDP IDFSTLKLSN KPISIAINNF GVTGSNCCLI VSSFKGNQTN
460 470 480 490 500
NNNNKSKSPK QYLIPFSTNS IKSLDLYKSR IDNNVEFKEF AENQIKSKSK
510 520 530 540 550
KLIQRSVAIA SNWDEFNLKS NTINTSNDKL TSNMLVSSNK KNATMVFVFC
560 570 580 590 600
GQGAQYSTMA KNLYDNEPIF KKSMDKIDSK LSEYYGFSIL EKLRSFNEND
610 620 630 640 650
LKGIQYSIIA QPSTCMVQIS LFELYCHWGI KPSIIVGHSL GEISSSYCSG
660 670 680 690 700
MIDLDTFCYL IYHRSMVQSK TNGLGRMLSI SIGENEYNSK YSSRYPELEI
710 720 730 740 750
ACYNSPSSIV IAGKELILNE IIKELKQDGV FCTILGSPTS FHTSSQIPVK
760 770 780 790 800
DEILKISFKS KQSTYPIFST VTTNLYDEMN PFDTKYVYDN IINPVRFTNT
810 820 830 840 850
ISNIYKHIEL NYSVNNNSNE IIFIEIAPHP TLSFYLKQMV PEDKKQSVSI
860 870 880 890 900
FSPLSKKKSN DLFEIQKLIS ELYCLGYNGI GFNIQLSNLN ENDNIQTSLS
910 920 930 940 950
LPLYQWEEQE YWKLDSLYQH HLSNGPSINH LGISNSNHTP YIKSYQTHID
960 970 980 990 1000
IQKKPFQWLK GHQIKGKYYF PGCGYIDNIL KIFGDNSEST TNPNKELPDI
1010 1020 1030 1040 1050
LISFIEFKTP LIFMDGVNQC LQTNIHSTGK KEYKALFHFK DEKSSSDWVQ
1060 1070 1080 1090 1100
TSTANFQLFS RGQGLNEDDE ESLFKYNIND LISNQCNLTK LSKQELYSHI
1110 1120 1130 1140 1150
KTKCGLNYSG DFQRVEKCYF GNNCSLSELS LSQGVNENRS TFFDSSIIDC
1160 1170 1180 1190 1200
CLHGSIGLID ENCQLVFEKL EGLTYYSSKV PTTTSQHSKI YVYSKLKPRI
1210 1220 1230 1240 1250
GDSYSASIIV MLENGTVLFE MENASFKSTT KIKDSLAMEY PTNEIYSCYL
1260 1270 1280 1290 1300
QSKDSLIPSL SSFDHIFKRK ITDEYVDQIK IYESFIPKLL FSNINKRCPE
1310 1320 1330 1340 1350
ITIAEIQSSE IEQLLLKYYK IKEDNDNKWL SRLFTFAFES IKQWYHNEDY
1360 1370 1380 1390 1400
DFENVLSPHN FKIFSKSTKI ISKLLFPLEN DNDEDSPQSL FEGGLLDKFY
1410 1420 1430 1440 1450
SSGFSAQNEL VGEIIQESIK PILNEKLVFR ILEFGGGVGS LSLLVLEKIN
1460 1470 1480 1490 1500
SLLIQYPNYQ IDIEYTWSDI SPSFITEAKA KFEKFNDRVN IIYKALNLEQ
1510 1520 1530 1540 1550
PLIGEKQGLK PQYFDYIIMF NVLHVIKDVK YGVEQIYQLL VPNGHLLFIE
1560 1570 1580 1590 1600
PIYKSIVGDG IFGVFDQWWS FQDTEIRKDR CCMNQQTWYK LLKSVNFNDD
1610 1620 1630 1640 1650
IKMTPELTCF VIQAQKPSIS NLSFSKSETT NYNNIIVFGN KDDSNLSNNF
1660 1670 1680 1690 1700
IKSIDNGNLQ FISTIEEFNK MTKYISNESI IYFIKSIDEL SVDNFVNITH
1710 1720 1730 1740 1750
EYTQINQKLM ELNSKCKHVL ITNDSTTTNY LSSSLIGAAR YYHECPLELF
1760 1770 1780 1790 1800
ILNFDTPSII ENQNLFKTIE PLINSSINIQ REFIINNHKV YYERIKNETK
1810 1820 1830 1840 1850
LKSIFKNSSS FESLEQVDNF MISLTPNLEY KVKVKPTSIL KENEVEIKVM
1860 1870 1880 1890 1900
STGLNYKDYL IYAGLVESVE PIFGIEFSGI ITNIGSGNKE FKVGDSVYGT
1910 1920 1930 1940 1950
GKSTTSSHII TDIDVISHKP SNISHSEASS IPVVYLTSYH SLYNIGALKN
1960 1970 1980 1990 2000
NETILIHSAT GGVGLSTLEI LKWKGHSGLI FVTVGSNEKE EYLRENYGDM
2010 2020 2030 2040 2050
ISGIYSTRNK NFVKQIKSKI SKLNPFGKSG VDFILNTLSS SDYMDSNFKC
2060 2070 2080 2090 2100
LNMSGRIVDL SITHLNSNEF TDNKKFKYNY GYHNIELQYV DKKIIKSTLS
2110 2120 2130 2140 2150
IISNAVSSND LQLIPITEYS IENVKDSIEF INERVHMGKI VVDHENQDSI
2160 2170 2180 2190 2200
INELIEKQKS IDKFDQSIFK QNYKLEPSLL GKNILITGQS GIVLEILKWI
2210 2220 2230 2240 2250
LRNSENNSID NIIILSKSSI KWEMELLINK TKLLNSNSIN SMGNYLNKIK
2260 2270 2280 2290 2300
FHFKSVDISD SGLTDKGIHE LLIENPDINN IDSIFHFAYT QATCNSDEVD
2310 2320 2330 2340 2350
LHHLTQSHSA KSMGAINLHN QSIKRNWKII NFIMSSSITS KTSSANQCGY
2360 2370 2380 2390 2400
ISSNNVLDAL SKYRISIGLP TICTNYGLIQ STGFVSRNES VAALLSGEGL
2410 2420 2430 2440 2450
LPISTNLILG TLDLQLQNQA QSSNLILSNF NFTSLNGLPQ KSLISKFDYQ
2460 2470 2480 2490 2500
ININEENEKS KSLLKDDNVE LTVDQLITFK ISELLSTDIL KLNKDIILVD
2510 2520 2530 2540 2550
YGVDSLVIIQ LKNWVDKEFS IPNALTIQQV QNSTINSFIQ LVKNSIDKKN

KK
Length:2,552
Mass (Da):289,094
Last modified:May 24, 2005 - v1
Checksum:i0515D8D76EBCB4FA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000177 Genomic DNA. Translation: EAL61791.1.
RefSeqiXP_635303.1. XM_630211.1.

Genome annotation databases

EnsemblProtistsiDDB0235302; DDB0235302; DDB_G0291614.
GeneIDi8628247.
KEGGiddi:DDB_G0291614.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000177 Genomic DNA. Translation: EAL61791.1.
RefSeqiXP_635303.1. XM_630211.1.

3D structure databases

ProteinModelPortaliQ54ED7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi44689.DDB0235302.

Proteomic databases

PaxDbiQ54ED7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiDDB0235302; DDB0235302; DDB_G0291614.
GeneIDi8628247.
KEGGiddi:DDB_G0291614.

Organism-specific databases

dictyBaseiDDB_G0291614. pks40.

Phylogenomic databases

eggNOGiKOG1202. Eukaryota.
ENOG410XNPJ. LUCA.
InParanoidiQ54ED7.
OMAiISARSTW.
PhylomeDBiQ54ED7.

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

PROiQ54ED7.

Family and domain databases

Gene3Di3.40.366.10. 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.
IPR013149. ADH_C.
IPR013154. ADH_N.
IPR011032. GroES-like.
IPR032821. KAsynt_C_assoc.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
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.
PF00107. ADH_zinc_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.
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 nameiPKS40_DICDI
AccessioniPrimary (citable) accession number: Q54ED7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 24, 2005
Last modified: September 7, 2016
This is version 84 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 pks40/pks41 in chromosome 6.

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.