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Protein

Probable polyketide synthase 1

Gene

stlA

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

Functioni

Probable polyketide synthase (By similarity). Produces only acylpyrones; in vitro.By similarity1 Publication

Catalytic activityi

3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + naringenin chalcone + 3 CO2.

Cofactori

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

Pathwayi: flavonoid biosynthesis

This protein is involved in the pathway flavonoid biosynthesis, which is part of Secondary metabolite biosynthesis.
View all proteins of this organism that are known to be involved in the pathway flavonoid biosynthesis and in Secondary metabolite biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei180For beta-ketoacyl synthase activityPROSITE-ProRule annotation1
Active sitei682For acyl/malonyl transferase activityPROSITE-ProRule annotation1
Active sitei2930PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

  • aggregation involved in sorocarp development Source: dictyBase
  • chemotaxis to cAMP Source: dictyBase
  • flavonoid biosynthetic process Source: UniProtKB-UniPathway
  • negative regulation of gene expression Source: dictyBase
  • polyketide biosynthetic process Source: dictyBase
  • positive regulation of gene expression Source: dictyBase
  • regulation of cAMP-mediated signaling Source: dictyBase
  • resorcinol metabolic process Source: dictyBase
  • signal transduction Source: dictyBase
  • sorocarp spore cell differentiation Source: dictyBase
  • sorocarp stalk cell differentiation Source: dictyBase
  • sorus development Source: dictyBase
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Flavonoid biosynthesis

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.
UniPathwayiUPA00154.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable polyketide synthase 1
Short name:
dipks1
Including the following 2 domains:
Polyketide synthase stlA (EC:2.3.1.-)
Chalcone synthase stlA (EC:2.3.1.74)
Alternative name(s):
Steely1
Gene namesi
Name:stlA
Synonyms:pks1
ORF Names:DDB_G0269364
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
Proteomesi
  • UP000002195 Componentsi: Chromosome 1, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0269364. stlA.

Subcellular locationi

GO - Cellular componenti

  • intracellular Source: dictyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003779011 – 3147Probable polyketide synthase 1Add BLAST3147

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2605O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PaxDbiQ55E72.
PRIDEiQ55E72.

Expressioni

Developmental stagei

Expressed during development. Expressed maximally in early development before cellular aggregation.1 Publication

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi44689.DDB0234164.

Structurei

Secondary structure

13147
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2788 – 2795Combined sources8
Beta strandi2797 – 2799Combined sources3
Helixi2803 – 2813Combined sources11
Helixi2818 – 2829Combined sources12
Helixi2845 – 2847Combined sources3
Helixi2849 – 2854Combined sources6
Helixi2857 – 2883Combined sources27
Helixi2887 – 2889Combined sources3
Beta strandi2892 – 2899Combined sources8
Helixi2906 – 2914Combined sources9
Beta strandi2921 – 2927Combined sources7
Helixi2929 – 2931Combined sources3
Helixi2932 – 2944Combined sources13
Beta strandi2951 – 2958Combined sources8
Helixi2961 – 2963Combined sources3
Beta strandi2967 – 2969Combined sources3
Helixi2970 – 2978Combined sources9
Beta strandi2982 – 2991Combined sources10
Beta strandi3000 – 3009Combined sources10
Beta strandi3016 – 3022Combined sources7
Beta strandi3025 – 3030Combined sources6
Helixi3034 – 3053Combined sources20
Turni3054 – 3056Combined sources3
Beta strandi3063 – 3070Combined sources8
Helixi3075 – 3084Combined sources10
Helixi3089 – 3092Combined sources4
Helixi3093 – 3102Combined sources10
Helixi3108 – 3118Combined sources11
Beta strandi3125 – 3133Combined sources9
Turni3134 – 3136Combined sources3
Beta strandi3137 – 3145Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H84X-ray2.90A/B2776-3147[»]
ProteinModelPortaliQ55E72.
SMRiQ55E72.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ55E72.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2573 – 2642Acyl carrierPROSITE-ProRule annotationAdd BLAST70

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni161 – 214Beta-ketoacyl synthaseAdd BLAST54
Regioni672 – 705Acyl/malonyl transferaseAdd BLAST34
Regioni2789 – 3147Chalcone synthaseAdd BLAST359

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi355 – 362Poly-Asp8
Compositional biasi470 – 478Poly-Asn9
Compositional biasi561 – 564Poly-Ser4
Compositional biasi576 – 581Poly-Thr6
Compositional biasi1684 – 1688Poly-Ser5
Compositional biasi2097 – 2100Poly-Gln4
Compositional biasi2647 – 2655Poly-Asn9
Compositional biasi2770 – 2774Poly-Gln5

Domaini

Modular protein possessing six classical catalytic domains and a type III polyketide synthase domain. May facilitate covalent transfer of steely N-terminal acyl products directly to the C-terminal type III PKS active sites, which catalyze both iterative polyketide extension and cyclization.

Sequence similaritiesi

In the C-terminal section; belongs to the chalcone/stilbene synthases family.Curated
Contains 1 acyl carrier domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1202. Eukaryota.
COG3321. LUCA.
COG3424. LUCA.
InParanoidiQ55E72.
OMAiTAHESHY.
PhylomeDBiQ55E72.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
3.40.366.10. 2 hits.
3.40.47.10. 4 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.
IPR012328. Chalcone/stilbene_synth_C.
IPR001099. Chalcone/stilbene_synthase_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.
PF02797. Chal_sti_synt_C. 1 hit.
PF00195. Chal_sti_synt_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. 5 hits.
SSF55048. SSF55048. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q55E72-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKNSKIQSP NSSDVAVIGV GFRFPGNSND PESLWNNLLD GFDAITQVPK
60 70 80 90 100
ERWATSFREM GLIKNKFGGF LKDSEWKNFD PLFFGIGPKE APFIDPQQRL
110 120 130 140 150
LLSIVWESLE DAYIRPDELR GSNTGVFIGV SNNDYTKLGF QDNYSISPYT
160 170 180 190 200
MTGSNSSLNS NRISYCFDFR GPSITVDTAC SSSLVSVNLG VQSIQMGECK
210 220 230 240 250
IAICGGVNAL FDPSTSVAFS KLGVLSENGR CNSFSDQASG YVRSEGAGVV
260 270 280 290 300
VLKSLEQAKL DGDRIYGVIK GVSSNEDGAS NGDKNSLTTP SCEAQSINIS
310 320 330 340 350
KAMEKASLSP SDIYYIEAHG TGTPVGDPIE VKALSKIFSN SNNNQLNNFS
360 370 380 390 400
TDGNDNDDDD DDNTSPEPLL IGSFKSNIGH LESAAGIASL IKCCLMLKNR
410 420 430 440 450
MLVPSINCSN LNPSIPFDQY NISVIREIRQ FPTDKLVNIG INSFGFGGSN
460 470 480 490 500
CHLIIQEYNN NFKNNSTICN NNNNNNNNID YLIPISSKTK KSLDKYLILI
510 520 530 540 550
KTNSNYHKDI SFDDFVKFQI KSKQYNLSNR MTTIANDWNS FIKGSNEFHN
560 570 580 590 600
LIESKDGEGG SSSSNRGIDS ANQINTTTTS TINDIEPLLV FVFCGQGPQW
610 620 630 640 650
NGMIKTLYNS ENVFKNTVDH VDSILYKYFG YSILNVLSKI DDNDDSINHP
660 670 680 690 700
IVAQPSLFLL QIGLVELFKY WGIYPSISVG HSFGEVSSYY LSGIISLETA
710 720 730 740 750
CKIVYVRSSN QNKTMGSGKM LVVSMGFKQW NDQFSAEWSD IEIACYNAPD
760 770 780 790 800
SIVVTGNEER LKELSIKLSD ESNQIFNTFL RSPCSFHSSH QEVIKGSMFE
810 820 830 840 850
ELSNLQSTGE TEIPLFSTVT GRQVLSGHVT AQHIYDNVRE PVLFQKTIES
860 870 880 890 900
ITSYIKSHYP SNQKVIYVEI APHPTLFSLI KKSIPSSNKN SSSVLCPLNR
910 920 930 940 950
KENSNNSYKK FVSQLYFNGV NVDFNFQLNS ICDNVNNDHH LNNVKQNSFK
960 970 980 990 1000
ETTNSLPRYQ WEQDEYWSEP LISRKNRLEG PTTSLLGHRI IYSFPVFQSV
1010 1020 1030 1040 1050
LDLQSDNYKY LLDHLVNGKP VFPGAGYLDI IIEFFDYQKQ QLNSSDSSNS
1060 1070 1080 1090 1100
YIINVDKIQF LNPIHLTENK LQTLQSSFEP IVTKKSAFSV NFFIKDTVED
1110 1120 1130 1140 1150
QSKVKSMSDE TWTNTCKATI SLEQQQPSPS STLTLSKKQD LQILRNRCDI
1160 1170 1180 1190 1200
SKLDKFELYD KISKNLGLQY NSLFQVVDTI ETGKDCSFAT LSLPEDTLFT
1210 1220 1230 1240 1250
TILNPCLLDN CFHGLLTLIN EKGSFVVESI SSVSIYLENI GSFNQTSVGN
1260 1270 1280 1290 1300
VQFYLYTTIS KATSFSSEGT CKLFTKDGSL ILSIGKFIIK STNPKSTKTN
1310 1320 1330 1340 1350
ETIESPLDET FSIEWQSKDS PIPTPQQIQQ QSPLNSNPSF IRSTILKDIQ
1360 1370 1380 1390 1400
FEQYCSSIIH KELINHEKYK NQQSFDINSL ENHLNDDQLM ESLSISKEYL
1410 1420 1430 1440 1450
RFFTRIISII KQYPKILNEK ELKELKEIIE LKYPSEVQLL EFEVIEKVSM
1460 1470 1480 1490 1500
IIPKLLFEND KQSSMTLFQD NLLTRFYSNS NSTRFYLERV SEMVLESIRP
1510 1520 1530 1540 1550
IVREKRVFRI LEIGAGTGSL SNVVLTKLNT YLSTLNSNGG SGYNIIIEYT
1560 1570 1580 1590 1600
FTDISANFII GEIQETMCNL YPNVTFKFSV LDLEKEIINS SDFLMGDYDI
1610 1620 1630 1640 1650
VLMAYVIHAV SNIKFSIEQL YKLLSPRGWL LCIEPKSNVV FSDLVFGCFN
1660 1670 1680 1690 1700
QWWNYYDDIR TTHCSLSESQ WNQLLLNQSL NNESSSSSNC YGGFSNVSFI
1710 1720 1730 1740 1750
GGEKDVDSHS FILHCQKESI SQMKLATTIN NGLSSGSIVI VLNSQQLTNM
1760 1770 1780 1790 1800
KSYPKVIEYI QEATSLCKTI EIIDSKDVLN STNSVLEKIQ KSLLVFCLLG
1810 1820 1830 1840 1850
YDLLENNYQE QSFEYVKLLN LISTTASSSN DKKPPKVLLI TKQSERISRS
1860 1870 1880 1890 1900
FYSRSLIGIS RTSMNEYPNL SITSIDLDTN DYSLQSLLKP IFSNSKFSDN
1910 1920 1930 1940 1950
EFIFKKGLMF VSRIFKNKQL LESSNAFETD SSNLYCKASS DLSYKYAIKQ
1960 1970 1980 1990 2000
SMLTENQIEI KVECVGINFK DNLFYKGLLP QEIFRMGDIY NPPYGLECSG
2010 2020 2030 2040 2050
VITRIGSNVT EYSVGQNVFG FARHSLGSHV VTNKDLVILK PDTISFSEAA
2060 2070 2080 2090 2100
SIPVVYCTAW YSLFNIGQLS NEESILIHSA TGGVGLASLN LLKMKNQQQQ
2110 2120 2130 2140 2150
PLTNVYATVG SNEKKKFLID NFNNLFKEDG ENIFSTRDKE YSNQLESKID
2160 2170 2180 2190 2200
VILNTLSGEF VESNFKSLRS FGRLIDLSAT HVYANQQIGL GNFKFDHLYS
2210 2220 2230 2240 2250
AVDLERLIDE KPKLLQSILQ RITNSIVNGS LEKIPITIFP STETKDAIEL
2260 2270 2280 2290 2300
LSKRSHIGKV VVDCTDISKC NPVGDVITNF SMRLPKPNYQ LNLNSTLLIT
2310 2320 2330 2340 2350
GQSGLSIPLL NWLLSKSGGN VKNVVIISKS TMKWKLQTMI SHFVSGFGIH
2360 2370 2380 2390 2400
FNYVQVDISN YDALSEAIKQ LPSDLPPITS VFHLAAIYND VPMDQVTMST
2410 2420 2430 2440 2450
VESVHNPKVL GAVNLHRISV SFGWKLNHFV LFSSITAITG YPDQSIYNSA
2460 2470 2480 2490 2500
NSILDALSNF RRFMGLPSFS INLGPMKDEG KVSTNKSIKK LFKSRGLPSL
2510 2520 2530 2540 2550
SLNKLFGLLE VVINNPSNHV IPSQLICSPI DFKTYIESFS TMRPKLLHLQ
2560 2570 2580 2590 2600
PTISKQQSSI INDSTKASSN ISLQDKITSK VSDLLSIPIS KINFDHPLKH
2610 2620 2630 2640 2650
YGLDSLLTVQ FKSWIDKEFE KNLFTHIQLA TISINSFLEK VNGLSTNNNN
2660 2670 2680 2690 2700
NNNSNVKSSP SIVKEEIVTL DKDQQPLLLK EHQHIIISPD IRINKPKRES
2710 2720 2730 2740 2750
LIRTPILNKF NQITESIITP STPSLSQSDV LKTPPIKSLN NTKNSSLINT
2760 2770 2780 2790 2800
PPIQSVQQHQ KQQQKVQVIQ QQQQPLSRLS YKSNNNSFVL GIGISVPGEP
2810 2820 2830 2840 2850
ISQQSLKDSI SNDFSDKAET NEKVKRIFEQ SQIKTRHLVR DYTKPENSIK
2860 2870 2880 2890 2900
FRHLETITDV NNQFKKVVPD LAQQACLRAL KDWGGDKGDI THIVSVTSTG
2910 2920 2930 2940 2950
IIIPDVNFKL IDLLGLNKDV ERVSLNLMGC LAGLSSLRTA ASLAKASPRN
2960 2970 2980 2990 3000
RILVVCTEVC SLHFSNTDGG DQMVASSIFA DGSAAYIIGC NPRIEETPLY
3010 3020 3030 3040 3050
EVMCSINRSF PNTENAMVWD LEKEGWNLGL DASIPIVIGS GIEAFVDTLL
3060 3070 3080 3090 3100
DKAKLQTSTA ISAKDCEFLI HTGGKSILMN IENSLGIDPK QTKNTWDVYH
3110 3120 3130 3140
AYGNMSSASV IFVMDHARKS KSLPTYSISL AFGPGLAFEG CFLKNVV
Length:3,147
Mass (Da):352,195
Last modified:May 24, 2005 - v1
Checksum:i6B67391AB6596F46
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000005 Genomic DNA. Translation: EAL72032.1.
RefSeqiXP_645909.1. XM_640817.1.

Genome annotation databases

EnsemblProtistsiEAL72032; EAL72032; DDB_G0269364.
GeneIDi8616850.
KEGGiddi:DDB_G0269364.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000005 Genomic DNA. Translation: EAL72032.1.
RefSeqiXP_645909.1. XM_640817.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H84X-ray2.90A/B2776-3147[»]
ProteinModelPortaliQ55E72.
SMRiQ55E72.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi44689.DDB0234164.

Proteomic databases

PaxDbiQ55E72.
PRIDEiQ55E72.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiEAL72032; EAL72032; DDB_G0269364.
GeneIDi8616850.
KEGGiddi:DDB_G0269364.

Organism-specific databases

dictyBaseiDDB_G0269364. stlA.

Phylogenomic databases

eggNOGiKOG1202. Eukaryota.
COG3321. LUCA.
COG3424. LUCA.
InParanoidiQ55E72.
OMAiTAHESHY.
PhylomeDBiQ55E72.

Enzyme and pathway databases

UniPathwayiUPA00154.
ReactomeiR-DDI-163765. ChREBP activates metabolic gene expression.
R-DDI-199220. Vitamin B5 (pantothenate) metabolism.
R-DDI-75105. Fatty Acyl-CoA Biosynthesis.

Miscellaneous databases

EvolutionaryTraceiQ55E72.
PROiQ55E72.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
3.40.366.10. 2 hits.
3.40.47.10. 4 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.
IPR012328. Chalcone/stilbene_synth_C.
IPR001099. Chalcone/stilbene_synthase_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.
PF02797. Chal_sti_synt_C. 1 hit.
PF00195. Chal_sti_synt_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. 5 hits.
SSF55048. SSF55048. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPKS1_DICDI
AccessioniPrimary (citable) accession number: Q55E72
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: May 24, 2005
Last modified: November 2, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Miscellaneous

In reference to their hybrid nature and to their discovery in D.discoideum, authors term these type I FAS-type III PKS fusion enzymes 'steely'.1 Publication
Encoded by one of the numerous copies of polyketide synthase genes localized in chromosome 1.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.