Q54FI3 (PKS37_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable polyketide synthase 37
Short name=dipks37

Including the following 2 domains:

1. Polyketide synthase stlB
   EC=2.3.1.-
2. Chalcone synthase stlB
   EC=2.3.1.74
   Alternative name(s):
   Steely2

Gene names

Name:	stlB
Synonyms:	pks37
ORF Names:	DDB_G0290853

Organism

Dictyostelium discoideum (Slime mold) [Reference proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	2968 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Does make the polyketide skeleton of dif-1. Ref.2
Catalytic activity	3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + naringenin chalcone + 3 CO2.
Cofactor	Binds 1 phosphopantetheine covalently By similarity.
Pathway	Secondary metabolite biosynthesis; flavonoid biosynthesis.
Subcellular location	Membrane; Multi-pass membrane protein Potential.
Developmental stage	Expressed during development. Coordinately expressed with dmtA. Ref.2
Domain	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.
Disruption phenotype	Developed to the slug stage, in which dif-1 accumulation is maximal, though the Steely2- mutant slugs were thin and tended to break up. However, two independent Steely2 mutant strains both failed to accumulate any detectable dif-1 at this or any other stage of development. Ref.2
Miscellaneous	Encoded by one of the numerous copies of polyketide synthase genes localized in chromosome 5. In reference to their hybrid nature and to their discovery in D.discoideum, authors (Ref.2) term these type I FAS-type III PKS fusion enzymes 'steely'.
Sequence similarities	Contains 1 acyl carrier domain.

Ontologies

Keywords
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Phosphopantetheine
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	DIF-1 biosynthetic process Inferred from mutant phenotype Ref.2. Source: dictyBase flavonoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway polyketide biosynthetic process Inferred from direct assay Ref.2. Source: dictyBase sorocarp morphogenesis Inferred from mutant phenotype PubMed 18402932. Source: dictyBase sorocarp stalk cell differentiation Inferred from mutant phenotype PubMed 18402932. Source: dictyBase
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intracellular Inferred by curator Ref.2. Source: dictyBase
Molecular_function	naringenin-chalcone synthase activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2968	2968	Probable polyketide synthase 37		PRO_0000377902
Regions
	Transmembrane	1839 – 1859	21	Helical; Potential
	Transmembrane	1869 – 1889	21	Helical; Potential
	Domain	2426 – 2495	70	Acyl carrier
	Region	179 – 232	54	Beta-ketoacyl synthase
	Region	708 – 742	35	Acyl/malonyl transferase
	Region	2707 – 2968	262	Chalcone synthase
	Compositional bias	2 – 28	27	Asn-rich
	Compositional bias	465 – 469	5	Poly-Thr
	Compositional bias	475 – 479	5	Poly-Ser
	Compositional bias	585 – 588	4	Poly-Asn
	Compositional bias	597 – 608	12	Poly-Asn
	Compositional bias	609 – 617	9	Poly-Ser
	Compositional bias	618 – 621	4	Poly-Asn
	Compositional bias	674 – 677	4	Poly-Gly
	Compositional bias	978 – 982	5	Poly-Gln
	Compositional bias	1076 – 1082	7	Poly-Thr
	Compositional bias	1170 – 1180	11	Poly-Thr
	Compositional bias	1346 – 1355	10	Poly-Ser
	Compositional bias	1524 – 1528	5	Poly-Gly
	Compositional bias	1535 – 1543	9	Poly-Ser
	Compositional bias	1683 – 1686	4	Poly-Ser
	Compositional bias	1821 – 1826	6	Poly-Ser
	Compositional bias	2376 – 2381	6	Poly-Gly
	Compositional bias	2567 – 2571	5	Poly-Ser
Sites
	Active site	198	1	For beta-ketoacyl synthase activity By similarity
	Active site	718	1	For acyl/malonyl transferase activity By similarity
	Active site	2747	1	By similarity
Amino acid modifications
	Modified residue	2458	1	O-(pantetheine 4'-phosphoryl)serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54FI3 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 98AA21F6256A8A57	FASTA	2,968	329,909
	10 20 30 40 50 60 MNNNKSINDL SGNSNNNIAN SNINNYNNLI KKEPIAIIGI GCRFPGNVSN YSDFVNIIKN 70 80 90 100 110 120 GSDCLTKIPD DRWNADIISR KQWKLNNRIG GYLKNIDQFD NQFFGISPKE AQHIDPQQRL 130 140 150 160 170 180 LLHLAIETLE DGKISLDEIK GKKVGVFIGS SSGDYLRGFD SSEINQFTTP GTNSSFLSNR 190 200 210 220 230 240 LSYFLDVNGP SMTVNTACSA SMVAIHLGLQ SLWNGESELS MVGGVNIISS PLQSLDFGKA 250 260 270 280 290 300 GLLNQETDGR CYSFDPRASG YVRSEGGGIL LLKPLSAALR DNDEIYSLLL NSANNSNGKT 310 320 330 340 350 360 PTGITSPRSL CQEKLIQQLL RESSDQFSID DIGYFECHGT GTQMGDLNEI TAIGKSIGML 370 380 390 400 410 420 KSHDDPLIIG SVKASIGHLE GASGICGVIK SIICLKEKIL PQQCKFSSYN PKIPFETLNL 430 440 450 460 470 480 KVLTKTQPWN NSKRICGVNS FGVGGSNSSL FLSSFDKSTT ITEPTTTTTI ESLPSSSSSF 490 500 510 520 530 540 DNLSVSSSIS TNNDNDKVSN IVNNRYGSSI DVITLSVTSP DKEDLKIRAN DVLESIKTLD 550 560 570 580 590 600 DNFKIRDISN LTNIRTSHFS NRVAIIGDSI DSIKLNLQSF IKGENNNNKS IILPLINNGN 610 620 630 640 650 660 NNNNNNNNSS GSSSSSSNNN NICFIFSGQG QQWNKMIFDL YENNKTFKNE MNNFSKQFEM 670 680 690 700 710 720 ISGWSIIDKL YNSGGGGNEE LINETWLAQP SIVAVQYSLI KLFSKDIGIE GSIVLGHSLG 730 740 750 760 770 780 ELMAAYYCGI INDFNDLLKL LYIRSTLQNK TNGSGRMHVC LSSKAEIEQL ISQLGFNGRI 790 800 810 820 830 840 VICGNNTMKS CTISGDNESM NQFTKLISSQ QYGSVVHKEV RTNSAFHSHQ MDIIKDEFFK 850 860 870 880 890 900 LFNQYFPTNQ ISTNQIYDGK SFYSTCYGKY LTPIECKQLL SSPNYWWKNI RESVLFKESI 910 920 930 940 950 960 EQILQNHQQS LTFIEITCHP ILNYFLSQLL KSSSKSNTLL LSTLSKNSNS IDQLLILCSK 970 980 990 1000 1010 1020 LYVNNLSSIK WNWFYDKQQQ QQSESLVSSN FKLPGRRWKL EKYWIENCQR QMDRIKPPMF 1030 1040 1050 1060 1070 1080 ISLDRKLFSV TPSFEVRLNQ DRFQYLNDHQ IQDIPLVPFS FYIELVYASI FNSISTTTTN 1090 1100 1110 1120 1130 1140 TTASTMFEIE NFTIDSSIII DQKKSTLIGI NFNSDLTKFE IGSINSIGSG SSSNNNFIEN 1150 1160 1170 1180 1190 1200 KWKIHSNGII KYGTNYLKSN SKSNSFNEST TTTTTTTTTT KCFKSFNSNE FYNEIIKYNY 1210 1220 1230 1240 1250 1260 NYKSTFQCVK EFKQFDKQGT FYYSEIQFKK NDKQVIDQLL SKQLPSDFRC IHPCLLDAVL 1270 1280 1290 1300 1310 1320 QSAIIPATNK TNCSWIPIKI GKLSVNIPSN SYFNFKDQLL YCLIKPSTST STSPSTYFSS 1330 1340 1350 1360 1370 1380 DIQVFDKKNN NLICELTNLE FKGINSSSSS SSSSSTINSN VEANYESKIE ETNHDEDEDE 1390 1400 1410 1420 1430 1440 ELPLVSEYVW CKEELINQSI KFTDNYQTVI FCSTNLNGND LLDSIITSAL ENGHDENKIF 1450 1460 1470 1480 1490 1500 IVSPPPVESD QYNNRIIINY TNNESDFDAL FAIINSTTSI SGKSGLFSTR FIILPNFNSI 1510 1520 1530 1540 1550 1560 TFSSGNSTPL ITNVNGNGNG KSCGGGGGST NNTISNSSSS ISSIDNGNNE DEEMVLKSFN 1570 1580 1590 1600 1610 1620 DSNLSLFHLQ KSIIKNNIKG RLFLITNGGQ SISSSTPTST YNDQSYVNLS QYQLIGQIRV 1630 1640 1650 1660 1670 1680 FSNEYPIMEC SMIDIQDSTR IDLITDQLNS TKLSKLEIAF RDNIGYSYKL LKPSIFDNSS 1690 1700 1710 1720 1730 1740 LPSSSSEIET TATTKDEEKN NSINYNNNYY RVELSDNGII SDLKIKQFRQ MKCGVGQVLV 1750 1760 1770 1780 1790 1800 RVEMCTLNFR DILKSLGRDY DPIHLNSMGD EFSGKVIEIG EGVNNLSVGQ YVFGINMSKS 1810 1820 1830 1840 1850 1860 MGSFVCCNSD LVFPIPIPTP SSSSSSNENI DDQEIISKLL NQYCTIPIVF LTSWYSIVIQ 1870 1880 1890 1900 1910 1920 GRLKKGEKIL IHSGCGGVGL ATIQISMMIG AEIHVTVGSN EKKQYLIKEF GIDEKRIYSS 1930 1940 1950 1960 1970 1980 RSLQFYNDLM VNTDGQGVDM VLNSLSGEYL EKSIQCLSQY GRFIEIGKKD IYSNSSIHLE 1990 2000 2010 2020 2030 2040 PFKNNLSFFA VDIAQMTENR RDYLREIMID QLLPCFKNGS LKPLNQHCFN SPCDLVKAIR 2050 2060 2070 2080 2090 2100 FMSSGNHIGK ILINWSNLNN DKQFINHHSV VHLPIQSFSN RSTYIFTGFG GLTQTLLKYF 2110 2120 2130 2140 2150 2160 STESDLTNVI IVSKNGLDDN SGSGSGNNEK LKLINQLKES GLNVLVEKCD LSSIKQVYKL 2170 2180 2190 2200 2210 2220 FNKIFDNDAS GSDSGDFSDI KGIFHFASLI NDKRILKHNL ESFNYVYNSK ATSAWNLHQV 2230 2240 2250 2260 2270 2280 SLKYNLNLDH FQTIGSVITI LGNIGQSNYT CANRFVEGLT HLRIGMGLKS SCIHLASIPD 2290 2300 2310 2320 2330 2340 VGMASNDNVL NDLNSMGFVP FQSLNEMNLG FKKLLSSPNP IVVLGEINVD RFIEATPNFR 2350 2360 2370 2380 2390 2400 AKDNFIITSL FNRIDPLLLV NESQDFIINN NINNNGGGGD GSFDDLNQLE DEGQQGFGNG 2410 2420 2430 2440 2450 2460 DGYVDDNIDS VSMLSGTSSI FDNDFYTKSI RGMLCDILEL KDKDLNNTVS FSDYGLDSLL 2470 2480 2490 2500 2510 2520 SSELSNTIQK NFSILIPSLT LVDNSTINST VELIKNKLKN STTSSISSSV SKKVSFKKNT 2530 2540 2550 2560 2570 2580 QPLIIPTTAP ISIIKTQSYI KSEIIESLPI SSSTTIKPLV FDNLVYSSSS SNNSNSKNEL 2590 2600 2610 2620 2630 2640 TSPPPSAKRE SVLPIISEDN NSDNDSSMAT VIYEISPIAA PYHRYQTDVL KEITQLTPHK 2650 2660 2670 2680 2690 2700 EFIDNIYKKS KIRSRYCFND FSEKSMADIN KLDAGERVAL FREQTYQTVI NAGKTVIERA 2710 2720 2730 2740 2750 2760 GIDPMLISHV VGVTSTGIMA PSFDVVLIDK LGLSINTSRT MINFMGCGAA VNSMRAATAY 2770 2780 2790 2800 2810 2820 AKLKPGTFVL VVAVEASATC MKFNFDSRSD LLSQAIFTDG CVATLVTCQP KSSLVGKLEI 2830 2840 2850 2860 2870 2880 IDDLSYLMPD SRDALNLFIG PTGIDLDLRP ELPIAINRHI NSAITSWLKK NSLQKSDIEF 2890 2900 2910 2920 2930 2940 FATHPGGAKI ISAVHEGLGL SPEDLSDSYE VMKRYGNMIG VSTYYVLRRI LDKNQTLLQE 2950 2960 GSLGYNYGMA MAFSPGASIE AILFKLIK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Biosynthesis of Dictyostelium discoideum differentiation-inducing factor by a hybrid type I fatty acid-type III polyketide synthase." Austin M.B., Saito T., Bowman M.E., Haydock S., Kato A., Moore B.S., Kay R.R., Noel J.P. Nat. Chem. Biol. 2:494-502(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
[3]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000171 Genomic DNA. Translation: EAL62021.1.
RefSeq	XP_635518.1. XM_630426.1.
3D structure databases
ProteinModelPortal	Q54FI3.
ModBase	Search...
Protein-protein interaction databases
STRING	44689.DDBDRAFT_0219613.
Proteomic databases
PRIDE	Q54FI3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0234163; DDB0234163; DDB_G0290853.
GeneID	8627855.
KEGG	ddi:DDB_G0290853.
Organism-specific databases
dictyBase	DDB_G0290853. stlB.
Phylogenomic databases
eggNOG	COG3424.
InParanoid	Q54FI3.
OMA	ASECHEV.
Enzyme and pathway databases
UniPathway	UPA00154.
Family and domain databases
Gene3D	1.10.1200.10. 1 hit. 3.40.366.10. 2 hits. 3.40.47.10. 4 hits. 3.40.50.720. 2 hits.
InterPro	IPR001227. Ac_transferase_dom. IPR009081. Acyl_carrier_prot-like. IPR014043. Acyl_transferase. IPR016035. Acyl_Trfase/lysoPLipase. IPR013149. ADH_C. IPR013154. ADH_GroES-like. IPR012328. Chalcone/stilbene_synth_C. IPR001099. Chalcone/stilbene_synthase_N. IPR011032. GroES-like. IPR018201. Ketoacyl_synth_AS. IPR014031. Ketoacyl_synth_C. IPR014030. Ketoacyl_synth_N. IPR016036. Malonyl_transacylase_ACP-bd. IPR016040. NAD(P)-bd_dom. IPR020843. PKS_ER. IPR013968. PKS_KR. IPR016039. Thiolase-like. IPR016038. Thiolase-like_subgr. [Graphical view]
Pfam	PF00698. Acyl_transf_1. 1 hit. PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. PF02797. Chal_sti_synt_C. 1 hit. PF00195. Chal_sti_synt_N. 1 hit. PF00109. ketoacyl-synt. 1 hit. PF02801. Ketoacyl-synt_C. 1 hit. PF08659. KR. 1 hit. PF00550. PP-binding. 1 hit. [Graphical view]
SMART	SM00829. PKS_ER. 1 hit. [Graphical view]
SUPFAM	SSF47336. ACP_like. 1 hit. SSF52151. Acyl_Trfase/lysoPlipase. 1 hit. SSF50129. GroES_like. 1 hit. SSF55048. Malonyl_transacylase_ACP-bd. 1 hit. SSF53901. Thiolase-like. 3 hits.
PROSITE	PS50075. ACP_DOMAIN. 1 hit. PS00606. B_KETOACYL_SYNTHASE. 1 hit. PS00441. CHALCONE_SYNTH. False negative. PS00012. PHOSPHOPANTETHEINE. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PKS37_DICDI

Accession

Primary (citable) accession number: Q54FI3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 16, 2009
Last sequence update:	May 24, 2005
Last modified:	May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)