pks21

Functionⁱ

Probable polyketide synthase.By similarity

Miscellaneous

Encoded by one of the numerous copies of polyketide synthase genes and clustered as a triplet pks19/pks20/pks21 in chromosome 3.

Cofactorⁱ

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

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Active siteⁱ	176	For beta-ketoacyl synthase activityPROSITE-ProRule annotation		1
Active siteⁱ	642	For acyl/malonyl transferase activityPROSITE-ProRule annotation		1

GO - Molecular functionⁱ

oxidoreductase activity Source: InterPro
transferase activity Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Transferase

Molecular function

Transferase

Enzyme and pathway databases

Reactomeⁱ	R-DDI-163765 ChREBP activates metabolic gene expression R-DDI-199220 Vitamin B5 (pantothenate) metabolism R-DDI-75105 Fatty acyl-CoA biosynthesis

Reactomeⁱ

R-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 21 (EC:2.3.1.-) Short name: dipks21
Gene namesⁱ	Name:pks21 ORF Names:DDB_G0282029
Organismⁱ	Dictyostelium discoideum (Slime mold)
Taxonomic identifierⁱ	44689 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Amoebozoa › Mycetozoa › Dictyostelids › Dictyosteliales › Dictyosteliaceae › Dictyostelium
Proteomesⁱ	UP000002195 Componentsⁱ: Chromosome 3, Unassembled WGS sequence

Organism-specific databases

dictyBaseⁱ	DDB_G0282029 pks21

dictyBaseⁱ

DDB_G0282029 pks21

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000371384	1 – 2779	Probable polyketide synthase 21Add BLAST		2779

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	2319	O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation		1

Keywords - PTMⁱ

Phosphopantetheine, Phosphoprotein

Proteomic databases

PaxDbⁱ	B0G138
PRIDEⁱ	B0G138

Interactionⁱ

Protein-protein interaction databases

STRINGⁱ	44689.DDB0235174

STRINGⁱ

44689.DDB0235174

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	B0G138
SMRⁱ	B0G138
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	2282 – 2359	CarrierPROSITE-ProRule annotationAdd BLAST		78

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	157 – 210	Beta-ketoacyl synthaseAdd BLAST		54
Regionⁱ	632 – 665	Acyl/malonyl transferaseAdd BLAST		34

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	456 – 461	Poly-Gln		6
Compositional biasⁱ	1364 – 1367	Poly-Asn		4

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

Phylogenomic databases

eggNOGⁱ	ENOG410ISPY Eukaryota KOG1202 Eukaryota COG3320 LUCA COG3321 LUCA
InParanoidⁱ	B0G138
PhylomeDBⁱ	B0G138

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd05235 SDR_e1, 1 hit
Gene3Dⁱ	1.10.1200.10, 1 hit 3.40.366.10, 1 hit 3.40.47.10, 1 hit
InterProⁱ	View protein in InterPro IPR001227 Ac_transferase_dom_sf IPR036736 ACP-like_sf IPR014043 Acyl_transferase IPR016035 Acyl_Trfase/lysoPLipase IPR011032 GroES-like_sf 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 IPR036291 NAD(P)-bd_dom_sf IPR020801 PKS_acyl_transferase IPR020841 PKS_Beta-ketoAc_synthase_dom IPR020807 PKS_dehydratase IPR020843 PKS_ER IPR013968 PKS_KR IPR009081 PP-bd_ACP IPR010080 Thioester_reductase-like_dom IPR016039 Thiolase-like
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00698 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 PF07993 NAD_binding_4, 1 hit PF14765 PS-DH, 1 hit
SMARTⁱ	View protein in SMART SM00827 PKS_AT, 1 hit SM00829 PKS_ER, 1 hit SM00825 PKS_KS, 1 hit
SUPFAMⁱ	SSF47336 SSF47336, 1 hit SSF50129 SSF50129, 1 hit SSF51735 SSF51735, 3 hits SSF52151 SSF52151, 2 hits SSF53901 SSF53901, 1 hit SSF55048 SSF55048, 1 hit
PROSITEⁱ	View protein in PROSITE PS00606 B_KETOACYL_SYNTHASE, 1 hit PS50075 CARRIER, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

B0G138-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MKLENKEIAI VGIGFRIPQG KESINNGSVS HLWNNLKNGF SGIVETSERW 
        60         70         80         90        100
SDNINLLGEV NNKFGGLLPL KEWSDFDPVH FAINPSEVPL MDPQTRLLLK 
       110        120        130        140        150
CTWEALEDAF IDPIDIRGSN TSCFIGCSTL DYSTTNRDFN ETSENYFASN 
       160        170        180        190        200
VLHTISNRLS FSYDIRGPSM TIDTACSSSL NSIAMGFQSI QNGTSNLSIV 
       210        220        230        240        250
GGVSLLLDPY ISKSFSFLNM LSKKGKCKPF DSEADGYIRA ESCGIVILKP 
       260        270        280        290        300
LSDAIRDGNN IYCVINSFSS NVDGGGLNDK SNFYSPSKQS QSDNIKLALK 
       310        320        330        340        350
SANMKASDIS FVECHGTGTP TGDPIEVEGV SMALNSSKTS TPSKPLLIGS 
       360        370        380        390        400
LKSNIGHSEA ASGVASLIKC CLMFKNKHYA PNVNFDQPNP KINFKDWNIK 
       410        420        430        440        450
VVTEAIPFTN NNEKPVSMVI NNFGVTGSNC CLILSQFIEQ SINQNGNGHS 
       460        470        480        490        500
YPAESQQQQQ QRFLIPFSAN SVKSLKNYED LIINDIKIST NSFKEFVKNQ 
       510        520        530        540        550
IYSKSKKLYQ RSVLISSNWD QLKTKNKYFK TNNDKSSNIT IKRNQPLVVI 
       560        570        580        590        600
VFGGQGSQWN KMAQQLYECE PIFRSSMDKF NKELSKYYGY SVLDKLRSIK 
       610        620        630        640        650
DDDIISIHQP IIAQPSILML QISLFELYKH WGINVSFIVG HSLGEIATSY 
       660        670        680        690        700
CSGMVDFQTV CKLIYHRSIS QNNTNGCGKM LSVNISHSEF IELYSNKYPT 
       710        720        730        740        750
IEVACYNSPT SIVIAGNENI LKEISLNLKE NNIFCAFLGS LSSFHTSSQH 
       760        770        780        790        800
STKNEILPLD IPSKQSRIPT FSTVTTNLFN HETTPFNSSY VYENIIQPVR 
       810        820        830        840        850
FSQTISNLYQ HIENNKLGNE LIFIEVSPHP SLSFYLKQMI PKSSSYFNSV 
       860        870        880        890        900
SVLTSTNKKN SNDLDEIHST ISQIYCLGYD VNFKCQFNHN DDDVSSIRNS 
       910        920        930        940        950
KVNISLPNYQ FDEQHYWKVD INFEQYRLNG PNVFNSLGKS MINYSSNNKS 
       960        970        980        990       1000
YESIIDINRN PFKYLKDHIV KGKYYFPGIG YADNIMKLYP NQDIIINNLE 
      1010       1020       1030       1040       1050
FLAPFVLKEN VKHTLQTNVY QLGNTDYRVT FNIKDNKTNQ WVQTCTGNFQ 
      1060       1070       1080       1090       1100
LISLKDNNND HSSKYDINQL LSECNFTTLS KQEVYKHSRS ITGITHLGAF 
      1110       1120       1130       1140       1150
QGIEELYFGN DCIISKIQVN TENFDIDGKP VYQTYDKSFF NTALLDSCSQ 
      1160       1170       1180       1190       1200
TIVGFITNSS QFVFERLEGL KVYSENIPTD KLKYKNIYCQ AKFISLESDS 
      1210       1220       1230       1240       1250
YKSSVLVLLE DGTKLLEMDC ISLHSTLPLL NSLLINNPTT ELFTNNLQCK 
      1260       1270       1280       1290       1300
DSLVNILSID NNQTFSSISS SNTVTEIIKQ TIKPIINEKI VFRILQSFSD 
      1310       1320       1330       1340       1350
LELSKQIIET LNQIFDDNSL QEIDIEFTII DNSNDKLPTL HDSSLIFKND 
      1360       1370       1380       1390       1400
ITQLKPSYYD IIINNNNDGD DETIIKSIFN ILSSNGLLLI IGDDIGDKYN 
      1410       1420       1430       1440       1450
IDSLINLGFN ENKIQKSNKV IQSQKSTILS NELTVVPNNK NDNIIIYCEK 
      1460       1470       1480       1490       1500
ESKYTNEFMK LISNNHISCK QTIISNINEF NQLLPSITND SIIYFIKSME 
      1510       1520       1530       1540       1550
QLEMNNFKQI TMEYIEINQQ LLKHSLTCKH VLITIDSQIK NYLSSSIIGT 
      1560       1570       1580       1590       1600
ARYFNEFPSL NLYSIDFDNQ LSISSLLNKI INQLIENSNN HIQREYIIRN 
      1610       1620       1630       1640       1650
NSIYYEILKN EKNIKSNFNS NSFEDNDFMT LLDSTNLEYK LASKPKKLKK 
      1660       1670       1680       1690       1700
NQIEVKVLAT GINYKDYLIY RGLVVIDENV SISKNPLGLE FSGIITRISN 
      1710       1720       1730       1740       1750
ENQNCEFKVG DNVFGIACDT TASHVIADVL YVSHKPENIS HVEAASLPVI 
      1760       1770       1780       1790       1800
FSTCLHGMFN IGNFNIDDDE VILIHSATGG IGLATLEILK WKGHKSPIFV 
      1810       1820       1830       1840       1850
TVGSKDKEQY LIDNYGSFIT GIYSSRNKNY VNEIKSKLNQ LYGTTGKFNG 
      1860       1870       1880       1890       1900
VDLIINTLPN EFTHSNFLCL KERGKIIDLS ITHLNNNEFL NFNNFKFNKS 
      1910       1920       1930       1940       1950
YHNIELMHIN KKVVSRLLKS ISNALNENKL KPIPITTFQI EDVKEAIEYI 
      1960       1970       1980       1990       2000
NQRKHIGKIV LDHSCSNGSI GSDGLLNQLI ESDNNEKNHT ILKYDFKIDT 
      2010       2020       2030       2040       2050
KNIIGKNIII TGQSGIILEI LKWLIKYSPT ESFENIIILS KSSLKWELEL 
      2060       2070       2080       2090       2100
LINKTISRKD NNTKFHFKSV DVGDPIEMRK SINQILLENP NIDNIDSIFH 
      2110       2120       2130       2140       2150
YAFAQITKEV EEIDIESLDI SHNAKTMGAI NLHEISIEKS WKLKQFVMAS 
      2160       2170       2180       2190       2200
SIASLFGSFN QCSYVSANLV LDSLSRYRKS IGLPSTCTNW GAIKSAGFVS 
      2210       2220       2230       2240       2250
RNELVSKMLD DQGFIPIPTN IILGSLDLQL QNSNKNSNLI VSKFNYDSIK 
      2260       2270       2280       2290       2300
KLSSETSTFQ RLDFILNSIK EKDNDSNGGE NSVSESIQTK ILNKISELLS 
      2310       2320       2330       2340       2350
IEQSKINTDI RLSDYGADSL TSVQLKNFID KDIKSNVITL QQLQNNTIDM 
      2360       2370       2380       2390       2400
NIQTILEQIK KLDSNETKGK SKNIIKKDSA PTLDYWRNEM KLDESIQAIK 
      2410       2420       2430       2440       2450
MNPIDFRNDS KVFLTGATGF LGVHLLSNLI KSPNCSVVYC LIRNKKSEPN 
      2460       2470       2480       2490       2500
PINAIINNLK HHKLYHFHNE FELSKIKVIV GNLASPLLGL SKLDFDYISN 
      2510       2520       2530       2540       2550
QINLIINSGA DINLASNYEE SKVVNIGGFI ELIKLSTTGD YQKPIVGFSS 
      2560       2570       2580       2590       2600
VSVFFNASNC KEFDEETVIP TIENINNLPG GYMKSKVVVE NLLREVAKRG 
      2610       2620       2630       2640       2650
IPSMLIRPPI IFSHEETGIG HDSDFFQLII QSCYAVKKYP KIDKNILTSP 
      2660       2670       2680       2690       2700
IGWISLNTIK MIGNEKCWNK SSSNQLNIYS LNSEVSAMNP SFSFLEKQYG 
      2710       2720       2730       2740       2750
CEMVEYEQWK NIINQSKILS CVKLKTFHSL DDLYNIYNLG NGFGVSKKTK 
      2760       2770 
ELLQSMNSYE GGMVNEKMIQ NHINYIFKN

Length:2,779

Mass (Da):314,195

Last modified:March 18, 2008 - v1

Checksum:ⁱ8853A4F20089A375

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AAFI02000044 Genomic DNA Translation: EDR41070.1
NCBI Reference Sequences More...RefSeqⁱ	XP_001733001.1, XM_001732949.1

Genome annotation databases

EnsemblProtistsⁱ	EDR41070; EDR41070; DDB_G0282029
GeneIDⁱ	8623374
KEGGⁱ	ddi:DDB_G0282029

Entry informationⁱ

Entry nameⁱ	PKS21_DICDI
Accessionⁱ	B0G138Primary (citable) accession number: B0G138
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	May 5, 2009
	Last sequence update:	March 18, 2008
	Last modified:	May 23, 2018
	This is version 73 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

UniProtKB - B0G138 (PKS21_DICDI)

Your basket is currently empty. ⁱ

Probable polyketide synthase 21

Select a section on the left to see content.

Functionⁱ

Miscellaneous

Cofactorⁱ

Sites

GO - Molecular functionⁱ

Keywordsⁱ

Enzyme and pathway databases

Names & Taxonomyⁱ

Organism-specific databases

PTM / Processingⁱ

Molecule processing

Amino acid modifications

Keywords - PTMⁱ

Proteomic databases

Interactionⁱ

Protein-protein interaction databases

Structureⁱ

3D structure databases

Family & Domainsⁱ

Domains and Repeats

Region

Compositional bias

Domainⁱ

Phylogenomic databases

Family and domain databases

Sequenceⁱ

Sequence databases

Genome annotation databases

Similar proteinsⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ

UniProt is an ELIXIR core data resource

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - B0G138 (PKS21_DICDI)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Probable polyketide synthase 21

pks21

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Compositional bias

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

UniProt is an ELIXIR core data resource

Your basket is currently empty. ⁱ

Functionⁱ

GO - Molecular functionⁱ

Names & Taxonomyⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ