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Protein

Narbonolide/10-deoxymethynolide synthase PikA1, modules 1 and 2

Gene

pikAI

Organism
Streptomyces venezuelae
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of 12- and 14-membered ring macrolactone antibiotics such as methymycin and neomethymycin, and pikromycin and narbomycin, respectively. Component of the pikromycin PKS which catalyzes the biosynthesis of both precursors 10-deoxymethynolide (12-membered ring macrolactone) and narbonolide (14-membered ring macrolactone) (PubMed:18512859, PubMed:19437523). Chain elongation through PikAI, PikAII and PikAIII followed by thioesterase catalyzed termination results in the production of 10-deoxymethynolide, while continued elongation through PikAIV, followed by thioesterase (TE) catalyzed cyclization results in the biosynthesis of the narbonolide.1 Publication3 Publications

Catalytic activityi

Malonyl-CoA + 5 (2S)-methylmalonyl-CoA + 5 NADPH = 10-deoxymethynolide + 6 CoA + 6 CO2 + 5 NADP+ + 2 H2O.1 Publication1 Publication
Malonyl-CoA + 6 (2S)-methylmalonyl-CoA + 5 NADPH = narbonolide + 7 CoA + 7 CO2 + 5 NADP+ + 2 H2O.1 Publication1 Publication

Cofactori

pantetheine 4'-phosphate1 PublicationNote: Binds 3 phosphopantetheines covalently.Curated

Pathwayi: Antibiotic biosynthesis

This protein is involved in Antibiotic biosynthesis.2 Publications
View all proteins of this organism that are known to be involved in Antibiotic biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei724Acyl-ester intermediate; for acyltransferase 1 activityCurated1
Active sitei1281Acyl-thioester intermediate; for beta-ketoacyl synthase 2 activityPROSITE-ProRule annotation1 Publication1
Active sitei1740Acyl-ester intermediate; for acyltransferase 2 activityPROSITE-ProRule annotationBy similarity1
Binding sitei2318NADP (Beta-ketoacyl reductase 1)By similarity1
Active sitei2355For beta-ketoacyl reductase 1 activityBy similarity1
Active sitei2776Acyl-thioester intermediate; for beta-ketoacyl synthase 3 activityPROSITE-ProRule annotation1
Active sitei3273Acyl-ester intermediate; for acyltransferase 3 activityPROSITE-ProRule annotationBy similarity1
Binding sitei4211NADP (Beta-ketoacyl reductase 2)Curated1
Active sitei4250For beta-ketoacyl reductase 2 activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi2216 – 2219NADP (Beta-ketoacyl reductase 1)By similarity4
Nucleotide bindingi2239 – 2242NADP (Beta-ketoacyl reductase 1)By similarity4
Nucleotide bindingi2268 – 2269NADP (Beta-ketoacyl reductase 1)By similarity2
Nucleotide bindingi2340 – 2341NADP (Beta-ketoacyl reductase 1)By similarity2
Nucleotide bindingi4108 – 4111NADP (Beta-ketoacyl reductase 2)Curated4
Nucleotide bindingi4132 – 4135NADP (Beta-ketoacyl reductase 2)Curated4
Nucleotide bindingi4161 – 4162NADP (Beta-ketoacyl reductase 2)Curated2
Nucleotide bindingi4235 – 4236NADP (Beta-ketoacyl reductase 2)Curated2

GO - Molecular functioni

  • phosphopantetheine binding Source: UniProtKB
  • transferase activity, transferring acyl groups other than amino-acyl groups Source: UniProtKB

GO - Biological processi

  • macrolide biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Antibiotic biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18411.

Names & Taxonomyi

Protein namesi
Recommended name:
Narbonolide/10-deoxymethynolide synthase PikA1, modules 1 and 2Curated (EC:2.3.1.2391 Publication1 Publication, EC:2.3.1.2401 Publication1 Publication)
Alternative name(s):
Narbonolide/10-deoxymethynolide synthase PikAICurated
Pikromycin polyketide synthase component PikAI1 Publication
Short name:
Pikromycin PKS component PikAI1 Publication
Type I modular polyketide synthase PikAI1 Publication
Short name:
PKS1 Publication
Gene namesi
Name:pikAI1 Publication
OrganismiStreptomyces venezuelae
Taxonomic identifieri54571 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene are unable to produce methymycin, neomethymycin, narbomycin and pikromycin.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1281C → A: Does not produce any detectable levels of methymycin or pikromycin. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004363571 – 4613Narbonolide/10-deoxymethynolide synthase PikA1, modules 1 and 2Add BLAST4613

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1045O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei2530O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei4442O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Interactioni

Subunit structurei

Homodimer (By similarity). Pikromycin PKS consists of a combination of multimodular (PikAI and PikAII) and monomodular (PikAIII and PikAIV) polypeptides each coding for a functional synthase subunit which participates in 1 (monomodular) or 2 (multimodular) of the six FAS-like elongation steps required for formation of the polyketide. Module 1, 2, 3, 4, 5, and 6 participating in biosynthesis steps 1, 2, 3, 4, 5, and 6, respectively.By similarity2 Publications

Structurei

3D structure databases

ProteinModelPortaliQ9ZGI5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1012 – 1082Acyl carrier 1PROSITE-ProRule annotationAdd BLAST71
Domaini2497 – 2567Acyl carrier 2PROSITE-ProRule annotationAdd BLAST71
Domaini4409 – 4479Acyl carrier 3PROSITE-ProRule annotationAdd BLAST71

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni91 – 1082Loading domainCuratedAdd BLAST992
Regioni91 – 518Beta-ketoacyl synthase 1CuratedAdd BLAST428
Regioni634 – 917Acyltransferase 1CuratedAdd BLAST284
Regioni1111 – 2567Module 1CuratedAdd BLAST1457
Regioni1111 – 1539Beta-ketoacyl synthase 2CuratedAdd BLAST429
Regioni1650 – 1956Acyltransferase 2CuratedAdd BLAST307
Regioni2208 – 2385Beta-ketoacyl reductase 1CuratedAdd BLAST178
Regioni2606 – 4479Module 2CuratedAdd BLAST1874
Regioni2606 – 3032Beta-ketoacyl synthase 3CuratedAdd BLAST427
Regioni3180 – 3470Acyltransferase 3CuratedAdd BLAST291
Regioni3579 – 3877DehydrataseCuratedAdd BLAST299
Regioni4100 – 4281Beta-ketoacyl reductase 2CuratedAdd BLAST182

Sequence similaritiesi

Contains 3 acyl carrier domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

KOiK16000.

Family and domain databases

Gene3Di1.10.1200.10. 3 hits.
3.40.366.10. 7 hits.
3.40.47.10. 6 hits.
3.40.50.720. 3 hits.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR032821. KAsynt_C_assoc.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR016040. NAD(P)-bd_dom.
IPR020801. PKS_acyl_transferase.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR020807. PKS_dehydratase.
IPR013968. PKS_KR.
IPR020806. PKS_PP-bd.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 3 hits.
PF16197. KAsynt_C_assoc. 3 hits.
PF00109. ketoacyl-synt. 3 hits.
PF02801. Ketoacyl-synt_C. 3 hits.
PF08659. KR. 2 hits.
PF00550. PP-binding. 3 hits.
PF14765. PS-DH. 1 hit.
[Graphical view]
SMARTiSM00827. PKS_AT. 3 hits.
SM00826. PKS_DH. 1 hit.
SM00825. PKS_KS. 3 hits.
SM00823. PKS_PP. 3 hits.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 3 hits.
SSF51735. SSF51735. 4 hits.
SSF52151. SSF52151. 6 hits.
SSF53901. SSF53901. 6 hits.
SSF55048. SSF55048. 3 hits.
PROSITEiPS50075. ACP_DOMAIN. 3 hits.
PS00606. B_KETOACYL_SYNTHASE. 2 hits.
PS00012. PHOSPHOPANTETHEINE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ZGI5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSAGITRTG ARTPVTGRGA AAWDTGEVRV RRGLPPAGPD HAEHSFSRAP
60 70 80 90 100
TGDVRAELIR GEMSTVSKSE SEEFVSVSND AGSAHGTAEP VAVVGISCRV
110 120 130 140 150
PGARDPREFW ELLAAGGQAV TDVPADRWNA GDFYDPDRSA PGRSNSRWGG
160 170 180 190 200
FIEDVDRFDA AFFGISPREA AEMDPQQRLA LELGWEALER AGIDPSSLTG
210 220 230 240 250
TRTGVFAGAI WDDYATLKHR QGGAAITPHT VTGLHRGIIA NRLSYTLGLR
260 270 280 290 300
GPSMVVDSGQ SSSLVAVHLA CESLRRGESE LALAGGVSLN LVPDSIIGAS
310 320 330 340 350
KFGGLSPDGR AYTFDARANG YVRGEGGGFV VLKRLSRAVA DGDPVLAVIR
360 370 380 390 400
GSAVNNGGAA QGMTTPDAQA QEAVLREAHE RAGTAPADVR YVELHGTGTP
410 420 430 440 450
VGDPIEAAAL GAALGTGRPA GQPLLVGSVK TNIGHLEGAA GIAGLIKAVL
460 470 480 490 500
AVRGRALPAS LNYETPNPAI PFEELNLRVN TEYLPWEPEH DGQRMVVGVS
510 520 530 540 550
SFGMGGTNAH VVLEEAPGGC RGASVVESTV GGSAVGGGVV PWVVSAKSAA
560 570 580 590 600
ALDAQIERLA AFASRDRTDG VDAGAVDAGA VDAGAVARVL AGGRAQFEHR
610 620 630 640 650
AVVVGSGPDD LAAALAAPEG LVRGVASGVG RVAFVFPGQG TQWAGMGAEL
660 670 680 690 700
LDSSAVFAAA MAECEAALSP YVDWSLEAVV RQAPGAPTLE RVDVVQPVTF
710 720 730 740 750
AVMVSLARVW QHHGVTPQAV VGHSQGEIAA AYVAGALSLD DAARVVTLRS
760 770 780 790 800
KSIAAHLAGK GGMLSLALSE DAVLERLAGF DGLSVAAVNG PTATVVSGDP
810 820 830 840 850
VQIEELARAC EADGVRARVI PVDYASHSRQ VEIIESELAE VLAGLSPQAP
860 870 880 890 900
RVPFFSTLEG AWITEPVLDG GYWYRNLRHR VGFAPAVETL ATDEGFTHFV
910 920 930 940 950
EVSAHPVLTM ALPGTVTGLA TLRRDNGGQD RLVASLAEAW ANGLAVDWSP
960 970 980 990 1000
LLPSATGHHS DLPTYAFQTE RHWLGEIEAL APAGEPAVQP AVLRTEAAEP
1010 1020 1030 1040 1050
AELDRDEQLR VILDKVRAQT AQVLGYATGG QIEVDRTFRE AGCTSLTGVD
1060 1070 1080 1090 1100
LRNRINAAFG VRMAPSMIFD FPTPEALAEQ LLLVVHGEAA ANPAGAEPAP
1110 1120 1130 1140 1150
VAAAGAVDEP VAIVGMACRL PGGVASPEDL WRLVAGGGDA ISEFPQDRGW
1160 1170 1180 1190 1200
DVEGLYHPDP EHPGTSYVRQ GGFIENVAGF DAAFFGISPR EALAMDPQQR
1210 1220 1230 1240 1250
LLLETSWEAV EDAGIDPTSL RGRQVGVFTG AMTHEYGPSL RDGGEGLDGY
1260 1270 1280 1290 1300
LLTGNTASVM SGRVSYTLGL EGPALTVDTA CSSSLVALHL AVQALRKGEV
1310 1320 1330 1340 1350
DMALAGGVAV MPTPGMFVEF SRQRGLAGDG RSKAFAASAD GTSWSEGVGV
1360 1370 1380 1390 1400
LLVERLSDAR RNGHQVLAVV RGSALNQDGA SNGLTAPNGP SQQRVIRRAL
1410 1420 1430 1440 1450
ADARLTTSDV DVVEAHGTGT RLGDPIEAQA LIATYGQGRD DEQPLRLGSL
1460 1470 1480 1490 1500
KSNIGHTQAA AGVSGVIKMV QAMRHGLLPK TLHVDEPSDQ IDWSAGAVEL
1510 1520 1530 1540 1550
LTEAVDWPEK QDGGLRRAAV SSFGISGTNA HVVLEEAPVV VEGASVVEPS
1560 1570 1580 1590 1600
VGGSAVGGGV TPWVVSAKSA AALDAQIERL AAFASRDRTD DADAGAVDAG
1610 1620 1630 1640 1650
AVAHVLADGR AQFEHRAVAL GAGADDLVQA LADPDGLIRG TASGVGRVAF
1660 1670 1680 1690 1700
VFPGQGTQWA GMGAELLDSS AVFAAAMAEC EAALSPYVDW SLEAVVRQAP
1710 1720 1730 1740 1750
GAPTLERVDV VQPVTFAVMV SLARVWQHHG VTPQAVVGHS QGEIAAAYVA
1760 1770 1780 1790 1800
GALPLDDAAR VVTLRSKSIA AHLAGKGGML SLALNEDAVL ERLSDFDGLS
1810 1820 1830 1840 1850
VAAVNGPTAT VVSGDPVQIE ELAQACKADG FRARIIPVDY ASHSRQVEII
1860 1870 1880 1890 1900
ESELAQVLAG LSPQAPRVPF FSTLEGTWIT EPVLDGTYWY RNLRHRVGFA
1910 1920 1930 1940 1950
PAIETLAVDE GFTHFVEVSA HPVLTMTLPE TVTGLGTLRR EQGGQERLVT
1960 1970 1980 1990 2000
SLAEAWVNGL PVAWTSLLPA TASRPGLPTY AFQAERYWLE NTPAALATGD
2010 2020 2030 2040 2050
DWRYRIDWKR LPAAEGSERT GLSGRWLAVT PEDHSAQAAA VLTALVDAGA
2060 2070 2080 2090 2100
KVEVLTAGAD DDREALAARL TALTTGDGFT GVVSLLDGLV PQVAWVQALG
2110 2120 2130 2140 2150
DAGIKAPLWS VTQGAVSVGR LDTPADPDRA MLWGLGRVVA LEHPERWAGL
2160 2170 2180 2190 2200
VDLPAQPDAA ALAHLVTALS GATGEDQIAI RTTGLHARRL ARAPLHGRRP
2210 2220 2230 2240 2250
TRDWQPHGTV LITGGTGALG SHAARWMAHH GAEHLLLVSR SGEQAPGATQ
2260 2270 2280 2290 2300
LTAELTASGA RVTIAACDVA DPHAMRTLLD AIPAETPLTA VVHTAGALDD
2310 2320 2330 2340 2350
GIVDTLTAEQ VRRAHRAKAV GASVLDELTR DLDLDAFVLF SSVSSTLGIP
2360 2370 2380 2390 2400
GQGNYAPHNA YLDALAARRR ATGRSAVSVA WGPWDGGGMA AGDGVAERLR
2410 2420 2430 2440 2450
NHGVPGMDPE LALAALESAL GRDETAITVA DIDWDRFYLA YSSGRPQPLV
2460 2470 2480 2490 2500
EELPEVRRII DARDSATSGQ GGSSAQGANP LAERLAAAAP GERTEILLGL
2510 2520 2530 2540 2550
VRAQAAAVLR MRSPEDVAAD RAFKDIGFDS LAGVELRNRL TRATGLQLPA
2560 2570 2580 2590 2600
TLVFDHPTPL ALVSLLRSEF LGDEETADAR RSAALPATVG AGAGAGAGTD
2610 2620 2630 2640 2650
ADDDPIAIVA MSCRYPGDIR SPEDLWRMLS EGGEGITPFP TDRGWDLDGL
2660 2670 2680 2690 2700
YDADPDALGR AYVREGGFLH DAAEFDAEFF GVSPREALAM DPQQRMLLTT
2710 2720 2730 2740 2750
SWEAFERAGI EPASLRGSST GVFIGLSYQD YAARVPNAPR GVEGYLLTGS
2760 2770 2780 2790 2800
TPSVASGRIA YTFGLEGPAT TVDTACSSSL TALHLAVRAL RSGECTMALA
2810 2820 2830 2840 2850
GGVAMMATPH MFVEFSRQRA LAPDGRSKAF SADADGFGAA EGVGLLLVER
2860 2870 2880 2890 2900
LSDARRNGHP VLAVVRGTAV NQDGASNGLT APNGPSQQRV IRQALADARL
2910 2920 2930 2940 2950
APGDIDAVET HGTGTSLGDP IEAQGLQATY GKERPAERPL AIGSVKSNIG
2960 2970 2980 2990 3000
HTQAAAGAAG IIKMVLAMRH GTLPKTLHAD EPSPHVDWAN SGLALVTEPI
3010 3020 3030 3040 3050
DWPAGTGPRR AAVSSFGISG TNAHVVLEQA PDAAGEVLGA DEVPEVSETV
3060 3070 3080 3090 3100
AMAGTAGTSE VAEGSEASEA PAAPGSREAS LPGHLPWVLS AKDEQSLRGQ
3110 3120 3130 3140 3150
AAALHAWLSE PAADLSDADG PARLRDVGYT LATSRTAFAH RAAVTAADRD
3160 3170 3180 3190 3200
GFLDGLATLA QGGTSAHVHL DTARDGTTAF LFTGQGSQRP GAGRELYDRH
3210 3220 3230 3240 3250
PVFARALDEI CAHLDGHLEL PLLDVMFAAE GSAEAALLDE TRYTQCALFA
3260 3270 3280 3290 3300
LEVALFRLVE SWGMRPAALL GHSVGEIAAA HVAGVFSLAD AARLVAARGR
3310 3320 3330 3340 3350
LMQELPAGGA MLAVQAAEDE IRVWLETEER YAGRLDVAAV NGPEAAVLSG
3360 3370 3380 3390 3400
DADAAREAEA YWSGLGRRTR ALRVSHAFHS AHMDGMLDGF RAVLETVEFR
3410 3420 3430 3440 3450
RPSLTVVSNV TGLAAGPDDL CDPEYWVRHV RGTVRFLDGV RVLRDLGVRT
3460 3470 3480 3490 3500
CLELGPDGVL TAMAADGLAD TPADSAAGSP VGSPAGSPAD SAAGALRPRP
3510 3520 3530 3540 3550
LLVALLRRKR SETETVADAL GRAHAHGTGP DWHAWFAGSG AHRVDLPTYS
3560 3570 3580 3590 3600
FRRDRYWLDA PAADTAVDTA GLGLGTADHP LLGAVVSLPD RDGLLLTGRL
3610 3620 3630 3640 3650
SLRTHPWLAD HAVLGSVLLP GAAMVELAAH AAESAGLRDV RELTLLEPLV
3660 3670 3680 3690 3700
LPEHGGVELR VTVGAPAGEP GGESAGDGAR PVSLHSRLAD APAGTAWSCH
3710 3720 3730 3740 3750
ATGLLATDRP ELPVAPDRAA MWPPQGAEEV PLDGLYERLD GNGLAFGPLF
3760 3770 3780 3790 3800
QGLNAVWRYE GEVFADIALP ATTNATAPAT ANGGGSAAAA PYGIHPALLD
3810 3820 3830 3840 3850
ASLHAIAVGG LVDEPELVRV PFHWSGVTVH AAGAAAARVR LASAGTDAVS
3860 3870 3880 3890 3900
LSLTDGEGRP LVSVERLTLR PVTADQAAAS RVGGLMHRVA WRPYALASSG
3910 3920 3930 3940 3950
EQDPHATSYG PTAVLGKDEL KVAAALESAG VEVGLYPDLA ALSQDVAAGA
3960 3970 3980 3990 4000
PAPRTVLAPL PAGPADGGAE GVRGTVARTL ELLQAWLADE HLAGTRLLLV
4010 4020 4030 4040 4050
TRGAVRDPEG SGADDGGEDL SHAAAWGLVR TAQTENPGRF GLLDLADDAS
4060 4070 4080 4090 4100
SYRTLPSVLS DAGLRDEPQL ALHDGTIRLA RLASVRPETG TAAPALAPEG
4110 4120 4130 4140 4150
TVLLTGGTGG LGGLVARHVV GEWGVRRLLL VSRRGTDAPG ADELVHELEA
4160 4170 4180 4190 4200
LGADVSVAAC DVADREALTA VLDAIPAEHP LTAVVHTAGV LSDGTLPSMT
4210 4220 4230 4240 4250
TEDVEHVLRP KVDAAFLLDE LTSTPAYDLA AFVMFSSAAA VFGGAGQGAY
4260 4270 4280 4290 4300
AAANATLDAL AWRRRAAGLP ALSLGWGLWA ETSGMTGELG QADLRRMSRA
4310 4320 4330 4340 4350
GIGGISDAEG IALLDAALRD DRHPVLLPLR LDAAGLRDAA GNDPAGIPAL
4360 4370 4380 4390 4400
FRDVVGARTV RARPSAASAS TTAGTAGTPG TADGAAETAA VTLADRAATV
4410 4420 4430 4440 4450
DGPARQRLLL EFVVGEVAEV LGHARGHRID AERGFLDLGF DSLTAVELRN
4460 4470 4480 4490 4500
RLNSAGGLAL PATLVFDHPS PAALASHLDA ELPRGASDQD GAGNRNGNEN
4510 4520 4530 4540 4550
GTTASRSTAE TDALLAQLTR LEGALVLTGL SDAPGSEEVL EHLRSLRSMV
4560 4570 4580 4590 4600
TGETGTGTAS GAPDGAGSGA EDRPWAAGDG AGGGSEDGAG VPDFMNASAE
4610
ELFGLLDQDP STD
Length:4,613
Mass (Da):477,293
Last modified:May 1, 1999 - v1
Checksum:iA3BAF8D37CEC9383
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079138 Genomic DNA. Translation: AAC69329.1.
PIRiT17409.

Genome annotation databases

KEGGiag:AAC69329.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF079138 Genomic DNA. Translation: AAC69329.1.
PIRiT17409.

3D structure databases

ProteinModelPortaliQ9ZGI5.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAC69329.

Phylogenomic databases

KOiK16000.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-18411.

Family and domain databases

Gene3Di1.10.1200.10. 3 hits.
3.40.366.10. 7 hits.
3.40.47.10. 6 hits.
3.40.50.720. 3 hits.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR032821. KAsynt_C_assoc.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR016040. NAD(P)-bd_dom.
IPR020801. PKS_acyl_transferase.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR020807. PKS_dehydratase.
IPR013968. PKS_KR.
IPR020806. PKS_PP-bd.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 3 hits.
PF16197. KAsynt_C_assoc. 3 hits.
PF00109. ketoacyl-synt. 3 hits.
PF02801. Ketoacyl-synt_C. 3 hits.
PF08659. KR. 2 hits.
PF00550. PP-binding. 3 hits.
PF14765. PS-DH. 1 hit.
[Graphical view]
SMARTiSM00827. PKS_AT. 3 hits.
SM00826. PKS_DH. 1 hit.
SM00825. PKS_KS. 3 hits.
SM00823. PKS_PP. 3 hits.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 3 hits.
SSF51735. SSF51735. 4 hits.
SSF52151. SSF52151. 6 hits.
SSF53901. SSF53901. 6 hits.
SSF55048. SSF55048. 3 hits.
PROSITEiPS50075. ACP_DOMAIN. 3 hits.
PS00606. B_KETOACYL_SYNTHASE. 2 hits.
PS00012. PHOSPHOPANTETHEINE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPIKA1_STRVZ
AccessioniPrimary (citable) accession number: Q9ZGI5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 8, 2016
Last sequence update: May 1, 1999
Last modified: October 5, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Type I modular polyketide synthases (PKSs) catalyze the step-wise condensation of simple carboxylic acid derivatives. Organizationally, type I PKSs are arranged into modules, wherein each module is comprised of a set of catalytic activities that is responsible for a single elongation of the polyketide chain and the appropriate reductive processing of the beta-keto functionality. A minimal elongation module contains an acyl transferase (AT) domain, an acyl-carrier protein (ACP) domain, and a ketosynthase (KS) domain. The AT domain is responsible for loading the methylmalonyl-CoA extender unit onto the phosphopantetheinylated ACP domain. Subsequently, the KS domain decarboxylates and then condenses the ACP-bound extender unit with the growing polyketide chain obtained from the preceding module to yield an ACP-bound beta-ketoacyl intermediate. In addition to the three core domains, each elongation module may contain up to three additional domains: a ketoreductase (KR), dehydratase (DH), and an enoyl reductase (ER) that are responsible for the reductive processing of the beta-keto functionality prior to the next extension step. The presence of a KR domain alone gives rise to a beta-hydroxyl functionality, the presence of both a KR and a DH domain generates an alkene, while the combination of KR, DH, and ER results in complete reduction to the alkane. Finally, a thioesterase (TE) domain, typically found at the terminus of the last elongation module, catalyzes the termination of polyketide biosynthesis. The activity of this domain results in cleavage of the acyl chain from the adjacent ACP and formation of the macrocyclic ring.1 Publication

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.