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Protein

Enniatin synthase

Gene

ESYN1

Organism
Fusarium equiseti (Fusarium scirpi)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

A multifunctional enzyme which activates and then thioesterifies adenylated D-2-hydroxyisovaleric acid and a hydrophobic N-methyl-L-amino acid. Peptide bond formation and N-methylation of the amino acid occur before three enzyme-bound dipeptidols are condensed to a hexapeptidol. This then cyclizes to form enniatin.2 Publications

Cofactori

pantetheine 4'-phosphateCuratedNote: Binds 6 phosphopantetheines covalently.Curated

Enzyme regulationi

The N-methylation activity is inhibited by S-adenosyl-L-homocysteine and sinefugin.1 Publication

Pathwayi: enniatin biosynthesis

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

GO - Molecular functioni

GO - Biological processi

  • enniatin biosynthetic process Source: UniProtKB-UniPathway
  • nonribosomal peptide biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Methyltransferase, Transferase

Enzyme and pathway databases

UniPathwayiUPA00234.

Names & Taxonomyi

Protein namesi
Recommended name:
Enniatin synthase
Including the following 2 domains:
N-methylcyclopeptide synthetase (EC:6.3.2.-)
S-adenosyl-L-methionine-dependent N-methyltransferase (EC:2.1.1.-)
Gene namesi
Name:ESYN1
OrganismiFusarium equiseti (Fusarium scirpi)Imported
Taxonomic identifieri61235 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusariumFusarium incarnatum-equiseti species complex

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2106Y → A: Reduces S-adenosyl-L-methionine binding. 1 Publication1
Mutagenesisi2106Y → F: Has minimal effect on S-adenosyl-L-methionine binding. 1 Publication1
Mutagenesisi2106Y → S: Reduces S-adenosyl-L-methionine binding. 1 Publication1
Mutagenesisi2106Y → V: Reduces S-adenosyl-L-methionine binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001803061 – 3131Enniatin synthaseAdd BLAST3131

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei495O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei1047O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei2105O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei2538O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei2632O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PRIDEiQ00869.

Structurei

3D structure databases

ProteinModelPortaliQ00869.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini464 – 533Acyl carrier 1PROSITE-ProRule annotationAdd BLAST70
Domaini557 – 627Acyl carrier 2PROSITE-ProRule annotationAdd BLAST71
Domaini1015 – 1083Acyl carrier 3PROSITE-ProRule annotationAdd BLAST69
Domaini2049 – 2117Acyl carrier 4PROSITE-ProRule annotationAdd BLAST69
Domaini2505 – 2575Acyl carrier 5PROSITE-ProRule annotationAdd BLAST71
Domaini2599 – 2668Acyl carrier 6PROSITE-ProRule annotationAdd BLAST70

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni499 – 1074Domain 1 (D-2-hydroxyisovaleric-activating)Add BLAST576
Regioni1572 – 2566Domain 2 (valine-activating)Add BLAST995
Regioni2014 – 2447S-adenosyl-L-methionine-dependent N-methyl transferaseAdd BLAST434

Domaini

Consists of 2 homologous regions, domains 1 and 2. Domain 2 is interrupted by an insertion which contains the N-methyltransferase activity.1 Publication

Sequence similaritiesi

Contains 6 acyl carrier domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di1.10.1200.10. 3 hits.
3.40.50.150. 1 hit.
InterProiIPR010071. AA_adenyl_domain.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR020806. PKS_PP-bd.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF00501. AMP-binding. 2 hits.
PF00668. Condensation. 3 hits.
PF00550. PP-binding. 3 hits.
[Graphical view]
SMARTiSM00823. PKS_PP. 3 hits.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 3 hits.
SSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 2 hits.
PROSITEiPS50075. ACP_DOMAIN. 3 hits.
PS00455. AMP_BINDING. 2 hits.
PS00012. PHOSPHOPANTETHEINE. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q00869-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLHTPSDGQ QDPALASKTL CEQISRALGL GQDKIENIFP GTPFQRDVID
60 70 80 90 100
CAADDKQRAV GHAVFEIPKD IDAARLAAAW KETVLHTPAL RTCTFTSKSG
110 120 130 140 150
DVLQVVLRDS FVFSWMSGPS VDLKEAVVQD EAAAALAGPR CNRFVLLEDP
160 170 180 190 200
DTKERQLIWT FSHALVDSTF QERILRRVLK AYKDANDEHP RQFETPDSSQ
210 220 230 240 250
ATPEEDLQPN PSKMLKIPQA ADMDRAVEFW KDHLSGLKCF CLPAFVLSSV
260 270 280 290 300
YAHPDAKAEH RISYSSSAQQ KMSSATICRT ALAILLSRYT HSPEALFGIV
310 320 330 340 350
TEQTPLLEEQ LMLDGPTRTV VPIRVSCASE QSVSDIMSTI DSYDQTMRQF
360 370 380 390 400
AHAGLRNIAS AGDDESAACG FQTVLLVSDG DAQPASTWEI LKKTEEPEGF
410 420 430 440 450
IPCTNRALLL SCQMTSSGAH LTARYDQSII DAEQMARLLR QLGHLIQNLQ
460 470 480 490 500
TSTDLPVEKV DMMTQEDWLE IERWNSDSID AQDTLIHSEM LKWTSQSPNK
510 520 530 540 550
AAVAAWDGEW TYAELDNVSS RLAQHINSID LGKEHAIVPI YFEKSKWVVA
560 570 580 590 600
SMLAVLKAGH AFTLIDPSDP PARTAQVVQQ TSATVALTSK LHRETVQSTV
610 620 630 640 650
GRCIVVDEEF VKSLPQSSEL SASVKAHDLA YVIFTSGSTG IPKGIMIEHR
660 670 680 690 700
SFSSCAIKFG PALGITSDTR ALQFGSHAFG ACILEIMTTL IHGGCVCIPS
710 720 730 740 750
DDDRMNNVLE FINRTNVQLG HATPSYMGTF QPEVVPGLKT LVLVGEQMSA
760 770 780 790 800
SVNEVWAPRV QLLNGYGQSE SSSICCVAKI SPGSSEPNNI GHAVGAHSWI
810 820 830 840 850
VDPEDPNRLA PIGAVGELVI ESAGIARDYI VAPTQDKSPF IKTAPTWYPA
860 870 880 890 900
KQLPDGFKIY RTGDLACYAS DGSIVCLGRM DSQVKIRGQR VELGAVETHL
910 920 930 940 950
RQQMPDDMTI VVEAVKFSDS SSTTVLTAFL IGAGEKNSHI LDQRATREIN
960 970 980 990 1000
AKMEQVLPRH SIPAFYISMN NLPQTATGKV DRRKLRIMGS KILSQKTHST
1010 1020 1030 1040 1050
PSQQSQAAIS SGTDTYTKLE SIWITSLDLE PGSANMSATF FEMGGNSIIA
1060 1070 1080 1090 1100
IKMVNMARSN GIELKVSDIY QNPTLAGLKA IVIGTSLPYS LIPKVTRQGP
1110 1120 1130 1140 1150
VSEQSYAQNR MWFLDQLSEG ASWYLIPFAV RMRGPVDVDA LTRALLALEQ
1160 1170 1180 1190 1200
RHETLRTTFE NQDGVGVQII HDRLSKELQV IDALDGDEGG LKTLYKVETT
1210 1220 1230 1240 1250
TFDITSEAGW SSTLIRLGKD DHILSIVMHH IISDGWSIDV LRRELIQLYA
1260 1270 1280 1290 1300
AALQGKDPSS ALTPLPIQYS DFAVWQKQEA QAAEHERQLQ YWKKQLADSS
1310 1320 1330 1340 1350
PAKIPTDFPR PDLLSGDAGV VPVAIDGELY QKLRGFCNKH NSTAFSILLA
1360 1370 1380 1390 1400
AFRAAHYRLT AVDDAVIGIP IANRNRWELE NMIGFFVNTQ CMRIAVDETD
1410 1420 1430 1440 1450
TFESLVRQVR STTTAAFAHE DVPFERVVSA LQPGHRDLSR TPLAQIMFAV
1460 1470 1480 1490 1500
HSQKDLGRFE LEGIQSEPIA SKAYTRFDVE FHLFQQADGL KGSCNFATDL
1510 1520 1530 1540 1550
FKPETIQNVV SVFFQILRHG LDQPETCISV LPLTDGVEEL RRLDLLEIKR
1560 1570 1580 1590 1600
TNYPRDSSVV DVFREQAAAN PEVIAVTDSS SRLTYAELDN KSELLSRWLR
1610 1620 1630 1640 1650
RRNLTPETLV SVLAPRSCET IVAYVGILKA NLAYLPLDVR SPVTRMKDIL
1660 1670 1680 1690 1700
SSVSGNTIVL MGSGVEDPGF DLPQLELVRI TDTFDETIED VQDSPQPSAT
1710 1720 1730 1740 1750
SLAYVVFTSG STGKPKGVMI EHRAIVRLVK SDNFPGFPSP ARMSNVFNPA
1760 1770 1780 1790 1800
FDGAIWEINW MLLNGGTVVC IDYLTTLDGK ELAAVFAKER VNAAFFAPAM
1810 1820 1830 1840 1850
LKLYLVDARE ALKNLDFLIV GGERFDTKEA VEAMPLVRGK IANIYGPTEA
1860 1870 1880 1890 1900
GIISTCYNIP KDEAYTNGVP IGGSIYNSGA YVMDPNQQLV GLGVMGELVV
1910 1920 1930 1940 1950
TGDGVGRGYT NPELNKNRFI DITIEGKTFK AYRTGDRMRA RVGDGLLEFF
1960 1970 1980 1990 2000
GRMDNQFKIR GNRIEAGEVE SAMLSLKNVL NAAIVVRGGG EDEGPLEMVG
2010 2020 2030 2040 2050
FIVADDKNDT TEEEETGNQV EGWQDHFESG MYSDISTAVD QSAIGNDFKG
2060 2070 2080 2090 2100
WTSMYDGKDI DKGEMQEWLD DAIHTLHNGQ IPRDVLEIGT GSGMILFNLN
2110 2120 2130 2140 2150
PGLNSYVGLD PSKSAVEFVN RAVESSPKFA GKAKVHVGMA TDVNKLGEVH
2160 2170 2180 2190 2200
PDLVVFNSVV QYFPTPEYLA EVIDGLIAIP SVKRIFLGDI RSYATNGHFL
2210 2220 2230 2240 2250
AARAIHTLGT NNNATKDRVR QKIQELEDRE EEFLVEPAFF TTLKERRPDV
2260 2270 2280 2290 2300
VKHVEIIPKN MKATNELSAY RYTAVVHLRD ETDEPVYHIE KDSWVDFEAK
2310 2320 2330 2340 2350
QMDKTALLDH LRLSKDAMSV AVSNITYAHT AFERRIVESL DEDSKDDTKG
2360 2370 2380 2390 2400
TLDGAAWLSA VRSEAENRAS LTVPDILEIA KEAGFRVEVS AARQWSQSGA
2410 2420 2430 2440 2450
LDAVFHHFPP SSTDRTLIQF PTDNELRSSL TLANRPLQKL QRRRAALQVR
2460 2470 2480 2490 2500
EKLQTLVPSY MVPPNIVVLD TMPLNTNGKI DRKELTRRAR TLPKQQTAAP
2510 2520 2530 2540 2550
VPDFPISDIE ITLCEEATEV FGMKVEISDH FFQLGGHSLL ATKLISRIQH
2560 2570 2580 2590 2600
RLHVRVTVKD VFDSPVFADL AVIIRQGLAM QNPVAEGQDK QGWSSRVAPR
2610 2620 2630 2640 2650
TEVEKMLCEE FAAGLGVPVG ITDNFFDLGG HSLMATKLAV RIGRRLIRHH
2660 2670 2680 2690 2700
SQGHLRLPCA FQLAKKLESS HSKSYEESGD DIQMADYTAF QLLDLEDPQD
2710 2720 2730 2740 2750
FVQSQIRPQL DSCYGTIQDV YPSTQMQKAF LFDPTTGEPR GLVPFYIDFP
2760 2770 2780 2790 2800
SNADAETLTK AIGALVDKLD MFRTVFLEAA GDLYQVVVEH LNLPIETIET
2810 2820 2830 2840 2850
EKNVNTATGD YLDVHGKDPV RLGHPCIQFA ILKTASSVRV LLRMSHALYD
2860 2870 2880 2890 2900
GLSFEYIVRG LHVLYSGRNL PPPTQFARYM QYAAHSREEG YPFWREVLQN
2910 2920 2930 2940 2950
APMTVLHDTN NGMSEQEMPA SKAVHLSEVV NVPAQAIRNS TNTQATVFNT
2960 2970 2980 2990 3000
ACALVLAKES GSQDVVFGRI VSGRQGLPVV WQDIIGPCTN AVPVHARVDD
3010 3020 3030 3040 3050
GNPQRIIRDL RDQYLRTLPF ESLGFEEIKR NCTDWPEELT NFSVCVTYHN
3060 3070 3080 3090 3100
FEYHPESEVD NQKVEMGVLA KYVELSENEP LYDLAIAGEV EADGVNLKVT
3110 3120 3130
VVAKARLYNE ARIRHVLEEV CKTFNGLNEA L
Length:3,131
Mass (Da):346,499
Last modified:October 1, 2000 - v2
Checksum:iAD7663E91FAB67C4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z18755 Genomic DNA. Translation: CAA79245.2.
PIRiS39842.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z18755 Genomic DNA. Translation: CAA79245.2.
PIRiS39842.

3D structure databases

ProteinModelPortaliQ00869.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ00869.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00234.

Family and domain databases

Gene3Di1.10.1200.10. 3 hits.
3.40.50.150. 1 hit.
InterProiIPR010071. AA_adenyl_domain.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR020806. PKS_PP-bd.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF00501. AMP-binding. 2 hits.
PF00668. Condensation. 3 hits.
PF00550. PP-binding. 3 hits.
[Graphical view]
SMARTiSM00823. PKS_PP. 3 hits.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 3 hits.
SSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 2 hits.
PROSITEiPS50075. ACP_DOMAIN. 3 hits.
PS00455. AMP_BINDING. 2 hits.
PS00012. PHOSPHOPANTETHEINE. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiESYN_FUSEQ
AccessioniPrimary (citable) accession number: Q00869
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, 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.