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Entry version 21 (11 Dec 2019)
Sequence version 1 (07 Jan 2015)
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Protein

Non-reducing polyketide synthase andM

Gene

andM

Organism
Emericella variicolor (Aspergillus stellatus)
Status
Reviewed-Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of anditomin, a fungal meroterpenoid (PubMed:25216349). The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase andM (PubMed:25216349). DMOA is then converted to the phthalide compound 5,7-dihydroxy-4,6-dimethylphthalide (DHDMP) by the cytochrome P450 monooxygenase andK, which is further prenylated by the prenyltransferase andD to yield farnesyl-DHDMP (PubMed:25216349). Further epoxidation by the FAD-dependent monooxygenase andE leads to epoxyfarnesyl-DHDMP (PubMed:25216349). The next step involves the terpene cyclase andB that converts epoxyfarnesyl-DHDMP into preandiloid A through opening of the epoxide ring followed by the cyclization of the farnesyl moiety (PubMed:25216349). Preandiloid A is in turn oxidized at the C-3 hydroxyl group to yield preandiloid B by the dehydrogenase andC (PubMed:25216349). The dioxygenase andA is solely responsible for the dehydrogenation of preandiloid B leading to the enone preandiloid C, as well as for the intriguing structural rearrangement to generate the bicyclo[2.2.2]octane core, transforming preandiloid C into andiconin (PubMed:25216349). FAD-binding monooxygenase andJ then produces andilesin D which is reduced by dehydrogenase andI to yield andilesin A (PubMed:25216349). Action of acetyltransferase andG followed by a spontaneous acetate elimination leads then to andilesin B, which is in turn substrate of the short chain dehydrogenase andH to yield andilesin C (PubMed:25216349). Finally, the dioxygenase andF catalyzes the transformation of andilesin C to anditomin (PubMed:25216349).1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: terpenoid biosynthesis

This protein is involved in the pathway terpenoid biosynthesis, which is part of Secondary metabolite biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway terpenoid biosynthesis and in Secondary metabolite biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei542For beta-ketoacyl synthase activityPROSITE-ProRule annotation1
Active sitei984For acyl/malonyl transferase activityPROSITE-ProRule annotation1
Active sitei2216For thioesterase activityBy similarity1
Active sitei2367For thioesterase activityBy similarity1
Active sitei2399For thioesterase activityBy similarity1

<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

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionMethyltransferase, Multifunctional enzyme, Transferase

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-19041

UniPathway: a resource for the exploration and annotation of metabolic pathways

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UniPathwayi
UPA00213

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Non-reducing polyketide synthase andM1 Publication (EC:2.3.1.-1 Publication)
Alternative name(s):
Anditomin synthesis protein M1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:andM1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEmericella variicolor (Aspergillus stellatus)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri1549217 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004365891 – 2430Non-reducing polyketide synthase andMAdd BLAST2430

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1648O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

<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

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
A0A097ZPE0

Database of comparative protein structure models

More...
ModBasei
Search...

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1614 – 1688CarrierPROSITE-ProRule annotationAdd BLAST75

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni9 – 247N-terminal acylcarrier protein transacylase domain (SAT)Sequence analysisAdd BLAST239
Regioni377 – 740Ketosynthase (KS) domainSequence analysisAdd BLAST364
Regioni897 – 1194Malonyl-CoA:ACP transacylase (MAT) domainSequence analysisAdd BLAST298
Regioni1265 – 1567Product template (PT) domainSequence analysisAdd BLAST303
Regioni1840 – 2072Methyltransferase (CMeT) domainSequence analysisAdd BLAST233
Regioni2093 – 2430Thioesterase (TE) domainBy similarityAdd BLAST338

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Multidomain protein; including a starter unit:ACP transacylase (SAT) that selects the starter unit; a ketosynthase (KS) that catalyzes repeated decarboxylative condensation to elongate the polyketide backbone; a malonyl-CoA:ACP transacylase (MAT) that selects and transfers the extender unit malonyl-CoA; a product template (PT) domain that controls the immediate cyclization regioselectivity of the reactive polyketide backbone; and an acyl-carrier protein (ACP) that serves as the tether of the growing and completed polyketide via its phosphopantetheinyl arm (PubMed:25216349).By similarity1 Publication
The release of the polyketide chain from the non-reducing polyketide synthase is mediated by the thioesterase (TE) domain localized at the C-ter of the protein (By similarity).By similarity

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.1200.10, 1 hit
3.10.129.110, 1 hit
3.40.366.10, 1 hit
3.40.47.10, 1 hit
3.40.50.1820, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029058, AB_hydrolase
IPR013094, AB_hydrolase_3
IPR001227, Ac_transferase_dom_sf
IPR036736, ACP-like_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR041068, HTH_51
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR013217, Methyltransf_12
IPR020801, PKS_acyl_transferase
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR020807, PKS_dehydratase
IPR042104, PKS_dehydratase_sf
IPR009081, PP-bd_ACP
IPR006162, Ppantetheine_attach_site
IPR029063, SAM-dependent_MTases
IPR032088, SAT
IPR016039, Thiolase-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07859, Abhydrolase_3, 1 hit
PF00698, Acyl_transf_1, 1 hit
PF18558, HTH_51, 1 hit
PF00109, ketoacyl-synt, 1 hit
PF02801, Ketoacyl-synt_C, 1 hit
PF08242, Methyltransf_12, 1 hit
PF00550, PP-binding, 1 hit
PF14765, PS-DH, 1 hit
PF16073, SAT, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00827, PKS_AT, 1 hit
SM00825, PKS_KS, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47336, SSF47336, 1 hit
SSF52151, SSF52151, 1 hit
SSF53335, SSF53335, 1 hit
SSF53474, SSF53474, 1 hit
SSF53901, SSF53901, 1 hit
SSF55048, SSF55048, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00606, B_KETOACYL_SYNTHASE, 1 hit
PS50075, CARRIER, 1 hit
PS00012, PHOSPHOPANTETHEINE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

A0A097ZPE0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEASQGIAVL FGPQSADIEE AVSCIQAFVR ENPSATYLID IIQSLPSIWP
60 70 80 90 100
AIQDSWVPLA QIDGKRQLET LGSLFGGGAA TVPPKSSNIL ITPLTVLQHI
110 120 130 140 150
VELCRLRKRG SSLQIKDVQG FCVGFLAATA VASAHDETQF RSIVAKVIRL
160 170 180 190 200
AVCVGALVDL NELERGRAAS LAVRWSGEEG YSCMEKVLAA HPEAYISCLT
210 220 230 240 250
DTNRATITVP QELQRDIIRE MANQGLSVRS IPLCGRFHHP DHAPAVRQLM
260 270 280 290 300
QLCRSDDRFQ LPDSKTLQFP LRSNIDAELV PEGPLHDIAL QSILCLQSKW
310 320 330 340 350
HATVSAALES LTERNGNVPI AAIGPEQCLP RTARSRLRQT WGSTLVPMGT
360 370 380 390 400
GHTVNGNLTP SRATSPADSS SELIPTVQPI AITGMSCRYP QADSVEALWE
410 420 430 440 450
LLELGKCAVG PLPNKRFRMD ELLREPNGPF WGNYLEEPDV FDHRFFGISA
460 470 480 490 500
REAATMDPQQ RLLLQVAYEA MESAGYCGIR SSQVPEDVGC YIGVGSDDYT
510 520 530 540 550
DNVGSTHANA YSAPGTLQAF NTGRISHHFG WSGPSVVVDT ACSSAAVAIH
560 570 580 590 600
MACQGLYTGD CSIAVAGGVN VMTSPKVTQN LAAASFLSPT GASKAFDASA
610 620 630 640 650
DGYCRGEGAG LVVLRPLDQA LQNGDPVLGI ITGTAVNQGS NCSPITVPVS
660 670 680 690 700
RSQMSLYRKA LSASGVSPDD VTYVEAHGTG TQVGDPIEMD SIRNTFGGTH
710 720 730 740 750
RTEQLYVGSI KDNVGHTETS SGVAGLIKTI LMLQKQTIPK QANFSRLNPK
760 770 780 790 800
IPALDMDNVV IPTRSTDWKV STRVAMVTNY GAAGSNASII VRQPFTYPGG
810 820 830 840 850
TRTTLSHAPI FIAAKTAESL RTYCDNLLAS LRQIPVLPDH LVSDYAYNLA
860 870 880 890 900
TKQNRTMDCY IGFATDSPAS LTNQLAAVAS GAREVYSRSG KALPVVLCFG
910 920 930 940 950
GQNGNIVHIS QDLYTNTHLL QFHLADCEKA CQSLGLPSLF PTIFRADPIE
960 970 980 990 1000
DLVSLHSALF ATQYATAKCW IDSGLEVDRM IGHSFGQLTA LCVAGGLSLV
1010 1020 1030 1040 1050
DALRFISERA RLLEKHCSGK RGLMLSVEAS EEDVRGLVNG AGQAVDVTCY
1060 1070 1080 1090 1100
NGPRSFVIGG EKVAIEAFEK VATGFKTQRL ANTHAFHSHL MDPILPALRE
1110 1120 1130 1140 1150
VAQSMTFQPT TIPVEACSQD MEWTFVHAAQ LVTHTRQPVY FESAVRRIAN
1160 1170 1180 1190 1200
KYPTGAVWLE AGSASPVIPM IRRVVESSPN NHVYQPIDIR PPQAIANLSK
1210 1220 1230 1240 1250
ATSGLWSNGT HVQFWPFHKS QSNCYNSINL PPYQFTKTRH WIDYDPLAFM
1260 1270 1280 1290 1300
PSSAPKDAGP EEAKKLVQLL KQQSGECLFT INTKDLLYQT CTKGHAVVNQ
1310 1320 1330 1340 1350
NLCPASLYLE MVISAASHVC PVELSSTMPH VQNLCILAPL VLNPQGELQL
1360 1370 1380 1390 1400
RLSQQNGERD QWTFSLFTQQ GQTSTVHATG TIWLHAITNS SAIVSRFRSL
1410 1420 1430 1440 1450
NRLMIPSRPD SIENSPRSSG LKGAAIYQSF RRVVNYAEYY RGVENVFALT
1460 1470 1480 1490 1500
NEATGQVKID TALVKDSCCD PILIDNFIQV AGIHVNCLSE MSEDEVYVCS
1510 1520 1530 1540 1550
AVGEIFIGEA FMQRDCGASL SWRVYSNYDR LSRNQVACDV FVMNQESGQL
1560 1570 1580 1590 1600
AIAIMGATFT GVSIRALTRT LARLNNQQSS APEVHDAPIP QDTVRADAMP
1610 1620 1630 1640 1650
AATPAPLPST LQEVDNLPAV QGMLGDLLGV GLEELAPSCS LLEIGVDSLM
1660 1670 1680 1690 1700
STEVLTEIKK RFNVNITSAA LSEIPDIGGL VQVIFPGTSV SQTTVSQTAP
1710 1720 1730 1740 1750
NDSNAVVVES TPVGELSMLV QEAYDAFDAI RSMTDYSRET KWTGFYDIVF
1760 1770 1780 1790 1800
PKQMALVTAY VVEAFQALGH PLQSISAGGE VPLIPVLPQH EKVRNQFYAV
1810 1820 1830 1840 1850
LEFSRLVSRT TDGRIVRTKE QIPTEAASNL HDEIIRQFPH HASEHMLLRT
1860 1870 1880 1890 1900
TGSQLAECLS GDANPLALLF QDAEARRLMG DVYTNAPMFK SATMHLAGYL
1910 1920 1930 1940 1950
QGVLERVGSG RTVKILEIGA GTGGTTRYLV SQLAARGLRF EYTFTDISSS
1960 1970 1980 1990 2000
LVMLAKKGFK EYDFMRYMTL NIEQDPPQEL LGQYDIIIST NCIHATRNIA
2010 2020 2030 2040 2050
YSCSNIRRML RPDGILCLIE LTRNLFWFDL VFGLLEGWWL FDDGRKHALA
2060 2070 2080 2090 2100
SEHLWNETLD KAGYSWIDWS RNDLKESEFL RLIVASPSKP EMPLVTQETV
2110 2120 2130 2140 2150
KFDEKDGVSL LADIYYPSVA DDANQRRPIA LLLHGGGHIM LSRKDIRADQ
2160 2170 2180 2190 2200
TMLLLDAGFL PVSIDYRLCP ETSLIEGPMR DARDALRWAR QTLPTLQLQR
2210 2220 2230 2240 2250
EDIHPNGDQV VAIGWSTGGH LAMSLAWTAA ELAVAAPEAV LSFYCPTDYI
2260 2270 2280 2290 2300
DPFWSQPNFP FGKQIAPPGE IDIRAGMSPN PITAYNPPRS KRALGGWMST
2310 2320 2330 2340 2350
TDPRSRIALH MNWKGQTLPV LLNAAKTAPG EMLLDPTKED IVRVCPTSQA
2360 2370 2380 2390 2400
SAGNYRSPTF IIHGSLDDLI PMSQVRHTAK VMKANGVDVH LRELEGSIHL
2410 2420 2430
FDIASTYGDK PDEVQAVADG IQFLKDRVQC
Length:2,430
Mass (Da):265,244
Last modified:January 7, 2015 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5A07340105952070
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AB981314 Genomic DNA Translation: BAP81867.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB981314 Genomic DNA Translation: BAP81867.1

3D structure databases

SMRiA0A097ZPE0
ModBaseiSearch...

Enzyme and pathway databases

UniPathwayiUPA00213
BioCyciMetaCyc:MONOMER-19041

Family and domain databases

Gene3Di1.10.1200.10, 1 hit
3.10.129.110, 1 hit
3.40.366.10, 1 hit
3.40.47.10, 1 hit
3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058, AB_hydrolase
IPR013094, AB_hydrolase_3
IPR001227, Ac_transferase_dom_sf
IPR036736, ACP-like_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR041068, HTH_51
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR013217, Methyltransf_12
IPR020801, PKS_acyl_transferase
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR020807, PKS_dehydratase
IPR042104, PKS_dehydratase_sf
IPR009081, PP-bd_ACP
IPR006162, Ppantetheine_attach_site
IPR029063, SAM-dependent_MTases
IPR032088, SAT
IPR016039, Thiolase-like
PfamiView protein in Pfam
PF07859, Abhydrolase_3, 1 hit
PF00698, Acyl_transf_1, 1 hit
PF18558, HTH_51, 1 hit
PF00109, ketoacyl-synt, 1 hit
PF02801, Ketoacyl-synt_C, 1 hit
PF08242, Methyltransf_12, 1 hit
PF00550, PP-binding, 1 hit
PF14765, PS-DH, 1 hit
PF16073, SAT, 1 hit
SMARTiView protein in SMART
SM00827, PKS_AT, 1 hit
SM00825, PKS_KS, 1 hit
SUPFAMiSSF47336, SSF47336, 1 hit
SSF52151, SSF52151, 1 hit
SSF53335, SSF53335, 1 hit
SSF53474, SSF53474, 1 hit
SSF53901, SSF53901, 1 hit
SSF55048, SSF55048, 1 hit
PROSITEiView protein in PROSITE
PS00606, B_KETOACYL_SYNTHASE, 1 hit
PS50075, CARRIER, 1 hit
PS00012, PHOSPHOPANTETHEINE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<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 subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiANDM_EMEVA
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: A0A097ZPE0
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 6, 2016
Last sequence update: January 7, 2015
Last modified: December 11, 2019
This is version 21 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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