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UniProtKB - Q9Y8A5 (LOVB_ASPTE)

Entry version 116 (07 Apr 2021)
Sequence version 1 (01 Nov 1999)
Previous versions | rss
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Protein

Lovastatin nonaketide synthase, polyketide synthase component

Gene

lovB

Organism
Aspergillus terreus
Status
Reviewed-Annotation score:

Annotation score:5 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

Lovastatin nonaketide synthase; part of the gene cluster that mediates the biosynthesis of lovastatin (also known as mevinolin, mevacor or monacolin K), a hypolipidemic inhibitor of (3S)-hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR) (PubMed:10334994, PubMed:12929390, PubMed:21495633, PubMed:23023987). The first step in the biosynthesis of lovastatin is the production of dihydromonacolin L acid by the lovastatin nonaketide synthase lovB and the trans-acting enoyl reductase lovC via condensation of one acetyl-CoA unit and 8 malonyl-CoA units (PubMed:10334994, PubMed:10381407, PubMed:19900898, PubMed:23023987, PubMed:22733743). Dihydromonacolin L acid is released from lovB by the thioesterase lovG (PubMed:23653178). Next, dihydromonacolin L acid is oxidized by the dihydromonacolin L monooxygenase lovA twice to form monacolin J acid (PubMed:12929390, PubMed:21495633). The 2-methylbutyrate moiety of lovastatin is synthesized by the lovastatin diketide synthase lovF via condensation of one acetyl-CoA unit and one malonyl-CoA unit (PubMed:19530726, PubMed:21069965). Finally, the covalent attachment of this moiety to monacolin J acid is catalyzed by the transesterase lovD to yield lovastatin (PubMed:10334994, PubMed:17113998, PubMed:18988191, PubMed:19875080, PubMed:24727900). LovD has broad substrate specificity and can also convert monacolin J to simvastatin using alpha-dimethylbutanoyl-S-methyl-3-mercaptopropionate (DMB-S-MMP) as the thioester acyl donor, and can also catalyze the reverse reaction and function as hydrolase in vitro (PubMed:19875080). LovD has much higher activity with LovF-bound 2-methylbutanoate than with free diketide substrates (PubMed:21069965).14 Publications

<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 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

pantetheine 4'-phosphate1 PublicationNote: Binds 1 phosphopantetheine covalently.1 Publication

<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: lovastatin biosynthesis

This protein is involved in the pathway lovastatin biosynthesis, which is part of Polyketide biosynthesis.3 Publications
View all proteins of this organism that are known to be involved in the pathway lovastatin biosynthesis and in Polyketide 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 sitei181For beta-ketoacyl synthase activityPROSITE-ProRule annotation1
Active sitei656For malonyltransferase activityPROSITE-ProRule annotation1
Active sitei985For beta-hydroxyacyl dehydratase activityPROSITE-ProRule annotation1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionAcyltransferase, Methyltransferase, Multifunctional enzyme, Oxidoreductase, Transferase
LigandNADP, S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:MONOMER-18782

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.3.1.161, 536

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

More...UniPathwayi		UPA00875

<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:
Lovastatin nonaketide synthase, polyketide synthase component (EC:2.3.1.1612 Publications)
Short name:
LNKS
Alternative name(s):
Lovastatin biosynthesis cluster protein B1 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:lovBImported
<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>OrganismiAspergillus terreus
<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 identifieri33178 [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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Aspergillaceae › Aspergillus › Aspergillus subgen. Circumdati

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Lovastatin acts as a hypolipidemic agent that works as inhibitor of (3S)-hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR) which reduces HMG-CoA to mevalonate and is the key step in cholesterol biosynthesis (PubMed:6933445). Lovastatin, simvastatin and related compounds are widely used to treat hypercholesteremia and reduce the risk of cardiovascular disease (PubMed:6933445). Furthermore, statins such as lovastatin were found to be anticancer agents (PubMed:29236027, PubMed:29932104).3 Publications

<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_00001802881 – 3038Lovastatin nonaketide synthase, polyketide synthase componentAdd BLAST3038

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 residuei2498O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with LovC.

1 Publication

Protein-protein interaction databases

Database of interacting proteins

More...DIPi		DIP-60051N

Protein interaction database and analysis system

More...IntActi		Q9Y8A5, 1 interactor

<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		Q9Y8A5

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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>Domaini2463 – 2538CarrierPROSITE-ProRule annotation1 PublicationAdd BLAST76

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>Regioni11 – 450Ketosynthase (KS) domainSequence analysis1 PublicationAdd BLAST440
Regioni562 – 889Malonyl-CoA:ACP transacylase (MAT) domainSequence analysis1 PublicationAdd BLAST328
Regioni953 – 1263Dehydrogenase (DH) domainSequence analysis1 PublicationAdd BLAST311
Regioni1443 – 1543Methyltransferase (CMet) domainSequence analysis1 PublicationAdd BLAST101
Regioni2139 – 2437Ketoreductase (KR) domainSequence analysis1 PublicationAdd BLAST299
Regioni2602 – 2952Inactive Condensation domain1 PublicationAdd BLAST351

<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 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 dehydratase (DH) domain that reduces hydroxyl groups to enoyl groups; a methyltransferase (CMeT) domain responsible for the incorporation of methyl groups; a ketoreductase (KR) domain that catalyzes beta-ketoreduction steps; and an acyl-carrier protein (ACP) that serves as the tether of the growing and completed polyketide via its phosphopantetheinyl arm (PubMed:22733743). A C-terminal thioesterase (TE) domain that is often found in polyketide synthase proteins is not present in this protein, but lovB contains insteado a C-terminal condensation (C) domain that has lost its condensation activity, but has gained a novel function that is necessary for release of the final product (PubMed:23023987).2 Publications
Lacks an enoylreductase (ER) domain that reduces enoyl groups to alkyl group which function is performed by the trans-acting enoyl reductase lovC.1 Publication

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.10.129.110, 1 hit
3.30.559.10, 1 hit
3.40.366.10, 1 hit
3.40.47.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001227, Ac_transferase_dom_sf
IPR036736, ACP-like_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR023213, CAT-like_dom_sf
IPR001242, Condensatn
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR013217, Methyltransf_12
IPR036291, NAD(P)-bd_dom_sf
IPR032821, PKS_assoc
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR020807, PKS_dehydratase
IPR042104, PKS_dehydratase_sf
IPR013968, PKS_KR
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR029063, SAM-dependent_MTases
IPR016039, Thiolase-like

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF00668, Condensation, 1 hit
PF16197, KAsynt_C_assoc, 1 hit
PF00109, ketoacyl-synt, 1 hit
PF02801, Ketoacyl-synt_C, 1 hit
PF08659, KR, 1 hit
PF08242, Methyltransf_12, 1 hit
PF00550, PP-binding, 1 hit
PF14765, PS-DH, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00827, PKS_AT, 1 hit
SM00826, PKS_DH, 1 hit
SM00825, PKS_KS, 1 hit
SM00823, PKS_PP, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47336, SSF47336, 1 hit
SSF51735, SSF51735, 2 hits
SSF52151, SSF52151, 1 hit
SSF53335, SSF53335, 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

<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.

Q9Y8A5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAQSMYPNEP IVVVGSGCRF PGDANTPSKL WELLQHPRDV QSRIPKERFD 
        60         70         80         90        100
VDTFYHPDGK HHGRTNAPYA YVLQDDLGAF DAAFFNIQAG EAESMDPQHR 
       110        120        130        140        150
LLLETVYEAV TNAGMRIQDL QGTSTAVYVG VMTHDYETVS TRDLESIPTY 
       160        170        180        190        200
SATGVAVSVA SNRISYFFDW HGPSMTIDTA CSSSLVAVHL AVQQLRTGQS 
       210        220        230        240        250
SMAIAAGANL ILGPMTFVLE SKLSMLSPSG RSRMWDAGAD GYARGEAVCS 
       260        270        280        290        300
VVLKTLSQAL RDGDTIECVI RETGVNQDGR TTGITMPNHS AQEALIKATY 
       310        320        330        340        350
AQAGLDITKA EDRCQFFEAH GTGTPAGDPQ EAEAIATAFF GHEQVARSDG 
       360        370        380        390        400
NERAPLFVGS AKTVVGHTEG TAGLAGLMKA SFAVRHGVIP PNLLFDKISP 
       410        420        430        440        450
RVAPFYKNLR IPTEATQWPA LPPGQPRRAS VNSFGFGGTN AHAIIEEYME 
       460        470        480        490        500
PEQNQLRVSN NEDCPPMTGV LSLPLVLSAK SQRSLKIMME EMLQFLQSHP 
       510        520        530        540        550
EIHLHDLTWS LLRKRSVLPF RRAIVGHSHE TIRRALEDAI EDGIVSSDFT 
       560        570        580        590        600
TEVRGQPSVL GIFTGQGAQW PGMLKNLIEA SPYVRNIVRE LDDSLQSLPE 
       610        620        630        640        650
KYRPSWTLLD QFMLEGEASN VQYATFSQPL CCAVQIVLVR LLEAARIRFT 
       660        670        680        690        700
AVVGHSSGEI ACAFAAGLIS ASLAIRIAYL RGVVSAGGAR GTPGAMLAAG 
       710        720        730        740        750
MSFEEAQEIC ELDAFEGRIC VAASNSPDSV TFSGDANAID HLKGMLEDES 
       760        770        780        790        800
TFARLLKVDT AYHSHHMLPC ADPYMQALEE CGCAVADAGS PAGSVPWYSS 
       810        820        830        840        850
VDAENRQMAA RDVTAKYWKD NLVSPVLFSH AVQRAVVTHK ALDIGIEVGC 
       860        870        880        890        900
HPALKSPCVA TIKDVLSGVD LAYTGCLERG KNDLDSFSRA LAYLWERFGA 
       910        920        930        940        950
SSFDADEFMR AVAPDRPCMS VSKLLPAYPW DRSRRYWVES RATRHHLRGP 
       960        970        980        990       1000
KPHLLLGKLS EYSTPLSFQW LNFVRPRDIE WLDGHALQGQ TVFPAAGYIV 
      1010       1020       1030       1040       1050
MAMEAALMIA GTHAKQVKLL EILDMSIDKA VIFDDEDSLV ELNLTADVSR 
      1060       1070       1080       1090       1100
NAGEAGSMTI SFKIDSCLSK EGNLSLSAKG QLALTIEDVN PRTTSASDQH 
      1110       1120       1130       1140       1150
HLPPPEEEHP HMNRVNINAF YHELGLMGYN YSKDFRRLHN MQRADLRASG 
      1160       1170       1180       1190       1200
TLDFIPLMDE GNGCPLLLHP ASLDVAFQTV IGAYSSPGDR RLRCLYVPTH 
      1210       1220       1230       1240       1250
VDRITLVPSL CLATAESGCE KVAFNTINTY DKGDYLSGDI VVFDAEQTTL 
      1260       1270       1280       1290       1300
FQVENITFKP FSPPDASTDH AMFARWSWGP LTPDSLLDNP EYWATAQDKE 
      1310       1320       1330       1340       1350
AIPIIERIVY FYIRSFLSQL TLEERQQAAF HLQKQIEWLE QVLASAKEGR 
      1360       1370       1380       1390       1400
HLWYDPGWEN DTEAQIEHLC TANSYHPHVR LVQRVGQHLL PTVRSNGNPF 
      1410       1420       1430       1440       1450
DLLDHDGLLT EFYTNTLSFG PALHYARELV AQIAHRYQSM DILEIGAGTG 
      1460       1470       1480       1490       1500
GATKYVLATP QLGFNSYTYT DISTGFFEQA REQFAPFEDR MVFEPLDIRR 
      1510       1520       1530       1540       1550
SPAEQGFEPH AYDLIIASNV LHATPDLEKT MAHARSLLKP GGQMVILEIT 
      1560       1570       1580       1590       1600
HKEHTRLGFI FGLFADWWAG VDDGRCTEPF VSFDRWDAIL KRVGFSGVDS 
      1610       1620       1630       1640       1650
RTTDRDANLF PTSVFSTHAI DATVEYLDAP LASSGTVKDS YPPLVVVGGQ 
      1660       1670       1680       1690       1700
TPQSQRLLND IKAIMPPRPL QTYKRLVDLL DAEELPMKST FVMLTELDEE 
      1710       1720       1730       1740       1750
LFAGLTEETF EATKLLLTYA SNTVWLTENA WVQHPHQAST IGMLRSIRRE 
      1760       1770       1780       1790       1800
HPDLGVHVLD VDAVETFDAT FLVEQVLRLE EHTDELASST TWTQEPEVSW 
      1810       1820       1830       1840       1850
CKGRPWIPRL KRDLARNNRM NSSRRPIYEM IDSSRAPVAL QTARDSSSYF 
      1860       1870       1880       1890       1900
LESAETWFVP ESVQQMETKT IYVHFSCPHA LRVGQLGFFY LVQGHVQEGN 
      1910       1920       1930       1940       1950
REVPVVALAE RNASIVHVRP DYIYTEADNN LSEGGGSLMV TVLAAAVLAE 
      1960       1970       1980       1990       2000
TVISTAKCLG VTDSILVLNP PSICGQMLLH AGEEIGLQVH LATTSGNRSS 
      2010       2020       2030       2040       2050
VSAGDAKSWL TLHARDTDWH LRRVLPRGVQ ALVDLSADQS CEGLTQRMMK 
      2060       2070       2080       2090       2100
VLMPGCAHYR AADLFTDTVS TELHSGSRHQ ASLPAAYWEH VVSLARQGLP 
      2110       2120       2130       2140       2150
SVSEGWEVMP CTQFAAHADK TRPDLSTVIS WPRESDEATL PTRVRSIDAE 
      2160       2170       2180       2190       2200
TLFAADKTYL LVGLTGDLGR SLGRWMVQHG ACHIVLTSRN PQVNPKWLAH 
      2210       2220       2230       2240       2250
VEELGGRVTV LSMDVTSQNS VEAGLAKLKD LHLPPVGGIA FGPLVLQDVM 
      2260       2270       2280       2290       2300
LNNMELPMME MVLNPKVEGV RILHEKFSDP TSSNPLDFFV MFSSIVAVMG 
      2310       2320       2330       2340       2350
NPGQANYSAA NCYLQALAQQ RVASGLAAST IDIGAVYGVG FVTRAELEED 
      2360       2370       2380       2390       2400
FNAIRFMFDS VEEHELHTLF AEAVVAGRRA VHQQEQQRKF ATVLDMADLE 
      2410       2420       2430       2440       2450
LTTGIPPLDP ALKDRITFFD DPRIGNLKIP EYRGAKAGEG AAGSKGSVKE 
      2460       2470       2480       2490       2500
QLLQATNLDQ VRQIVIDGLS AKLQVTLQIP DGESVHPTIP LIDQGVDSLG 
      2510       2520       2530       2540       2550
AVTVGTWFSK QLYLDLPLLK VLGGASITDL ANEAAARLPP SSIPLVAATD 
      2560       2570       2580       2590       2600
GGAESTDNTS ENEVSGREDT DLSAAATITE PSSADEDDTE PGDEDVPRSH 
      2610       2620       2630       2640       2650
HPLSLGQEYS WRIQQGAEDP TVFNNTIGMF MKGSIDLKRL YKALRAVLRR 
      2660       2670       2680       2690       2700
HEIFRTGFAN VDENGMAQLV FGQTKNKVQT IQVSDRAGAE EGYRQLVQTR 
      2710       2720       2730       2740       2750
YNPAAGDTLR LVDFFWGQDD HLLVVAYHRL VGDGSTTENI FVEAGQLYDG 
      2760       2770       2780       2790       2800
TSLSPHVPQF ADLAARQRAM LEDGRMEEDL AYWKKMHYRP SSIPVLPLMR 
      2810       2820       2830       2840       2850
PLVGNSSRSD TPNFQHCGPW QQHEAVARLD PMVAFRIKER SRKHKATPMQ 
      2860       2870       2880       2890       2900
FYLAAYQVLL ARLTDSTDLT VGLADTNRAT VDEMAAMGFF ANLLPLRFRD 
      2910       2920       2930       2940       2950
FRPHITFGEH LIATRDLVRE ALQHARVPYG VLLDQLGLEV PVPTSNQPAP 
      2960       2970       2980       2990       3000
LFQAVFDYKQ GQAESGTIGG AKITEVIATR ERTPYDVVLE MSDDPTKDPL 
      3010       3020       3030 
LTAKLQSSRY EAHHPQAFLE SYMSLLSMFS MNPALKLA
Length:3,038
Mass (Da):335,005
Last modified:November 1, 1999 - 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:i1A944375E05DF403
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AF151722 Genomic DNA Translation: AAD39830.1

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ag:AAD39830

<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
AF151722 Genomic DNA Translation: AAD39830.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
7CPXelectron microscopy2.91A/B1-3038[»]
7CPYelectron microscopy3.60A/B1-3038[»]
SMRiQ9Y8A5
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-60051N
IntActiQ9Y8A5, 1 interactor

Genome annotation databases

KEGGiag:AAD39830

Enzyme and pathway databases

UniPathwayiUPA00875
BioCyciMetaCyc:MONOMER-18782
BRENDAi2.3.1.161, 536

Family and domain databases

Gene3Di3.10.129.110, 1 hit
3.30.559.10, 1 hit
3.40.366.10, 1 hit
3.40.47.10, 1 hit
InterProiView protein in InterPro
IPR001227, Ac_transferase_dom_sf
IPR036736, ACP-like_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR023213, CAT-like_dom_sf
IPR001242, Condensatn
IPR018201, Ketoacyl_synth_AS
IPR014031, Ketoacyl_synth_C
IPR014030, Ketoacyl_synth_N
IPR016036, Malonyl_transacylase_ACP-bd
IPR013217, Methyltransf_12
IPR036291, NAD(P)-bd_dom_sf
IPR032821, PKS_assoc
IPR020841, PKS_Beta-ketoAc_synthase_dom
IPR020807, PKS_dehydratase
IPR042104, PKS_dehydratase_sf
IPR013968, PKS_KR
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR029063, SAM-dependent_MTases
IPR016039, Thiolase-like
PfamiView protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF00668, Condensation, 1 hit
PF16197, KAsynt_C_assoc, 1 hit
PF00109, ketoacyl-synt, 1 hit
PF02801, Ketoacyl-synt_C, 1 hit
PF08659, KR, 1 hit
PF08242, Methyltransf_12, 1 hit
PF00550, PP-binding, 1 hit
PF14765, PS-DH, 1 hit
SMARTiView protein in SMART
SM00827, PKS_AT, 1 hit
SM00826, PKS_DH, 1 hit
SM00825, PKS_KS, 1 hit
SM00823, PKS_PP, 1 hit
SUPFAMiSSF47336, SSF47336, 1 hit
SSF51735, SSF51735, 2 hits
SSF52151, SSF52151, 1 hit
SSF53335, SSF53335, 1 hit
SSF53901, SSF53901, 1 hit
SSF55048, SSF55048, 1 hit
PROSITEiView protein in PROSITE
PS00606, B_KETOACYL_SYNTHASE, 1 hit
PS50075, CARRIER, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...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 nameiLOVB_ASPTE
<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: Q9Y8A5
<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: April 12, 2005
Last sequence update: November 1, 1999
Last modified: April 7, 2021
This is version 116 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

Keywords - Technical termi

3D-structure

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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