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UniProtKB - Q9Y7D5 (LOVF_ASPTE)

Entry version 119 (02 Dec 2020)
Sequence version 1 (01 Nov 1999)
Previous versions | rss
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Protein

Lovastatin diketide synthase lovF

Gene

lovF

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 diketide 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). 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: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).13 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'-phosphate2 PublicationsNote: Binds 1 phosphopantetheine covalently.2 Publications

<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 sitei183For beta-ketoacyl synthase activityPROSITE-ProRule annotation1
Active sitei635For malonyltransferase activityPROSITE-ProRule annotation1
Active sitei973For 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-18789

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 diketide synthase lovF1 Publication (EC:2.3.1.2442 Publications)
Short name:
LDKS1 Publication
Alternative name(s):
Lovastatin biosynthesis cluster protein F1 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:lovF1 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>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 subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Loss of lovastatin biosynthesis.1 Publication

<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_00004302681 – 2532Lovastatin diketide synthase lovFAdd BLAST2532

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 residuei2490O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		Q9Y7D5

<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 LovD.

1 Publication

<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		Q9Y7D5

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>Domaini2453 – 2530CarrierPROSITE-ProRule annotationAdd BLAST78

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>Regioni13 – 433Ketosynthase (KS) domainSequence analysis2 PublicationsAdd BLAST421
Regioni545 – 870Malonyl-CoA:ACP transacylase (MAT) domainSequence analysis2 PublicationsAdd BLAST326
Regioni941 – 1246Dehydrogenase (DH) domainSequence analysis2 PublicationsAdd BLAST306
Regioni1423 – 1607Methyltransferase (CMet) domainSequence analysis2 PublicationsAdd BLAST185
Regioni1825 – 2144Enoylreductase (ER) domainSequence analysis2 PublicationsAdd BLAST320
Regioni2168 – 2340Ketoreductase (KR) domainSequence analysis2 PublicationsAdd BLAST173

<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; an enoylreductase (ER) domain that reduces enoyl groups to alkyl group; 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.2 Publications

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

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
IPR013149, ADH_C
IPR011032, GroES-like_sf
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
IPR020843, PKS_ER
IPR013968, PKS_KR
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR006162, Ppantetheine_attach_site
IPR029063, SAM-dependent_MTases
IPR016039, Thiolase-like

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF00107, ADH_zinc_N, 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
SM00829, PKS_ER, 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
SSF50129, SSF50129, 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
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.

Q9Y7D5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTPLDAPGAP APIAMVGMGC RFGGGATDPQ KLWKLLEEGG SAWSKIPPSR 
        60         70         80         90        100
FNVGGVYHPN GQRVGSMHVR GGHFLDEDPA LFDASFFNMS TEVASCMDPQ 
       110        120        130        140        150
YRLILEVVYE ALEAAGIPLE QVSGSKTGVF AGTMYHDYQG SFQRQPEALP 
       160        170        180        190        200
RYFITGNAGT MLANRVSHFY DLRGPSVSID TACSTTLTAL HLAIQSLRAG 
       210        220        230        240        250
ESDMAIVAGA NLLLNPDVFT TMSNLGFLSS DGISYSFDSR ADGYGRGEGV 
       260        270        280        290        300
AAIVLKTLPD AVRDGDPIRL IVRETAINQD GRTPAISTPS GEAQECLIQD 
       310        320        330        340        350
CYQKAQLDPK QTSYVEAHGT GTRAGDPLEL AVISAAFPGQ QIQVGSVKAN 
       360        370        380        390        400
IGHTEAVSGL ASLIKVALAV EKGVIPPNAR FLQPSKKLLK DTHIQIPLCS 
       410        420        430        440        450
QSWIPTDGVR RASINNFGFG GANAHAIVEQ YGPFAETSIC PPNGYSGNYD 
       460        470        480        490        500
GNLGTDQAHI YVLSAKDENS CMRMVSRLCD YATHARPADD LQLLANIAYT 
       510        520        530        540        550
LGSRRSNFRW KAVCTAHSLT GLAQNLAGEG MRPSKSADQV RLGWVFTGQG 
       560        570        580        590        600
AQWFAMGREL IEMYPVFKEA LLECDGYIKE MGSTWSIIEE LSRPETESRV 
       610        620        630        640        650
DQAEFSLPLS TALQIALVRL LWSWNIQPVA VTSHSSGEAA AAYAIGALTA 
       660        670        680        690        700
RSAIGISYIR GALTARDRLA SVHKGGMLAV GLSRSEVGIY IRQVPLQSEE 
       710        720        730        740        750
CLVVGCVNSP SSVTVSGDLS AIAKLEELLH ADRIFARRLK VTQAFHSSHM 
       760        770        780        790        800
NSMTDAFRAG LTELFGADPS DAANASKDVI YASPRTGARL HDMNRLRDPI 
       810        820        830        840        850
HWVECMLHPV EFESAFRRMC LDENDHMPKV DRVIEIGPHG ALGGPIKQIM 
       860        870        880        890        900
QLPELATCDI PYLSCLSRGK SSLSTLRLLA SELIRAGFPV DLNAINFPRG 
       910        920        930        940        950
CEAARVQVLS DLPPYPWNHE TRYWKEPRIS QSARQRKGPV HDLIGLQEPL 
       960        970        980        990       1000
NLPLARSWHN VLRVSDLPWL RDHVVGSHIV FPGAGFVCMA VMGISTLCSS 
      1010       1020       1030       1040       1050
DHESDDISYI LRDVNFAQAL ILPADGEEGI DLRLTICAPD QSLGSQDWQR 
      1060       1070       1080       1090       1100
FLVHSITADK NDWTEHCTGL VRAEMDQPPS SLSNQQRIDP RPWSRKTAPQ 
      1110       1120       1130       1140       1150
ELWDSLHRVG IRHGPFFRNI TCIESDGRGS WCTFAIADTA SAMPHAYESQ 
      1160       1170       1180       1190       1200
HIVHPTTLDS AVQAAYTTLP FAGSRIKSAM VPARVGCMKI SSRLADLEAR 
      1210       1220       1230       1240       1250
DMLRAQAKMH SQSPSALVTD VAVFDEADPV GGPVMELEGL VFQSLGASLG 
      1260       1270       1280       1290       1300
TSDRDSTDPG NTCSSWHWAP DISLVNPGWL EKTLGTGIQE HEISLILELR 
      1310       1320       1330       1340       1350
RCSVHFIQEA MESLSVGDVE RLSGHLAKFY AWMQKQLACA QNGELGPESS 
      1360       1370       1380       1390       1400
SWTRDSEQAR CSLRSRVVAG STNGEMICRL GSVLPAILRR EVDPLEVMMD 
      1410       1420       1430       1440       1450
GHLLSRYYVD ALKWSRSNAQ ASELVRLCCH KNPRARILEI GGGTGGCTQL 
      1460       1470       1480       1490       1500
VVDSLGPNPP VGRYDFTDVS AGFFEAARKR FAGWQNVMDF RKLDIEDDPE 
      1510       1520       1530       1540       1550
AQGFVCGSYD VVLACQVLHA TSNMQRTLTN VRKLLKPGGK LILVETTRDE 
      1560       1570       1580       1590       1600
LDLFFTFGLL PGWWLSEEPE RQSTPSLSPT MWRSMLHTTG FNGVEVEARD 
      1610       1620       1630       1640       1650
CDSHEFYMIS TMMSTAVQAT PMSCSVKLPE VLLVYVDSST PMSWISDLQG 
      1660       1670       1680       1690       1700
EIRGRNCSVT SLQALRQVPP TEGQICVFLG EVEHSMLGSV TNDDFTLLTS 
      1710       1720       1730       1740       1750
MLQLAGGTLW VTQGATMKSD DPLKALHLGL LRTMRNESHG KRFVSLDLDP 
      1760       1770       1780       1790       1800
SRNPWTGDSR DAIVSVLDLI SMSDEKEFDY AERDGVIHVP RAFSDSINGG 
      1810       1820       1830       1840       1850
EEDGYALEPF QDSQHLLRLD IQTPGLLDSL HFTKRNVDTY EPDKLPDDWV 
      1860       1870       1880       1890       1900
EIEPRAFGLN FRDIMVAMGQ LESNVMGFEC AGVVTSLSET ARTIAPGLAV 
      1910       1920       1930       1940       1950
GDRVCALMNG HWASRVTTSR TNVVRIPETL SFPHAASIPL AFTTAYISLY 
      1960       1970       1980       1990       2000
TVARILPGET VLIHAGAGGV GQAAIILAQL TGAEVFTTAG SETKRNLLID 
      2010       2020       2030       2040       2050
KFHLDPDHVF SSRDSSFVDG IKTRTRGKGV DVVLNSLAGP LLQKSFDCLA 
      2060       2070       2080       2090       2100
RFGRFVEIGK KDLEQNSRLD MSTFVRNVSF SSVDILYWQQ AKPAEIFQAM 
      2110       2120       2130       2140       2150
SEVILLWERT AIGLIHPISE YPMSALEKAF RTMQSGQHVG KIVVTVAPDD 
      2160       2170       2180       2190       2200
AVLVRQERMP LFLKPNVSYL VAGGLGGIGR RICEWLVDRG ARYLIILSRT 
      2210       2220       2230       2240       2250
ARVDPVVTSL QERGCTVSVQ ACDVADESQL EAALQQCRAE EMPPIRGVIQ 
      2260       2270       2280       2290       2300
GAMVLKDALV SQMTADGFHA ALRPKVQGSW NLHRIASDVD FFVMLSSLVG 
      2310       2320       2330       2340       2350
VMGGAGQANY AAAGAFQDAL AEHRMAHNQP AVTIDLGMVQ SIGYVAETDS 
      2360       2370       2380       2390       2400
AVAERLQRIG YQPLHEEEVL DVLEQAISPV CSPAAPTRPA VIVTGINTRP 
      2410       2420       2430       2440       2450
GPHWAHADWM QEARFAGIKY RDPLRDNHGA LSLTPAEDDN LHARLNRAIS 
      2460       2470       2480       2490       2500
QQESIAVIME AMSCKLISMF GLTDSEMSAT QTLAGIGVDS LVAIELRNWI 
      2510       2520       2530 
TAKFNVDISV FELMEGRTIA KVAEVVLQRY KA
Length:2,532
Mass (Da):276,641
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:iC486622B89D58B2E
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
AF141925 Genomic DNA Translation: AAD34559.1

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ag:AAD34559

<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
AF141925 Genomic DNA Translation: AAD34559.1

3D structure databases

SMRiQ9Y7D5
ModBaseiSearch...

Proteomic databases

PRIDEiQ9Y7D5

Genome annotation databases

KEGGiag:AAD34559

Enzyme and pathway databases

UniPathwayiUPA00875
BioCyciMetaCyc:MONOMER-18789

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
InterProiView protein in InterPro
IPR001227, Ac_transferase_dom_sf
IPR036736, ACP-like_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR013149, ADH_C
IPR011032, GroES-like_sf
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
IPR020843, PKS_ER
IPR013968, PKS_KR
IPR020806, PKS_PP-bd
IPR009081, PP-bd_ACP
IPR006162, Ppantetheine_attach_site
IPR029063, SAM-dependent_MTases
IPR016039, Thiolase-like
PfamiView protein in Pfam
PF00698, Acyl_transf_1, 1 hit
PF00107, ADH_zinc_N, 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
SM00829, PKS_ER, 1 hit
SM00825, PKS_KS, 1 hit
SM00823, PKS_PP, 1 hit
SUPFAMiSSF47336, SSF47336, 1 hit
SSF50129, SSF50129, 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
PS00012, PHOSPHOPANTETHEINE, 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 nameiLOVF_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: Q9Y7D5
<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: September 3, 2014
Last sequence update: November 1, 1999
Last modified: December 2, 2020
This is version 119 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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