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Entry version 91 (02 Dec 2020)
Sequence version 1 (11 Oct 2005)
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Protein

Lovastatin diketide synthase mokB

Gene

mokB

Organism
Monascus pilosus (Red mold)
Status
Reviewed-Annotation score:

Annotation score:4 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

Diketide synthase; part of the gene cluster that mediates the biosynthesis of monakolin K, also known as lovastatin, and which acts as a potent competitive inhibitor of HMG-CoA reductase (PubMed:18578535). Monakolin K biosynthesis is performed in two stages (PubMed:19693441). The first stage is catalyzed by the nonaketide synthase mokA, which belongs to type I polyketide synthases and catalyzes the iterative nine-step formation of the polyketide (PubMed:18578535, PubMed:19693441). This PKS stage completed by the action of dehydrogenase mokE, which catalyzes the NADPH-dependent reduction of the unsaturated tetra-, penta- and heptaketide intermediates that arise during the mokA-mediated biosynthesis of the nonaketide chain and leads to dihydromonacolin L (PubMed:19693441). Covalently bound dihydromonacolin L is released from mokA by the mokD esterase (By similarity). Conversion of dihydromonacolin L into monacolin L and then monacolin J is subsequently performed with the participation of molecular oxygen and P450 monoogygenase mokC (PubMed:19693441). Finally, mokF performs the conversion of monacoline J to monacoline K through the addition of the side-chain diketide moiety (2R)-2-methylbutanoate produced by the diketide synthase mokB (PubMed:19693441).1 PublicationBy similarity1 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 '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'-phosphateBy similarityNote: Binds 1 phosphopantetheine covalently.By similarity

<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.1 Publication
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

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

Enzyme and pathway databases

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 mokB1 Publication (EC:2.3.1.2441 Publication)
Alternative name(s):
Monacolin K biosynthesis 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:mokB1 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>OrganismiMonascus pilosus (Red mold)Imported
<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 identifieri89488 [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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeMonascus

<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

Monacoline K acts as an inhibitor of HMG-CoA reductase involved in cholesterogenesis (PubMed:21821946). Its hypocholesterolemic activity might be useful for lowering cholesterol levels in the blood and reduce artherosclerosis and coronary heart disease (PubMed:21821946).1 Publication

<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

Imairs the production of monacolin K and leads to the accumulation of the monacolin J intermediate (PubMed:19693441).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_00004362811 – 2547Lovastatin diketide synthase mokBAdd BLAST2547

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi1340 ↔ 1379PROSITE-ProRule annotation
<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 residuei2501O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Disulfide bond, Phosphopantetheine, Phosphoprotein

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expression is controlled by the monacolin K cluster transcription regulator mokH (PubMed:19968298).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
Q3S2U6

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>Domaini2459 – 2541CarrierPROSITE-ProRule annotationAdd BLAST83

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>Regioni3 – 432Beta-ketoacyl synthaseBy similarityAdd BLAST430
Regioni545 – 890Acyl and malonyl transferaseBy similarityAdd BLAST346
Regioni973 – 985Dehydratase-likeBy similarityAdd BLAST13
Regioni1510 – 1547MethyltransferaseBy similarityAdd BLAST38

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
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
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, 3 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.

Q3S2U6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKATAASGTP TPIAVVGMGC RFAGGATDPQ ALWKLLEQGG STWSKTPSSR
60 70 80 90 100
FNVSGVYHPN GQRVGSMHVR GGHFLDQDPA LFDASFFNMT SEVASCMDPQ
110 120 130 140 150
QRLILEVVYE ALEAAGIPLE SVAGSNTAVF SGAMYHDYQD SLHRNPETLP
160 170 180 190 200
RYFITGNAGT MMSSRVSHFY DLRGPSVTVD TACSTTLTAL HLAIQSIRAG
210 220 230 240 250
EADMAIVAGS NLLLNSDVFV TMSNLGFLSP DGISYSFDPR ANGYGRGEGV
260 270 280 290 300
AAIILKALPR ALRDGDPIRL VVRETALNQD GRTPAITGPS PEAQACLIRE
310 320 330 340 350
CYQKAGLDPR QTSYVEAHGT GTPTGDPLEL AAISAAFQGQ PLQIGSVKAN
360 370 380 390 400
LGHTEAASGL ASVMKVALAL EKGIVPPSAR FLQPSKKLLE ERKFQIPLSS
410 420 430 440 450
QLWLPIDGIC RASINNFGFG GANAHAIVER YDPAARISTS KPNGHIRPHD
460 470 480 490 500
SHVEADRGKI YVLSAKDEHS CQEMISRLRD YLNRANPTDE RQFLANMAYT
510 520 530 540 550
LASRRSNLRW KAACRAHSLA SLLSVLVSDG TRPRRSAEKA RLGWVFTGQG
560 570 580 590 600
AQWFAMGREL IEAYPVFKEA LIECDGYIKG MGANWSIIDE LRRGEAESRV
610 620 630 640 650
NEAEFSLPLS TAIQVALVRL LWSWGIRPAA ITSHSSGEVA AAYAVGAFSA
660 670 680 690 700
RSAIGISYIR GALIAKTQPA PTTKGGMLAV GLSRSEVGEY ITRVQQQGEE
710 720 730 740 750
YLVVGCINSP SNVTVSGDLS AVVRLEELLH ADQIFARRLK VTQAFHSHHM
760 770 780 790 800
QPLSGEFREA LVEVFNADIT DTTNACQDVV YASPKTGKRL DDCNHLRDPM
810 820 830 840 850
HWVESMLFPV EFESSFREMC FDRKDQAQEV DKIIEIGPHG VLSGAIKQIL
860 870 880 890 900
QLPELAAFDI SYLSCLSRGK SAVDTIQLLA MDLLQGGYPV DLNAVNFPYG
910 920 930 940 950
CEAAEVQVLS DLPTYPWNHK TRYWKEPRIS RAARQRKIPV HDLIGVQEPL
960 970 980 990 1000
CPPLLHLWQN VLRISDVPWI RDHVVGSRIL FPGAGFISMV IDGLSQICNH
1010 1020 1030 1040 1050
DPETCGLSYI LRDVDLAQAL ILPTDGDEGV DLRLTIRAAD QKSLGMRDWQ
1060 1070 1080 1090 1100
RFSVYSIAGD KDDWTEHCTG LIRAQVDHPV SSSSIQQKTN PPQWSRKMAP
1110 1120 1130 1140 1150
QDLWASLHAT GICHGPLFQN IERIESDGQA SWCTLTVADT VATMPHAYES
1160 1170 1180 1190 1200
QHIVHPTTLD SAIQAAYTVL PFMGTLMKTA MVPSRIGGMK IPASFASLEP
1210 1220 1230 1240 1250
GDMLCAQAKI KNQGLSAFTT DVAVFNESDM DEEAGIELEG LTFQSLGAVI
1260 1270 1280 1290 1300
SDSRRDLTEN ESTYSSWHWA PDITLTNSTW LERILSTGTQ SQEIGVMLEL
1310 1320 1330 1340 1350
RRCTVHFIQE AIENLTTEDV ERLSGHLVKF YCWMQAQLAC ATNGELGQDS
1360 1370 1380 1390 1400
ADWLRDSEQE RQSLRSRVVA ATNNGEMICR LGPKLSAILR GELDPLELMM
1410 1420 1430 1440 1450
DGQLLSRYYI RAIKWSRSNT QASELVRLCC HKNPRARILE IGGGTGGCTQ
1460 1470 1480 1490 1500
LIVNALGPTK PVGRYDFTDV SAGFFEAARK RFSGWQDVMD FRKLDIEGDP
1510 1520 1530 1540 1550
EVQGFDCGSY DVVLACQVLH ATSNMQRTLN NVRKLLKPGG KLILVETTRD
1560 1570 1580 1590 1600
QLDLFFTFGL LPGWWLSEEP ERQLTPSLSP ELWRSVLSAT GFSGVDLEVR
1610 1620 1630 1640 1650
DCDSDEFYMI STMMSTATPG TPATTLNGPA EVLLVHAGSP PPMDWLQNLQ
1660 1670 1680 1690 1700
VALGGKNSSI TSLKALQGVS DLKGKMCVFL GEMDRTLLES VVSDDFTSLT
1710 1720 1730 1740 1750
SMLQYSQGTL WVTRGAAMAS DDPRKALHLG LLRTLRNENH GRRFVSLDLD
1760 1770 1780 1790 1800
PLRDPWTAQS CDAIVNVLNA VGASHEKEFE YAERDGTIHV PRTFSDSSSS
1810 1820 1830 1840 1850
EKEDLVVLEP FQNETRLVRL DVQTPGLLDS LHFKLCSADE AWSSELPEDW
1860 1870 1880 1890 1900
VEIEPRAFGL NFRDIMVAMG QLESNRVMGF ECAGVVTRLS KAATTGAGGL
1910 1920 1930 1940 1950
AIGDRVCALM KGHWASRVRT ARTNVICIPG TLSFEQAASI PLAFTTAYTS
1960 1970 1980 1990 2000
LYTVARLQRG EKVLIHGGAG GVGQAAIILA QLVGAEVFTT AGTHSKRNFL
2010 2020 2030 2040 2050
IDKFKLAPDH VFSSRDSGFI EGIRACTNGK GVDVVLNSLA GPLLQYSFDC
2060 2070 2080 2090 2100
LVNFGRFVEI GKKDLEQNSR LNMATFARNV SFSSIDILYW EEAKSAEIFR
2110 2120 2130 2140 2150
ALTEIMRLLE QKTIDLIGPI SEYPMSAIEK AFRTMQSGQH VGKLVVATAE
2160 2170 2180 2190 2200
TDMIPVRRGT MPVALKLDAS YLIVGGLGGI GRRICEWMVD HGARHLLILS
2210 2220 2230 2240 2250
RSGRTDPFVT GLQKRGCVVR IHSCDVADES QLHAVLQQCH EDNMPPIRGI
2260 2270 2280 2290 2300
IQAAMVLKDA LVSQMTADDF HVALRPKVQG SWNLHKIASE VDFFIMLSSL
2310 2320 2330 2340 2350
VGVMGGAGQA NYAAAGAFQD ALAQHRVAQG KPAVTIDLGM VKSIGYVAET
2360 2370 2380 2390 2400
DPAVAERLAR IGYQPMHEEE VLAVLERAMS PSSSSAPPSS NPTIPASPAV
2410 2420 2430 2440 2450
IVTGINTGPG PHFTNADWMQ EARFAGIKYR DPLKDDRGGA LSSSQPADED
2460 2470 2480 2490 2500
SVRARLSRAS TEEEATALVV QVMGHRLVTM FGLTESEMSA TQTLSSVGVD
2510 2520 2530 2540
SLVAIELRNW ITAQLNVDIS VFELMEGRTI AEVAEVVVKK YGVGSKV
Length:2,547
Mass (Da):278,173
Last modified:October 11, 2005 - 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:i9DA298ACBBBAA000
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
DQ176595 Genomic DNA Translation: ABA02240.1

<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
DQ176595 Genomic DNA Translation: ABA02240.1

3D structure databases

SMRiQ3S2U6
ModBaseiSearch...

Enzyme and pathway databases

UniPathwayiUPA00875

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
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
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, 3 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

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiMOKB_MONPI
<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: Q3S2U6
<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: May 11, 2016
Last sequence update: October 11, 2005
Last modified: December 2, 2020
This is version 91 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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