Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 106 (02 Dec 2020)
Sequence version 1 (01 Mar 2003)
Previous versions | rss
Add a publicationFeedback
Protein

Compactin diketide synthase mlcB

Gene

mlcB

Organism
Penicillium citrinum
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 compactin, also known as mevastatin or ML-236B, and which acts as a potent competitive inhibitor of HMG-CoA reductase (PubMed:12172803, PubMed:12242508). Compactin biosynthesis is performed in two stages (PubMed:12172803). The first stage is catalyzed by the nonaketide synthase mlcA, which belongs to type I polyketide synthases and catalyzes the iterative nine-step formation of the polyketide (PubMed:12172803). This PKS stage is completed by the action of dehydrogenase mlcG, which catalyzes the NADPH-dependent reduction of the unsaturated tetra-, penta- and heptaketide intermediates that arise during the mlcA-mediated biosynthesis of the nonaketide chain and leads to dihydro-ML-236C carboxylate (PubMed:12172803). Covalently bound dihydro-ML-236C carboxylate is released from mlcA by the mlcF esterase (PubMed:12172803). Conversion of dihydro-ML-236C carboxylate into ML-236A carboxylate is subsequently performed with the participation of molecular oxygen and P450 monoogygenase mlcC (PubMed:12172803). Finally, mlcH performs the conversion of ML-236A carboxylate to ML-236B/compactin carboxylate through the addition of the side-chain diketide moiety produced by the diketide synthase mlcB (PubMed:12172803).2 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'-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: Polyketide biosynthesis

This protein is involved in Polyketide biosynthesis.Curated
View all proteins of this organism that are known to be involved 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 sitei202For beta-ketoacyl synthase activityPROSITE-ProRule annotation1
Active sitei658For malonyltransferase activityPROSITE-ProRule annotation1
Active sitei998For 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

<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:
Compactin diketide synthase mlcB1 Publication (EC:2.3.1.2441 Publication)
Alternative name(s):
Compactin 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:mlcB
<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>OrganismiPenicillium citrinum
<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 identifieri5077 [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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

<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

Compactin (also known as mevastatin or ML-236B) and the intermediary metabolites Ml-236C and ML-236A are inhibitors of HMG-CoA reductase involved in cholesterogenesis (PubMed:1010803). Their hypocholesterolemic activity might be useful for lowering cholesterol levels in the blood and reduce artherosclerosis and coronary heart disease (PubMed:1010803).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

Impairs the production of compactin and leads to the accumulation of the ML-236A intermediate (PubMed:12172803).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_00004362821 – 2563Compactin diketide synthase mlcBAdd BLAST2563

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 residuei2522O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

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 induced at the beginning of the stationary phase, which is consistent with the timing of compactin production (PubMed:12172803). Expression is controlled by the ML-236B/compactin cluster transcription regulator mlcR (PubMed:12436257).2 Publications

<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
Q8J0F5

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>Domaini2485 – 2562CarrierPROSITE-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>Regioni22 – 452Beta-ketoacyl synthaseBy similarityAdd BLAST431
Regioni568 – 915Acyl and malonyl transferaseBy similarityAdd BLAST348
Regioni998 – 1010Dehydratase-likeBy similarityAdd BLAST13
Regioni1542 – 1579MethyltransferaseBy 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
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.

Q8J0F5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNNTPAVTAT ATATATATAM AGSACSNTST PIAIVGMGCR FAGDATSPQK
60 70 80 90 100
LWEMVERGGS AWSKVPSSRF NVRGVYHPNG ERVGSTHVKG GHFIDEDPAL
110 120 130 140 150
FDAAFFNMTT EVASCMDPQY RLMLEVVYES LESAGITIDG MAGSNTSVFG
160 170 180 190 200
GVMYHDYQDS LNRDPETVPR YFITGNSGTM LSNRISHFYD LRGPSVTVDT
210 220 230 240 250
ACSTTLTALH LACQSLRTGE SDTAIVIGAN LLLNPDVFVT MSNLGFLSPD
260 270 280 290 300
GISYSFDPRA NGYGRGEGIA ALVIKALPNA LRDQDPIRAV IRETALNQDG
310 320 330 340 350
KTPAITAPSD VAQKSLIQEC YDKAGLDMSL TSYVEAHGTG TPTGDPLEIS
360 370 380 390 400
AISAAFKGHP LHLGSVKANI GHTEAASGLA SIIKVALALE KGLIPPNARF
410 420 430 440 450
LQKNSKLMLD QKNIKIPMSA QDWPVKDGTR RASVNNFGFG GSNAHVILES
460 470 480 490 500
YDRASLALPE DQVHVNGNSE HGRVEDGSKQ SRIYVVRAKD EQACRRTIAS
510 520 530 540 550
LRDYIKSVAD IDGEPFLASL AYTLGSRRSI LPWTSVYVAD SLGGLVSALS
560 570 580 590 600
DESNQPKRAN EKVRLGFVFT GQGAQWHAMG RELVNTFPVF KQAILECDGY
610 620 630 640 650
IKQLGASWNF MEELHRDELT TRVNDAEYSL PLSTAIQIAL VRLLWSWGIR
660 670 680 690 700
PTGITSHSSG EAAAAYAAGA LSARSAIGIT YIRGVLTTKP KPALAAKGGM
710 720 730 740 750
MAVGLGRSET NVYISRLNQE DGCVVVGCIN SQCSVTVSGD LGAIEKLEKL
760 770 780 790 800
LHADGIFTRK LKVTEAFHSS HMRPMADAFG ASLRDLFNSD NNNDNPNADT
810 820 830 840 850
SKGVLYSSPK TGSRMTDLKL LLDPTHWMDS MLQPVEFESS LREMCFDPNT
860 870 880 890 900
KEKAVDVIIE IGPHGALGGP INQVMQDLGL KGTDINYLSC LSRGRSSLET
910 920 930 940 950
MYRAATELIS KGYGLKMDAI NFPHGRKEPR VKVLSDLPAY PWNHQTRYWR
960 970 980 990 1000
EPRGSRESKQ RTHPPHTLIG SRESLSPQFA PKWKHVLRLS DIPWIRDHVV
1010 1020 1030 1040 1050
GSSIIFPGAG FISMAIEGFS QVCPPVAGAS INYNLRDVEL AQALIIPADA
1060 1070 1080 1090 1100
EAEVDLRLTI RSCEERSLGT KNWHQFSVHS ISGENNTWTE HCTGLIRSES
1110 1120 1130 1140 1150
ERSHLDCSTV EASRRLNLGS DNRSIDPNDL WESLHANGIC HGPIFQNIQR
1160 1170 1180 1190 1200
IQNNGQGSFC RFSIADTASA MPHSYENRHI VHPTTLDSVI QAAYTVLPYA
1210 1220 1230 1240 1250
GTRMKTAMVP RRLRNVKISS SLADLEAGDA LDAQASIKDR NSQSFSTDLA
1260 1270 1280 1290 1300
VFDDYDSGSS PSDGIPVIEI EGLVFQSVGS SFSDQKSDSN DTENACSSWV
1310 1320 1330 1340 1350
WAPDISLGDS TWLKEKLSTE AETKETELMM DLRRCTINFI QEAVTDLTNS
1360 1370 1380 1390 1400
DIQHLDGHLQ KYFDWMNVQL DLARQNKLSP ASCDWLSDDA EQKKCLQARV
1410 1420 1430 1440 1450
AGESVNGEMI SRLGPQLIAM LRRETEPLEL MMQDQLLSRY YVNAIKWSRS
1460 1470 1480 1490 1500
NAQASELIRL CAHKNPRSRI LEIGGGTGGC TKLIVNALGN TKPIDRYDFT
1510 1520 1530 1540 1550
DVSAGFFESA REQFADWQDV MTFKKLDIES DPEQQGFECA TYDVVVACQV
1560 1570 1580 1590 1600
LHATRCMKRT LSNVRKLLKP GGNLILVETT RDQLDLFFTF GLLPGWWLSE
1610 1620 1630 1640 1650
EPERKSTPSL TTDLWNTMLD TSGFNGVELE VRDCEDDEFY MISTMLSTAR
1660 1670 1680 1690 1700
KENTTPDTVA ESEVLLLHGA LRPPSSWLES LQAAICEKTS SSPSINALGE
1710 1720 1730 1740 1750
VDTTGRTCIF LGEMESSLLG EVGSETFKSI TAMLNNCNAL LWVSRGAAMS
1760 1770 1780 1790 1800
SEDPWKALHI GLLRTIRNEN NGKEYVSLDL DPSRNAYTHE SLYAICNIFN
1810 1820 1830 1840 1850
GRLGDLSEDK EFEFAERNGV IHVPRLFNDP HWKDQEAVEV TLQPFEQPGR
1860 1870 1880 1890 1900
RLRMEVETPG LLDSLQFRDD EGREGKDLPD DWVEIEPKAF GLNFRDVMVA
1910 1920 1930 1940 1950
MGQLEANRVM GFECAGVITK LGGAAAASQG LRLGDRVCAL LKGHWATRTQ
1960 1970 1980 1990 2000
TPYTNVVRIP DEMGFPEAAS VPLAFTTAYI ALYTTAKLRR GERVLIHSGA
2010 2020 2030 2040 2050
GGVGQAAIIL SQLAGAEVFV TAGTQAKRDF VGDKFGINPD HIFSSRNDLF
2060 2070 2080 2090 2100
VDGIKAYTGG LGVHVVLNSL AGQLLQASFD CMAEFGRFVE IGKKDLEQNS
2110 2120 2130 2140 2150
RLDMLPFTRD VSFTSIDLLS WQRAKSEEVS EALNHVTKLL ETKAIGLIGP
2160 2170 2180 2190 2200
IQQHSLSNIE KAFRTMQSGQ HVGKVVVNVS GDELVPVGDG GFSLKLKPDS
2210 2220 2230 2240 2250
SYLVAGGLGG IGKQICQWLV DHGAKHLIIL SRSAKASPFI TSLQNQQCAV
2260 2270 2280 2290 2300
YLHACDISDQ DQVTKVLRLC EEAHAPPIRG IIQGAMVLKD ALLSRMTLDE
2310 2320 2330 2340 2350
FNAATRPKVQ GSWYLHKIAQ DVDFFVMLSS LVGVMGGAGQ ANYAAAGAFQ
2360 2370 2380 2390 2400
DALAHHRRAH GMPAVTIDLG MVKSVGYVAE TGRGVADRLA RIGYKPMHEK
2410 2420 2430 2440 2450
DVMDVLEKAI LCSSPQFPSP PAAVVTGINT SPGAHWTEAN WIQEQRFVGL
2460 2470 2480 2490 2500
KYRQVLHADQ SFVSSHKKGP DGVRAQLSRV TSHDEAISIV LKAMTEKLMR
2510 2520 2530 2540 2550
MFGLAEDDMS SSKNLAGVGV DSLVAIELRN WITSEIHVDV SIFELMNGNT
2560
IAGLVELVVA KCS
Length:2,563
Mass (Da):280,159
Last modified:March 1, 2003 - 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:i304BFF399BFBFEFC
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
AB072893 Genomic DNA Translation: BAC20566.1

<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
AB072893 Genomic DNA Translation: BAC20566.1

3D structure databases

SMRiQ8J0F5
ModBaseiSearch...

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 nameiMLCB_PENCI
<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: Q8J0F5
<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: March 1, 2003
Last modified: December 2, 2020
This is version 106 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again