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P15368

- FAS2_PENPA

UniProt

P15368 - FAS2_PENPA

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Protein

Fatty acid synthase subunit alpha

Gene
FAS2
Organism
Penicillium patulum (Penicillium griseofulvum)
Status
Reviewed - Annotation score: 5 out of 5 - Protein inferred from homologyi

Functioni

Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase.UniRule annotation

Catalytic activityi

Acetyl-CoA + n malonyl-CoA + 2n NADPH = long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP+.UniRule annotation
Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO2 + [acyl-carrier-protein].UniRule annotation
(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei1275 – 12751For beta-ketoacyl synthase activity By similarity
Metal bindingi1743 – 17431Magnesium By similarity
Metal bindingi1744 – 17441Magnesium; via carbonyl oxygen By similarity
Metal bindingi1745 – 17451Magnesium By similarity
Binding sitei1769 – 17691Acetyl-CoA By similarity
Binding sitei1779 – 17791Acetyl-CoA By similarity
Metal bindingi1843 – 18431Magnesium By similarity
Metal bindingi1844 – 18441Magnesium; via carbonyl oxygen By similarity

GO - Molecular functioni

  1. 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity Source: UniProtKB-EC
  2. 3-oxoacyl-[acyl-carrier-protein] synthase activity Source: UniProtKB-EC
  3. fatty-acyl-CoA synthase activity Source: UniProtKB-EC
  4. holo-[acyl-carrier-protein] synthase activity Source: InterPro
  5. magnesium ion binding Source: InterPro

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-KW
  2. macromolecule biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Transferase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

Magnesium, Metal-binding, NAD, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid synthase subunit alpha (EC:2.3.1.86)
Including the following 3 domains:
Acyl carrier
3-oxoacyl-[acyl-carrier-protein] reductase (EC:1.1.1.100)
Alternative name(s):
Beta-ketoacyl reductase
3-oxoacyl-[acyl-carrier-protein] synthase (EC:2.3.1.41)
Alternative name(s):
Beta-ketoacyl synthase
Gene namesi
Name:FAS2
OrganismiPenicillium patulum (Penicillium griseofulvum)
Taxonomic identifieri5078 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaePenicillium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18571857Fatty acid synthase subunit alphaUniRule annotationPRO_0000180285Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei174 – 1741O-(pantetheine 4'-phosphoryl)serine By similarity

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PRIDEiP15368.

Interactioni

Subunit structurei

[Alpha6beta6] hexamers of two multifunctional subunits (alpha and beta).

Structurei

3D structure databases

ProteinModelPortaliP15368.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini134 – 295162Acyl carrierAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni? – 1857Beta-ketoacyl synthaseUniRule annotation
Regioni648 – 845198Beta-ketoacyl reductaseUniRule annotationAdd
BLAST
Regioni1743 – 17453Acetyl-CoA binding By similarity
Regioni1788 – 180417Acetyl-CoA binding By similarityAdd
BLAST
Regioni1812 – 18154Acetyl-CoA binding By similarity
Regioni1842 – 18443Acetyl-CoA binding By similarity

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.366.10. 1 hit.
3.40.47.10. 3 hits.
3.40.50.720. 1 hit.
3.90.470.20. 1 hit.
HAMAPiMF_00101. AcpS.
InterProiIPR008278. 4-PPantetheinyl_Trfase_SF.
IPR001227. Ac_transferase_dom.
IPR002582. ACPS.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR026025. FAS_alpha_yeast.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016040. NAD(P)-bd_dom.
IPR004568. PPantethiene-prot_Trfase_dom.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamiPF01648. ACPS. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
PIRSFiPIRSF000454. FAS_yeast_alpha. 1 hit.
ProDomiPD004282. PPantethiene-prot_Trfase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF52151. SSF52151. 1 hit.
SSF53901. SSF53901. 4 hits.
SSF56214. SSF56214. 1 hit.
TIGRFAMsiTIGR00556. pantethn_trn. 1 hit.
PROSITEiPS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P15368-1 [UniParc]FASTAAdd to Basket

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MRPEVEQELA HTLLVELLAY QFASPVRWIE TQDVILAEQR TERIVEIGPA     50
DTLGGMARRT LASKYEAYDA ATSVQRQILC YNKDAKEIYY DVDPVEEEPE 100
ATEPAPSATP AAPAAAPAAG APPPPPSAGP AASVEDIPVT AVDILRTLVA 150
QKLKKSLADV PLSKAIKDLV GGKSTLQNEI LGDLGKEFGS TPEKPEDVPL 200
DELGASMQAT FNGQLGKQSS SLIARMVSSK MPGGFNITSV RKYLETRWGL 250
GSGRQDGVLL LALTMEPAAR LGSEVDAKAY LDDVTNKYAA SAGVNLSAPV 300
AGGDSGGAGG GMVMDPAAID ALTKDQRALF KQQLEIIARY LKMDLRGGEK 350
AHVISQETQK ALQAQLDLWQ AEHGDFYASG IEPSFDQLKA RVYDSSWNWA 400
RQDALSMYYD IIFGRLQVVD REIVSQCIRI MNRSNPLLLD FMQYHIDNCP 450
TERGETYQLA KELGQQLIEN CREVLEVAPV YKDVAVPTGP QTTIDARGNI 500
SYKETPRTSA RKLEHYVKHM AEGGPISEYS NRTKVQNDLK SVYKLIRKQH 550
RLSKSSQLQF DALYKDVVHA LGMNESQIIP QENGHSKKGG RSAAKRNTPT 600
RPGKVETIPF LHLKKKTEHG WDYNKKLTGI YLNVTESAAK DGLSFQGKNV 650
LMTGAGAGSI GAEVLQGLIS GGAQVIVTTS RFSREVTEYY QAMYARYGAR 700
GSQLVVVPFN QGSKQDVEAL VEYIYDTKKG LGWDLDFVVP FAAIPENGRE 750
IDSIDSKSEL AHRIMLTNLL RLLGSVKTQK QAHGFETRPA QVILPLSPNH 800
GTFGNDGLYS ESKLALETLF NRWYSENWGH YLTICGAVIG WTRGTGLMSG 850
NNMVAEGVEK LGVRTFSQQE MAFNLLGLMS PAIVNLCQLD PVFADLNGGL 900
QFIPDLKGLM TKLRTDIMET SDVRQAVMKE TAIEHNIVNG EDSGVLYKKV 950
IAEPRANIKF EFPNLPDWEK EVKPLNENLK GMVNLDKVVV VTGFSEVGPW 1000
GNSRTRWEME SKGKFSLEGC VEMAWIMGLI KHHNGPLKGQ AYSGWVDAKT 1050
GEPVDDKDVK PKYEKHILEH TGIRLIEPEL FKGYDPKKKQ LLQEIVIQED 1100
LEPFEASKET AEEFKREHGD KVEIFEIPES GEYTVRLCKG ATMLIPKALQ 1150
FDRLVAGQVP TGWDASRYGI PDDIISQVDP VTLFVLVCTA EAMLSAGVTD 1200
PYEFYKYVHL SEVGNCIGSG IGGTHRLRGM YKDRFLDKPL QKDILQESFI 1250
NTMSAWVNML LLSSTGPIKT PVGCCATAVE SVDIGYETIV EGKARVCFVG 1300
GFDDFQEEGS YEFANMKATS NAEDEFAHGR TPQEMSRPTT TTRAGFMESQ 1350
GCGMQLIMTA QLALDMGVPI HGIIALTTTA TDKIGRSVRS VPAPGQGVLT 1400
TARENPGKFP SPLLDIKYRR RQLDLRKKQI NEWQEAELLY LQEEAEAMKA 1450
QSDETFNEAE YMQERAQHIE REAIRQEKDA QYSLGNNFWK QDSRIAPLRG 1500
AMATWGLTVD DIDVASFHGT STVANDKNES DVICQQMKHL GRSKGNAVMG 1550
IFQKYLTGHP KGAAGAWMFN GCLQVLDSGL VPGNRNADNV DKVMEKFDYI 1600
VYPSRSIQTD GVKAFSVTSF GFGQKGAQVI GIHPKYLYAT LDQAQYEAYK 1650
TKVEARQKKA YRYFHNGLIN NSIFVAKSKA PYEDEQQSKV FLNPDYRVSV 1700
DKKTSELKFS TTAPEAKQSE STRQTLESLA KANATENSKI GVDVEHIDSV 1750
NIENETFVER NFTQSEQDYC RKAASPQSSF AGRWSAKEAV FKSLGVSSKG 1800
AGAALKDIEI GVDANGAPVV NLHGAAAAAA KQAGVKQVSV SISHSDSQAV 1850
AVAVSQF 1857
Length:1,857
Mass (Da):204,466
Last modified:April 1, 1990 - v1
Checksum:i34BAFD547D93FEE6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M37461 Genomic DNA. Translation: AAA33695.1.
PIRiS01787.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M37461 Genomic DNA. Translation: AAA33695.1 .
PIRi S01787.

3D structure databases

ProteinModelPortali P15368.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P15368.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.40.366.10. 1 hit.
3.40.47.10. 3 hits.
3.40.50.720. 1 hit.
3.90.470.20. 1 hit.
HAMAPi MF_00101. AcpS.
InterProi IPR008278. 4-PPantetheinyl_Trfase_SF.
IPR001227. Ac_transferase_dom.
IPR002582. ACPS.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR026025. FAS_alpha_yeast.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016040. NAD(P)-bd_dom.
IPR004568. PPantethiene-prot_Trfase_dom.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view ]
Pfami PF01648. ACPS. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF000454. FAS_yeast_alpha. 1 hit.
ProDomi PD004282. PPantethiene-prot_Trfase. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF52151. SSF52151. 1 hit.
SSF53901. SSF53901. 4 hits.
SSF56214. SSF56214. 1 hit.
TIGRFAMsi TIGR00556. pantethn_trn. 1 hit.
PROSITEi PS00606. B_KETOACYL_SYNTHASE. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Isolation and sequence analysis of the fatty acid synthetase FAS2 gene from Penicillium patulum."
    Wiesner P., Beck J., Beck K.-F., Ripka S., Mueller G., Luecke S., Schweizer E.
    Eur. J. Biochem. 177:69-79(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiFAS2_PENPA
AccessioniPrimary (citable) accession number: P15368
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: February 19, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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