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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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei1275 – 12751For beta-ketoacyl synthase activityBy similarity
Metal bindingi1743 – 17431MagnesiumBy similarity
Metal bindingi1744 – 17441Magnesium; via carbonyl oxygenBy similarity
Metal bindingi1745 – 17451MagnesiumBy similarity
Binding sitei1769 – 17691Acetyl-CoABy similarity
Binding sitei1779 – 17791Acetyl-CoABy similarity
Metal bindingi1843 – 18431MagnesiumBy similarity
Metal bindingi1844 – 18441Magnesium; via carbonyl oxygenBy 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 alphaPRO_0000180285Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei174 – 1741O-(pantetheine 4'-phosphoryl)serineBy 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.
ModBaseiSearch...
MobiDBiSearch...

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 synthase
Regioni648 – 845198Beta-ketoacyl reductaseAdd
BLAST
Regioni1743 – 17453Acetyl-CoA bindingBy similarity
Regioni1788 – 180417Acetyl-CoA bindingBy similarityAdd
BLAST
Regioni1812 – 18154Acetyl-CoA bindingBy similarity
Regioni1842 – 18443Acetyl-CoA bindingBy similarity

Sequence similaritiesi

Contains 1 acyl carrier domain.Curated

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

« Hide

        10         20         30         40         50
MRPEVEQELA HTLLVELLAY QFASPVRWIE TQDVILAEQR TERIVEIGPA
60 70 80 90 100
DTLGGMARRT LASKYEAYDA ATSVQRQILC YNKDAKEIYY DVDPVEEEPE
110 120 130 140 150
ATEPAPSATP AAPAAAPAAG APPPPPSAGP AASVEDIPVT AVDILRTLVA
160 170 180 190 200
QKLKKSLADV PLSKAIKDLV GGKSTLQNEI LGDLGKEFGS TPEKPEDVPL
210 220 230 240 250
DELGASMQAT FNGQLGKQSS SLIARMVSSK MPGGFNITSV RKYLETRWGL
260 270 280 290 300
GSGRQDGVLL LALTMEPAAR LGSEVDAKAY LDDVTNKYAA SAGVNLSAPV
310 320 330 340 350
AGGDSGGAGG GMVMDPAAID ALTKDQRALF KQQLEIIARY LKMDLRGGEK
360 370 380 390 400
AHVISQETQK ALQAQLDLWQ AEHGDFYASG IEPSFDQLKA RVYDSSWNWA
410 420 430 440 450
RQDALSMYYD IIFGRLQVVD REIVSQCIRI MNRSNPLLLD FMQYHIDNCP
460 470 480 490 500
TERGETYQLA KELGQQLIEN CREVLEVAPV YKDVAVPTGP QTTIDARGNI
510 520 530 540 550
SYKETPRTSA RKLEHYVKHM AEGGPISEYS NRTKVQNDLK SVYKLIRKQH
560 570 580 590 600
RLSKSSQLQF DALYKDVVHA LGMNESQIIP QENGHSKKGG RSAAKRNTPT
610 620 630 640 650
RPGKVETIPF LHLKKKTEHG WDYNKKLTGI YLNVTESAAK DGLSFQGKNV
660 670 680 690 700
LMTGAGAGSI GAEVLQGLIS GGAQVIVTTS RFSREVTEYY QAMYARYGAR
710 720 730 740 750
GSQLVVVPFN QGSKQDVEAL VEYIYDTKKG LGWDLDFVVP FAAIPENGRE
760 770 780 790 800
IDSIDSKSEL AHRIMLTNLL RLLGSVKTQK QAHGFETRPA QVILPLSPNH
810 820 830 840 850
GTFGNDGLYS ESKLALETLF NRWYSENWGH YLTICGAVIG WTRGTGLMSG
860 870 880 890 900
NNMVAEGVEK LGVRTFSQQE MAFNLLGLMS PAIVNLCQLD PVFADLNGGL
910 920 930 940 950
QFIPDLKGLM TKLRTDIMET SDVRQAVMKE TAIEHNIVNG EDSGVLYKKV
960 970 980 990 1000
IAEPRANIKF EFPNLPDWEK EVKPLNENLK GMVNLDKVVV VTGFSEVGPW
1010 1020 1030 1040 1050
GNSRTRWEME SKGKFSLEGC VEMAWIMGLI KHHNGPLKGQ AYSGWVDAKT
1060 1070 1080 1090 1100
GEPVDDKDVK PKYEKHILEH TGIRLIEPEL FKGYDPKKKQ LLQEIVIQED
1110 1120 1130 1140 1150
LEPFEASKET AEEFKREHGD KVEIFEIPES GEYTVRLCKG ATMLIPKALQ
1160 1170 1180 1190 1200
FDRLVAGQVP TGWDASRYGI PDDIISQVDP VTLFVLVCTA EAMLSAGVTD
1210 1220 1230 1240 1250
PYEFYKYVHL SEVGNCIGSG IGGTHRLRGM YKDRFLDKPL QKDILQESFI
1260 1270 1280 1290 1300
NTMSAWVNML LLSSTGPIKT PVGCCATAVE SVDIGYETIV EGKARVCFVG
1310 1320 1330 1340 1350
GFDDFQEEGS YEFANMKATS NAEDEFAHGR TPQEMSRPTT TTRAGFMESQ
1360 1370 1380 1390 1400
GCGMQLIMTA QLALDMGVPI HGIIALTTTA TDKIGRSVRS VPAPGQGVLT
1410 1420 1430 1440 1450
TARENPGKFP SPLLDIKYRR RQLDLRKKQI NEWQEAELLY LQEEAEAMKA
1460 1470 1480 1490 1500
QSDETFNEAE YMQERAQHIE REAIRQEKDA QYSLGNNFWK QDSRIAPLRG
1510 1520 1530 1540 1550
AMATWGLTVD DIDVASFHGT STVANDKNES DVICQQMKHL GRSKGNAVMG
1560 1570 1580 1590 1600
IFQKYLTGHP KGAAGAWMFN GCLQVLDSGL VPGNRNADNV DKVMEKFDYI
1610 1620 1630 1640 1650
VYPSRSIQTD GVKAFSVTSF GFGQKGAQVI GIHPKYLYAT LDQAQYEAYK
1660 1670 1680 1690 1700
TKVEARQKKA YRYFHNGLIN NSIFVAKSKA PYEDEQQSKV FLNPDYRVSV
1710 1720 1730 1740 1750
DKKTSELKFS TTAPEAKQSE STRQTLESLA KANATENSKI GVDVEHIDSV
1760 1770 1780 1790 1800
NIENETFVER NFTQSEQDYC RKAASPQSSF AGRWSAKEAV FKSLGVSSKG
1810 1820 1830 1840 1850
AGAALKDIEI GVDANGAPVV NLHGAAAAAA KQAGVKQVSV SISHSDSQAV

AVAVSQF
Length:1,857
Mass (Da):204,466
Last modified:April 1, 1990 - v1
Checksum:i34BAFD547D93FEE6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M37461 Genomic DNA. Translation: AAA33695.1.
PIRiS01787.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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: October 1, 2014
This is version 109 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