Reviewed, UniProtKB/Swiss-Prot P15368 (FAS2_PENPA)

Names and origin

Protein names

Recommended name:
    Fatty acid synthase subunit alpha
    EC=2.3.1.86
Including the following 3 domains:
    1- Recommended name:
            Acyl carrier
    2- Recommended name:
            3-oxoacyl-[acyl-carrier-protein] reductase
              EC=1.1.1.100
        Alternative name(s):
            Beta-ketoacyl reductase
    3- Recommended name:
            3-oxoacyl-[acyl-carrier-protein] synthase
              EC=2.3.1.41
        Alternative name(s):
            Beta-ketoacyl synthase

Gene names

Name:

FAS2

Organism

Penicillium patulum (Penicillium griseofulvum)

Taxonomic identifier

5078 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Penicillium

Protein attributes

Sequence length	1857 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	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 activity	Acetyl-CoA + n malonyl-CoA + 2n NADH + 2n NADPH = long-chain-acyl-CoA + n CoA + n CO2 + 2n NAD+ + 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.
Subunit structure	[Alpha6beta6] hexamers of two multifunctional subunits (alpha and beta).
Sequence similarities	Belongs to the fungal fatty acid synthetase subunit alpha family. Contains 1 acyl carrier domain.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Ligand	NAD NADP Phosphopantetheine
Molecular function	Oxidoreductase Transferase
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW macromolecule biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	3-oxoacyl-[acyl-carrier-protein] reductase activity Inferred from electronic annotation. Source: EC 3-oxoacyl-[acyl-carrier-protein] synthase activity Inferred from electronic annotation. Source: EC fatty-acyl-CoA synthase activity Inferred from electronic annotation. Source: EC holo-[acyl-carrier-protein] synthase activity Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphopantetheine binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1857	1857	Fatty acid synthase subunit alpha		PRO_0000180285
Regions
	Domain	1 – ?		Acyl carrier
	Region	648 – 845	198	Beta-ketoacyl reductase
	Region	? – 1857		Beta-ketoacyl synthase
Sites
	Active site	1275	1	For beta-ketoacyl synthase activity By similarity
Amino acid modifications
	Modified residue	174	1	O-(pantetheine 4'-phosphoryl)serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P15368-1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 34BAFD547D93FEE6	FASTA	1,857	204,466
	10 20 30 40 50 60 MRPEVEQELA HTLLVELLAY QFASPVRWIE TQDVILAEQR TERIVEIGPA DTLGGMARRT 70 80 90 100 110 120 LASKYEAYDA ATSVQRQILC YNKDAKEIYY DVDPVEEEPE ATEPAPSATP AAPAAAPAAG 130 140 150 160 170 180 APPPPPSAGP AASVEDIPVT AVDILRTLVA QKLKKSLADV PLSKAIKDLV GGKSTLQNEI 190 200 210 220 230 240 LGDLGKEFGS TPEKPEDVPL DELGASMQAT FNGQLGKQSS SLIARMVSSK MPGGFNITSV 250 260 270 280 290 300 RKYLETRWGL GSGRQDGVLL LALTMEPAAR LGSEVDAKAY LDDVTNKYAA SAGVNLSAPV 310 320 330 340 350 360 AGGDSGGAGG GMVMDPAAID ALTKDQRALF KQQLEIIARY LKMDLRGGEK AHVISQETQK 370 380 390 400 410 420 ALQAQLDLWQ AEHGDFYASG IEPSFDQLKA RVYDSSWNWA RQDALSMYYD IIFGRLQVVD 430 440 450 460 470 480 REIVSQCIRI MNRSNPLLLD FMQYHIDNCP TERGETYQLA KELGQQLIEN CREVLEVAPV 490 500 510 520 530 540 YKDVAVPTGP QTTIDARGNI SYKETPRTSA RKLEHYVKHM AEGGPISEYS NRTKVQNDLK 550 560 570 580 590 600 SVYKLIRKQH RLSKSSQLQF DALYKDVVHA LGMNESQIIP QENGHSKKGG RSAAKRNTPT 610 620 630 640 650 660 RPGKVETIPF LHLKKKTEHG WDYNKKLTGI YLNVTESAAK DGLSFQGKNV LMTGAGAGSI 670 680 690 700 710 720 GAEVLQGLIS GGAQVIVTTS RFSREVTEYY QAMYARYGAR GSQLVVVPFN QGSKQDVEAL 730 740 750 760 770 780 VEYIYDTKKG LGWDLDFVVP FAAIPENGRE IDSIDSKSEL AHRIMLTNLL RLLGSVKTQK 790 800 810 820 830 840 QAHGFETRPA QVILPLSPNH GTFGNDGLYS ESKLALETLF NRWYSENWGH YLTICGAVIG 850 860 870 880 890 900 WTRGTGLMSG NNMVAEGVEK LGVRTFSQQE MAFNLLGLMS PAIVNLCQLD PVFADLNGGL 910 920 930 940 950 960 QFIPDLKGLM TKLRTDIMET SDVRQAVMKE TAIEHNIVNG EDSGVLYKKV IAEPRANIKF 970 980 990 1000 1010 1020 EFPNLPDWEK EVKPLNENLK GMVNLDKVVV VTGFSEVGPW GNSRTRWEME SKGKFSLEGC 1030 1040 1050 1060 1070 1080 VEMAWIMGLI KHHNGPLKGQ AYSGWVDAKT GEPVDDKDVK PKYEKHILEH TGIRLIEPEL 1090 1100 1110 1120 1130 1140 FKGYDPKKKQ LLQEIVIQED LEPFEASKET AEEFKREHGD KVEIFEIPES GEYTVRLCKG 1150 1160 1170 1180 1190 1200 ATMLIPKALQ FDRLVAGQVP TGWDASRYGI PDDIISQVDP VTLFVLVCTA EAMLSAGVTD 1210 1220 1230 1240 1250 1260 PYEFYKYVHL SEVGNCIGSG IGGTHRLRGM YKDRFLDKPL QKDILQESFI NTMSAWVNML 1270 1280 1290 1300 1310 1320 LLSSTGPIKT PVGCCATAVE SVDIGYETIV EGKARVCFVG GFDDFQEEGS YEFANMKATS 1330 1340 1350 1360 1370 1380 NAEDEFAHGR TPQEMSRPTT TTRAGFMESQ GCGMQLIMTA QLALDMGVPI HGIIALTTTA 1390 1400 1410 1420 1430 1440 TDKIGRSVRS VPAPGQGVLT TARENPGKFP SPLLDIKYRR RQLDLRKKQI NEWQEAELLY 1450 1460 1470 1480 1490 1500 LQEEAEAMKA QSDETFNEAE YMQERAQHIE REAIRQEKDA QYSLGNNFWK QDSRIAPLRG 1510 1520 1530 1540 1550 1560 AMATWGLTVD DIDVASFHGT STVANDKNES DVICQQMKHL GRSKGNAVMG IFQKYLTGHP 1570 1580 1590 1600 1610 1620 KGAAGAWMFN GCLQVLDSGL VPGNRNADNV DKVMEKFDYI VYPSRSIQTD GVKAFSVTSF 1630 1640 1650 1660 1670 1680 GFGQKGAQVI GIHPKYLYAT LDQAQYEAYK TKVEARQKKA YRYFHNGLIN NSIFVAKSKA 1690 1700 1710 1720 1730 1740 PYEDEQQSKV FLNPDYRVSV DKKTSELKFS TTAPEAKQSE STRQTLESLA KANATENSKI 1750 1760 1770 1780 1790 1800 GVDVEHIDSV NIENETFVER NFTQSEQDYC RKAASPQSSF AGRWSAKEAV FKSLGVSSKG 1810 1820 1830 1840 1850 AGAALKDIEI GVDANGAPVV NLHGAAAAAA KQAGVKQVSV SISHSDSQAV AVAVSQF

References

[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: 3053172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	M37461 Genomic DNA. Translation: AAA33695.1.
PIR	S01787.
3D structure databases
HSSP	HSSP built from PDB template 1F80 based on UniProtKB P96618.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.1.1.100. 3108. 2.3.1.41. 3108. 2.3.1.86. 3108.
Family and domain databases
InterPro	IPR008278. 4-PPantetheinyl_Trfase. IPR018201. Ketoacyl_synth_AS. IPR014031. Ketoacyl_synth_C. IPR014030. Ketoacyl_synth_N. IPR016040. NAD(P)-bd_dom. IPR006162. PPantetheine_attach_site. IPR004568. PPantethiene-prot_Trfase. IPR016038. Thiolase-like_subgr. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.
Pfam	PF01648. ACPS. 1 hit. PF00109. ketoacyl-synt. 1 hit. PF02801. Ketoacyl-synt_C. 1 hit. [Graphical view]
ProDom	PD004282. ACPS. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00556. pantethn_trn. 1 hit.
PROSITE	PS00606. B_KETOACYL_SYNTHASE. 1 hit. PS00012. PHOSPHOPANTETHEINE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FAS2_PENPA

Accession

Primary (citable) accession number: P15368

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	September 22, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)