Reviewed, UniProtKB/Swiss-Prot P43098 (FAS2_CANAL)

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

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	1885 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 – 1885	1885	Fatty acid synthase subunit alpha		PRO_0000180284
Regions
	Domain	1 – ?		Acyl carrier
	Region	1157 – 1885	729	Beta-ketoacyl synthase
Sites
	Active site	1304	1	For beta-ketoacyl synthase activity By similarity
Amino acid modifications
	Modified residue	181	1	O-(pantetheine 4'-phosphoryl)serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P43098-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 4835D57F362372E0	FASTA	1,885	207,589
	10 20 30 40 50 60 MKPEIEQELS HTLLTELLAY QFASPVRWIE TQDVFLKQHN TERIIEIGPS PTLAGMANRT 70 80 90 100 110 120 IKAKYESYDA ALSLQRQVLC YSKDAKEIYY KPDPADLAPK ETPKQEESTP SAPAAATPTP 130 140 150 160 170 180 AAAAAPTPAP APASAGPVES IPDEPVKANL LIHVLVAQKL KKPLDAVPMT KAIKDLVNGK 190 200 210 220 230 240 STVQNEILGD LGKEFGSTPE KPEDTPLEEL AEQFQDSFSG QLGKTSTSLI GRLMSSKMPG 250 260 270 280 290 300 GFSITTARKY LESRFGLGAG RQDSVLLMAL TNEPANRLGS EADAKTFFDG IAQKYASSAG 310 320 330 340 350 360 ISLSSGAGSG AGAANSGGAV VDSAALDALT AENKKLAKQQ LEVLARYLQS RLKQGSLKSF 370 380 390 400 410 420 IKEKEASAVL QKELDLWEAE HGEFYAKGIQ PTFSALKSRT YDSYWNWARQ DVLSMYFDII 430 440 450 460 470 480 FGKLTSVDRE TINQCIQIMN RANPTLIKFM QYHIDHCPEY KGETYKLAKR LGQQLIDNCK 490 500 510 520 530 540 QVLTEDPVYK DVSRITGPKT KVSAKGNIEY EETQKDSVRK FEQYVYEMAQ GGAMTKVSQP 550 560 570 580 590 600 TIQEDLARVY KAISKQASKD SKLELQRVYE DLLKVVESSK EIETEQLTKD ILQAATVPTT 610 620 630 640 650 660 PTEEVDDPCT PSSDDEIASL PDKTSIIQPV SSTIPSQTIP FLHIQKKTKD GWEYNKKLSS 670 680 690 700 710 720 LYLDGLESAA INGLTFKDKY VLVTGAGAGS IGAEILQGLI SGGAKVIVTT SRFSKKVTEY 730 740 750 760 770 780 YQNMYARYGA AGSTLIVVPF NQGSKQDVDA LVQYIYDEPK KGGLGWDLDA IIPFAAIPEN 790 800 810 820 830 840 GNGLDNIDSK SEFAHRIMLT NLLRLLGAVK SKKPTDTRPA QCILPLSPNH GTFGFDGLYS 850 860 870 880 890 900 ESKISLETLF NRWYSEDWGS KLTVCGAVIG WTRGTGLMSA NNIIAEGIEK LGVRTFSQKE 910 920 930 940 950 960 MAFNILGLLT PEIVQLCQEE PVMADLNGGL QFIDNLKDFT SKLRTDLLET ADIRRAVSIE 970 980 990 1000 1010 1020 SAIEQKVVNG DNVDANYSKV MVEPRANMKF DFPTLKSYDE IKQIAPELEG MLDLENVVVV 1030 1040 1050 1060 1070 1080 TGFAEVGPWG NSRTRWEMEA YGEFSLEGAI EMAWIMGFIK YHNGNLQGKP YSGWVDAKTQ 1090 1100 1110 1120 1130 1140 TPIDEKDIKS KYEEEILEHS GIRLIEPELF NGYDPKKKQM IQEIVVQHDL EPFECSKETA 1150 1160 1170 1180 1190 1200 EQYKHEHGEK CEIFEIEESG EYTVRILKGA TLYVPKALRF DRLVAGQIPT GWDARTYGIP 1210 1220 1230 1240 1250 1260 EDTISQVDPI TLYVLVATVE ALLSAGITDP YEFYKYVHVS EVGNCSGSGM GGVSALRGMF 1270 1280 1290 1300 1310 1320 KDRYADKPVQ NDILQESFIN TMSAWVNMLL LSSSGPIKTP VGACATAVES VDIGIETILS 1330 1340 1350 1360 1370 1380 GKAKVVLVGG YDDFQEEGSY EFANMNATSN SIEEFKHGRT PKEMSRPTTT TRNGFMEAQG 1390 1400 1410 1420 1430 1440 SGIQVIMTAD LALKMGVPIH AVLAMTATAT DKIGRSVPAP GKGILTTARE HHGNLKYPSP 1450 1460 1470 1480 1490 1500 LLNIKYRKRQ LNKRLEQIKS WEETELSYLQ EEAELAKEEF GDEFSMHEFL KERTEEVYRE 1510 1520 1530 1540 1550 1560 SKRQVSDAKK QWGNSFYKSD PRIAPLRGAL AAFNLTIDDI GVASFHGTST VANDKNESAT 1570 1580 1590 1600 1610 1620 INNMMKHLGR SEGNPVFGVF QKYLTGHPKG AAGAWMLNGA IQILESGLVP GNRNADNVDK 1630 1640 1650 1660 1670 1680 LLEQYEYVLY PSRSIQTDGI KAVSVTSFGF GQKGAQAVVV HPDYLFAVLD RSTYEEYATK 1690 1700 1710 1720 1730 1740 VSARNKKTYR YMHNAITRNT MFVAKDKAPY SDELEQPVYL DPLARVEENK KKLVFSDKTI 1750 1760 1770 1780 1790 1800 QSNQSYVGEV AQKTAKALST LNKSSKGVGV DVELLSAINI DNETFIERNF TGNEVEYCLN 1810 1820 1830 1840 1850 1860 TAHPQASFTG TWSAKEAVFK ALGVESKGAG ASLIDIEITR DVNGAPKVIL HGEAKKAAAK 1870 1880 AGVKNVNISI SHDDFQATAV ALSEF

References

[1]	"Analysis and expression of the Candida albicans FAS2 gene." Southard S.B., Cihlar R.L. Gene 156:133-138(1995) [PubMed: 7737507] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 4918.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L29063 Genomic DNA. Translation: AAA34345.1.
PIR	JC4086.
3D structure databases
HSSP	HSSP built from PDB template 1FTF based on UniProtKB Q9F7T5.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.1.1.100. 1124. 2.3.1.41. 1124. 2.3.1.86. 1124.
Family and domain databases
InterPro	IPR008278. 4-PPantetheinyl_Trfase. IPR001227. Ac_transferase_reg. IPR000794. Beta-ketoacyl_synthase. 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:3.40.366.10. Ac_transferase_reg. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.
PANTHER	PTHR11712. Ketoacyl_synth. 1 hit.
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_CANAL

Accession

Primary (citable) accession number: P43098

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	September 22, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)