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P43098

- FAS2_CANAX

UniProt

P43098 - FAS2_CANAX

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Protein
Fatty acid synthase subunit alpha
Gene
FAS2
Organism
Candida albicans (Yeast)
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 sitei1304 – 13041For beta-ketoacyl synthase activity By similarity
Metal bindingi1771 – 17711Magnesium By similarity
Metal bindingi1772 – 17721Magnesium; via carbonyl oxygen By similarity
Metal bindingi1773 – 17731Magnesium By similarity
Binding sitei1797 – 17971Acetyl-CoA By similarity
Binding sitei1807 – 18071Acetyl-CoA By similarity
Metal bindingi1871 – 18711Magnesium By similarity
Metal bindingi1872 – 18721Magnesium; 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
Complete GO annotation...

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
OrganismiCandida albicans (Yeast)
Taxonomic identifieri5476 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18851885Fatty acid synthase subunit alphaUniRule annotation
PRO_0000180284Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei181 – 1811O-(pantetheine 4'-phosphoryl)serine By similarity

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP43098.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini141 – 302162Acyl carrier
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1157 – 1885729Beta-ketoacyl synthaseUniRule annotation
Add
BLAST
Regioni1771 – 17733Acetyl-CoA binding By similarity
Regioni1816 – 183217Acetyl-CoA binding By similarity
Add
BLAST
Regioni1840 – 18434Acetyl-CoA binding By similarity
Regioni1870 – 18723Acetyl-CoA binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG4982.

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.

P43098-1 [UniParc]FASTAAdd to Basket

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MKPEIEQELS HTLLTELLAY QFASPVRWIE TQDVFLKQHN TERIIEIGPS     50
PTLAGMANRT IKAKYESYDA ALSLQRQVLC YSKDAKEIYY KPDPADLAPK 100
ETPKQEESTP SAPAAATPTP AAAAAPTPAP APASAGPVES IPDEPVKANL 150
LIHVLVAQKL KKPLDAVPMT KAIKDLVNGK STVQNEILGD LGKEFGSTPE 200
KPEDTPLEEL AEQFQDSFSG QLGKTSTSLI GRLMSSKMPG GFSITTARKY 250
LESRFGLGAG RQDSVLLMAL TNEPANRLGS EADAKTFFDG IAQKYASSAG 300
ISLSSGAGSG AGAANSGGAV VDSAALDALT AENKKLAKQQ LEVLARYLQS 350
RLKQGSLKSF IKEKEASAVL QKELDLWEAE HGEFYAKGIQ PTFSALKSRT 400
YDSYWNWARQ DVLSMYFDII FGKLTSVDRE TINQCIQIMN RANPTLIKFM 450
QYHIDHCPEY KGETYKLAKR LGQQLIDNCK QVLTEDPVYK DVSRITGPKT 500
KVSAKGNIEY EETQKDSVRK FEQYVYEMAQ GGAMTKVSQP TIQEDLARVY 550
KAISKQASKD SKLELQRVYE DLLKVVESSK EIETEQLTKD ILQAATVPTT 600
PTEEVDDPCT PSSDDEIASL PDKTSIIQPV SSTIPSQTIP FLHIQKKTKD 650
GWEYNKKLSS LYLDGLESAA INGLTFKDKY VLVTGAGAGS IGAEILQGLI 700
SGGAKVIVTT SRFSKKVTEY YQNMYARYGA AGSTLIVVPF NQGSKQDVDA 750
LVQYIYDEPK KGGLGWDLDA IIPFAAIPEN GNGLDNIDSK SEFAHRIMLT 800
NLLRLLGAVK SKKPTDTRPA QCILPLSPNH GTFGFDGLYS ESKISLETLF 850
NRWYSEDWGS KLTVCGAVIG WTRGTGLMSA NNIIAEGIEK LGVRTFSQKE 900
MAFNILGLLT PEIVQLCQEE PVMADLNGGL QFIDNLKDFT SKLRTDLLET 950
ADIRRAVSIE SAIEQKVVNG DNVDANYSKV MVEPRANMKF DFPTLKSYDE 1000
IKQIAPELEG MLDLENVVVV TGFAEVGPWG NSRTRWEMEA YGEFSLEGAI 1050
EMAWIMGFIK YHNGNLQGKP YSGWVDAKTQ TPIDEKDIKS KYEEEILEHS 1100
GIRLIEPELF NGYDPKKKQM IQEIVVQHDL EPFECSKETA EQYKHEHGEK 1150
CEIFEIEESG EYTVRILKGA TLYVPKALRF DRLVAGQIPT GWDARTYGIP 1200
EDTISQVDPI TLYVLVATVE ALLSAGITDP YEFYKYVHVS EVGNCSGSGM 1250
GGVSALRGMF KDRYADKPVQ NDILQESFIN TMSAWVNMLL LSSSGPIKTP 1300
VGACATAVES VDIGIETILS GKAKVVLVGG YDDFQEEGSY EFANMNATSN 1350
SIEEFKHGRT PKEMSRPTTT TRNGFMEAQG SGIQVIMTAD LALKMGVPIH 1400
AVLAMTATAT DKIGRSVPAP GKGILTTARE HHGNLKYPSP LLNIKYRKRQ 1450
LNKRLEQIKS WEETELSYLQ EEAELAKEEF GDEFSMHEFL KERTEEVYRE 1500
SKRQVSDAKK QWGNSFYKSD PRIAPLRGAL AAFNLTIDDI GVASFHGTST 1550
VANDKNESAT INNMMKHLGR SEGNPVFGVF QKYLTGHPKG AAGAWMLNGA 1600
IQILESGLVP GNRNADNVDK LLEQYEYVLY PSRSIQTDGI KAVSVTSFGF 1650
GQKGAQAVVV HPDYLFAVLD RSTYEEYATK VSARNKKTYR YMHNAITRNT 1700
MFVAKDKAPY SDELEQPVYL DPLARVEENK KKLVFSDKTI QSNQSYVGEV 1750
AQKTAKALST LNKSSKGVGV DVELLSAINI DNETFIERNF TGNEVEYCLN 1800
TAHPQASFTG TWSAKEAVFK ALGVESKGAG ASLIDIEITR DVNGAPKVIL 1850
HGEAKKAAAK AGVKNVNISI SHDDFQATAV ALSEF 1885
Length:1,885
Mass (Da):207,589
Last modified:November 1, 1995 - v1
Checksum:i4835D57F362372E0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L29063 Genomic DNA. Translation: AAA34345.1.
PIRiJC4086.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L29063 Genomic DNA. Translation: AAA34345.1 .
PIRi JC4086.

3D structure databases

ProteinModelPortali P43098.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG4982.

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

Entry informationi

Entry nameiFAS2_CANAX
AccessioniPrimary (citable) accession number: P43098
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 19, 2014
This is version 101 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

Similar proteinsi