SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P34731

- FAS1_CANAX

UniProt

P34731 - FAS1_CANAX

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Fatty acid synthase subunit beta

Gene
FAS1
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 beta subunit contains domains for: [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase.

Catalytic activityi

Acetyl-CoA + n malonyl-CoA + 2n NADPH = long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP+.
Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein].
Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier-protein].
A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H2O.
An acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH.
Oleoyl-[acyl-carrier-protein] + H2O = [acyl-carrier-protein] + oleate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei261 – 2611For acetyltransferase activity By similarity
Active sitei1796 – 17961For malonyltransferase activity By similarity

GO - Molecular functioni

  1. [acyl-carrier-protein] S-acetyltransferase activity Source: UniProtKB-EC
  2. [acyl-carrier-protein] S-malonyltransferase activity Source: UniProtKB-EC
  3. 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity Source: UniProtKB-EC
  4. enoyl-[acyl-carrier-protein] reductase (NADH) activity Source: UniProtKB-EC
  5. fatty-acyl-CoA synthase activity Source: UniProtKB-EC
  6. myristoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
  7. oleoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC
  8. palmitoyl-[acyl-carrier-protein] hydrolase activity Source: UniProtKB-EC

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase, Lyase, Oxidoreductase, Transferase

Keywords - Biological processi

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

Keywords - Ligandi

NAD, NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Fatty acid synthase subunit beta (EC:2.3.1.86)
Including the following 5 domains:
3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC:4.2.1.59)
Enoyl-[acyl-carrier-protein] reductase [NADH] (EC:1.3.1.9)
[Acyl-carrier-protein] acetyltransferase (EC:2.3.1.38)
[Acyl-carrier-protein] malonyltransferase (EC:2.3.1.39)
S-acyl fatty acid synthase thioesterase (EC:3.1.2.14)
Gene namesi
Name:FAS1
OrganismiCandida albicans (Yeast)
Taxonomic identifieri5476 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Subcellular locationi

GO - Cellular componenti

  1. fatty acid synthase complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20372037Fatty acid synthase subunit betaPRO_0000180280Add
BLAST

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliP34731.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1506 – 1634129MaoC-likeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 453453Acetyltransferase By similarityAdd
BLAST
Regioni465 – 798334Enoyl reductase By similarityAdd
BLAST
Regioni1132 – 1612481Dehydratase By similarityAdd
BLAST
Regioni1613 – 1833221Malonyl/palmitoyl transferase By similarityAdd
BLAST

Sequence similaritiesi

Contains 1 MaoC-like domain.

Phylogenomic databases

eggNOGiCOG0331.

Family and domain databases

Gene3Di3.10.129.10. 2 hits.
3.20.20.70. 1 hit.
3.40.366.10. 5 hits.
InterProiIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013785. Aldolase_TIM.
IPR013565. DUF1729.
IPR003965. Fatty_acid_synthase.
IPR016452. Fatty_acid_Synthase_bsu_fun.
IPR029069. HotDog_dom.
IPR002539. MaoC_dom.
[Graphical view]
PfamiPF00698. Acyl_transf_1. 1 hit.
PF08354. DUF1729. 1 hit.
PF01575. MaoC_dehydratas. 1 hit.
[Graphical view]
PIRSFiPIRSF005562. FAS_yeast_beta. 1 hit.
PRINTSiPR01483. FASYNTHASE.
SUPFAMiSSF52151. SSF52151. 5 hits.
SSF54637. SSF54637. 2 hits.

Sequencei

Sequence statusi: Complete.

P34731-1 [UniParc]FASTAAdd to Basket

« Hide

MSTHRPFQLT HGSIEHTLLV PNDLFFNYSQ LKDEFIKTLP EPTEGFAGDD     50
EPSSPAELYG KFIGFISNAQ FPQIVELSLK DFESRFLDNN NDNIHSFAVK 100
LLDDETYPTT IAKVKENIVK NYYKAVKSIN KVESNLLYHC KHDAKLVAIF 150
GGQGNTDDYF EELRELYTLY QGLIEDLLVS IAEKLNQLHP SFDKIYTQGL 200
NILSWLKHPE TTPDQDYLLS VPVSCPVICV IQLCHYTITC KVLGLTPGEF 250
RNSLKWSTGH SQGLVTAVTI AASDSWDSFL KNSLTAVSLL LFIGSRCLST 300
YPRTSLPPTM LQDSLDNGEG RPSPMLSVRD LSIKQVEKFI EQTNSHLPRE 350
KHIAISLING ARNLVLSGPP ESLYGFNLNL RNQKAPMGLD QSRVPFSERK 400
LKCSNRFLPI FAPFHSHLLA DATELILDDV KEHGLSFEGL KIPVYDTFDG 450
SDFQALKEPI IDRVVKLITE LPVHWEEATN HKATHILDFG PGGVSGLGVL 500
THRNKEGTGA RIILAGTLDS NPIDDEYGFK HEIFQTSADK AIKWAPDWLK 550
ELRPTLVKNS EGKIYVKTKF SQLLGRAPLM VAGMTPTTVN TDIVSASLNA 600
GYHIELAGGG YFSPVMMTRA IDDIVSRIKP GYGLGINLIY VNPFMLQWGI 650
PLIKDLREKG YPIQSLTIGA GVPSIEVATE YIEDLGLTHL GLKPGSVDAI 700
SQVIAIAKAH PTFPIVLQWT GGRGGGHHSF EDFHQPIIQM YSKIRRCSNI 750
VLVAGSGFGS DEDTYPYLSG YWSEKFNYPP MPFDGVLFGS RVMTSKESHT 800
SLAAKKLIVE CKGVPDQQWE QTYKKPTGGI ITVRSEMGEP IHKIATRGVM 850
FWKELDDTIF NLPKNKLLDA LNKKRDHIIK KLNNDFQKPW FGKNANGVCD 900
LQEMTYKEVA NRLVELMYVK KSHRWIDVSL RNMYGDFLRR VEERFTSSAG 950
TVSLLQNFNQ LNEPEQFTAD FFEKFPQAGK QLISEEDCDY FLMLAARPGQ 1000
KPVPFVPVLD ERFEFFFKKD SLWQSEDLES VVDEDVQRTC ILHGPVASQY 1050
TSKVDEPIGD ILNSIHEGHI ARLIKEEYAG DESKIPVVEY FGGKKPASVS 1100
ATSVNIIDGN QVVYEIDSEL PNKQEWLDLL AGTELNWLQA FISTDRIVQG 1150
SKHVSNPLHD ILTPAKHSKV TIDKKTKKLT AFENIKGDLL PVVEIELVKP 1200
NTIQLSLIEH RTADTNPVAL PFLYKYNPAD GFAPILEIME DRNERIKEFY 1250
WKLWFGSSVP YSNDINVEKA ILGDEITISS QTISEFTHAI GNKCDAFVDR 1300
PGKATLAPMD FAIVIGWKAI IKAIFPKSVD GDLLKLVHLS NGYKMITGAA 1350
PLKKGDVVST KAEIKAVLNQ PSGKLVEVVG TIYREGKPVM EVTSQFLYRG 1400
EYNDYCNTFQ KVTETPVQVA FKSAKDLAVL RSKEWFHLEK DVQFDVLTFR 1450
CESTYKFKSA NVYSSIKTTG QVLLELPTKE VIQVGSVDYE AGTSYGNPVT 1500
DYLSRNGKTI EESVIFENAI PLSSGEELTS KAPGTNEPYA IVSGDYNPIH 1550
VSRVFAAYAK LPGTITHGMY SSASIRALVE EWAANNVAAR VRAFKCDFVG 1600
MVLPNDTLQT TMEHVGMING RKIIKVETRN VETELPVLIG EAEIEQPTTT 1650
YVFTGQGSQE QGMGMELYNS SEVAREVWDK ADRHFVNNYG FSILDIVQNN 1700
PNELTIHFGG AKGRAIRDNY IGMMFETIGE DGALKSEKIF KDIDETTTSY 1750
TFVSPTGLLS ATQFTQPALT LMEKAAYEDI KSKGLIPSDI MFAGHSLGEY 1800
SALSSLANVM PIESLVDVVF YRGMTMQVAV PRDELGRSNY GMVAVNPSRV 1850
SATFDDSALR FVVDEVANKT KWLLEIVNYN VENQQYVAAG DLRALDTLTN 1900
VLNVLKINKI DIVKLQEQMS IEKVKEHLYE IVDEVAAKSL AKPQPIDLER 1950
GFAVIPLKGI SVPFHSSYLM SGVKPFQRFL CKKIPKSSVK PQDLIGKYIP 2000
NLTAKPFELT KEYFQSVYDL TKSEKIKSIL DNWEQYE 2037
Length:2,037
Mass (Da):227,919
Last modified:February 1, 1994 - v1
Checksum:iD37BDD0DB9A8ADDA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X74952 Genomic DNA. Translation: CAA52907.1.
PIRiS37178.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X74952 Genomic DNA. Translation: CAA52907.1 .
PIRi S37178.

3D structure databases

ProteinModelPortali P34731.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0331.

Family and domain databases

Gene3Di 3.10.129.10. 2 hits.
3.20.20.70. 1 hit.
3.40.366.10. 5 hits.
InterProi IPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013785. Aldolase_TIM.
IPR013565. DUF1729.
IPR003965. Fatty_acid_synthase.
IPR016452. Fatty_acid_Synthase_bsu_fun.
IPR029069. HotDog_dom.
IPR002539. MaoC_dom.
[Graphical view ]
Pfami PF00698. Acyl_transf_1. 1 hit.
PF08354. DUF1729. 1 hit.
PF01575. MaoC_dehydratas. 1 hit.
[Graphical view ]
PIRSFi PIRSF005562. FAS_yeast_beta. 1 hit.
PRINTSi PR01483. FASYNTHASE.
SUPFAMi SSF52151. SSF52151. 5 hits.
SSF54637. SSF54637. 2 hits.
ProtoNeti Search...

Publicationsi

  1. "Isolation and sequence of the Candida albicans FAS1 gene."
    Zhao X.-J., Cihlar R.L.
    Gene 147:119-124(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 4918.

Entry informationi

Entry nameiFAS1_CANAX
AccessioniPrimary (citable) accession number: P34731
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: September 3, 2014
This is version 88 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