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P34731

- FAS1_CANAX

UniProt

P34731 - FAS1_CANAX

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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 activityBy similarity
Active sitei1796 – 17961For malonyltransferase activityBy 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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida

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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 453453AcetyltransferaseBy similarityAdd
BLAST
Regioni465 – 798334Enoyl reductaseBy similarityAdd
BLAST
Regioni1132 – 1612481DehydrataseBy similarityAdd
BLAST
Regioni1613 – 1833221Malonyl/palmitoyl transferaseBy similarityAdd
BLAST

Sequence similaritiesi

Contains 1 MaoC-like domain.Curated

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

        10         20         30         40         50
MSTHRPFQLT HGSIEHTLLV PNDLFFNYSQ LKDEFIKTLP EPTEGFAGDD
60 70 80 90 100
EPSSPAELYG KFIGFISNAQ FPQIVELSLK DFESRFLDNN NDNIHSFAVK
110 120 130 140 150
LLDDETYPTT IAKVKENIVK NYYKAVKSIN KVESNLLYHC KHDAKLVAIF
160 170 180 190 200
GGQGNTDDYF EELRELYTLY QGLIEDLLVS IAEKLNQLHP SFDKIYTQGL
210 220 230 240 250
NILSWLKHPE TTPDQDYLLS VPVSCPVICV IQLCHYTITC KVLGLTPGEF
260 270 280 290 300
RNSLKWSTGH SQGLVTAVTI AASDSWDSFL KNSLTAVSLL LFIGSRCLST
310 320 330 340 350
YPRTSLPPTM LQDSLDNGEG RPSPMLSVRD LSIKQVEKFI EQTNSHLPRE
360 370 380 390 400
KHIAISLING ARNLVLSGPP ESLYGFNLNL RNQKAPMGLD QSRVPFSERK
410 420 430 440 450
LKCSNRFLPI FAPFHSHLLA DATELILDDV KEHGLSFEGL KIPVYDTFDG
460 470 480 490 500
SDFQALKEPI IDRVVKLITE LPVHWEEATN HKATHILDFG PGGVSGLGVL
510 520 530 540 550
THRNKEGTGA RIILAGTLDS NPIDDEYGFK HEIFQTSADK AIKWAPDWLK
560 570 580 590 600
ELRPTLVKNS EGKIYVKTKF SQLLGRAPLM VAGMTPTTVN TDIVSASLNA
610 620 630 640 650
GYHIELAGGG YFSPVMMTRA IDDIVSRIKP GYGLGINLIY VNPFMLQWGI
660 670 680 690 700
PLIKDLREKG YPIQSLTIGA GVPSIEVATE YIEDLGLTHL GLKPGSVDAI
710 720 730 740 750
SQVIAIAKAH PTFPIVLQWT GGRGGGHHSF EDFHQPIIQM YSKIRRCSNI
760 770 780 790 800
VLVAGSGFGS DEDTYPYLSG YWSEKFNYPP MPFDGVLFGS RVMTSKESHT
810 820 830 840 850
SLAAKKLIVE CKGVPDQQWE QTYKKPTGGI ITVRSEMGEP IHKIATRGVM
860 870 880 890 900
FWKELDDTIF NLPKNKLLDA LNKKRDHIIK KLNNDFQKPW FGKNANGVCD
910 920 930 940 950
LQEMTYKEVA NRLVELMYVK KSHRWIDVSL RNMYGDFLRR VEERFTSSAG
960 970 980 990 1000
TVSLLQNFNQ LNEPEQFTAD FFEKFPQAGK QLISEEDCDY FLMLAARPGQ
1010 1020 1030 1040 1050
KPVPFVPVLD ERFEFFFKKD SLWQSEDLES VVDEDVQRTC ILHGPVASQY
1060 1070 1080 1090 1100
TSKVDEPIGD ILNSIHEGHI ARLIKEEYAG DESKIPVVEY FGGKKPASVS
1110 1120 1130 1140 1150
ATSVNIIDGN QVVYEIDSEL PNKQEWLDLL AGTELNWLQA FISTDRIVQG
1160 1170 1180 1190 1200
SKHVSNPLHD ILTPAKHSKV TIDKKTKKLT AFENIKGDLL PVVEIELVKP
1210 1220 1230 1240 1250
NTIQLSLIEH RTADTNPVAL PFLYKYNPAD GFAPILEIME DRNERIKEFY
1260 1270 1280 1290 1300
WKLWFGSSVP YSNDINVEKA ILGDEITISS QTISEFTHAI GNKCDAFVDR
1310 1320 1330 1340 1350
PGKATLAPMD FAIVIGWKAI IKAIFPKSVD GDLLKLVHLS NGYKMITGAA
1360 1370 1380 1390 1400
PLKKGDVVST KAEIKAVLNQ PSGKLVEVVG TIYREGKPVM EVTSQFLYRG
1410 1420 1430 1440 1450
EYNDYCNTFQ KVTETPVQVA FKSAKDLAVL RSKEWFHLEK DVQFDVLTFR
1460 1470 1480 1490 1500
CESTYKFKSA NVYSSIKTTG QVLLELPTKE VIQVGSVDYE AGTSYGNPVT
1510 1520 1530 1540 1550
DYLSRNGKTI EESVIFENAI PLSSGEELTS KAPGTNEPYA IVSGDYNPIH
1560 1570 1580 1590 1600
VSRVFAAYAK LPGTITHGMY SSASIRALVE EWAANNVAAR VRAFKCDFVG
1610 1620 1630 1640 1650
MVLPNDTLQT TMEHVGMING RKIIKVETRN VETELPVLIG EAEIEQPTTT
1660 1670 1680 1690 1700
YVFTGQGSQE QGMGMELYNS SEVAREVWDK ADRHFVNNYG FSILDIVQNN
1710 1720 1730 1740 1750
PNELTIHFGG AKGRAIRDNY IGMMFETIGE DGALKSEKIF KDIDETTTSY
1760 1770 1780 1790 1800
TFVSPTGLLS ATQFTQPALT LMEKAAYEDI KSKGLIPSDI MFAGHSLGEY
1810 1820 1830 1840 1850
SALSSLANVM PIESLVDVVF YRGMTMQVAV PRDELGRSNY GMVAVNPSRV
1860 1870 1880 1890 1900
SATFDDSALR FVVDEVANKT KWLLEIVNYN VENQQYVAAG DLRALDTLTN
1910 1920 1930 1940 1950
VLNVLKINKI DIVKLQEQMS IEKVKEHLYE IVDEVAAKSL AKPQPIDLER
1960 1970 1980 1990 2000
GFAVIPLKGI SVPFHSSYLM SGVKPFQRFL CKKIPKSSVK PQDLIGKYIP
2010 2020 2030
NLTAKPFELT KEYFQSVYDL TKSEKIKSIL DNWEQYE
Length:2,037
Mass (Da):227,919
Last modified:February 1, 1994 - v1
Checksum:iD37BDD0DB9A8ADDA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74952 Genomic DNA. Translation: CAA52907.1.
PIRiS37178.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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: October 29, 2014
This is version 90 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