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P34229

- FAS1_YARLI

UniProt

P34229 - FAS1_YARLI

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Protein

Fatty acid synthase subunit beta

Gene

FAS1

Organism
Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
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 sitei286 – 2861For acetyltransferase activityBy similarity
Active sitei1842 – 18421For 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
Ordered Locus Names:YALI0B15059g
OrganismiYarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Taxonomic identifieri284591 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeYarrowia
ProteomesiUP000001300: Chromosome B

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 – 20862086Fatty acid synthase subunit betaPRO_0000180283Add
BLAST

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi4952.P34229.

Structurei

3D structure databases

ProteinModelPortaliP34229.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1550 – 1680131MaoC-likeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 480480AcetyltransferaseAdd
BLAST
Regioni492 – 879388Enoyl reductaseAdd
BLAST
Regioni1166 – 1657492DehydrataseAdd
BLAST
Regioni1658 – 1879222Malonyl/palmitoyl transferaseAdd
BLAST

Sequence similaritiesi

Contains 1 MaoC-like domain.Curated

Phylogenomic databases

eggNOGiCOG0331.
HOGENOMiHOG000177963.
InParanoidiP34229.
KOiK00668.
OMAiKLQHVGM.
OrthoDBiEOG76QFRJ.

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.

P34229-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MYPTTGVNTP QSAASLRPLV LSHGQTEHSL LVPTSLYINC TTLRDQFYAS
60 70 80 90 100
LPPATEDKAD DDEPSSSTEL LAAFLGFTAK TVEEEPGPYD DVLSLVLNEF
110 120 130 140 150
ETRYLRGNDI HAVASSLLQD EDVPTTVGKI KRVIRAYYAA RIACNRPIKA
160 170 180 190 200
HSSALFRAAS EDSDNVSLYA IFGGQGNTED YFEELREIYD IYQGLVGDFI
210 220 230 240 250
RECGAQLLAL SRDHIAAEKI YTKGFDIVKW LEHPETIPDF EYLISAPISV
260 270 280 290 300
PIIGVIQLAH YAVTCRVLGL NPGQVRDNLK GATGHSQGLI TAIAISASDS
310 320 330 340 350
WDEFYNSASR ILKIFFFIGV RVQQAYPSTF LPPSTLEDSV KQGEGKPTPM
360 370 380 390 400
LSIRDLSLNQ VQEFVDATNL HLPEDKQIVV SLINGPRNVV VTGPPQSLYG
410 420 430 440 450
LCLVLRKQKA ETGLDQSRVP HSQRKLKFTH RFLPITSPFH SYLLEKSTDL
460 470 480 490 500
IINDLESSGV EFVSSELKVP VYDTFDGSVL SQLPKGIVSR LVNLITHLPV
510 520 530 540 550
KWEKATQFQA SHIVDFGPGG ASGLGLLTHK NKDGTGVRTI LAGVIDQPLE
560 570 580 590 600
FGFKQELFDR QESSIVFAQN WAKEFSPKLV KISSTNEVYV DTKFSRLTGR
610 620 630 640 650
APIMVAGMTP TTVNPKFVAA TMNSGYHIEL GGGGYFAPGM MTKALEHIEK
660 670 680 690 700
NTPPGSGITI NLIYVNPRLI QWGIPLIQEL RQKGFPIEGL TIGAGVPSLE
710 720 730 740 750
VANEWIQDLG VKHIAFKPGS IEAISSVIRI AKANPDFPII LQWTGGRGGG
760 770 780 790 800
HHSFEDFHAP ILQMYSKIRR CSNIVLIAGS GFGASTDSYP YLTGSWSRDF
810 820 830 840 850
DYPPMPFDGI LVGSRVMVAK EAFTSLGAKQ LIVDSPGVED SEWEKTYDKP
860 870 880 890 900
TGGVITVLSE MGEPIHKLAT RGVLFWHEMD KTVFSLPKKK RLEVLKSKRA
910 920 930 940 950
YIIKRLNDDF QKTWFAKNAQ GQVCDLEDLT YAEVIQRLVD LMYVKKESRW
960 970 980 990 1000
IDVTLRNLAG TFIRRVEERF STETGASSVL QSFSELDSEP EKVVERVFEL
1010 1020 1030 1040 1050
FPASTTQIIN AQDKDHFLML CLNPMQKPVP FIPVLDDNFE FFFKKDSLWQ
1060 1070 1080 1090 1100
CEDLAAVVDE DVGRICILQG PVAVKHSKIV NEPVKEILDS MHEGHIKQLL
1110 1120 1130 1140 1150
EDGEYAGNMA NIPQVECFGG KPAQNFGDVA LDSVMVLDDL NKTVFKIETG
1160 1170 1180 1190 1200
TSALPSAADW FSLLAGDKNS WRQVFLSTDT IVQTTKMISN PLHRLLEPIA
1210 1220 1230 1240 1250
GLQVEIEHPD EPENTVISAF EPINGKVTKV LELRKGAGDV ISLQLIEARG
1260 1270 1280 1290 1300
VDRVPVALPL EFKYQPQIGY APIVEVMTDR NTRIKEFYWK LWFGQDSKFE
1310 1320 1330 1340 1350
IDTDITEEII GDDVTISGKA IADFVHAVGN KGEAFVGRST SAGTVFAPMD
1360 1370 1380 1390 1400
FAIVLGWKAI IKAIFPRAID ADILRLVHLS NGFKMMPGAD PLQMGDVVSA
1410 1420 1430 1440 1450
TAKIDTVKNS ATGKTVAVRG LLTRDGKPVM EVVSEFFYRG EFSDFQNTFE
1460 1470 1480 1490 1500
RREEVPMQLT LKDAKAVAIL CSKEWFEYNG DDTKDLEGKT IVFRNSSFIK
1510 1520 1530 1540 1550
YKNETVFSSV HTTGKVLMEL PSKEVIEIAT VNYQAGESHG NPVIDYLERN
1560 1570 1580 1590 1600
GTTIEQPVEF EKPIPLSKAD DLLSFKAPSS NEPYAGVSGD YNPIHVSRAF
1610 1620 1630 1640 1650
ASYASLPGTI THGMYSSAAV RSLIEVWAAE NNVSRVRAFS CQFQGMVLPN
1660 1670 1680 1690 1700
DEIVTRLEHV GMINGRKIIK VTSTNRETEA VVLSGEAEVE QPISTFVFTG
1710 1720 1730 1740 1750
QGSQEQGMGM DLYASSEVAK KVWDKADEHF LQNYGFSIIK IVVENPKELD
1760 1770 1780 1790 1800
IHFGGPKGKK IRDNYISMMF ETIDEKTGNL ISEKIFKEID ETTDSFTFKS
1810 1820 1830 1840 1850
PTGLLSATQF TQPALTLMEK ASFEDMKAKG LVPVDATFAG HSLGEYSALA
1860 1870 1880 1890 1900
SLGDVMPIES LVDVVFYRGM TMQVAVPRDA QGRSNYGMCA VNPSRISTTF
1910 1920 1930 1940 1950
NDAALRFVVD HISEQTKWLL EIVNYNVENS QYVTAGDLRA LDTLTNVLNV
1960 1970 1980 1990 2000
LKLEKINIDK LLESLPLEKV KEHLSEIVTE VAKKSVAKPQ PIELERGFAV
2010 2020 2030 2040 2050
IPLKGISVPF HSSYLRNGVK PFQNFLVKKV PKNAVKPANL IGKYIPNLTA
2060 2070 2080
KPFEITKEYF EEVYKLTGSE KVKSIINNWE SYESKQ
Length:2,086
Mass (Da):231,342
Last modified:October 11, 2004 - v2
Checksum:i060F6CEA44F235B2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 1111MYPTTGVNTPQ → M in CAA42211. (PubMed:2034224)CuratedAdd
BLAST
Sequence conflicti529 – 5302HK → TR in CAA42211. (PubMed:2034224)Curated
Sequence conflicti1240 – 12401V → G in CAA42211. (PubMed:2034224)Curated
Sequence conflicti1612 – 16121H → Q in CAA42211. (PubMed:2034224)Curated
Sequence conflicti2077 – 20771N → D in CAA42211. (PubMed:2034224)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X59690 Genomic DNA. Translation: CAA42211.1.
CR382128 Genomic DNA. Translation: CAG83163.1.
PIRiS15999.
RefSeqiXP_500912.1. XM_500912.1.

Genome annotation databases

EnsemblFungiiCAG83163; CAG83163; YALI0_B15059g.
GeneIDi2907339.
KEGGiyli:YALI0B15059g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X59690 Genomic DNA. Translation: CAA42211.1 .
CR382128 Genomic DNA. Translation: CAG83163.1 .
PIRi S15999.
RefSeqi XP_500912.1. XM_500912.1.

3D structure databases

ProteinModelPortali P34229.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 4952.P34229.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CAG83163 ; CAG83163 ; YALI0_B15059g .
GeneIDi 2907339.
KEGGi yli:YALI0B15059g.

Phylogenomic databases

eggNOGi COG0331.
HOGENOMi HOG000177963.
InParanoidi P34229.
KOi K00668.
OMAi KLQHVGM.
OrthoDBi EOG76QFRJ.

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

« Hide 'large scale' publications
  1. "The pentafunctional FAS1 genes of Saccharomyces cerevisiae and Yarrowia lipolytica are co-linear and considerably longer than previously estimated."
    Koettig H., Rottner G., Beck K.-F., Schweizer M., Schweizer E.
    Mol. Gen. Genet. 226:310-314(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 32338 / CX-161-1B.
  2. "Genome evolution in yeasts."
    Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.
    , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
    Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CLIB 122 / E 150.

Entry informationi

Entry nameiFAS1_YARLI
AccessioniPrimary (citable) accession number: P34229
Secondary accession number(s): Q6CEK0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: October 11, 2004
Last modified: October 29, 2014
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3