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.

P34229

- FAS1_YARLI

UniProt

P34229 - FAS1_YARLI

(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, YALI0B15059g
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 activity By similarity
Active sitei1842 – 18421For 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
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.

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.

Phylogenomic databases

eggNOGiCOG0331.
HOGENOMiHOG000177963.
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

MYPTTGVNTP QSAASLRPLV LSHGQTEHSL LVPTSLYINC TTLRDQFYAS     50
LPPATEDKAD DDEPSSSTEL LAAFLGFTAK TVEEEPGPYD DVLSLVLNEF 100
ETRYLRGNDI HAVASSLLQD EDVPTTVGKI KRVIRAYYAA RIACNRPIKA 150
HSSALFRAAS EDSDNVSLYA IFGGQGNTED YFEELREIYD IYQGLVGDFI 200
RECGAQLLAL SRDHIAAEKI YTKGFDIVKW LEHPETIPDF EYLISAPISV 250
PIIGVIQLAH YAVTCRVLGL NPGQVRDNLK GATGHSQGLI TAIAISASDS 300
WDEFYNSASR ILKIFFFIGV RVQQAYPSTF LPPSTLEDSV KQGEGKPTPM 350
LSIRDLSLNQ VQEFVDATNL HLPEDKQIVV SLINGPRNVV VTGPPQSLYG 400
LCLVLRKQKA ETGLDQSRVP HSQRKLKFTH RFLPITSPFH SYLLEKSTDL 450
IINDLESSGV EFVSSELKVP VYDTFDGSVL SQLPKGIVSR LVNLITHLPV 500
KWEKATQFQA SHIVDFGPGG ASGLGLLTHK NKDGTGVRTI LAGVIDQPLE 550
FGFKQELFDR QESSIVFAQN WAKEFSPKLV KISSTNEVYV DTKFSRLTGR 600
APIMVAGMTP TTVNPKFVAA TMNSGYHIEL GGGGYFAPGM MTKALEHIEK 650
NTPPGSGITI NLIYVNPRLI QWGIPLIQEL RQKGFPIEGL TIGAGVPSLE 700
VANEWIQDLG VKHIAFKPGS IEAISSVIRI AKANPDFPII LQWTGGRGGG 750
HHSFEDFHAP ILQMYSKIRR CSNIVLIAGS GFGASTDSYP YLTGSWSRDF 800
DYPPMPFDGI LVGSRVMVAK EAFTSLGAKQ LIVDSPGVED SEWEKTYDKP 850
TGGVITVLSE MGEPIHKLAT RGVLFWHEMD KTVFSLPKKK RLEVLKSKRA 900
YIIKRLNDDF QKTWFAKNAQ GQVCDLEDLT YAEVIQRLVD LMYVKKESRW 950
IDVTLRNLAG TFIRRVEERF STETGASSVL QSFSELDSEP EKVVERVFEL 1000
FPASTTQIIN AQDKDHFLML CLNPMQKPVP FIPVLDDNFE FFFKKDSLWQ 1050
CEDLAAVVDE DVGRICILQG PVAVKHSKIV NEPVKEILDS MHEGHIKQLL 1100
EDGEYAGNMA NIPQVECFGG KPAQNFGDVA LDSVMVLDDL NKTVFKIETG 1150
TSALPSAADW FSLLAGDKNS WRQVFLSTDT IVQTTKMISN PLHRLLEPIA 1200
GLQVEIEHPD EPENTVISAF EPINGKVTKV LELRKGAGDV ISLQLIEARG 1250
VDRVPVALPL EFKYQPQIGY APIVEVMTDR NTRIKEFYWK LWFGQDSKFE 1300
IDTDITEEII GDDVTISGKA IADFVHAVGN KGEAFVGRST SAGTVFAPMD 1350
FAIVLGWKAI IKAIFPRAID ADILRLVHLS NGFKMMPGAD PLQMGDVVSA 1400
TAKIDTVKNS ATGKTVAVRG LLTRDGKPVM EVVSEFFYRG EFSDFQNTFE 1450
RREEVPMQLT LKDAKAVAIL CSKEWFEYNG DDTKDLEGKT IVFRNSSFIK 1500
YKNETVFSSV HTTGKVLMEL PSKEVIEIAT VNYQAGESHG NPVIDYLERN 1550
GTTIEQPVEF EKPIPLSKAD DLLSFKAPSS NEPYAGVSGD YNPIHVSRAF 1600
ASYASLPGTI THGMYSSAAV RSLIEVWAAE NNVSRVRAFS CQFQGMVLPN 1650
DEIVTRLEHV GMINGRKIIK VTSTNRETEA VVLSGEAEVE QPISTFVFTG 1700
QGSQEQGMGM DLYASSEVAK KVWDKADEHF LQNYGFSIIK IVVENPKELD 1750
IHFGGPKGKK IRDNYISMMF ETIDEKTGNL ISEKIFKEID ETTDSFTFKS 1800
PTGLLSATQF TQPALTLMEK ASFEDMKAKG LVPVDATFAG HSLGEYSALA 1850
SLGDVMPIES LVDVVFYRGM TMQVAVPRDA QGRSNYGMCA VNPSRISTTF 1900
NDAALRFVVD HISEQTKWLL EIVNYNVENS QYVTAGDLRA LDTLTNVLNV 1950
LKLEKINIDK LLESLPLEKV KEHLSEIVTE VAKKSVAKPQ PIELERGFAV 2000
IPLKGISVPF HSSYLRNGVK PFQNFLVKKV PKNAVKPANL IGKYIPNLTA 2050
KPFEITKEYF EEVYKLTGSE KVKSIINNWE SYESKQ 2086
Length:2,086
Mass (Da):231,342
Last modified:October 11, 2004 - v2
Checksum:i060F6CEA44F235B2
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 1111MYPTTGVNTPQ → M in CAA42211. 1 PublicationAdd
BLAST
Sequence conflicti529 – 5302HK → TR in CAA42211. 1 Publication
Sequence conflicti1240 – 12401V → G in CAA42211. 1 Publication
Sequence conflicti1612 – 16121H → Q in CAA42211. 1 Publication
Sequence conflicti2077 – 20771N → D in CAA42211. 1 Publication

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.
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: September 3, 2014
This is version 104 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

Similar proteinsi