Reviewed, UniProtKB/Swiss-Prot P34229 (FAS1_YARLI)

Names and origin

Protein names

Recommended name:
    Fatty acid synthase subunit beta
    EC=2.3.1.86
Including the following 5 domains:
    1- Recommended name:
            3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase
              EC=4.2.1.61
    2- Recommended name:
            Enoyl-[acyl-carrier-protein] reductase [NADH]
              EC=1.3.1.9
    3- Recommended name:
            [Acyl-carrier-protein] acetyltransferase
              EC=2.3.1.38
    4- Recommended name:
            [Acyl-carrier-protein] malonyltransferase
              EC=2.3.1.39
    5- Recommended name:
            S-acyl fatty acid synthase thioesterase
              EC=3.1.2.14

Gene names

Name:	FAS1
Ordered Locus Names:	YALI0B15059g

Organism

Yarrowia lipolytica (Candida lipolytica) [Complete proteome]

Taxonomic identifier

4952 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › Yarrowia

Protein attributes

Sequence length	2086 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	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 activity	Acetyl-CoA + n malonyl-CoA + 2n NADH + 2n NADPH = long-chain-acyl-CoA + n CoA + n CO2 + 2n NAD+ + 2n NADP+. Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein]. Malonyl-CoA + [acyl-carrier-protein] = CoA + malonyl-[acyl-carrier-protein]. (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] = hexadec-2-enoyl-[acyl-carrier-protein] + H2O. Acyl-[acyl-carrier-protein] + NAD+ = trans-2,3-dehydroacyl-[acyl-carrier-protein] + NADH. Oleoyl-[acyl-carrier-protein] + H2O = [acyl-carrier-protein] + oleate.
Subunit structure	[Alpha6beta6] hexamers of two multifunctional subunits (alpha and beta).
Sequence similarities	Belongs to the fungal fatty acid synthetase subunit beta family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis
Ligand	NAD NADP
Molecular function	Hydrolase Lyase Oxidoreductase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	fatty acid biosynthetic process Non-traceable author statement. Source: UniProtKB oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	fatty acid synthase complex Non-traceable author statement. Source: UniProtKB
Molecular function	3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity Inferred from electronic annotation. Source: EC [acyl-carrier-protein] S-acetyltransferase activity Inferred from electronic annotation. Source: EC [acyl-carrier-protein] S-malonyltransferase activity Inferred from electronic annotation. Source: EC enoyl-[acyl-carrier-protein] reductase (NADH) activity Inferred from electronic annotation. Source: EC fatty-acyl-CoA synthase activity Non-traceable author statement. Source: UniProtKB oleoyl-[acyl-carrier-protein] hydrolase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2086	2086	Fatty acid synthase subunit beta		PRO_0000180283
Regions
	Region	1 – 480	480	Acetyltransferase
	Region	492 – 879	388	Enoyl reductase
	Region	1166 – 1657	492	Dehydratase
	Region	1658 – 1879	222	Malonyl/palmitoyl transferase
Sites
	Active site	286	1	For acetyltransferase activity By similarity
	Active site	1842	1	For malonyltransferase activity By similarity
Experimental info
	Sequence conflict	1 – 11	11	MYPTTGVNTPQ → M Ref.1
	Sequence conflict	529 – 530	2	HK → TR in CAA42211. Ref.1
	Sequence conflict	1240	1	V → G in CAA42211. Ref.1
	Sequence conflict	1612	1	H → Q in CAA42211. Ref.1
	Sequence conflict	2077	1	N → D in CAA42211. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P34229-1 [UniParc]. Last modified October 11, 2004. Version 2. Checksum: 060F6CEA44F235B2	FASTA	2,086	231,342
	10 20 30 40 50 60 MYPTTGVNTP QSAASLRPLV LSHGQTEHSL LVPTSLYINC TTLRDQFYAS LPPATEDKAD 70 80 90 100 110 120 DDEPSSSTEL LAAFLGFTAK TVEEEPGPYD DVLSLVLNEF ETRYLRGNDI HAVASSLLQD 130 140 150 160 170 180 EDVPTTVGKI KRVIRAYYAA RIACNRPIKA HSSALFRAAS EDSDNVSLYA IFGGQGNTED 190 200 210 220 230 240 YFEELREIYD IYQGLVGDFI RECGAQLLAL SRDHIAAEKI YTKGFDIVKW LEHPETIPDF 250 260 270 280 290 300 EYLISAPISV PIIGVIQLAH YAVTCRVLGL NPGQVRDNLK GATGHSQGLI TAIAISASDS 310 320 330 340 350 360 WDEFYNSASR ILKIFFFIGV RVQQAYPSTF LPPSTLEDSV KQGEGKPTPM LSIRDLSLNQ 370 380 390 400 410 420 VQEFVDATNL HLPEDKQIVV SLINGPRNVV VTGPPQSLYG LCLVLRKQKA ETGLDQSRVP 430 440 450 460 470 480 HSQRKLKFTH RFLPITSPFH SYLLEKSTDL IINDLESSGV EFVSSELKVP VYDTFDGSVL 490 500 510 520 530 540 SQLPKGIVSR LVNLITHLPV KWEKATQFQA SHIVDFGPGG ASGLGLLTHK NKDGTGVRTI 550 560 570 580 590 600 LAGVIDQPLE FGFKQELFDR QESSIVFAQN WAKEFSPKLV KISSTNEVYV DTKFSRLTGR 610 620 630 640 650 660 APIMVAGMTP TTVNPKFVAA TMNSGYHIEL GGGGYFAPGM MTKALEHIEK NTPPGSGITI 670 680 690 700 710 720 NLIYVNPRLI QWGIPLIQEL RQKGFPIEGL TIGAGVPSLE VANEWIQDLG VKHIAFKPGS 730 740 750 760 770 780 IEAISSVIRI AKANPDFPII LQWTGGRGGG HHSFEDFHAP ILQMYSKIRR CSNIVLIAGS 790 800 810 820 830 840 GFGASTDSYP YLTGSWSRDF DYPPMPFDGI LVGSRVMVAK EAFTSLGAKQ LIVDSPGVED 850 860 870 880 890 900 SEWEKTYDKP TGGVITVLSE MGEPIHKLAT RGVLFWHEMD KTVFSLPKKK RLEVLKSKRA 910 920 930 940 950 960 YIIKRLNDDF QKTWFAKNAQ GQVCDLEDLT YAEVIQRLVD LMYVKKESRW IDVTLRNLAG 970 980 990 1000 1010 1020 TFIRRVEERF STETGASSVL QSFSELDSEP EKVVERVFEL FPASTTQIIN AQDKDHFLML 1030 1040 1050 1060 1070 1080 CLNPMQKPVP FIPVLDDNFE FFFKKDSLWQ CEDLAAVVDE DVGRICILQG PVAVKHSKIV 1090 1100 1110 1120 1130 1140 NEPVKEILDS MHEGHIKQLL EDGEYAGNMA NIPQVECFGG KPAQNFGDVA LDSVMVLDDL 1150 1160 1170 1180 1190 1200 NKTVFKIETG TSALPSAADW FSLLAGDKNS WRQVFLSTDT IVQTTKMISN PLHRLLEPIA 1210 1220 1230 1240 1250 1260 GLQVEIEHPD EPENTVISAF EPINGKVTKV LELRKGAGDV ISLQLIEARG VDRVPVALPL 1270 1280 1290 1300 1310 1320 EFKYQPQIGY APIVEVMTDR NTRIKEFYWK LWFGQDSKFE IDTDITEEII GDDVTISGKA 1330 1340 1350 1360 1370 1380 IADFVHAVGN KGEAFVGRST SAGTVFAPMD FAIVLGWKAI IKAIFPRAID ADILRLVHLS 1390 1400 1410 1420 1430 1440 NGFKMMPGAD PLQMGDVVSA TAKIDTVKNS ATGKTVAVRG LLTRDGKPVM EVVSEFFYRG 1450 1460 1470 1480 1490 1500 EFSDFQNTFE RREEVPMQLT LKDAKAVAIL CSKEWFEYNG DDTKDLEGKT IVFRNSSFIK 1510 1520 1530 1540 1550 1560 YKNETVFSSV HTTGKVLMEL PSKEVIEIAT VNYQAGESHG NPVIDYLERN GTTIEQPVEF 1570 1580 1590 1600 1610 1620 EKPIPLSKAD DLLSFKAPSS NEPYAGVSGD YNPIHVSRAF ASYASLPGTI THGMYSSAAV 1630 1640 1650 1660 1670 1680 RSLIEVWAAE NNVSRVRAFS CQFQGMVLPN DEIVTRLEHV GMINGRKIIK VTSTNRETEA 1690 1700 1710 1720 1730 1740 VVLSGEAEVE QPISTFVFTG QGSQEQGMGM DLYASSEVAK KVWDKADEHF LQNYGFSIIK 1750 1760 1770 1780 1790 1800 IVVENPKELD IHFGGPKGKK IRDNYISMMF ETIDEKTGNL ISEKIFKEID ETTDSFTFKS 1810 1820 1830 1840 1850 1860 PTGLLSATQF TQPALTLMEK ASFEDMKAKG LVPVDATFAG HSLGEYSALA SLGDVMPIES 1870 1880 1890 1900 1910 1920 LVDVVFYRGM TMQVAVPRDA QGRSNYGMCA VNPSRISTTF NDAALRFVVD HISEQTKWLL 1930 1940 1950 1960 1970 1980 EIVNYNVENS QYVTAGDLRA LDTLTNVLNV LKLEKINIDK LLESLPLEKV KEHLSEIVTE 1990 2000 2010 2020 2030 2040 VAKKSVAKPQ PIELERGFAV IPLKGISVPF HSSYLRNGVK PFQNFLVKKV PKNAVKPANL 2050 2060 2070 2080 IGKYIPNLTA KPFEITKEYF EEVYKLTGSE KVKSIINNWE SYESKQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2034224] [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: 15229592] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIB 122 / E 150.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X59690 Genomic DNA. Translation: CAA42211.1. CR382128 Genomic DNA. Translation: CAG83163.1.
PIR	S15999.
RefSeq	XP_500912.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2907339.
KEGG	yli:YALI0B15059g.
Phylogenomic databases
HOGENOM	P34229.
OMA	P34229. SATQFTQ.
Enzyme and pathway databases
BRENDA	1.3.1.9. 3602. 2.3.1.38. 3602. 2.3.1.39. 3602. 2.3.1.86. 3602. 3.1.2.14. 3602. 4.2.1.61. 3602.
Family and domain databases
InterPro	IPR001227. Ac_transferase_reg. IPR014043. Acyl_transferase. IPR013565. DUF1729. IPR003965. Fatty_acid_synthase. IPR016452. Fatty_acid_Synthase_bsu_fun. IPR002539. MaoC_deHydtase. [Graphical view]
Gene3D	G3DSA:3.40.366.10. Ac_transferase_reg. 2 hits.
Pfam	PF00698. Acyl_transf_1. 1 hit. PF08354. DUF1729. 1 hit. PF01575. MaoC_dehydratas. 1 hit. [Graphical view]
PIRSF	PIRSF005562. FAS_yeast_beta. 1 hit.
PRINTS	PR01483. FASYNTHASE.
ProtoNet	Search...

Entry information

Entry name

FAS1_YARLI

Accession

Primary (citable) accession number: P34229
Secondary accession number(s): Q6CEK0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	October 11, 2004
Last modified:	May 5, 2009
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)