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Q9UUG0

- FAS1_SCHPO

UniProt

Q9UUG0 - FAS1_SCHPO

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Protein

Fatty acid synthase subunit beta

Gene

fas1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 sitei270 – 2701For acetyltransferase activityBy similarity
Active sitei1361 – 13611For dehydratase activitySequence Analysis
Active sitei1828 – 18281For malonyltransferase activityBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. fatty acid biosynthetic process Source: PomBase
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
ORF Names:SPAC926.09c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome I

Organism-specific databases

PomBaseiSPAC926.09c.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: PomBase
  2. fatty acid synthase complex Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20732073Fatty acid synthase subunit betaPRO_0000180281Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1122 – 11221Phosphoserine1 Publication
Modified residuei2073 – 20731Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UUG0.
PaxDbiQ9UUG0.

Interactioni

Subunit structurei

[Alpha6beta6] hexamers of two multifunctional subunits (alpha and beta).1 Publication

Protein-protein interaction databases

BioGridi279916. 17 interactions.
MINTiMINT-4713190.
STRINGi4896.SPAC926.09c-1.

Structurei

3D structure databases

ProteinModelPortaliQ9UUG0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1558 – 1667110MaoC-likeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 459459AcetyltransferaseAdd
BLAST
Regioni470 – 858389Enoyl reductaseAdd
BLAST
Regioni1155 – 1644490DehydrataseAdd
BLAST
Regioni1645 – 2073429Malonyl/palmitoyl transferaseAdd
BLAST

Sequence similaritiesi

Contains 1 MaoC-like domain.Curated

Phylogenomic databases

eggNOGiCOG0331.
HOGENOMiHOG000177963.
InParanoidiQ9UUG0.
KOiK00668.
OMAiKLQHVGM.
OrthoDBiEOG76QFRJ.
PhylomeDBiQ9UUG0.

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.

Q9UUG0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVEAEQVHQS LRSLVLSYAH FSPSILIPAS QYLLAAQLRD EFLSLHPAPS
60 70 80 90 100
AESVEKEGAE LEFEHELHLL AGFLGLIAAK EEETPGQYTQ LLRIITLEFE
110 120 130 140 150
RTFLAGNEVH AVVHSLGLNI PAQKDVVRFY YHSCALIGQT TKFHGSALLD
160 170 180 190 200
ESSVKLAAIF GGQGYEDYFD ELIELYEVYA PFAAELIQVL SKHLFTLSQN
210 220 230 240 250
EQASKVYSKG LNVLDWLAGE RPERDYLVSA PVSLPLVGLT QLVHFSVTAQ
260 270 280 290 300
ILGLNPGELA SRFSAASGHS QGIVVAAAVS ASTDSASFME NAKVALTTLF
310 320 330 340 350
WIGVRSQQTF PTTTLPPSVV ADSLASSEGN PTPMLAVRDL PIETLNKHIE
360 370 380 390 400
TTNTHLPEDR KVSLSLVNGP RSFVVSGPAR SLYGLNLSLR KEKADGQNQS
410 420 430 440 450
RIPHSKRKLR FINRFLSISV PFHSPYLAPV RSLLEKDLQG LQFSALKVPV
460 470 480 490 500
YSTDDAGDLR FEQPSKLLLA LAVMITEKVV HWEEACGFPD VTHIIDFGPG
510 520 530 540 550
GISGVGSLTR ANKDGQGVRV IVADSFESLD MGAKFEIFDR DAKSIEFAPN
560 570 580 590 600
WVKLYSPKLV KNKLGRVYVD TRLSRMLGLP PLWVAGMTPT SVPWQFCSAI
610 620 630 640 650
AKAGFTYELA GGGYFDPKMM REAIHKLSLN IPPGAGICVN VIYINPRTYA
660 670 680 690 700
WQIPLIRDMV AEGYPIRGVT IAAGIPSLEV ANELISTLGV QYLCLKPGSV
710 720 730 740 750
EAVNAVISIA KANPTFPIVL QWTGGRAGGH HSFEDFHSPI LLTYSAIRRC
760 770 780 790 800
DNIVLIAGSG FGGADDTEPY LTGEWSAAFK LPPMPFDGIL FGSRLMVAKE
810 820 830 840 850
AHTSLAAKEA IVAAKGVDDS EWEKTYDGPT GGIVTVLSEL GEPIHKLATR
860 870 880 890 900
GIMFWKELDD TIFSLPRPKR LPALLAKKQY IIKRLNDDFQ KVYFPAHIVE
910 920 930 940 950
QVSPEKFKFE AVDSVEDMTY AELLYRAIDL MYVTKEKRWI DVTLRTFTGK
960 970 980 990 1000
LMRRIEERFT QDVGKTTLIE NFEDLNDPYP VAARFLDAYP EASTQDLNTQ
1010 1020 1030 1040 1050
DAQFFYSLCS NPFQKPVPFI PAIDDTFEFY FKKDSLWQSE DLAAVVGEDV
1060 1070 1080 1090 1100
GRVAILQGPM AAKHSTKVNE PAKELLDGIN ETHIQHFIKK FYAGDEKKIP
1110 1120 1130 1140 1150
IVEYFGGVPP VNVSHKSLES VSVTEEAGSK VYKLPEIGSN SALPSKKLWF
1160 1170 1180 1190 1200
ELLAGPEYTW FRAIFTTQRV AKGWKLEHNP VRRIFAPRYG QRAVVKGKDN
1210 1220 1230 1240 1250
DTVVELYETQ SGNYVLAARL SYDGETIVVS MFENRNALKK EVHLDFLFKY
1260 1270 1280 1290 1300
EPSAGYSPVS EILDGRNDRI KHFYWALWFG EEPYPENASI TDTFTGPEVT
1310 1320 1330 1340 1350
VTGNMIEDFC RTVGNHNEAY TKRAIRKRMA PMDFAIVVGW QAITKAIFPK
1360 1370 1380 1390 1400
AIDGDLLRLV HLSNSFRMVG SHSLMEGDKV TTSASIIAIL NNDSGKTVTV
1410 1420 1430 1440 1450
KGTVYRDGKE VIEVISRFLY RGTFTDFENT FEHTQETPMQ LTLATPKDVA
1460 1470 1480 1490 1500
VLQSKSWFQL LDPSQDLSGS ILTFRLNSYV RFKDQKVKSS VETKGIVLSE
1510 1520 1530 1540 1550
LPSKAIIQVA SVDFQSVDCH GNPVIEFLKR NGKPIEQPVE FENGGYSVIQ
1560 1570 1580 1590 1600
VMDEGYSPVF VTPPTNSPYA EVSGDYNPIH VSPTFAAFVE LPGTHGITHG
1610 1620 1630 1640 1650
MYTSAAARRF VETYAAQNVP ERVKHYEVTF VNMVLPNTEL ITKLSHTGMI
1660 1670 1680 1690 1700
NGRKIIKVEV LNQETSEPVL VGTAEVEQPV SAYVFTGQGS QEQGMGMDLY
1710 1720 1730 1740 1750
ASSPVARKIW DSADKHFLTN YGFSIIDIVK HNPHSITIHF GGSKGKKIRD
1760 1770 1780 1790 1800
NYMAMAYEKL MEDGTSKVVP VFETITKDST SFSFTHPSGL LSATQFTQPA
1810 1820 1830 1840 1850
LTLMEKSAFE DMRSKGLVQN DCAFAGHSLG EYSALSAMGD VLSIEALVDL
1860 1870 1880 1890 1900
VFLRGLTMQN AVHRDELGRS DYGMVAANPS RVSASFTDAA LRFIVDHIGQ
1910 1920 1930 1940 1950
QTNLLLEIVN YNVENQQYVV SGNLLSLSTL GHVLNFLKVQ KIDFEKLKET
1960 1970 1980 1990 2000
LTIEQLKEQL TDIVEACHAK TLEQQKKTGR IELERGYATI PLKIDVPFHS
2010 2020 2030 2040 2050
SFLRGGVRMF REYLVKKIFP HQINVAKLRG KYIPNLTAKP FEISKEYFQN
2060 2070
VYDLTGSQRI KKILQNWDEY ESS
Length:2,073
Mass (Da):230,561
Last modified:May 1, 2000 - v1
Checksum:iD928270838E7C7C4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti222 – 2221P → R in BAA36384. (PubMed:9693066)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB010274 Genomic DNA. Translation: BAA36384.1.
CU329670 Genomic DNA. Translation: CAB54157.1.
D89148 mRNA. Translation: BAA13810.1.
PIRiT39207.
T42424.
T43311.
RefSeqiNP_594370.1. NM_001019791.2.

Genome annotation databases

EnsemblFungiiSPAC926.09c.1; SPAC926.09c.1:pep; SPAC926.09c.
GeneIDi2543497.
KEGGispo:SPAC926.09c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB010274 Genomic DNA. Translation: BAA36384.1 .
CU329670 Genomic DNA. Translation: CAB54157.1 .
D89148 mRNA. Translation: BAA13810.1 .
PIRi T39207.
T42424.
T43311.
RefSeqi NP_594370.1. NM_001019791.2.

3D structure databases

ProteinModelPortali Q9UUG0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 279916. 17 interactions.
MINTi MINT-4713190.
STRINGi 4896.SPAC926.09c-1.

Proteomic databases

MaxQBi Q9UUG0.
PaxDbi Q9UUG0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPAC926.09c.1 ; SPAC926.09c.1:pep ; SPAC926.09c .
GeneIDi 2543497.
KEGGi spo:SPAC926.09c.

Organism-specific databases

PomBasei SPAC926.09c.

Phylogenomic databases

eggNOGi COG0331.
HOGENOMi HOG000177963.
InParanoidi Q9UUG0.
KOi K00668.
OMAi KLQHVGM.
OrthoDBi EOG76QFRJ.
PhylomeDBi Q9UUG0.

Miscellaneous databases

NextBioi 20804508.

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. "Cloning of the fatty acid synthetase beta subunit from fission yeast, coexpression with the alpha subunit, and purification of the intact multifunctional enzyme complex."
    Niwa H., Katayama E., Yanagida M., Morikawa K.
    Protein Expr. Purif. 13:403-413(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
    Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
    DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1725-2073.
    Strain: PR745.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1122 AND SER-2073, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiFAS1_SCHPO
AccessioniPrimary (citable) accession number: Q9UUG0
Secondary accession number(s): P78799
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 113 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

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3