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Q9UUG0

- FAS1_SCHPO

UniProt

Q9UUG0 - FAS1_SCHPO

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Protein
Fatty acid synthase subunit beta
Gene
fas1, SPAC926.09c
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 activity By similarity
Active sitei1361 – 13611For dehydratase activity Reviewed prediction
Active sitei1828 – 18281For malonyltransferase activity By similarity

GO - Molecular functioni

  1. 3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity Source: UniProtKB-EC
  2. 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity Source: PomBase
  3. [acyl-carrier-protein] S-acetyltransferase activity Source: PomBase
  4. [acyl-carrier-protein] S-malonyltransferase 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
Complete GO annotation...

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 beta
PRO_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.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 459459Acetyltransferase
Add
BLAST
Regioni470 – 858389Enoyl reductase
Add
BLAST
Regioni1155 – 1644490Dehydratase
Add
BLAST
Regioni1645 – 2073429Malonyl/palmitoyl transferase
Add
BLAST

Sequence similaritiesi

Contains 1 MaoC-like domain.

Phylogenomic databases

eggNOGiCOG0331.
HOGENOMiHOG000177963.
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

MVEAEQVHQS LRSLVLSYAH FSPSILIPAS QYLLAAQLRD EFLSLHPAPS     50
AESVEKEGAE LEFEHELHLL AGFLGLIAAK EEETPGQYTQ LLRIITLEFE 100
RTFLAGNEVH AVVHSLGLNI PAQKDVVRFY YHSCALIGQT TKFHGSALLD 150
ESSVKLAAIF GGQGYEDYFD ELIELYEVYA PFAAELIQVL SKHLFTLSQN 200
EQASKVYSKG LNVLDWLAGE RPERDYLVSA PVSLPLVGLT QLVHFSVTAQ 250
ILGLNPGELA SRFSAASGHS QGIVVAAAVS ASTDSASFME NAKVALTTLF 300
WIGVRSQQTF PTTTLPPSVV ADSLASSEGN PTPMLAVRDL PIETLNKHIE 350
TTNTHLPEDR KVSLSLVNGP RSFVVSGPAR SLYGLNLSLR KEKADGQNQS 400
RIPHSKRKLR FINRFLSISV PFHSPYLAPV RSLLEKDLQG LQFSALKVPV 450
YSTDDAGDLR FEQPSKLLLA LAVMITEKVV HWEEACGFPD VTHIIDFGPG 500
GISGVGSLTR ANKDGQGVRV IVADSFESLD MGAKFEIFDR DAKSIEFAPN 550
WVKLYSPKLV KNKLGRVYVD TRLSRMLGLP PLWVAGMTPT SVPWQFCSAI 600
AKAGFTYELA GGGYFDPKMM REAIHKLSLN IPPGAGICVN VIYINPRTYA 650
WQIPLIRDMV AEGYPIRGVT IAAGIPSLEV ANELISTLGV QYLCLKPGSV 700
EAVNAVISIA KANPTFPIVL QWTGGRAGGH HSFEDFHSPI LLTYSAIRRC 750
DNIVLIAGSG FGGADDTEPY LTGEWSAAFK LPPMPFDGIL FGSRLMVAKE 800
AHTSLAAKEA IVAAKGVDDS EWEKTYDGPT GGIVTVLSEL GEPIHKLATR 850
GIMFWKELDD TIFSLPRPKR LPALLAKKQY IIKRLNDDFQ KVYFPAHIVE 900
QVSPEKFKFE AVDSVEDMTY AELLYRAIDL MYVTKEKRWI DVTLRTFTGK 950
LMRRIEERFT QDVGKTTLIE NFEDLNDPYP VAARFLDAYP EASTQDLNTQ 1000
DAQFFYSLCS NPFQKPVPFI PAIDDTFEFY FKKDSLWQSE DLAAVVGEDV 1050
GRVAILQGPM AAKHSTKVNE PAKELLDGIN ETHIQHFIKK FYAGDEKKIP 1100
IVEYFGGVPP VNVSHKSLES VSVTEEAGSK VYKLPEIGSN SALPSKKLWF 1150
ELLAGPEYTW FRAIFTTQRV AKGWKLEHNP VRRIFAPRYG QRAVVKGKDN 1200
DTVVELYETQ SGNYVLAARL SYDGETIVVS MFENRNALKK EVHLDFLFKY 1250
EPSAGYSPVS EILDGRNDRI KHFYWALWFG EEPYPENASI TDTFTGPEVT 1300
VTGNMIEDFC RTVGNHNEAY TKRAIRKRMA PMDFAIVVGW QAITKAIFPK 1350
AIDGDLLRLV HLSNSFRMVG SHSLMEGDKV TTSASIIAIL NNDSGKTVTV 1400
KGTVYRDGKE VIEVISRFLY RGTFTDFENT FEHTQETPMQ LTLATPKDVA 1450
VLQSKSWFQL LDPSQDLSGS ILTFRLNSYV RFKDQKVKSS VETKGIVLSE 1500
LPSKAIIQVA SVDFQSVDCH GNPVIEFLKR NGKPIEQPVE FENGGYSVIQ 1550
VMDEGYSPVF VTPPTNSPYA EVSGDYNPIH VSPTFAAFVE LPGTHGITHG 1600
MYTSAAARRF VETYAAQNVP ERVKHYEVTF VNMVLPNTEL ITKLSHTGMI 1650
NGRKIIKVEV LNQETSEPVL VGTAEVEQPV SAYVFTGQGS QEQGMGMDLY 1700
ASSPVARKIW DSADKHFLTN YGFSIIDIVK HNPHSITIHF GGSKGKKIRD 1750
NYMAMAYEKL MEDGTSKVVP VFETITKDST SFSFTHPSGL LSATQFTQPA 1800
LTLMEKSAFE DMRSKGLVQN DCAFAGHSLG EYSALSAMGD VLSIEALVDL 1850
VFLRGLTMQN AVHRDELGRS DYGMVAANPS RVSASFTDAA LRFIVDHIGQ 1900
QTNLLLEIVN YNVENQQYVV SGNLLSLSTL GHVLNFLKVQ KIDFEKLKET 1950
LTIEQLKEQL TDIVEACHAK TLEQQKKTGR IELERGYATI PLKIDVPFHS 2000
SFLRGGVRMF REYLVKKIFP HQINVAKLRG KYIPNLTAKP FEISKEYFQN 2050
VYDLTGSQRI KKILQNWDEY ESS 2073
Length:2,073
Mass (Da):230,561
Last modified:May 1, 2000 - v1
Checksum:iD928270838E7C7C4
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti222 – 2221P → R in BAA36384. 1 Publication

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...

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.
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: September 3, 2014
This is version 111 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

Similar proteinsi