FAS2_USTMA
ID FAS2_USTMA Reviewed; 3704 AA.
AC A0A0D1DNX1;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Fatty acid synthase 2 {ECO:0000303|PubMed:17850255};
DE EC=2.3.1.- {ECO:0000305|PubMed:17850255};
DE AltName: Full=Ustilagic acid biosynthesis cluster protein fas2 {ECO:0000303|PubMed:17850255};
GN Name=fas2 {ECO:0000303|PubMed:17850255}; ORFNames=UMAG_06460;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=15932999; DOI=10.1128/aem.71.6.3033-3040.2005;
RA Hewald S., Josephs K., Boelker M.;
RT "Genetic analysis of biosurfactant production in Ustilago maydis.";
RL Appl. Environ. Microbiol. 71:3033-3040(2005).
RN [4]
RP FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=17850255; DOI=10.1111/j.1365-2958.2007.05941.x;
RA Teichmann B., Linne U., Hewald S., Marahiel M.A., Boelker M.;
RT "A biosynthetic gene cluster for a secreted cellobiose lipid with
RT antifungal activity from Ustilago maydis.";
RL Mol. Microbiol. 66:525-533(2007).
RN [5]
RP INDUCTION.
RX PubMed=20173069; DOI=10.1128/aem.02211-09;
RA Teichmann B., Liu L., Schink K.O., Boelker M.;
RT "Activation of the ustilagic acid biosynthesis gene cluster in Ustilago
RT maydis by the C2H2 zinc finger transcription factor Rua1.";
RL Appl. Environ. Microbiol. 76:2633-2640(2010).
CC -!- FUNCTION: Fatty acid synthase; part of the gene cluster that mediates
CC the biosynthesis of the glycolipid biosurfactant ustilagic acid (UA)
CC (PubMed:15932999, PubMed:17850255). UA is a secreted cellobiose
CC glycolipid that is toxic for many microorganisms and confers biocontrol
CC activity to U.maydis (PubMed:15932999, PubMed:17850255). UA consists of
CC 15,16-dihydroxypalmitic or 2,15,16-trihydroxypalmitic acid, which is O-
CC glycosidically linked to cellobiose at its terminal hydroxyl group
CC (PubMed:17850255). In addition, the cellobiose moiety is acetylated and
CC acylated with a short-chain hydroxy fatty acid (PubMed:17850255). UA
CC biosynthesis starts with omega-hydroxylation of palmitic acid catalyzed
CC by the cytochrome P450 monooxygenase cyp1 (PubMed:17850255). Terminal
CC hydroxylation of palmitic acid precedes subterminal hydroxylation
CC catalyzed by the cytochrome P450 monooxygenase cyp2 (PubMed:17850255).
CC Sequential glucosylation of the hydroxy fatty acid is probably
CC catalyzed by the glycosyltransferase ugt1 (Probable). The cellobiose
CC lipid is further decorated by acetylation of the proximal glucose
CC residue and by acylation with a short-chain beta-hydroxy fatty acid at
CC the distal glucose residue (Probable). The acyltransferase uat1 may be
CC a good candidate for catalyzing either acetylation or acylation of the
CC cellobiose lipid (Probable). The fatty acid synthase fas2 may be
CC involved in synthesis of the carbon backbone of the short-chain beta-
CC hydroxy fatty acid esterified to the cellobiose disaccharide
CC (Probable). The secreted UA consists of a mixture of both alpha-
CC hydroxylated and non-hydroxylated glycolipids; therefore, alpha-
CC hydroxylation of the long-chain fatty, catalyzed by the fatty acid
CC hydroxylase ahd1, occurs late in UA biosynthesis and may be the last
CC step before secretion (PubMed:17850255). {ECO:0000269|PubMed:15932999,
CC ECO:0000269|PubMed:17850255, ECO:0000305|PubMed:17850255}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:17850255}.
CC -!- INDUCTION: Expression is strongly induced under conditions of nitrogen
CC starvation (PubMed:17850255). Expression is positively regulated by the
CC cluster-specific transcription factor rua1 that recognizes and binds to
CC the specific 5'-T/G-G/T-C-G-C-A-T-A/T-C/T-C/T-G/A-3' upstream
CC activating sequence found in all promoters of the UA biosynthesis genes
CC (PubMed:20173069). {ECO:0000269|PubMed:17850255,
CC ECO:0000269|PubMed:20173069}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the fungal fatty acid
CC synthetase subunit beta family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the thiolase-like
CC superfamily. Fungal fatty acid synthetase subunit alpha family.
CC {ECO:0000305}.
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DR EMBL; CM003162; KIS65756.1; -; Genomic_DNA.
DR RefSeq; XP_011392728.1; XM_011394426.1.
DR SMR; A0A0D1DNX1; -.
DR STRING; 5270.UM06460P0; -.
DR EnsemblFungi; KIS65756; KIS65756; UMAG_06460.
DR GeneID; 23566042; -.
DR KEGG; uma:UMAG_06460; -.
DR VEuPathDB; FungiDB:UMAG_06460; -.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR OMA; APLVHGM; -.
DR OrthoDB; 2668at2759; -.
DR Proteomes; UP000000561; Chromosome 23.
DR GO; GO:0005835; C:fatty acid synthase complex; IBA:GO_Central.
DR GO; GO:0004317; F:3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:InterPro.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:InterPro.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.40.366.10; -; 3.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR013565; Fas1/AflB-like_central.
DR InterPro; IPR040899; Fas_alpha_ACP.
DR InterPro; IPR040883; FAS_meander.
DR InterPro; IPR041550; FASI_helical.
DR InterPro; IPR003965; Fatty_acid_synthase.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR002539; MaoC-like_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032088; SAT.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08354; DUF1729; 1.
DR Pfam; PF18325; Fas_alpha_ACP; 1.
DR Pfam; PF18314; FAS_I_H; 1.
DR Pfam; PF17951; FAS_meander; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR Pfam; PF16073; SAT; 1.
DR PRINTS; PR01483; FASYNTHASE.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52151; SSF52151; 2.
DR SUPFAM; SSF53901; SSF53901; 2.
DR SUPFAM; SSF54637; SSF54637; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; NADP; Oxidoreductase; Phosphopantetheine; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..3704
FT /note="Fatty acid synthase 2"
FT /id="PRO_0000452760"
FT DOMAIN 1624..1730
FT /note="MaoC-like"
FT /evidence="ECO:0000255"
FT DOMAIN 2265..2343
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 27..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..475
FT /note="Acetyltransferase (AT) domain"
FT /evidence="ECO:0000250|UniProtKB:Q8TGA1"
FT REGION 639..887
FT /note="Enoyl reductase (ER) domain"
FT /evidence="ECO:0000250|UniProtKB:Q8TGA1"
FT REGION 1216..1709
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000250|UniProtKB:Q8TGA1"
FT REGION 1747..2112
FT /note="Malonyl/palmitoyl transferase (MT/PT) domain"
FT /evidence="ECO:0000250|UniProtKB:Q8TGA1"
FT REGION 2733..2969
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000250|UniProtKB:Q8TGA2, ECO:0000255"
FT REGION 3072..3612
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000250|UniProtKB:Q8TGA2"
FT ACT_SITE 3359
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000250|UniProtKB:Q8TGA2"
FT MOD_RES 2303
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 3704 AA; 404963 MW; 7816C57DEB104093 CRC64;
MDASRLSRSS STSFTSVLSP FEPASVAVSA HGSPPSSASP GPDDKAFSVD GTQTPPHQLG
VVLITSPFNS EVTVSLSVPI RDFLDRHNLV QVRDEFVNHL RSLLASSPGQ EPAIDSVALL
VHLLLYLAEN LSSAEHRPRH ARLSLLEAAW ASFHSENLDS VDVHTFARSL SPEKASLVLR
AHFEAYAALQ QSGISVAIRV PALLQSVQKR QAGLYALFGG QGNNHGYFSE LQTLFDTYRP
LVEPIVAAAT ARFSHLLSRI DAARSGPYAF HSQGLDVLAW LQRRTDRPTE AYLASVPISG
PLLSLTQLIQ FYVAAKSSGM TVPQFRSHFE AVSGHSQGIV SATAMAMAID DEHYIECVAM
AAEFLFQIGS VSQLCYGDRT VSDETSMESV EAGFGPPSSM LVISAPSRAF IEVRVALFNT
IVPEHRRIHA ALINAPTTAV LAGHASDLVS FARDVSAISA PAKLDQARIP FSKRKPSLRL
KFLPISLPYH SPLLADVTLS QVLAPIDAQK WQAHPLALPV HSTTDGANMQ QLPSSSILDS
LRVQMCTAPV DWIQAVQPSA TITHFVDFGT GGASGIGNIT ARNLSGRGFK VLTVSGTHKE
SAEFYRLDPT PNAQPWGSKF QPRLLRTPQG KVILDTPMSR LLGKPPIMVA GMTPTTVQAS
LNAATIQAGY HIELAGGGLH DESKLRSRVQ EILAKAPAAS GLTLNSLYIN PRQWSFQLPA
WLQLSREGAP IDGLCVAAGI PSPDKAQELL TSLKQAGLRH VSFKPGSLDG IKQVCKIAQQ
NPGFPILLQW TGGRAGGHHS AEDFHDPIIH SYEIIRSCPN LVLVAGSGFT SADSFWPYLS
GQWSVKRGLP PMPFDGVLFG SWAMTAKEAA TSLPVKQLIA STQGCSDKDW QKTYDAPIGG
IMTVLSEMGE LVHQVANRAT LLWSELDRDL FKLSKDKQLV YLAKNKERLV QRLNDDFQRV
WFARDGQGKI LYDVQDMTYA DVADRMLSLM FIAAQARWID LGYRNLLGDW CRRIEERFSK
ASKTYQLQSY AQFDRSPELE LHRLLDHYPD CKTTLLTSED VEYFHTMCWR RGQKPPPFIT
RLGEDFGHQF KKDSLWQSED LDAVVDADPQ RVCILHGPVA ASDTAPVDQP IAEMLGSVEK
GLVQHVLDHF YKGDLNNVPV AEYLDATATG SPAVRTSPIR TVCSRIKIDS GEHVAVFSVN
SSAVKNPVAF LDSVVGEQPS WIRALVHSSR VSLGRQLRSN PLQRLLALRE GQLFQIHTSV
DGHNVKRLQV YGCHRSYGEQ SNDFLAVDIV RRSDTKTSSG ADIDVFIYEQ RGSEAIPLLL
QFEYTPSTSC ALIREVEHGR NDRIRRFYWK MWFGEDMPAD AQLDRVSSFT TEPRPVSSAQ
IPDGGAIAVD PTISAGWEAI MKTVVSSCDA DLLSLVHLGH EFQTIGGALP VASGDICSVR
SYASSITNSE TGKILTVKAT ISRVEAAGSD AVPVVQVTSR FFYKGKYADH HRCFTETDFA
FLLVLQDEAA VQVFKSKDWL ELDQGVHEVK VGTELILRGT TVVPRYKNAK EMLDLRVQGA
VFVRQGVEEN QIGLIEFDAD APLSSDPIVA YLERHGTRLQ NANEYSTVPI SNAYKLAEGV
LTTPKTNEPY SRASLDFNPI HINPYFANLA ELPATIGHGM STFAECQKWM DEAMKSTEPH
NKTTVPSCTA FKADFTAMVV PGDQLSVQLR HKAMSDGQKV VQIDASNQRG ELVLQGTARY
QQPRSVYVFT GQGSQAKVMG MELYRQSATA RAIWDEAEQH LAQSLGLSIL EIVRENPKTK
TVYFGGAQGQ SIRRNYMALQ HETIDEQGRS IRTPIFPSIH ANSRSYTFES PKGLLFATQF
TQIALVLFEL AYFRHLQKEG IIVEDAVFAG HSLGEYAALA SVAGMMRLRD LVDVVFYRGL
TMQSAVPRIN GRSDYGMVAV APIKAFPKIN DVDAALAQVV DRVSQASGQL LQTVNYNVRR
QQSVVAGHEV ALAALSRVLD KCGSKALSVA NEAELVAEVT SAVEAAQSTA KTSGIELKRG
IATIPLAGID VPFHSKFLSN GIDPFRRFLD SRLDIETVRP EALVGRYIPN LVARIFTLER
AYIEHVSEVT RSEVLANILA NWDEALLDRR RLTRTLVIEL LAYQFASPVL WSQTQTLLFQ
DASFERLIEF GPTPTLVGMA SKTLAADFSE KDRKLGLKRT LLCVGKNDAD ILYSFEAEEE
VNPTDSPKAT PEPAVSKAAL AAAATPAVAA ATTAVAQVAA PALDDERLDP LLTVRSILAQ
KQKVKIADIP PSKSIKQLTG GRSTLQNELV GDLGAEFVEL PERAEELTLE ELAAALRPGY
SGELGKYTNG LIARLSASKL PGSFGLTALK AHLTARYGFQ SGRISAILLY TLTEEPAKRL
TGDAEAISWI DGVAAVYAKD TSITLPAPGG AAGGAGATAG ATALVSSKEL VALQSKMQAL
SEKQIQVLTE HLGLDADASL SQLAKLSTES ASLHKALDSV SAEHGDAYIK GIQGIFSAAK
ARTFKSFWNW SRQNLEELFA DILQDRVSDD STLLARIIQV WNQLDDVGIL EQQLDQLQRS
GVAGSDRVTS LFDPLLRQAK SGALKTAPRF IDVSVPLRPS TRLDSRGNIV YQQVPRDGME
TILDYVTSMT SDKESKASAG QASSKSLIGR LEDLAQILSR LDEDQTSDVS IGSRPALWAC
KKVNSTWSRD DDLTEIYFRG LAKLAERGSS YAGLDVLLTG VGQGSIAFEV MRRFLRGGAR
VIVTTSTFSP KKLRMYGDTY RHDGARGAQL IVLPFNQGSF KDTQALVDHV YTSMGIDIDV
LVPFAAISEN GRNIDGIDDK SELAHRIMLT NVIRLMGCIK SAKAQRGILH RPTQVILPLS
FNHGVLGGDG LYGPSKIGLE TLLNTFESED WSRYLSVAGA RIGMCRGTDL MASSDIVAES
LERHFGFRTF STGEMAFNLL GLVEPEFASV NQTQPILLDL TGRASSLASP GKAMRDAHQE
WQRKSDIKKA LLSENRHDFK TTSSTRVTED HYRRVEIEPR SLHHFAYPEL NSQQVCDQIA
KGTCHLDLDQ VIVISGFAEV GPWGSSRTRW EREVSETWSL EGLVEMAWLT GHIKHFNGRL
ADGRSYIGWV DTKTGEPVAD AQMRARYARQ VEQHAGIRLV EPELMHGFDP ERKVIQQEIE
LTHDLGPLEI SAGEAERFRL AHGDKAIVWQ DEETKSWYLR LKKGASVFLP KASRFDRHVA
AQMPTGWDPA RYGIPSDIVS QTDETALYAL VCIAEALVQS GIDDPYELYK HVHVSEVGTS
LGSAMGGLRS LAKMFKDRRQ DVEVQKDILQ ETFINTVAGW TNLLLLSSCG PIKPTVGACA
TALQSLDVAA ETIRCGKAKI MIAGGYESIS EESMTEFANM KATASSDEAF AAGLAPEELS
KPMTSGRSGF VEAQGCGVQI VMSAATAIRI GAPINGIVAY TQTATDRQGR SIPAPGKGVL
AATVPLQRAM SGWGLDGNDV GVISMHGTST KANDKNESNV YHTMLGKLGR AEGRAVPAMA
QKWLCGHGKG GAAAWAINGL MQSINDGIVA GNRNADDISE ELRAYNRIVY PSRSIRYSRE
RLHAGLVTSF GFGQVGGIAM ILHASHLFGR LDREAFELYK ARRNKRQQIT YRRMHSLFIK
GDLVRIKEDA PYSPEDETAV LLDIDARAEL SSEGSYRIVP SIYA
