ID A0A2T2NQ79_CORCC Unreviewed; 2081 AA.
AC A0A2T2NQ79;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 28-JAN-2026, entry version 35.
DE RecName: Full=Fatty acid synthase subunit beta {ECO:0000256|ARBA:ARBA00068309};
DE EC=1.3.1.9 {ECO:0000256|ARBA:ARBA00012996};
DE EC=2.3.1.38 {ECO:0000256|ARBA:ARBA00013256};
DE EC=2.3.1.39 {ECO:0000256|ARBA:ARBA00013258};
DE EC=2.3.1.86 {ECO:0000256|ARBA:ARBA00012878};
DE EC=3.1.2.14 {ECO:0000256|ARBA:ARBA00012480};
DE EC=4.2.1.59 {ECO:0000256|ARBA:ARBA00013167};
GN ORFNames=BS50DRAFT_574115 {ECO:0000313|EMBL:PSN67416.1};
OS Corynespora cassiicola Philippines.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Corynesporascaceae; Corynespora.
OX NCBI_TaxID=1448308 {ECO:0000313|EMBL:PSN67416.1, ECO:0000313|Proteomes:UP000240883};
RN [1] {ECO:0000313|EMBL:PSN67416.1, ECO:0000313|Proteomes:UP000240883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philippines {ECO:0000313|EMBL:PSN67416.1,
RC ECO:0000313|Proteomes:UP000240883};
RX PubMed=29551995; DOI=10.3389/fmicb.2018.00276;
RA Lopez D., Ribeiro S., Label P., Fumanal B., Venisse J.S., Kohler A.,
RA de Oliveira R.R., Labutti K., Lipzen A., Lail K., Bauer D., Ohm R.A.,
RA Barry K.W., Spatafora J., Grigoriev I.V., Martin F.M., Pujade-Renaud V.;
RT "Genome-Wide Analysis of Corynespora cassiicola Leaf Fall Disease Putative
RT Effectors.";
RL Front. Microbiol. 9:276-276(2018).
CC -!- FUNCTION: Fatty acid synthetase catalyzes the formation of long-chain
CC fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit
CC contains domains for: [acyl-carrier-protein] acetyltransferase and
CC malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-
CC [acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-
CC protein] dehydratase. {ECO:0000256|ARBA:ARBA00058855}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + holo-
CC [ACP] + H(+); Xref=Rhea:RHEA:15057, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:9924, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78783; EC=3.1.2.14;
CC Evidence={ECO:0000256|ARBA:ARBA00048536};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O;
CC Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;
CC Evidence={ECO:0000256|ARBA:ARBA00001055};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] +
CC NADH + H(+); Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00048572};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + n malonyl-CoA + 2n NADPH + 4n H(+) = a long-
CC chain-acyl-CoA + n CoA + n CO2 + 2n NADP(+).; EC=2.3.1.86;
CC Evidence={ECO:0000256|ARBA:ARBA00048237};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[ACP] + acetyl-CoA = acetyl-[ACP] + CoA;
CC Xref=Rhea:RHEA:41788, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78446; EC=2.3.1.38;
CC Evidence={ECO:0000256|ARBA:ARBA00048835};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[ACP] + malonyl-CoA = malonyl-[ACP] + CoA;
CC Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449; EC=2.3.1.39;
CC Evidence={ECO:0000256|ARBA:ARBA00048462};
CC -!- SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional subunits
CC (alpha and beta). {ECO:0000256|ARBA:ARBA00033756}.
CC -!- SIMILARITY: Belongs to the fungal fatty acid synthetase subunit beta
CC family. {ECO:0000256|ARBA:ARBA00010009, ECO:0000256|PIRNR:PIRNR005562}.
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DR EMBL; KZ678135; PSN67416.1; -; Genomic_DNA.
DR STRING; 1448308.A0A2T2NQ79; -.
DR OrthoDB; 5417908at2759; -.
DR Proteomes; UP000240883; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0019171; F:(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004312; F:fatty acid synthase activity; IEA:InterPro.
DR GO; GO:0016297; F:fatty acyl-[ACP] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd03447; FAS_MaoC; 1.
DR FunFam; 1.20.1050.120:FF:000001; Fatty acid synthase beta subunit dehydratase; 1.
DR FunFam; 1.20.930.70:FF:000001; Fatty acid synthase beta subunit dehydratase; 1.
DR FunFam; 3.10.129.10:FF:000017; Fatty acid synthase beta subunit dehydratase; 1.
DR FunFam; 3.20.20.70:FF:000078; Fatty acid synthase beta subunit dehydratase; 1.
DR FunFam; 3.30.1120.100:FF:000001; Fatty acid synthase beta subunit dehydratase; 1.
DR FunFam; 3.10.129.10:FF:000015; Fatty acid synthase subunit beta; 1.
DR FunFam; 3.20.20.70:FF:000169; Fatty acid synthase subunit beta; 1.
DR FunFam; 3.30.70.3330:FF:000001; Fatty acid synthase subunit beta dehydratase; 1.
DR FunFam; 3.40.366.10:FF:000003; Fatty acid synthase subunit beta dehydratase; 1.
DR Gene3D; 1.20.1050.120; -; 1.
DR Gene3D; 1.20.930.70; -; 1.
DR Gene3D; 3.30.1120.100; -; 1.
DR Gene3D; 3.30.70.3330; -; 1.
DR Gene3D; 6.10.140.1400; -; 1.
DR Gene3D; 6.10.60.10; -; 1.
DR Gene3D; 6.20.240.10; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 2.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 3.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase_dom.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR039569; FAS1-like_DH_region.
DR InterPro; IPR016452; Fas1/AflB-like.
DR InterPro; IPR013565; Fas1/AflB-like_central.
DR InterPro; IPR041099; FAS1_N.
DR InterPro; IPR040883; FAS_meander.
DR InterPro; IPR003965; Fatty_acid_synthase.
DR InterPro; IPR050830; Fungal_FAS.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR002539; MaoC-like_dom.
DR InterPro; IPR032088; SAT.
DR PANTHER; PTHR10982:SF21; FATTY ACID SYNTHASE SUBUNIT BETA; 1.
DR PANTHER; PTHR10982; MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08354; Fas1-AflB-like_hel; 1.
DR Pfam; PF13452; FAS1_DH_region; 1.
DR Pfam; PF22235; FAS1_thioest_ins; 1.
DR Pfam; PF17951; FAS_meander; 1.
DR Pfam; PF17828; FAS_N; 1.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR Pfam; PF16073; SAT; 1.
DR PIRSF; PIRSF005562; FAS_yeast_beta; 1.
DR PRINTS; PR01483; FASYNTHASE.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 2.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR005562};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR005562};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR005562};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR005562};
KW Reference proteome {ECO:0000313|Proteomes:UP000240883};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR005562}.
FT DOMAIN 1687..1987
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 282
FT /note="For acetyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
FT ACT_SITE 1831
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
SQ SEQUENCE 2081 AA; 231912 MW; 3D43C75A0EF7A035 CRC64;
MYGSGPQTGI STPRSQASLR PLPLSHGSLE YTLLIPTALH FNAQQLRDAF KATLPEPTDE
LAQDDEPSSV PELVARYLGF VAQEVEEGDD PGSFEEVLKL VVNEFERAFL RGNEVHALAA
TLPGITEKKL ITIRSYYAAR AAVERPIKHH ESALFREAAD ENAFIYAVLG GQGNIEEYFD
ELREIYTTYP SFVEDFIAAE AQHLLSLARD PRAEKLFSKG LDVMRWLTNK ESQPDTDYLV
SAPVSLPLIG LTQLAHYVVT CRVLGSHPGH IRSRLAGVTG HSQGVVTAAA IAEAKNWETF
EQAAKNAITI LFWIGTRSQQ AYPRTSLAPS VLQDSVDNGE GTPTPMLSIR DLSRKAVQEH
IDATNAHLPT ERHIAISLVN SARNFVVTGP PISLYGLNLR LRKVKAPTGL DQTRIPFTDR
KVRFVNRFLP ITAPFHSPYL TEASKQLEED LKDIKIPAKD LGIPMYDTSS GKDIRDDDAD
NIVPALVRMI TNDPVNWEQA TVFPKATHIL DFGPGGISGL GVLTNRNKEG TGVRVILAGA
VDGQNAEVGY KPEIFDRDAE HAVKYAVDWV KEHGPRLVKT STGQTYVDTK MSRMLGLPPV
MVAGMTPTTV PWDFVAATMN AGYSIELAGG GYYNEKTMTA AISKVEKVIP PGRGININLI
YVNPRAMAWQ IPLLGKLRAE GVPIEGLTIG AGVPSIEVAN EYIETLGIKH ISFKPGSTEA
IQQTINIAKA NPGFPVLLQW TGGRGGGHHS FEDFHQPILQ MYGRIRKCDN LILVAGSGFG
GAEDTYPYLT GTWSTRFGYP PMPYDGCMFG SRMMTAKEAH TSKNAKQAIV DAPGLDDADW
EKTYKGPAGG VITVRSEMGE PIHKLATRGV QFWHEMDQKI FALDKAKRIP ELKKMREHII
KKLNNDFQKV WFGRNKKGES VDLEDMTYAE VVQRMVDLMY VKHQSRWIDP SLKRLTGDFI
RRVEERFSKK DSESLIQNYE ELNDPYPIVE KVFKAFPEAE EQLINAQDVQ HFLLLCQRRG
QKPVPFVPVL DDTFEYFFKK DSLWQSEDLD AVVDQDVGRT CILQGPMAAR FSTKVDEPIK
EILDGIHNGH IEALLRDIYG GDESKVPVIE YFGSKRLTSP EGLEVDGLTV SQLENKVIYR
LSSAPNATLP DVDSWLQLLA GTHYSWRHAF FTADIFVQGQ RFQSNPAARI FAPTSGMMVE
INHPNEPAKT VVTVKEPHHG GKHVKTIEVS LQSREIVLNM FEERTVLKKP AALPLKFVYR
PDVGYAPIHE VMDARNDRIK EFYYKIWFGD EVCPFDASLA SKFDGGRATV TSEAINDFVH
AVGNTGEAFV DRPGKEVFAP MDFAIVVGWK AITKPIFPRA IDGDLLKLVH LSNGFRMIPG
AEPLKKGDVL DTTAQINAVI NQESGKMVEV CGTITRDSEP VMEVTSQFLY RGAYTDYENT
FQRKTETPMQ LHLATSKDVA ILRSKEWFNF EEPEIELLDK TLTFKLQTFV RYKNKTAFAE
VETTGEVLLE LPTKEVIQIA SVDYRSGDSY GNPVLDYLER NGSAIDQPVN FENPIPLNGK
TPLTLKAPAS NETYARVSGD YNPIHVSRVF SSYANLPGTI THGMYSSAAV RSLVETWAAE
NHVGRVRGFH VNLVGMVLPD DMLDVKLQHV GMVSGRKIIK IEVSNKETED KVLLGEAEVE
QPTTSYVFTG QGSQEQGMGM DLYASSPVAK EVWDRADKHF MDNYGFAITN IVKNNPKELT
IHFGGPRGKA IRQNYMSMTF ETVGADGSIK SEKIFKEIDE NTTSYTYRSP TGLLSATQFT
QPALTLMEKA SFEDMRAKGL VQRDSSFAGH SLGEYSALAA LAEVMPIESL VSVVFYRGLT
MQVAVERDET GRSNYSMCAV NPSRISKTFN EQALQYVVEN ISEQTGWLLE IVNYNIANMQ
YVCAGDLRAL DCLTNVTNYL KAQKIDIQEL MQSMSLEDVK AHLVEIIKEC AKQTEAKPKP
LDLQRGFATI PLKGIDVPFH STFLRSGVKP FRSFLLKKIH KTSIDPSKLI GKYIPNVTAK
PFELTKEYFE DVYRLTNSPK IGNILANWDK YEEKEESKVA A
//
