ORYB_ASPOR
ID ORYB_ASPOR Reviewed; 2026 AA.
AC Q2TXG3;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Fatty acid synthase subunit beta {ECO:0000303|PubMed:30104550};
DE EC=2.3.1.86 {ECO:0000305|PubMed:30104550};
DE AltName: Full=S-acyl fatty acid synthase thioesterase {ECO:0000250|UniProtKB:Q8TGA1};
DE EC=3.1.2.14 {ECO:0000250|UniProtKB:Q8TGA1};
DE Includes:
DE RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase {ECO:0000250|UniProtKB:Q8TGA1};
DE EC=4.2.1.59 {ECO:0000250|UniProtKB:Q8TGA1};
DE Includes:
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000250|UniProtKB:Q8TGA1};
DE EC=1.3.1.9 {ECO:0000250|UniProtKB:Q8TGA1};
DE Includes:
DE RecName: Full=[Acyl-carrier-protein] acetyltransferase {ECO:0000250|UniProtKB:Q8TGA1};
DE EC=2.3.1.38 {ECO:0000250|UniProtKB:Q8TGA1};
DE Includes:
DE RecName: Full=[Acyl-carrier-protein] malonyltransferase {ECO:0000250|UniProtKB:Q8TGA1};
DE EC=2.3.1.39 {ECO:0000250|UniProtKB:Q8TGA1};
DE AltName: Full=Oryzines biosynthesis cluster protein oryfasB {ECO:0000303|PubMed:30104550};
GN Name=oryfasB {ECO:0000303|PubMed:30104550}; ORFNames=AO090010000156;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [2]
RP FUNCTION, AND PATHWAY.
RX PubMed=30104550; DOI=10.3390/jof4030096;
RA Wasil Z., Kuhnert E., Simpson T.J., Cox R.J.;
RT "Oryzines A & B, maleidride congeners from Aspergillus oryzae and their
RT putative biosynthesis.";
RL J. Fungi 4:0-0(2018).
CC -!- FUNCTION: Fatty acid synthase beta subunit; part of the gene cluster
CC that mediates the biosynthesis of oryzines, natural products with an
CC unusual maleidride backbone (PubMed:30104550). The two subunits of the
CC fungal fatty acid synthase oryfasA and oryfasB probably form octenoic
CC acid (Probable). This fatty acid is most likely activated by the acyl-
CC CoA ligase oryP to give octenyl-CoA before the citrate synthase-like
CC protein oryE catalyzes condensation with oxaloacetate to form
CC tricarboxylic acid (Probable). The next steps of the pathways are
CC conjectural, but a favorite possible route has been proposed, beginning
CC with decarboxylation and concomitant dehydration by the decarboxylase
CC oryM, followed by tautomerization, which may lead to the production of
CC a diene intermediate (Probable). Reduction of this diene intermediate
CC could give the known metabolite piliformic acid (Probable). On the
CC pathway to oryzine B and oryzine A, however, hydroxylation of the diene
CC by the alpha-ketoglutarate-dependent dioxygenase oryG and lactonisation
CC by the lactonohydrolases oryH or oryL could give oryzine B directly
CC (Probable). Finally, enoyl reduction by the dehydrogenase oryD would
CC then convert oryzine B into oryzine A (Probable).
CC {ECO:0000269|PubMed:30104550, ECO:0000305|PubMed:30104550}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain
CC fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+);
CC Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:83139; EC=2.3.1.86;
CC Evidence={ECO:0000250|UniProtKB:Q8TGA1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + holo-[ACP] = 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:0000250|UniProtKB:Q8TGA1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
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:0000250|UniProtKB:Q8TGA1};
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:0000250|UniProtKB:Q8TGA1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] +
CC H(+) + NADH; 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:0000250|UniProtKB:Q8TGA1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) +
CC holo-[ACP]; 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:0000250|UniProtKB:Q8TGA1};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:30104550}.
CC -!- SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional subunits
CC (alpha and beta). {ECO:0000250|UniProtKB:P19097}.
CC -!- SIMILARITY: Belongs to the fungal fatty acid synthetase subunit beta
CC family. {ECO:0000305}.
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DR EMBL; AP007175; BAE66060.1; -; Genomic_DNA.
DR RefSeq; XP_001827193.1; XM_001827141.1.
DR AlphaFoldDB; Q2TXG3; -.
DR SMR; Q2TXG3; -.
DR STRING; 510516.Q2TXG3; -.
DR EnsemblFungi; BAE66060; BAE66060; AO090010000156.
DR GeneID; 5999327; -.
DR KEGG; aor:AO090010000156; -.
DR VEuPathDB; FungiDB:AO090010000156; -.
DR HOGENOM; CLU_000114_5_0_1; -.
DR OMA; VELLFWI; -.
DR Proteomes; UP000006564; Chromosome 8.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
DR GO; GO:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008693; F:3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004317; F:3-hydroxypalmitoyl-[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-EC.
DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016295; F:myristoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004320; F:oleoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016296; F:palmitoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.40.366.10; -; 3.
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; IPR016452; Fas1/AflB-like.
DR InterPro; IPR013565; Fas1/AflB-like_central.
DR InterPro; IPR040883; FAS_meander.
DR InterPro; IPR003965; Fatty_acid_synthase.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR039569; MaoC-like_dehydrat_N.
DR InterPro; IPR002539; MaoC-like_dom.
DR InterPro; IPR032088; SAT.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08354; DUF1729; 1.
DR Pfam; PF17951; FAS_meander; 1.
DR Pfam; PF13452; MaoC_dehydrat_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; SSF52151; 2.
DR SUPFAM; SSF54637; SSF54637; 2.
PE 3: Inferred from homology;
KW Hydrolase; Lyase; Multifunctional enzyme; NAD; NADP; Oxidoreductase;
KW Reference proteome; Transferase.
FT CHAIN 1..2026
FT /note="Fatty acid synthase subunit beta"
FT /id="PRO_0000450484"
FT DOMAIN 1512..1625
FT /note="MaoC-like"
FT /evidence="ECO:0000255"
FT REGION 148..526
FT /note="Acetyltransferase (AT) domain"
FT /evidence="ECO:0000255"
FT REGION 579..824
FT /note="Enoyl reductase (ER) domain"
FT /evidence="ECO:0000255"
FT REGION 1130..1604
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000255"
FT REGION 1643..2016
FT /note="Malonyl/palmitoyl transferase (MT/PT) domain"
FT /evidence="ECO:0000255"
FT ACT_SITE 268
FT /note="For acetyltransferase activity"
FT /evidence="ECO:0000255|PIRSR:PIRSR005562-1"
FT ACT_SITE 1788
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000255|PIRSR:PIRSR005562-1"
SQ SEQUENCE 2026 AA; 224257 MW; 3E3CB598EDAD7E4D CRC64;
MASTPSSGSY DLAIVTPTED HSLRSFSLSQ GNVQQTFLVS TQDGAFLDQQ KASFLQSYSK
DQSILGLVFE FLQFLLDEAC PPAPLGAFLG AIESQCVRDA NIHDLIVSEP EAKNIIRTYY
RAHAVAGLNP RPAPSGLFST VNIEAHRILM AFGGQGSTNL VCVDELADLY SLYQPLLEPL
IASVAPALAS LSREPSTLQH YLGREIDLYS WLTIPESRPD RAFTATAAVS FPIIGLLDMA
HYYVLGKLLD SDSPKRLRSA LQGLTGHSQG IIVAAAVAQA DTWASFLAQA QWAIRLLFWM
GYECHTAAPA SPLSSAAIRD SIEHGEGSPS WLLSVRGLRS PALDALITDC NRRLPESEHL
SIGLINTERN IVVAGSPRSL RGLCLRLREI EADDGQDQSR VPFRQRKPVV HHTFLPVSAP
FHSSHLRAAA DRVKERFPDA SSPQVGDLLT AVYHTRTGQD MREMFSPSNN LIHSLVEAVA
CETVDWPATL QVSRSKPPSH IVLLSSSRLS DLVSEIVDGR GVRIIAGTVL APTDPAVLGG
KAELLTTKPS QAPTPWAELF KARLVAGPDG RPILETRLSQ LLQAPPIITA GMTPTTVHWD
FVAAVMQAGY HVELAGGGYF DAAGMTTAIE KLAAHVPPGR GITCNLIYAS PHSIAFQIPL
IRSMIQRGIP IDGLTIGAGV PSQDVVNEWI QTLGIKHLSL KPGSIAAIYE VIEIAKKHPT
FPIILQWTGG RGGGHHSCED FHEPLLQTYR DIRRCSNLYL VVGSGFGQAD QMHPYITGEW
SLSFGRPVMP CDGILIGSRM MVAREAHTSP QAKELILAAA GVADSEWEQS FKKPTGGVLT
VQSEMGQPIH KLATRGVRLW HEMDKTIFSL PRDKRVAALN ARKAEIIRRL SADFAKPWFG
YNAAGDAVDL EDMTYTEVIA RLIRLVYVSH QHRWIDPSYR QLVLDFTYRT LERVSNADYA
TDKLDLSQPE QFVEQVQQLC PAATTRRLHP DDVRFFLTIC KQRGRKPVNF IPALDEDFEY
WFKKDSLWQS EDVDSIIDQD ADRVCILQGP VAVQYSRRAD QSAREILDEI HHGLANHFEE
GPSQSDRPSL AISEMVSARV TVTESNTHRI IRPTSESLPS VEDWQAFLAS QVTGSVRSAI
MAEEVLRGSQ RQANPLRRVL EPRTGQSIQI PLDGRDLRLV EDAKNRPLVH IKPSGDQEVA
VDFYYYDFVE TPGNLRFTYK FDSKSLSLVE NLDGRDDRVK LFYAHLWLGR ADLSYHRLSE
VFEGEEITLS SDLHRHLHNA LRHTVPDATA SATTNTLPLE AAIIAAWKPL MEPLFVAELQ
GDLLRLVHLS NSIRYTPGAA PLEVNDVVAT KSQVRAVTIK ETGKTISVEA QIFRSKTLVA
TVTSEFFIKG SFSDYETTFS HQDEAAIELK VQSAIDEALL RDREWFLLDD PTQSLIDKTL
VFRLHTVTRW KDQSTFTSLK TTGSIYTKHW NGTEQKVGTV ASEVVECHGN PVIDFLQRKG
TVVQEKVPLK HPGLIDNGSR TIRLPLDNAL YSSVSKDYNP IHTSSVFARF ADLPGTITHG
MYTAAVSRAV TECLAADGET GRLRSFSASF VGMVLPGDQL TVRIRHEAMC HGRMVLSVAA
YREGTDEKVL QGEAEVEQRT SAYLFTGQGS QAQNMGMQLY DSSAVARSVW DEVDRRLLDQ
YGWSILNVVR ANPKQITIHF RGARGRRIRD NYLAMRTETR MPDGSTRLEP ILRDLTAKSE
SYTFFDSRGL LYATQFAQPA ILLMEKAAFE DMKANGLIQE GAAFAGHSLG EYGVLASLVD
FLPFEMMMSV VFYRGLVMQF TMERDSNGHT GFSMVAVSPK RVGKYFDEAM LRIVVDLIHR
QSGKLLEIVN FNVEAEQYVC AGHVRNIYIL SGILDLLSRS ATGPQLVASL RSASDPAITD
VAKEIAVYLE KAPQLNNPTE LKRGRATIPL QGIDVPFHSS HLRSGVSVYR RFLEERIQAE
NVQVDRLVGK FIPNVMGKPF AIDRSYLEEA AAVTGSSVLR ELALAA
