ORYA_ASPOR
ID ORYA_ASPOR Reviewed; 1777 AA.
AC Q2TXF0;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Fatty acid synthase subunit alpha {ECO:0000303|PubMed:30104550};
DE EC=2.3.1.86 {ECO:0000305|PubMed:30104550};
DE AltName: Full=Oryzines biosynthesis cluster protein oryfasA {ECO:0000303|PubMed:30104550};
DE Includes:
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase {ECO:0000250|UniProtKB:P19097};
DE EC=1.1.1.100 {ECO:0000250|UniProtKB:P19097};
DE AltName: Full=Beta-ketoacyl reductase {ECO:0000250|UniProtKB:P19097};
DE Includes:
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase {ECO:0000250|UniProtKB:P19097};
DE EC=2.3.1.41 {ECO:0000250|UniProtKB:P19097};
GN Name=oryfasA {ECO:0000303|PubMed:30104550}; ORFNames=AO090010000171;
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 alpha 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:0000305|PubMed:30104550};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP]
CC + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC EC=2.3.1.41; Evidence={ECO:0000250|UniProtKB:P19097};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC Evidence={ECO:0000250|UniProtKB:P19097};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:30104550}.
CC -!- SUBUNIT: Fatty acid synthase is composed of alpha and beta subunits.
CC {ECO:0000250|UniProtKB:P19097}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Fungal fatty acid
CC synthetase subunit alpha family. {ECO:0000305}.
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DR EMBL; AP007175; BAE66073.1; -; Genomic_DNA.
DR RefSeq; XP_001827206.1; XM_001827154.1.
DR AlphaFoldDB; Q2TXF0; -.
DR SMR; Q2TXF0; -.
DR STRING; 510516.Q2TXF0; -.
DR EnsemblFungi; BAE66073; BAE66073; AO090010000171.
DR GeneID; 5999340; -.
DR KEGG; aor:AO090010000171; -.
DR VEuPathDB; FungiDB:AO090010000171; -.
DR HOGENOM; CLU_000114_0_0_1; -.
DR OMA; AFMLTSF; -.
DR Proteomes; UP000006564; Chromosome 8.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.90.470.20; -; 1.
DR HAMAP; MF_00101; AcpS; 1.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR InterPro; IPR002582; ACPS.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR040899; Fas_alpha_ACP.
DR InterPro; IPR026025; FAS_alpha_yeast.
DR InterPro; IPR041550; FASI_helical.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR004568; Ppantetheine-prot_Trfase_dom.
DR InterPro; IPR002347; SDR_fam.
DR InterPro; IPR016039; Thiolase-like.
DR Pfam; PF01648; ACPS; 1.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF18325; Fas_alpha_ACP; 1.
DR Pfam; PF18314; FAS_I_H; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR PIRSF; PIRSF000454; FAS_yeast_alpha; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR SUPFAM; SSF56214; SSF56214; 1.
DR TIGRFAMs; TIGR00556; pantethn_trn; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW Lipid metabolism; Magnesium; Metal-binding; Multifunctional enzyme; NADP;
KW Oxidoreductase; Phosphopantetheine; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..1777
FT /note="Fatty acid synthase subunit alpha"
FT /id="PRO_0000450483"
FT DOMAIN 151..237
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 101..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..803
FT /note="Ketoreductase (KR) domain"
FT /evidence="ECO:0000250|UniProtKB:Q8TGA2, ECO:0000255"
FT REGION 1013..1528
FT /note="Ketosynthase (KS) domain"
FT /evidence="ECO:0000250|UniProtKB:Q8TGA2, ECO:0000255"
FT ACT_SITE 1193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 1193
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT BINDING 1661..1663
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P19097"
FT BINDING 1661
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P19097"
FT BINDING 1706..1716
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P19097"
FT BINDING 1730..1734
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P19097"
FT BINDING 1760..1762
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P19097"
FT MOD_RES 186
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1777 AA; 194716 MW; B54A4D275307F121 CRC64;
MVQRKDPPSE QLRAYTLLIE LLSYQFAFPV RWIETQNDLI QRNNTIQRFV EVGPSNVLAN
MAKKTAKGQY AEEDLVRCVD RQYLSHADDA QHIYYQYDEE APVESADNEP AQPAASSTPA
APAPVAAPPV VVQTAPQPAA QAAVAVPDVD LSAIDVVISI VAQKIRKAFD EVPAAKSIRD
LSAGKSTLQN ELIGQLDAEF RGLPEGSEDL ALEALASHFT NFSGRPGKVM GGHIDRLVAA
RMPAGFNQAK IRDYLSSHWG LGLNRQTTVL CYAVTMEPAA RLADAGQATQ FLDSVVSRYG
GKAGIALQKR AEGGASQTSA VAQVDLASLE TLKKEQNEYL HKQFQLLAKH LDLDGVAQPS
QTQVQGEDTD RLAEWDAEFD EEFLTGMRTI FDPRKARRYD SWWNTAREDL MALLHDIRPA
AEDKASQRYQ SLVNRWSPEL EQMLEHSAQD DTTKEKAQML LDDVRASGVA NGPVFRYTQP
AMAPETKVDA NGRIQYSEVP RRQLHGENKA STLNYAQVVA ARHRDVPYAH LRSRAGVDWK
YDDQLTDMFL NILSTGASTG LSFTGRRVLV TGAGVGSIGA DIVAGLLAGG AHVIVTTSRQ
PSDVAASFRQ LYAKVGAPGS ELIVLPFNQA SKRDCEELIN HIYDEQSGYG WDLDFIIPFA
AISEIGRQID KIDSKSELAH RAMLVNLLRL LGFIKQQKEK RGFDCRPTGV LLPLSPNHGN
FGGDGLYSES KLGLETLFNR FHSEGWSDFL CIIGAVIGWT RGTGLMSANN IVAQGMEDSL
DILTFSAPEM AFNILSLLSG DILEVADDEP IYADLSGGLQ GVSDLKDKIS AIRKKIVSDS
RIRQALVAEN LHEQKVLRGT KPAEGNVQPP LKRRSNIEPA FPPLSDYNSV TAGLQSLKGM
VDLSRTVVVV GYSELGPWGS SRTRWEMEHE GRLSLEGYTE LAWMMGLIKH FDGDLKGKPY
TGWVDSKTKE AVDEADIEEK YGQHILGHAG IRVIEPELSE GYDPSQKEIM HEVVIDEDLP
PFEAPQGVAQ AFKLRHGDKV ILTPIEGSES VKVVVKSGAV FMVPKAMAFN RFVAGQLPSG
WDPTRYGIPE DIVAQVDPMT VYVLCCVSEA MYSAGLEDPF ELYRHIHVSE LANCVGTGAG
GLLAMRGVYR DRYLDRPVQS DILQESFLNA MNAWTNMLLM GAAGPIKSPS GTCATSVESM
DIACEAIQTL KAKVAIVGGS DDFQEEMSYE FGNMKATANA EDELEKGYLP SEMSRPTASS
RSGFVESAGC GIQLVMSAEL ALQMGLPIYG IVAYSQMAGD KVGRSVPAPG QGVLTAARES
IDAAQSPLLD VQYRKARLDE AVSEIKRWRH KESQKLIAST TSKEFKDLDA HLQHINNIAA
TRIRDAQWTW NNNIRHIDPT IAPMRAALAT WGLSVDDIQV ASFHGTSTKA NDKNESNVIN
QQMTHLSRTV GNPLLVICQK SLTGHPKGAA GAWMFNGCLQ ALQTGIVPGN RNADNVDVAL
QQFKHLVYPS QTIHTSGIKA FMLTSFGFGQ KGGLVVGIAP RYLFSTITAN KFEDYRERVL
QRQQKIIPVF QRRMAQGRLF QIKDQSAWTS DQEKDVFLNP QARVAQKSTG EYSFPTTVAP
VASSLPARTV SDDKQLFARS SDQWLRDSIS KEQGNVSVGV DIESISSVNI EDEIFLERNF
TPGELKYCQG SPDKQASLSG RWAAKEAIFK SLQIPSEGAG AAMRDIEIVS NGAQPPTVLL
HNRAKSAADA QKVEEVQVSI THSPESAMAI ALARRRL
