ID A0A072PGA7_9EURO Unreviewed; 2088 AA.
AC A0A072PGA7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Fatty acid synthase subunit beta, fungi type {ECO:0000313|EMBL:KEF59174.1};
GN ORFNames=A1O9_04018 {ECO:0000313|EMBL:KEF59174.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF59174.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF59174.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF59174.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001214};
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 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:0000256|ARBA:ARBA00000175};
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:0000256|ARBA:ARBA00000343};
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:0000256|ARBA:ARBA00001540};
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:0000256|ARBA:ARBA00000936};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KEF59174.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMGV01000003; KEF59174.1; -; Genomic_DNA.
DR RefSeq; XP_013261764.1; XM_013406310.1.
DR STRING; 1182545.A0A072PGA7; -.
DR GeneID; 25278951; -.
DR VEuPathDB; FungiDB:A1O9_04018; -.
DR HOGENOM; CLU_000114_5_0_1; -.
DR OrthoDB; 5488314at2759; -.
DR Proteomes; UP000027920; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004317; F:(3R)-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:InterPro.
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:0016297; F:acyl-[acyl-carrier-protein] hydrolase 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:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd03447; FAS_MaoC; 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.
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; IPR041099; FAS1_N.
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 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; PF17951; FAS_meander; 1.
DR Pfam; PF17828; FAS_N; 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; FabD/lysophospholipase-like; 2.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR005562};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
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:UP000027920};
KW Transferase {ECO:0000256|PIRNR:PIRNR005562}.
FT DOMAIN 1689..2010
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT ACT_SITE 281
FT /note="For acetyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
FT ACT_SITE 1833
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
SQ SEQUENCE 2088 AA; 231336 MW; 50E0F88295FAFEE5 CRC64;
MYSGGATGTH TPRSSQNLRP LILTHGSLDY AFLIPTALHF QASQLKDAFN ASLPAPTDEL
AQDDEPSSNA ELVARYIGFI AAEVDDDEEA AGFVEVLKVV LNEFERSFMH ANDVHALAAS
LPGITAKKLV VVQCYYAGRA AVARPIKPHD SALLRAADDE EASIYTVFGG QGNIEEYFDE
LREVYTTYPS FVRDLVESSA ELLQSLARSP KADKFYTKGL DILGWLADPD SQPDTDYLVS
APVSLPLIGL VQLAHYQVTC KVLGRTPADV NERFNGTTGH SQGVVTAAAI ATATSWESFA
RAAKEAITML FWIGMRSQQA YPRTSLAPSI LQDSTEAGEG MPTPMLSVRD LSKKQLQEHI
DATNEHLPTD RHIAISLINS ARNFVVTGAP ISLHGLNLRL RKVKAPTGLD QNRIPYTERK
VRFVNRFLPI TAPFHSPLLT EAYKHILEDL SDIKIPASRL TIPVFDTNTG EDLRASQDKD
IVPALVRMIT QDPVHWEQAT VFPGASHILD FGPGGISGLG VLTNRNKDGT GVRVILAGAM
DGTNAEVGYK PELFDRDEEH AVKYAINWVK EHGPRLVKTS VGQIYVDTKM SRLLGVPPLM
VAGMTPCTVP WDFVSATMNA GYHIELAGGG YYNGKSMTEA LTKIEKAIPP GRGITVNLIY
VNPRAMGWQI PLLAQLRADG VPIEGLTIGA GVPSIEVAQE YIDTLGIKHI AFKPGSMDAI
QAVINIAKAN PTFPVILQWT GGRGGGHHSF EDFHQPVLQM YGRIRKCQNI ILVAGSGFGG
SEDTYPYLTG TWAGKFGYPP MPFDGVLFGS RMMTAKEAYT STNAKKAIVE AEGADDSQWE
KTYKGPTGGV ITVRSEMGEP IHKLATRGVK FWAEMDQKIF SLDKKKRVAE LKKQREHIIK
KLNDDFQKVW FGRNFAGETV DLEDMTYAEV VRRMVDLMYI KHQSRWIEVS LRNLTVDFIR
RVEERFTTGA GKPSLIQSYA EFENPFEPLE KVLAAYPEAE SQLINAQDVQ HFLLLCQRRG
QKPVPFVPSL DDNFEFWFKK DSLWQSEDLD AVVDQDVGRT CILQGPMAAK YSTKIDEPVK
DILDGITNDH IQGLVNDVYG GRESSVPVVE YFGGKIISSP ESVTELDGVT VIPDGSRITY
RLSSSPSATL PSIDDWIQLL AGKSYSWRHA LFTTDVFVQG ARYQNNPLKR ILAPTRGLTV
EIAHPKDPSK TSIVVKEPSQ SGKAVKTLDI NLVGKNEILM NMWEERTAEG GAVALPFKFV
YHPETGYAPI HEVMEGRNDR IKEFYYRIWF GEKDVPFDTP TTNKFDGGKA TVVTQDIADF
VHAVGNTGEA FVDRPGKEVF APMDFAIVVG WKAITKPIFP RAIDGDLLKL VHLSNGFRML
PGAEPLKVGD ELHTSARINA VINQEAGKMV EVCGTITRDG KPVMEVTSQF LYRGNYTDYE
NTFQRKDETP VQITLSSSKD VAVLRSKEWF QLDEPDIDLL GQTLTFRLSS LVRFKNRNVF
QSVETVGQVL LELPTKEIIQ VASVEYDAGV SHGNPVVDYL QRHGQTIEQP VNFENAIPLS
GKTPLSLKAP ASNETYARVS GDYNPIHVSR IFASYANLPG TITHGMYSSA AVRSLVETWA
AENNIGRVRS YHVSLVGMVL PNDDLEVKLE HVGMVAGRKI IKIETSNKET GDKVLLAEAE
VEQPVSSYVF TGQGSQEQGM GMDLYGRSEV AKEVWDRADR HFMDNYGLSI INIVKNNPKE
LTIHFGGPRG KAIRQNYMAM TFETINADGS VKSEKIFKEI DENTTSYTYR SPTGLLSATQ
FTQPALTLME KASFEDMRSK GLIQRDSSFA GHSLGEYSAL ASIAEVMPIE SLVSVVFYRG
LTMQVAVERD EQGRSNYSMC AVNPSRISKT FNEQALQYVV ENIAESTGWL VEIVNYNVAN
MQYVCAGDLR ALDCMTNVLN VLKLQKIDIQ ALMQTMSLDD VKAHLMEIIG ECRKKTEAKP
QPIELERGFA VIPLKGIDVP FHSTFLRSGV KPFRSFLLKK INKTSIDPAK LIGKYIPNVT
AKPFEITKEY FEEVYRLTNS PRLAKILEDW DKYENAGGSG IRRLSTVA
//
