ID W9YMG0_9EURO Unreviewed; 2088 AA.
AC W9YMG0;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Fatty acid synthase subunit beta {ECO:0000313|EMBL:EXJ90406.1};
GN ORFNames=A1O1_03507 {ECO:0000313|EMBL:EXJ90406.1};
OS Capronia coronata CBS 617.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ90406.1, ECO:0000313|Proteomes:UP000019484};
RN [1] {ECO:0000313|EMBL:EXJ90406.1, ECO:0000313|Proteomes:UP000019484}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ90406.1,
RC ECO:0000313|Proteomes:UP000019484};
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 Capronia coronata CBS 617.96.";
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:EXJ90406.1}.
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DR EMBL; AMWN01000003; EXJ90406.1; -; Genomic_DNA.
DR RefSeq; XP_007722600.1; XM_007724410.1.
DR STRING; 1182541.W9YMG0; -.
DR GeneID; 19158399; -.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR HOGENOM; CLU_000114_5_0_1; -.
DR OrthoDB; 5488314at2759; -.
DR Proteomes; UP000019484; 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; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 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:UP000019484};
KW Transferase {ECO:0000256|PIRNR:PIRNR005562}.
FT DOMAIN 181..572
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 232150 MW; E2D4EEB573B328EF CRC64;
MYSGGATGTH TPRSSQNLRP LSLTHGSLEY SFLIPTALHF QAAQLHDTFK ASLPEPTDEL
AQDEEPSSRA ELVARFIGFI AAELDEDEEA SGFVEVLKVV LNEFERSFMH ANDVHALAAT
LPGITAKKLE VVKCYYAGRA AVARPIKPHD SALFRAADDE EASIYTVFGG QGNIEEYFDE
LREIYNTYPS FTKDLIEASA ELLQNLARSP KADKFYSKGL DILRWLEDRE TQPDTDYLVS
APVSLPLIGL VQLAHYQVTC KVLGRTPGEI NEHFNGTTGH SQGVVTAAAI ATATSWESFS
KVARDAITML FWIGMRSQQA YPRTSIAPSI LQDSLEAGEG VPTPMLSVRD LSLKQLQEHI
DATNEHLPPD RHIAISLINS ARNFVVTGAP ISLHGLNLRL RKVKAPTGLD QNRIPYTERK
VRFVNRFLPI TAPFHSPLLS EAFKTIKEDL SEIRVPASRL NIPVFDTNTG EDLRAQHDKD
IVPSLVRMIT QDPVHWEQAT VFENATHILD FGPGGISGLG VLTNRNKDGT GVRVILAGAM
DGTNAEVGYK PELFDRDEEH AVKYATNWVK EHGPKLVKTS VGQTYVDTKM SRLLGVPPLM
VAGMTPTTVP WDFVAATMNA GYHIELAGGG YYNAKTMTEA LTKIEKSIPP GRGITVNLIY
VNPRAMGWQI PLLGQLRADG VPIEGLTIGA GVPSIEVAQE YIDTLGIKHI SFKPGSMDAI
QAVINIAKAN PTFPVILQWT GGRGGGHHSF EDFHQPILLM YGRIRKCQNI ILVAGSGFGG
SEDTYPYLTG AWSRKFGYPP MPYDGFLFGS RMMTAKEAHT SYNAKKAIVE APGVDDTEWE
KTYKGPAGGV ITVRSEMGEP IHKLATRGVK FWAEMDQKIF SLDKKKRVAE LKKQRDYIIK
KLNDDFQKVW FGRNAAGETV DLEDMTYAEV VRRMVELMYV KHQSRWIDTS LRNLTVDFIR
RVEERFTVGS GKPSLIQSYA ELETPFVVVE KVLAAYPTAE TQLISAQDVQ HFLLLCQRRG
QKPVPFVPSL DENFEFWFKK DSLWQAEDLD AVVDQDVGRT CILQGPMAAK YSTKIDEPVK
DILDGIHNAH IKGLVQDVYG GRESAVPVVE YFGGKIINSP ESVVELDGVT VIPDGSRTTY
RLSQSPSAPL PDADSWTQLL AGKTYSWRHA LFTTDVFVQG ARYQNNPLKR ILAPIRGMTV
EIAHPKDPSK TTIVVKEPNQ SGQMAKTLDI GLVGKNEILM NMWKEDTAEG EPVALPLRFI
YHPETGYAPI HEVMEGRNDR IKEFYYRIWF GEKDVPFDIP TTNTFDGGKA TVNAQGIADF
VHAVGNTAEA FVDRPGKEVF APMDFAIVVG WKAITKPIFP RLIDGDLLKL VHLSNGFRML
PGAEPLKVGD DLHTTARINA VINQESGKMV EVCGTITRQG HPVMEVTSQF LYRGNYTDYE
NTFQRKDETP MQVTLATSKD VSVLRSKEWF HLDEPDIDLL GQTLTFRLSS LIRFKNKTVF
ENVETVGQVL LELPSREVIQ VASVEYDAGA SHGNPVVDYL QRHGQSIEQP VNFENPIPLS
GKTPLSLKAP ASNETYARVS GDYNPIHVSR LFASYANLPG TITHGMYSSA AVRSLVETWA
AENNIGRVRS YHVSLVGMVL PNDDLEVKLE HVGMIAGRKI IKIETSNKET GDKVLLAEAE
VEQPVSSYVF TGQGSQEQGM GMDLYARSAV AKEVWDRADR HFLDNYGLSI INIVKNNPKE
LTVHFGGPRG KAIRQNYMAM TFETVNADGS IKSEKIFKEI NEKTTSYTYR SPTGLLSATQ
FTQPALTLME KASFEDMRSK GLIQRDSSFA GHSLGEYSAL ASIAEVMPIE SLVSVVFYRG
LTMQVAVERD EQGRSNYSMC AVNPSRISKT FNEQALQYVV ENIAETTGWL IEIVNYNVAN
MQYVCAGDLR ALDCMTNVLN VLKLQKIDIQ ALMQQMSLED VKAHLVDIIG ECRKKTDAKP
QPIELERGFA VIPLKGIDVP FHSTFLRSGV KPFRSFLLKK INKTSIDPAK LIGKYIPNVT
ARPFEITKEY FEEVYRLTNS PRLAKILEDW DKYENASEAG TRRLSTVA
//
