ID F0X8I7_GROCL Unreviewed; 2098 AA.
AC F0X8I7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Fatty acid synthase beta subunit dehydratase {ECO:0000313|EMBL:EFX05327.1};
GN ORFNames=CMQ_3396 {ECO:0000313|EMBL:EFX05327.1};
OS Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS (Graphiocladiella clavigera).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN [1] {ECO:0000313|EMBL:EFX05327.1, ECO:0000313|Proteomes:UP000007796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
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 -!- 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; GL629735; EFX05327.1; -; Genomic_DNA.
DR RefSeq; XP_014174809.1; XM_014319334.1.
DR STRING; 655863.F0X8I7; -.
DR GeneID; 25976491; -.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR HOGENOM; CLU_000114_5_0_1; -.
DR InParanoid; F0X8I7; -.
DR OrthoDB; 5488314at2759; -.
DR Proteomes; UP000007796; 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; 3.30.70.2430; -; 1.
DR Gene3D; 6.10.140.1400; -; 1.
DR Gene3D; 6.10.250.1850; -; 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:UP000007796};
KW Transferase {ECO:0000256|PIRNR:PIRNR005562}.
FT DOMAIN 1694..2015
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 286
FT /note="For acetyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
FT ACT_SITE 1838
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
SQ SEQUENCE 2098 AA; 233672 MW; 9E230295CAA8F310 CRC64;
MYGTGTGPHT GVSTPRTSSS LRPLTISHGS LETSFLIPTS LHFHASRLKE AFAVTLPAPT
DELAQDDEPS SIPELVARYM GFIAHEVEQG EDDAQGSYEE VLKLILNDFE RVFLRGNEVH
VIAAGLPGID AKKLVLLRSY YAARLVSNRT IRPHVSALFR AADDGSANLY SIFGGQGNIE
EYFEELRELF ETYPAFVGDL ISNSAELLQN LSKHPNAEKL YSKGLDVMTW LRHPETTPDV
DYLVSAPVSF PLIGLVQLAH YEVTCKVLGT HPGLLRERIQ GTTGHSQGIV LAAITAAADS
WESYAELAKS ALSILFWIGA RSQQTFPRTS ITPSMLQDSI DNGEGIPTPM LSIRDLSQGE
VQKHIDATNQ YLPADRHIAV SLVNSPRNLV VTGPPISLYG LNLQLRKVKA PTGLEQTRIP
YTERKVRFVN RFLPITAPFH SQYLEKATTL INEDLAGIQI DSKTLGTAVF DTNTGKDMRR
SVRGNIVPTL VRLITRDPVY WELATAFPEA THVLDFGPGG ISGLGILTSR NKEGTGVRVI
LAGSVTGTVS EVGYKPELFD RDEENAVKYA IDWVREYGPK LVKTKSGKTY VDTKMSRLLG
LPPVMVAGMT PTTVAWDFVA AAMNAGYHIE LGGGGYYSAK TMTENLLKIE GAIKAGRGIS
INLIYVNPHA MAWQIPLIGR LRAEGVPIEG LTIGAGVPSI EVAQEYIETL GLKHIAFKPG
SMDAIQSVIN IAKANPKFPV ILQWTGGRGG GHHSFEDFHQ PILQMYSRIR RSDNIILVAG
SGFGGTEDTY PYITGAWSKK YGYPPMPFDG CLFGSRMMVS KEAHTSKNAK KAIVDAEGLD
DSEWEKTYKG AAGGVITVRS EMGEPIHKLA TRGVRFWAEM DQKIFTLPKE KRIVELKKNR
DYIIKKLNDD FQKVWFGRNK AGETVDLEDM TYGEVVRRMV ELLYVKHEKR WIDPSFETLT
GDFIHRVEER FTATSNQLSR LQSYSDLDEP YSAIEDILSH YPEAENQIIN AQDVQHFLLL
CQRRGQKPVT FVPALDENFE FFFKKDSLWQ SEDLEAVIGQ DVGRTCILQG PAAVRYSKVV
DEPIQDILDG IHEGHIAGLT KDVYNGDVSA IPTIEYFGGK WTESDVPVDL ESVSESYDEH
KNIYRIAYAA NVSLPPVDEW LSLIAGKSHS WRHALLLSDV LVQGKKYQTN PIKRVFAPVR
GLFVEIRYPN EPDKTEIIVK EQPRQNHYVD VVHVKLSAEN EIVVNVIKQT SALGKPVNLP
LKFRYRPEAG YAPIHEVMED RNERIKKFYW RVWFGDEPID LNADVRGKFD GGKAMIAGED
INDFVHAVGN TGEAFVDREG KEMFAPMDFA IVVGWKAITK PIFPQTIDGD LLKLVHLSNE
FRMLPGADPL KKGDEVSTTA RVNAVINQES GKMVEVCGTI EREGKAVMEV TSQFLYRGEY
TDFENTFQRK IEKPVQIHLA TSKEVAVLRS KQWFVLNDQH DIPLLGQTLT FRLESLMKFK
NKTVFSSVET RGQVLLELPT KEVVQVASVE YEAGVSNGNP VIDYLERNGS AIEQPINFEN
PIPLSGKSPL VLRAPASNET YARVSGDYNP IHVSRVFANY ANLPGTITHG MYSSAAVRSL
VETWAAENDI GRVRSFHASL VGMVLPNDDI NVKLQHVGMI SGRKIVKVEA VNKETEEKVL
LGEAEIEQPV TAYVFTGQGS QEQGMGMDLY DSSPVAKDVW DRADKYLMET YGFAITNIVK
NNPKELTIHF GGPRGKQIRQ NYMTMTFETV MADGSIKSER IFKDINETTL SYTYRSPTGL
LSATQFTQPA LTLMEKASFE DMKAKGLVPR DSTFAGHSLG EYSALAALAD VMPIESLVSV
VFYRGLTMQV AVERDASGRS NYSMCAVNPS RISKTFNEEA LRFVVNSIAE ETKWLLEIVN
FNIANMQYVC AGDLRALDTL AGVTNFLKVQ KIDIDQMKAQ LKLEEVREHL NEIIRGCAQE
TEKKPKPLEL ERGFATIPLR GIDVPFHSTF LRSGVKPFRS FLLKKINKTT IDPAKLIGKY
IPNVTARPFE LTKEYFEDVY RLTNSPRIGH VLANWDKYQD DGVANGVSGT QSEELSEA
//
