ID T5A2W2_OPHSC Unreviewed; 2092 AA.
AC T5A2W2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Fatty acid synthase beta subunit dehydratase {ECO:0000313|EMBL:EQK99784.1};
GN ORFNames=OCS_04503 {ECO:0000313|EMBL:EQK99784.1};
OS Ophiocordyceps sinensis (strain Co18 / CGMCC 3.14243) (Yarsagumba
OS caterpillar fungus) (Hirsutella sinensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=911162 {ECO:0000313|EMBL:EQK99784.1, ECO:0000313|Proteomes:UP000019374};
RN [1] {ECO:0000313|EMBL:EQK99784.1, ECO:0000313|Proteomes:UP000019374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Co18 / CGMCC 3.14243 {ECO:0000313|Proteomes:UP000019374};
RC TISSUE=Fruit-body {ECO:0000313|EMBL:EQK99784.1};
RX DOI=10.1007/s11434-013-5929-5;
RA Hu X., Zhang Y., Xiao G., Zheng P., Xia Y., Zhang X., St Leger R.J.,
RA Liu X., Wang C.;
RT "Genome survey uncovers the secrets of sex and lifestyle in caterpillar
RT fungus.";
RL Chin. Sci. Bull. 58:2846-2854(2013).
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}.
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; KE653158; EQK99784.1; -; Genomic_DNA.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR HOGENOM; CLU_000114_5_0_1; -.
DR Proteomes; UP000019374; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000019374};
KW Transferase {ECO:0000256|PIRNR:PIRNR005562}.
FT DOMAIN 1686..1976
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT REGION 2070..2092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1939..1966
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 286
FT /note="For acetyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
FT ACT_SITE 1830
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
SQ SEQUENCE 2092 AA; 231967 MW; 2FEBE91BFBA0FA82 CRC64;
MYGTGTGPQT GLSTPRSNNS LRPLTLIHGS LETSFLVPTS LHFHASQLKD RFVASLPAAT
DELAQDDEPS SVPELVARYL GFVAREVEDG EDDTQGSYEE VLKLVLNEFE RAFLRGNEAH
AIAATLPGIE AKKLEVIRSY YLARAVSNRT IKPHESALLR ASDDGSAEIY TIFGGQGNIE
EYFEELREAF QTYPSFVGEL ITSAAEQLQT LSNHPSAEKM FPKGLDIMSW LQHPDSTPDV
EYLISAPVSF PLISLVQMAH YEVACKVLGI DPGQFRERIS GTTGHSQGIV MAAATAAADS
WDSWRAIVSS TLAILFWIGT RSQQAFPTTS MTPTMLRESM DNGEGSPTPM LSIRDLSQQE
VQKHIDATNQ YLPSHRHISV SLVNSPRNLV VTGPPTSLYG LNSQLRKVKA PTGLDQTRVP
YTERKVRFVN RFLPITAPFH SKYLAEATAM IDEDLKDVRI DSGSLRIPVF DTNTGEDLRA
QVKGNVVPAL VRLITRDPVN WEKATVFPGA THVLDFGPGG VSGLGILTSR NKEGTGVRVI
LAGTVDGTIT EVGYKPELFD RDEENAVRYA IDWVKEFGPR LVKTSSGRKY VDTKMSRLLG
LPPIMVAGMT PCTVPWDFVA ATMNAGYHIE LGGGGYFNAK RMTDALTKIE NAIPSGRGIA
VNLLYVNPRA LAWQIPLLGR LRSEGVPIEG LAIGAGVPSI EVAQEYIETL GLKHIAFKPG
SVDAIQAVIN IAKANPSFPV ILQWTGGRGG GHHSFEDFHQ PVLQMYNRIR RQENIILVAG
SGFGGAEDTY PYITGPFPFD GCLFGSRMMV AKEAHTSKDA KQAIIDAPGL DDGEWEKTYK
GPAGGVITVR SEMGEPIHKL ATRGVRFWSE MDRKIFSLPK EKRVAELKKS REYIIKKLND
DFQKVWFGCN KAGKSVDLED MTYAEVVRRL VELLFVKHQS RWIDPSFARL AGDFIHRVEE
RFTVSPGQPS LLQNYSDLDE PFSTVDRILA KYPDAETQII NAQDVQHFLL LCMRPGQKPV
TFIPALDENF EYFFKKDSLW QSEDLDAVIG QDVERTCILQ GPMAARFSTI VDEPVKDILD
GIHNAHIAAL ERDYYNNDES SIPAVEYFGG KLVESEIPLD VEGLTVNYDT RKNTYRLSSS
ATAAMPSVDS WLTLLAGPNR NWRYALLMSE IVAQGQKFQT NPMRRIFAPT RGLFVEIQYP
NEPQKTAIIV REQPRHNQYV DVIEVRLTGK NEILVNMVKD TTAVGKPVAL PLKFTYHPEA
GYAPIREVMQ DRNDRIKEFY WKAWFGNDPL DLDAVVTSKF DGGRTTITKE AIRDFVHAVG
NTGEAFVDRP GKIVYAPMDF AIVVGWKAIT KPIFPRTIDG DLLKLVHLSN RFRMIPGAEP
LKEGDEISTT AQINAVINQE SGKMVEVCGT IARDGQPVME VTSQFLYRGM YSDYENTFQR
KVETPVQVYL ATSKDVAVLR SKHWFAIDEV PSDIDLLGQT LTFRLQSLMR YRNRDVFSSV
ETRGQVLLEL PTKEVIQVAS VDYEAGESHG NPVIDYLERN GSPLDQPINF DHPIPLSGKT
PLQLRAPASN ETYARVSGDY NPIHVSRVFS SYANLPGTIT HGMYSSAAVR SLVETWAAEN
DIGRVRSFHA SLVGMVLPND AIQVKLQHVG MVAGRKIVKV EVSNTETEEK VLLGEAEIEQ
PVTAYVFTGQ GSQEQGMGME LYASSPVAKE VWDRADKYLL DNYGFSITNI VKNNPKEHTI
HFGGPRGKAI RQNYMAMTFE TVATDSSIKS ERIFKDINES TTSYTYRSPT GLLSATQFTQ
PALTLMEKAS FEDMKAKGLV PRDSTFAGHS LGEYSALAAL ADVMPIESLV SVVFYRGLTM
QVAVERDASG RSNYSMCAVN PSRISKTFNE EALQFVVNNI AEETGWLLEI VNYNIANMQY
VCAGDLRALD TLAGVTNFVK KQQIDIEEMR SNIEEAKGAL REIIRGCAEA TLRKPQPLEL
DRGFATIPLR GIDVPFHSTF LRSGVKPFRS FLLKKINKTT IDPSKLVGKY IPNVTAKPFA
LSKEYFEEVY KLTNSPKIGA VLANWDKYAQ DDGKASSDSG ASVEYEGPGA AA
//
