ID A0A0A1UVB3_9HYPO Unreviewed; 2110 AA.
AC A0A0A1UVB3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Fatty acid synthase beta subunit FAS1B {ECO:0000313|EMBL:EXV00968.1};
GN ORFNames=X797_005990 {ECO:0000313|EMBL:EXV00968.1};
OS Metarhizium robertsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=568076 {ECO:0000313|EMBL:EXV00968.1, ECO:0000313|Proteomes:UP000030151};
RN [1] {ECO:0000313|EMBL:EXV00968.1, ECO:0000313|Proteomes:UP000030151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2575 {ECO:0000313|EMBL:EXV00968.1,
RC ECO:0000313|Proteomes:UP000030151};
RA Giuliano Garisto Donzelli B., Roe B.A., Macmil S.L., Krasnoff S.B.,
RA Gibson D.M.;
RT "The genome sequence of the entomopathogenic fungus Metarhizium robertsii
RT ARSEF 2575.";
RL Submitted (FEB-2014) 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 -!- 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:EXV00968.1}.
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DR EMBL; JELW01000010; EXV00968.1; -; Genomic_DNA.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR HOGENOM; CLU_000114_5_0_1; -.
DR OrthoDB; 5488314at2759; -.
DR Proteomes; UP000030151; 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; 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 Transferase {ECO:0000256|PIRNR:PIRNR005562}.
FT DOMAIN 1695..2055
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT REGION 2089..2110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1956..1983
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 1847
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
SQ SEQUENCE 2110 AA; 233938 MW; 62EF96236DF36CB5 CRC64;
MYGTGTGPQT GISTPRSSAS LRPLTLIHGS LETSFLVPTS LHFHASQIKD RFVASLPTAT
DELAQDDEPS SVAELVARYL GFVAKEVEDG EDDAQGSYEE VLKLVLNEFE RAFLRGNEVH
AIAAALPGIE MKKLEVIRSY YMARAVSNRT IKPHESALFR AAGDGSADIY TIFGGQGNIE
EYFDELRQVF QTYSSFIGEL VTSAAEQLRT LSTNPSAEKM FPKGLDIMNW LQHPDSTPDV
EYLISAPVSF PLIGLVQMAH YEVTCKTLGV HPGMLRERIS GSTGHSQGIV MAAATSAADD
WESWREIVSS TLSILFWVGT RSQQAFPTTS MTPTMLRESI EHGEGNPTPM LSIRDLSQQE
VQKHIDATNQ YLPPHRHINI SLINSPRNLV VTGPPTSLYG LNSRLRKVKA PTGLDQTRVP
YTDRKVRFVN RFLPITAPFH SKYLAEATEM IDADLKNISI DAEDLGIPVF DTNTGKDLRT
EVKGNIVPAL VRLITRDPVN WEKATIFPDA THILDFGPGG VSGLGTLTSR NKEGTGVRVI
LAGTIEGTMN EVGYKPEIFD RDEENALRYA IDWVKEFGPR LVKTSGGRKY LDTKMSRLLG
LPPIVVAGMT PCTVPWDFVA ATMNAGYHIE LAGGGYFMPG MMTDALLKIE KAIPSGRGIT
VNLIYVNPRA MAWQIPLLGK LRAEGVPIEG LTIGAGVPSI EVAQEYIETL GLKHIGFKPG
SVEAIQAVVN IAKANPNFPV LLQWTGGRGG GHHSFEDFHQ PILQMYGRIR RQENIILVAG
SGFGGAEDTY PYITGDWAKK YGYPPMPFDG CLFGSRMMVA KEAHTSKDAK QAIIDAPGLV
DSEWEKTYKG PAGGVITVRS EMGEPIHKLA TRGVRFWAEM DQKIFGLPKE KRVAELKKNR
DYIIKRLNDD FQKVWFGCNK QGKACDLEDM TYGEVVRRMV ELLYVKHQQR WIDPTYVKLT
GDFIHRVEER FTSTAGKASL LQNYADLNEP FSTVERILSH YPEAETQIIN AQDVQHFLML
CLQPTQKPVT FIPSLDDNFE FFFKKDSLWQ SEDLDAVIGQ DVGRTCILQG PAAVKYSTVV
DEPIKDILDG IHESHIKMLT RDMYNNEEGS IPFVEYFGGK LVESEIPLDV EGLTVAYDTH
KNTYRLSSAA SASLPSLESW LALLAGPNRN WRHALLMSDV VVQGQKFQTN PLKRIFAPTR
GLFVEIQYPN DPSKTTIIVR EQPRHNQYVD VIEVKLVGKN EILVNLIKDT TALGRPVAMP
LKFTYNPEAG YAPIREVMTD RNDRIKEFYW KAWFGEEPLN LDALITSTFD GGRTTITSEA
INDFVHAVGN TGEAFVDRPG KIVYAPMDFA IVVGWKAITK PIFPRTIDGD LLKLVHLSNQ
FRMIPGAEPL KKGDEVATTA QVNAVINQEA GKMVEVCGTI SRDGKPVMEV TSQFLYRGKY
SDYENTFQRK IETPVQVHLA TTKDVAVLRS KQWFNSDELP SDIDLLGQTL TFKLQSLVRY
KNKNVLSSAE TRGQVLLELP TKEVIQVASV DYEAGESHGN PVMDYLERHG SPLDQPILFE
NPIPLSGKTP LQLRAPSSNE TYARVSGDYN PIHVSRVFST YANLPGTITH GMYSSAAVRS
LVETWAAEND IGRVRSFQAT FAGMVLPNDD IQVKLQHVGM VAGRKIIKVE VSNTESEEKV
LLGEAEVEQP VTAYVFTGQG SQEQGMGMEL YGSSPVAKEV WDRADKYLLD NYDAAANQGP
GFSITNIVKN NPKELTIHFG GPRGKAIRQN YMAMTFETVA ADGSIKSERI FKEIDESTTS
YTYRSPTGLL SATQFTQPAL TLMEKASFED MKSKGLVPRD STFAGHSLGE YSALAALADV
MPIESLVSVV FYRGLTMQVA VERDAAGRSN YSMCAVNPSR ISKTFNEEAL QFVVNNIAEE
TGWLLEIVNY NIANMQYVCA GDLRALDTLA GVTNFLKMQQ IDIEQMRSNI EEAKDALRKI
IRGCAEATLK KPLPLELERG FATIPLRGID VPFHSTFLRS GVKPFRSFLL KKINKTTIDP
SKLVGKYIPN VTAKPFELTK EYFEDVYKLT NSPKIGAVLA NWDKYTQEDE SKAVSDSSSS
VGYDGPGAAA
//
