ID Q0CPX6_ASPTN Unreviewed; 2091 AA.
AC Q0CPX6;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Fatty acid synthase beta subunit dehydratase {ECO:0000313|EMBL:EAU34705.1};
GN ORFNames=ATEG_04258 {ECO:0000313|EMBL:EAU34705.1};
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU34705.1, ECO:0000313|Proteomes:UP000007963};
RN [1] {ECO:0000313|Proteomes:UP000007963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) 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}.
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DR EMBL; CH476599; EAU34705.1; -; Genomic_DNA.
DR RefSeq; XP_001213436.1; XM_001213436.1.
DR STRING; 341663.Q0CPX6; -.
DR EnsemblFungi; EAU34705; EAU34705; ATEG_04258.
DR GeneID; 4319863; -.
DR VEuPathDB; FungiDB:ATEG_04258; -.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR HOGENOM; CLU_000114_5_0_1; -.
DR OMA; HFMDNYG; -.
DR OrthoDB; 5488314at2759; -.
DR Proteomes; UP000007963; 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:UP000007963};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR005562}.
FT DOMAIN 1692..2013
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT ACT_SITE 286
FT /note="For acetyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
FT ACT_SITE 1836
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
SQ SEQUENCE 2091 AA; 232240 MW; 121260E3D798B27D CRC64;
MYGTSTAPQT GINTPRSSQS LRPLILSHGS LEFSFLVPTS IHFHASQLKD TFTASLPQPT
DELAQDEEPS SVAELVARYI GHVAHEVEEG EDDAQGTYLE VLKLALNEFE RAFMRGNDVH
AVAASLPGIT SKKVLVVQAY YAGRAAAGRP TKPYDSALFR AAADEKASIY SVFGGQGNIE
EYFDELREVY TTYPSFVEDL ITSSAELLLS LSREPEANKL YPKGLDIIQW LHDRDSQPDT
DYLVSAPVSL PLIGLVQLAH FVVTCKVLGK EPGDILSRFN GTTGHSQGVV TAAAIASATS
WESFHKAAKN ALTMLFWIGL RSQQAYPRTS IAPSVLQDSI ENGEGTPTPM LSIRDLPRAA
VQEHIDMTNQ HLPEDRHIAI SLVNSARNFV VTGPPLSLYG LNLRLRKVKA PTGLDQNRVP
YTQRKVRFVN RFLPITAPFH SQYLYSAYDR ILEDLEDVEI AGKSLVIPVY GTQSGEDLRA
MGDANIVPAL VRMITHDAVN WEQATVFPSA THILDFGPGG ISGLGVLTNR NKDGTGVRVV
LAGAMDGTNA EVGYKPELFD RDEHAVKYAI DWVKEFGPRL VKNATGQTFV DTKMSRLLGI
PPVMVAGMTP TTVPWDFVAA TMNAGFHIEL AGGGYYNAKT MTEAITKIEK QIPPGRGITV
NLIYVNPRAM AWQIPLIGKL RADGVPIEGL TIGAGVPSIE VANEYIETLG IKHIAFKPGS
VDAIQQVINI AKANPKFPVI LQWTGGRGGG HHSFEDFHQP ILQMYSRIRR YDNIVLVAGS
GFGGSEDTYP YLSGTWSSRF GYPPMPFDGC LFGSRMMIAK EAHTSKNAKK AIADAPGLDD
QDWEKTYKGA AGGVVTVLSE MGEPIHKLAT RGVLFWHEMD QKIFKLDKAK RVPELKKQRD
YIIKKLNDDF QKVWFGRNAA GETVDLEDMT YTEVVHRMVD LMYVKHESRW IDDSLKKLTG
DFIRRVEERF TAGEARPSLL QNYSELDTPY PAIDNILAAY PEAATQLINA QDVQHFLLLC
QRRGQKPVPF VPSLDENFEY WFKKDSLWQS EDLEAVVGQD VGRTCILQGP MAAKFSNVID
EPVYDILNGI HQGHIKSLIK DVYNGDESRV PIIEYFGGHL TEAVEEPDVD GLTISEDGNK
ISYRLSSTPS ANLPDLNRWL HLLAGTSYSW RHAIFMADVY VQGHRFQTNP MKRIVAPTPG
MYVEVVNPND PSKTIISVRE PYQSGKLVKT VEVKMHENNQ IGITLFEGRT AEGGVVPLTF
LFTYHPEAGY APIREVMDSR NDRIKEFYYR IWFGNKDVPF DTPTTATFDG GRETITSQAV
ADFVHAVGNT GEAFVDRPGK EVFAPMDFAI VAGWKAITKP IFPRTIDGDL LKLVHLSNGF
KMVPGAQPLK VGDVLDTTAQ INAVINQESG KMVEVCGTIR RDGKPIMHVT SQFLYRGAYV
DFENTFQRKD EVPMQVHLTS SRDVAILRSK EWFRMDEPEV ELLGQTLTFR LQSLIRFKNK
SVFSHVQTVG QVLLELPTKE VIQVASVDYE AGASHGNPVI DYLERNGTSI EQPVYFENPI
PLSGKTPLTL RAPASNETYA RVSGDYNPIH VSRVFSSYAN LPGTITHGMY SSAAVRSYVE
TWAAENNIGR VRGFHVSLVG MVLPNDMITV KLQHVGMIAG RKIIKVEASN QDTEDKVLLG
EAEVEQPATS YVFTGQGSQE QGMGMELYNN SPVAREVWDR ADRHFIENYG LSIIDIVKNN
PKELTVYFGG PRGKAIRQNY MSMTFETVNA DGTIKSEKIF KEIDESTSSY TYRSPSGLLS
ATQFTQPALT LMEKASFEDM RSKGLVQRDS SFAGHSLGEY SALAALADVM PIESLVSVVF
YRGLTMQVAV ERDEQGRSNY SMCAVNPSRI SKTFNEQGLQ YVVENISEQT GWLLEIVNYN
VANMQYVAAG DLRALDCLTN LLNYLKAQNI DIPALMQSMS LEDVKAHLVK IIQECVKQTE
SKPKPIVLER GFATIPLRGI DVPFHSTFLR SGVKPFRSFL LKKINKTTID PSKLVGKYIP
NVTARPFEIT KEYFEDVYRL TNSPRIAHIL ANWDKYEEGT ESVSRSTGAT A
//
