ID W6QG31_PENRF Unreviewed; 2082 AA.
AC W6QG31;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Fatty acid synthase subunit beta {ECO:0000313|EMBL:CDM34931.1};
GN Name=FAS1 {ECO:0000313|EMBL:CDM34931.1};
GN ORFNames=PROQFM164_S03g001658 {ECO:0000313|EMBL:CDM34931.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM34931.1};
RN [1] {ECO:0000313|EMBL:CDM34931.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM34931.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
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; HG792017; CDM34931.1; -; Genomic_DNA.
DR STRING; 1365484.W6QG31; -.
DR OMA; HFMDNYG; -.
DR OrthoDB; 5488314at2759; -.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR005562}.
FT DOMAIN 1689..2010
FT /note="Malonyl-CoA:ACP transacylase (MAT)"
FT /evidence="ECO:0000259|SMART:SM00827"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 285
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 2082 AA; 231044 MW; D6419B70B4319714 CRC64;
MYGTLTGPQT GINTPRSSQS LRPLTLSHGS LEFSFLVPTS LHFHASQLKD SFTASLPEPT
DELAQDDEPS SVTELVARYI GHVAHEIEDE DDAQGNYLEV LKLALNEFER AFMRGNDVHA
VAAALPGIVA KKNQVVEAYY AGRAAAGRPT KPYDSALFRA ASDEAAGIYS VFGGQGNIEE
YFDELRNIYT TYPSFVEELI TSSAELLQTL SHEPEASKLY PKGMDILQWL QDRDAQPDID
YLVSAPVSLP LIGLVQLSHY MVTCKVLGRQ PGDILGRFLG TTGHSQGVVT AAAIATATSW
ESFATAARNA LTMLFWIGLR SQQAYPRTSI APSVLQDSVE NGEGTPTPML SIRDLSLAAV
QEHIDATNQH LPEDRHISIS LVNSARNFVV TGPPISLYGL NVRLRKVKAP TGLDQNRVPF
TQRKVRFVNR FLPITAPFHS QYLVSAYDRI LEDLEDVVEI SAKSLEIPVF HTKTGEDLRQ
LGDKDIVPAL VRMITHDAVN WEKATVFPHA THILDFGPGG ISGLGVLTNR NKDGTGVRVI
LAGEMDGTNA EVGYKPELFD RDEHSVKYAV DWVKEHGPRL TKTSTGQTYV DTKMSRLLGI
PPVMVAGMTP TTVAWDFVAA TMNAGYHIEL AGGGYYNAKT MTEAITKIEK AIPPGRGITI
NLIYVNPRAM AWQIPLIGRL RAEGVPIEGL TIGAGVPSIE VANEYIETLG IKHIAFKPGS
VDAIQQVINV AKANPKFPII LQWTGGRGGG HHSFEDFHQP MLQMYSRIRK QDNIVLVAGS
GFGGSQDTYP YLSGTWSAKF GYPPMPFDGC LFGSRMMIAK EAHTSHNAKK AIADAPGVDD
AEWEKTYQKS TGGVITVLSE MGEPIHKLAT RGVLFWQEMD QKIFKLDKAK RVPELKKQRN
YIIKKLNDDF HKVWFGRNAA GETVDLEDMT YAEVVHRMVD LMYIKHESRW IDASLKRLTG
DFIRRVEERF TTAEGQASLL QSYSDLDTPY PTVDNILSAY PEAANQLINA QDVQHFLLLC
QKRGQKPVPF VPVLDENFEF FFKKDSLWQS EDLEAVVDQD VGRTCILQGP VAARFSNIID
EPVKDILDGV HQGHIAGLLR DVYGGDSTKI PVIEYFGGQL TNTTELESDD LVISEEPSKT
SFRLSSTAAL PDLDRWLGLL AGNVYSWRHA LFLADVFVQG HRFQSNPMKR IVAPTAGMYV
EISNPNDPAK TVISVREPYQ SGKLVKTVEA KINEKGQIML TLIEGRTAEN GVVPLNFLFT
YHPETGYAPI REVMGDRNDR IKEFYYRIWF GNKDVPFDTP TTATFSGGQK TITAQDVADF
VHAVGNTSEA FVDRPGKEVF APMDFAIVAG WQAITKPIFP RTIDGDLLKL VHLSNGFKMV
PGAQPLKVGD VLDTTAQINS IINQDSGKMV EVCGTIRRDN KPIMHVTSQF LYRGSYVDYE
NTFQRKDEVP IQVHLATSRD VAILRSKEWF RMDDSDVELL GQTLTFRLQS LIRFKNTTVF
SNVQTVGQVL LELPTKEIIQ VASVEYEAGD SHGNPVIDYL QRNGTSIEQP VYFENPIPLS
GKTALELRAP ASNETYARVS GDYNPIHVSR VFSSYANLPG TITHGMYSSA AVRSLVETWA
AENNIGRVRG FQVSLVGMVL PNDIITVKLQ HVGMIAGRKI IKVEASNKET EEKVMEGEAE
VEQPVTSYVF TGQGSQEQGM GMELYGSSPV AQEVWDRADR HFMENYGLSI IDIVKNNPKE
LTVYFGGPRG KAIRENYMAM TFESVNADGS IKSEKIFKEV DENTASYTYR SPTGLLSATQ
FTQPALTLME KASFEDMRTK GLVQRDSSFA GHSLGEYSAL AALADVMPIE SLVSVVFYRG
LTMQVAVERD AQGRSNYSMC AVNPSRISKT FNEQALQYVV ENISETTGWL LEIVNYNVAN
MQYVAAGDLR ALDCLTNLLN FLKAQNIDIP ALMESMSLED VKDHLVSIIQ ECVKQTEAKP
RPINLERGFA TIPLKGIDVP FHSTFLRSGV KPFRSFLLKK INKTTIDPSK LIGKYIPNVT
ARPFEITKEY FEDVYRLTNS PRIASILANW EKYEEGSENV PK
//
