ID D4DIB4_TRIVH Unreviewed; 2111 AA.
AC D4DIB4;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Malonyl-CoA:ACP transacylase (MAT) domain-containing protein {ECO:0000259|SMART:SM00827};
GN ORFNames=TRV_06922 {ECO:0000313|EMBL:EFE38406.1};
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE38406.1, ECO:0000313|Proteomes:UP000008383};
RN [1] {ECO:0000313|Proteomes:UP000008383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(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 -!- 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}.
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:EFE38406.1}.
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DR EMBL; ACYE01000402; EFE38406.1; -; Genomic_DNA.
DR RefSeq; XP_003019051.1; XM_003019005.1.
DR GeneID; 9582540; -.
DR KEGG; tve:TRV_06922; -.
DR HOGENOM; CLU_000114_5_0_1; -.
DR OrthoDB; 5488314at2759; -.
DR Proteomes; UP000008383; 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; SSF51395; FMN-linked oxidoreductases; 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|PIRNR:PIRNR005562}.
FT DOMAIN 1693..2034
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 ACT_SITE 286
FT /note="For acetyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
FT ACT_SITE 1837
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
SQ SEQUENCE 2111 AA; 234518 MW; 84CC8DAF2DB773F3 CRC64;
MFGPSTGPQT GINTPRSSQS LRPLNLSHGS LEFSFLVATS LHFHASQLKD SFAASLPEPT
DELAQDDEPS SVPDLVARYL GFIAHEVEEG EDDSLGSYIE VLKLVLNEFE RAFMRGNDVH
AVAGSIPGIP AKKLLMVENY YAARAAVNRP TKPHDSALLR AAMEGNAKLY SIYGGQGNIE
EYFDELREIY NTYPSFVEDL ISSSAELLQS LARDLDAIKL YSKGMDILRW LHDRDTQPDT
DYLVSAPVSL PLIGLVQLAH FMATCKAMGK EPGDVLDTFS GTTGHSQGII TAAAIATVTT
WESFAKAARA ALTMLFWIGL RSQQAYPRTS LAPSLLQDSI ENGEGIPTPM LSIRDLHRSA
VQEHIDATNQ HLPEDRHIAI SLVNSPRNFV VTGPPISLYG LNLRLRKVKA ATGLDQNRVP
FTQRKIRFVN RFLPITAPFH SQYLASAFEA IAEDVEDIKI PARSLRIPVY DTNTGKDISK
LGDEDIVPAL IRMITSDPVD WEKATVFSKA THIVDFGPGG ISGLGVLTNR NKDGTGVRVI
LGGLIDGTNA EVGYKPELFD RDEDHAVKYA VDWVEVYGPR LVKTSVGQTF VDTKMSRLLG
VPPIMVAGMT PTTVPWDFVA ATMNAGYQIE LGGGGYYNAK SMAAALTKIE KAIPPGRGIT
VNLIYVNPRA MAWQIPLLAK LRADGVPIEG LVIGAGVPSI EVANEYIETL GIKHIGFKPG
SLDAIQQVIN IAKANPSFPV ILQWTGGRGG GHHSFEDFHQ PVLQMYSRIR KCDNIVLVAG
SGFGGSTDTY PYLTGTWSRQ FGYPPMPFDG CLFGSRMMVA KEAHTSKAAK EAIVAAPGVD
DAKWEDTYKG AAGGVITVRS EMGEPIHKLA TRGVLFWAEM DQKIFSLDKA KRLPALKKHR
EYIIKKLNDD FQKVWFGRNS KGVTVDLEDM TYAEVVHRMV ELMYVKHEAR WIDDSLKRFT
GDFLRRVEER FATEKNRESR LQSYSQLDTP YPTVQEILDA YPASADQLIN AQDVQHFLQL
CQRRGQKPVP FVPSLDENFE FWFKKDSLWQ SEDIEAVVGQ DVGRVCILQG PMAAKYSTVI
DEPIKSILDG IHQDHIKGLI QDVYNGDESK VPTVEYFGGR LALVDDEDRD IDGLTISEDA
TRVSYRLSSS PSANLPELDR WLHLLAGNIY SWRYALFTTE VFIQGQRFQT NPIKRILAPT
RGMFVEITNP NDSLKTVISM REPCQSGKLV KTVEIRLVEK NRIALTLFEG RTAESGVVPL
PFYFTYHPET GYAPIREVME GRNDRIKEFY YRVWFGERTV PFDTPAAAIF DGGRTTVTAQ
AIADFVHAVG NTGEAFVERQ GKETFAPMDF AIVAGWKAIT KPIFPRTIDG DLLKLVHLSN
GFRMVPGAEP LKVGDILDTT AQINAIVNQD SGKMVEVCGT IKRDGEPIMH VTSQFLYRGN
YTDYETTFLR KDEVPMQVHL ATSKDVAVLQ SKEWFRLDEG NVELLGQTLT FRLQSLVRYK
DKTVFQNMQT TGQVLVELPT KEIIQVGSVD YDAGVSHGNP VIDYLQRHGS AIEQPVNFEN
PIPLSKSPLV LKAPASNETY ARVSGDYNPI HVSRVFSSYA NLPGTITHGM YTSAAVRSLV
ETWAAENNIG RVRSFHASLV GMVLPNDDLV VKLQHVGMIA GRKIIQVEAS NQNTEEKVLI
GEAEVEQPVS SYVFTGQGSQ EQGMGMDLYA TSPVAKEVWD RADRHFMENY GFSIIDIVKN
NPQELTVHFG GPRGKNIRQN YMSMTFETVN ADGSIKSEKI FKEVDEKTSS YTYKSPTGLL
SATQFTQPAL TLMEKASFED MRSKGLVQRD SSFAGHSLGE YSALAALAEV MPIESLVSVV
FYRGLTMQVA VERDEQGRSN YSMCAVNPSR ISQTFNEQAL QYVVENVSET TGWLLEIVNY
NVANMQYVCA GDVSLPKKGY NHFKTDILIS LQLRALDSLT NVLNVLKAQK IDIPALMQTM
SLEDVKSHLV QIIDECVKQT NAKPQPIVLE RGFATIPLKG IDVPFHSTFL RSGVKPFRSF
LLKKINKTTI DPSKLIGKYI PNVTARPFEL TREYFEDVYR LTNSPRIGNI LANWDKYEEP
QDTPAESTDS P
//
