ID A6RDC9_AJECN Unreviewed; 2082 AA.
AC A6RDC9;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Fatty acid synthase beta subunit dehydratase {ECO:0000313|EMBL:EDN11184.1};
GN ORFNames=HCAG_07637 {ECO:0000313|EMBL:EDN11184.1};
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN11184.1, ECO:0000313|Proteomes:UP000009297};
RN [1] {ECO:0000313|Proteomes:UP000009297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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; CH476663; EDN11184.1; -; Genomic_DNA.
DR STRING; 339724.A6RDC9; -.
DR VEuPathDB; FungiDB:HCAG_07637; -.
DR HOGENOM; CLU_000114_5_0_1; -.
DR OMA; HFMDNYG; -.
DR OrthoDB; 5488314at2759; -.
DR Proteomes; UP000009297; 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 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:UP000009297};
KW Transferase {ECO:0000256|PIRNR:PIRNR005562}.
FT DOMAIN 1693..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 1837
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR005562-1"
SQ SEQUENCE 2082 AA; 231313 MW; A0F81174271CF030 CRC64;
MYGTSTGPQT GINTPRSSQS LRPLILSHGS LEFSFLVPTS LHFHAQQLRD SFSASLPAPT
DELAQDDEPS SVQELVARYL GYVASQVEEG EDDAQGSYVE VLKLVLNEFE RAFMRGNDVH
AIASTLPGIT AKKLLVVQSY YAGRAAANRP TKPHDSALLR AAADGNAQLY SVYGGQGNIE
EYFDELREIY TTYPSFVEDF IASSAELLQS LSRDPDAIKL YSKGMDIVRW LEDRDSQPDT
DYLVSAPVSL PLIGLVQLAH YVTTCKVMGK QPGEVLERFS GTTGHSQGIV TAALIATATT
WDTFYKASKS ALTILFWIGM RSQQAYPRTS LAPSILQDSV ENGEGVPTPM LSIRDLARSA
VQEHIDATNQ HLPQDRHIAI SLVNSARNFV VTGPPISLYG LNLRLRKVKA PTGLDQTRVP
YTQRKVRFVN RFLPITAPFH SQYLASAFEQ ITEDLEDLAI PSKSLRIPVY DTNTGEDLRD
RDEDIVPALI RMITRDPVNW EKATVFPKAT HVLDFGPGGI SGLGVLTNRN KDGTGVRVIL
SGAMDGTNAE VGYKPELFDR DEEHAVKYAV DWVKEHGPRL VKTSVGQTFV DTKMSRLLGV
PPVMVAGMTP TTVPWDFVAA TMNAGYQIEL AGGGYYNAKT MTEALNKIEK NIPPGRGITV
NLIYVNPRAM GWQIPLIGKL RADGVPIEGL TIGAGVPSIE VANEYIQTLG IKHIGFKPGS
MDAIQQVINI AKANPTFPVI MQWTGGRGGG HHSFEDFHQP ILQMYSRIRR CDNIVLVAGS
GFGGSQDTYP YLTGSWSREF GYPPMPFDGC LFGSRMMTAK EAHTSKAAKQ AIVEAEGVDD
SRWEDTYSGP AGGVITVRSE MGEPIHKLAT RGVRFWHEMD QKIFSLDKAK RLPELKKQRD
YIIKKLNADF QKVWFGRNSQ GDTVDLEDMT YTEVVHRMVD LMYVKHESRW IDDSLKRLTG
DFIRRIEERF TSVEGQPSLL QNYTQLDTPY PAVDNILNAY PEATSQLISA QDVQHFLLLC
QRRGQKPVPF VPSLDENFEF WFKKDSLWQS EDLEAVVGQD VGRVCILQGP MAAKYSNTID
EPVKDILDGI HNDHIKGLVN DVYGGNESNV PVIEYFGGQL LLETDGESDI DGLTVSEDAT
KVSYRLSPST SANLPDLDRW LHLLAGRTYS WRYAMFTTEV FIQGQKFQTN PMKRILAPTP
GMFVEIQYPN DSRKTIISVR EPSPAGKLVK TVEVRTNGER EISLTLFEGR TAEGGVVPLC
FRFTYHPETG YAPIREVMDD RNDRIKEFYY RIWFGERNVP FDTPATAIFD GGKATVTSQA
IADFVHAVGN TGEAFVDRPG KEVFAPMDFA IVVGWKAITK PIFPRVIDGD LLKLVHLSNG
FRMIPGSEPL KVGDVLETTA QVNAVINQDS GKMVEVCGTI RREGKPIMEV TSQFLYRGSY
NDYETTFQRK EEVPMQIHLA SSKDVAVLQS KEWFRLDEPD VDLLGQTLTF RLQSLVRFKN
QTIFSSVQTI GQVLLELPTK EVIQVASVEY EAGTSHGNPV IDYLQRHGSA IEQPVNFENP
IPLSGKTPLT LRAPASNETY ARVSGDYNPI HVSRVFSSYA NLPGTITHGM YTSAAVRSLV
ETWAAENNIG RVRSFHASLV GMVLPNDDLV VVLQHIGMVA GRKIIKVEAS NQATEEKVLL
GEAEVEQPVS AYVFTGQGSQ EQGMGMDLYN SSAVAKEVWD RADKHFIENY GLSIINIVKN
NPQELTIHFG GPRGKIIRQN YMAMTFETVN ADGTIKSEKI FKDIDENSIS YTYRSPTGLL
SATQFTQPAL TLMEKASFED MRSKGLVQRD SSFAGHSLGE YSALAALADV MPIESLVSVV
FYRGLTMQVA VERDELGRSN YSMCAVNPSR ISKTFNEQAL QYVVENIAEQ TGWLLEIVNY
NIANLQYVCA GDLRALDTLT NVLNVLKAQK IDITTLMSTM SIDDLRAHLV EIITSCSQLT
NSKPQPITLE RGFATIPLKG IDVPFHSTFL RSGVKPFRSF LLKKINKTTI DPSKLIGKYI
PNVTAKPFEL TKEYFEDVYK LTNSPRIGAV LANWGKYEDG EK
//
