ID T5AF14_OPHSC Unreviewed; 1861 AA.
AC T5AF14;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Fatty acid synthase subunit alpha {ECO:0000256|ARBA:ARBA00014008};
DE EC=1.1.1.100 {ECO:0000256|ARBA:ARBA00012948};
DE EC=2.3.1.41 {ECO:0000256|ARBA:ARBA00013191};
DE EC=2.3.1.86 {ECO:0000256|ARBA:ARBA00012878};
GN ORFNames=OCS_03856 {ECO:0000313|EMBL:EQL00433.1};
OS Ophiocordyceps sinensis (strain Co18 / CGMCC 3.14243) (Yarsagumba
OS caterpillar fungus) (Hirsutella sinensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=911162 {ECO:0000313|EMBL:EQL00433.1, ECO:0000313|Proteomes:UP000019374};
RN [1] {ECO:0000313|EMBL:EQL00433.1, ECO:0000313|Proteomes:UP000019374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Co18 / CGMCC 3.14243 {ECO:0000313|Proteomes:UP000019374};
RC TISSUE=Fruit-body {ECO:0000313|EMBL:EQL00433.1};
RX DOI=10.1007/s11434-013-5929-5;
RA Hu X., Zhang Y., Xiao G., Zheng P., Xia Y., Zhang X., St Leger R.J.,
RA Liu X., Wang C.;
RT "Genome survey uncovers the secrets of sex and lifestyle in caterpillar
RT fungus.";
RL Chin. Sci. Bull. 58:2846-2854(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC Evidence={ECO:0000256|ARBA:ARBA00001572};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP]
CC + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC EC=2.3.1.41; Evidence={ECO:0000256|ARBA:ARBA00001402};
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 -!- SIMILARITY: Belongs to the thiolase-like superfamily. Fungal fatty acid
CC synthetase subunit alpha family. {ECO:0000256|ARBA:ARBA00007485,
CC ECO:0000256|PIRNR:PIRNR000454}.
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DR EMBL; KE652815; EQL00433.1; -; Genomic_DNA.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR HOGENOM; CLU_000114_0_0_1; -.
DR Proteomes; UP000019374; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IEA:InterPro.
DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004312; F:fatty acid synthase activity; IEA:InterPro.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR CDD; cd00828; elong_cond_enzymes; 1.
DR CDD; cd08950; KR_fFAS_SDR_c_like; 1.
DR Gene3D; 3.30.70.2490; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.90.25.70; -; 1.
DR Gene3D; 6.10.140.1390; -; 1.
DR Gene3D; 6.10.140.1410; -; 1.
DR Gene3D; 6.10.250.1930; -; 1.
DR Gene3D; 6.10.250.1940; -; 1.
DR Gene3D; 3.90.470.20; 4'-phosphopantetheinyl transferase domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00101; AcpS; 1.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR InterPro; IPR002582; ACPS.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR040899; Fas_alpha_ACP.
DR InterPro; IPR047224; FAS_alpha_su_C.
DR InterPro; IPR026025; FAS_alpha_yeast.
DR InterPro; IPR041550; FASI_helical.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR004568; Ppantetheine-prot_Trfase_dom.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR00556; pantethn_trn; 1.
DR PANTHER; PTHR10982:SF23; FATTY ACID SYNTHASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR10982; MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE; 1.
DR Pfam; PF01648; ACPS; 1.
DR Pfam; PF18325; Fas_alpha_ACP; 1.
DR Pfam; PF18314; FAS_I_H; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR PIRSF; PIRSF000454; FAS_yeast_alpha; 1.
DR SUPFAM; SSF56214; 4'-phosphopantetheinyl transferase; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR000454-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000454-3};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphopantetheine {ECO:0000256|PIRNR:PIRNR000454,
KW ECO:0000256|PIRSR:PIRSR000454-4};
KW Reference proteome {ECO:0000313|Proteomes:UP000019374};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000454}.
FT DOMAIN 142..220
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1093..1630
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT ACT_SITE 1276
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-1"
FT BINDING 1747
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1748
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1749
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1847
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT BINDING 1848
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-3"
FT MOD_RES 180
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-4"
SQ SEQUENCE 1861 AA; 204224 MW; 25CFBF0E7C898981 CRC64;
MRPEVEQELA HTLLIELLAY QFASPVRWIE TQDVFLAERT AERIVEIGPA DTLGIMAKRT
LASKYEAYDA AKSVQRQILC YNKDAKEIYY DVDPIEEESE PTAGSADALA LGAALGAAAP
APAAAAAAPP PPSSGPAAQV PDEPVQAIDI VRALIAQKLK KPLLDVPLSK AIKDLVGGKS
TLQNEILGDL GKEFGSTPEK PEDTPLDELG ASMQATFDGN LGKQSQSLIA RLISSKMPGG
FNITAARKYL EMRWGLGPGR QDGALLLALT MEPPSRLGSE GDAKGFLDDV TQKYSSNAGF
SLSTASAAGS DASAGGMMMA PAAIDALTKD QRALFKQQLE LFARYLKMDL RSGDKSYIDS
QKSEKVLQAQ LDLWTAEHGD FYASGIEPVF SPPKARTYDS SWNWARQDAL SMYFDIIFGR
LQAIDREIVS QCIRIMNRSN PKLLDFMQYH IDNCPTERGE TYKLAKELGQ QLIENCKDVL
NVSPVCKDVA VPTGPRTTVD ARGNLNYEEV PRASCRKLEH YVQQMAEGGK ISEYGNRTKV
QSDLQRIYKL IRQQHKMSKT SQLEIKSLYG DVLRSLAMNQ SQILPKDNGK SKKTSLKGAG
HNKGKVETIP FLHLKHKTLH GWDYSKRLTA VYLNCLEEAA KSGVTFQGKH VLMTGAGAGS
IGAEVLQGLI GGGARVVVTT SRFSREVTEY YQSMYTRYGS LGSQIVVVPF NQGSKQDVEA
LVEYIYDTKN GLGWDLDFVV PFAAISENGR QIDSVDSRSE LAHRIMLTNL IRLLGCVKAQ
KAERGFETRP AQVVLPLSPN HGTFGNDGLY SESKLGLETL FNRWSSESWA NYLTVCGAVI
GWTRGTGLMS GNNIVAEGVE AFGVRTFSQQ EMAFNLLGLM SPTIVDLCQA EPVFADLNGG
LQFIPNLNEA MTKLRKDIME TSEIRKAVAK ESALENAIVN GAESEALYKK NTIDPRANIK
FDFPTLPDWK SEVAPLHDTL KGMVDLEKVI VVTGFAEVGP WGNSRTRWEM EAHGEFSIEG
CVEMAWIMGL IKNHNGPLKG KPYSGWVDAK SGDPVDDKDV KTKYEKHILE HSGIRLIEPE
LFNGYDPNKK QMLHEVVIEE DLEPFEASKE TAEEFKREHG DKVEIFEIPD SGEYIIRMRK
GASLWIPKAL RFDRLVAGQI PTGWDPKRYG VPEDIISQVD PVTLFLLVST AEALLSCGIT
DPYEFYKYVH VSEVGNCVGS GMGGAAALRG MHKDRFLDKP LQNDILQESF INTMAAWVNM
LLISSSGPIK TPVGACATAV ESVDIGYETI MEGKARVCFV GGFDDFGEEG SYEFANMKAT
SNTVDEFAHG RTPKEMSRPT TTTRNGFMES QGCGIQVIMT ARLALDMGVP IYGILALTTT
ASDKIGRSVP APGQGVLTTA REHAGKFPSP LLDINHRRRQ IERRKKQIKQ WQESELEFVH
DEIEAMRAQG STFDEKEYAQ ERILHIGKEA ARQDKELLRS MGNNFWKSDP SIAPLRGALA
TWGLTIDDLG VASFHGTSTK ANDKNESSVI CQQLRHLGRK KGNAVLGIFQ KYLTGHPKGA
AGAWMMNGCL QVLNTGLVPG NRNADNVDPI MEDFDLIVYP SRSIQTDGIK AFSVTSFGFG
QKGAQAIGIH PKYLFATLDE RAYNEYCAKV EARQKKAYRF FHNGLINNSL FVAKSSPPYT
EEQLRTVLLN PDARVSEDKE TSELKYAANF MKQSEKTVSA SRASETQKVM EALAQKVASK
NSRIGVDVED ITAVNIDNET FLQRNFTAEE TSYCQKAPSP QSSFAGRWSA KEAVFKSLGV
ASKGAGAAMK DIEILKDDTG APTVSLHGEA AAAAKQAGVK SITLSISHSD TQAIAVAVAN
F
//
