ID A0A1R1PLZ9_ZANCU Unreviewed; 1681 AA.
AC A0A1R1PLZ9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Fatty acid synthase subunit alpha {ECO:0000313|EMBL:OMH81959.1};
DE Flags: Fragment;
GN ORFNames=AX774_g4577 {ECO:0000313|EMBL:OMH81959.1};
OS Zancudomyces culisetae (Gut fungus) (Smittium culisetae).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Zancudomyces.
OX NCBI_TaxID=1213189 {ECO:0000313|EMBL:OMH81959.1, ECO:0000313|Proteomes:UP000188320};
RN [1] {ECO:0000313|Proteomes:UP000188320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL-18-3 {ECO:0000313|Proteomes:UP000188320};
RA Wang Y., White M., Kvist S., Moncalvo J.-M.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:OMH81959.1}.
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DR EMBL; LSSK01000772; OMH81959.1; -; Genomic_DNA.
DR Proteomes; UP000188320; 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:InterPro.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004312; F:fatty acid synthase activity; IEA:InterPro.
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:InterPro.
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; -; 2.
DR Gene3D; 6.10.140.1410; -; 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 InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
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; 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; IPR016039; Thiolase-like.
DR PANTHER; PTHR10982:SF23; FATTY ACID SYNTHASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR10982; MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE; 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; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|PIRSR:PIRSR000454-4};
KW Reference proteome {ECO:0000313|Proteomes:UP000188320}.
FT DOMAIN 936..1486
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 1597..1631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1597..1611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1121
FT /note="For beta-ketoacyl synthase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-1"
FT MOD_RES 6
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000454-4"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OMH81959.1"
FT NON_TER 1681
FT /evidence="ECO:0000313|EMBL:OMH81959.1"
SQ SEQUENCE 1681 AA; 188826 MW; 2438EC71EC84E100 CRC64;
LVNGKSAMQN EIISDLQKEF QNQLPDKAEE MPLVELFGQL NNSSGGLGPF SSVRVSKLVN
SKMPGGFTIP KIKEMLNKKY GLGPLRADCL LLLGTTFEPE NRLANEKDMN SWLEIVANQY
AKIFGIQYSQ KSETSNVGTS GVTIDSKEFN EYVSHYKKLL SSQQIAISDF LGRDVSNESL
TTLDDIEASY RKAKHQLDIW ESEYDERYSD GIKPIFTSLK CRIFDSYWNW VEWQLERVFY
DTLNLTTDVK AGDLDSEKPY FVNKSTPRLV ASIRYKIKLL ESNKLVNLHN HYNIVQLKLF
LSDLLESCEM AVDKSPLYYG IMQYYGPKTT ISNKGDIEYN EVQREGINDI IDYINSMTFG
IDTGDRFDEQ NEQHLLTEEL LHKLSAALNL PEKLTSDDLE KISNEIRNVK NKTDGFKTKI
RTLNNVEKTH IKSGLLFEDY VKFADSMIYK DRLPFLHLRR RHRYDTFNYD KASTLYYLGA
LLDISFNGIT FASKNVLVTG CGKGSIGIEI VKALLMGGAN VIATTSKFSY SAAKRFEKLY
KKYGSKGSSL TLLPFNQSSQ QDVNSLVDYI FLPKKSRGLG MILDAVVPFG AMSEVGKDIT
NLDSVSEVAH RTMMVNILRL IGRVKINKEK YGIKMRSTMV FVPLSLNHGG FGGDGLYAES
KIGLETLFDK WAAESWGEYI SIAGVVVGWA RGTGLMNQNN ILAEAMEKQG GKTFSTKEVA
FNVLGLLHPE IRRLCDERPI YADISGGFGF ILEFSKKTFM IRQDLINQSL IQKQIKYETS
FDFKMTEGEN VEDIYKQVEI KQRSNLRIDF PKLRDYSELK EKFGVGEMLN LDKTVVVVGF
GEVGPFGSAE TRWDMEIHDE YSNDGCIMLG WIMGFIRYHR GTLPNGQQYQ GWVDAKSGDP
VEDTKIKLIY GKLITEHSGL RRVDPELLEG YDPDCRKVIR EVVIHEKMKP IKTTEEEARY
FKLKHKETVE IWKGSGDDWF VRFLAGTKIF LPKASKFEWF VSGLVPKFWT AERYGLPLEI
CKRIDDLTAF CLVATNDAFM RAGIEDPYEL FKFVHVSEIG NSIGSAVGGS KLAFTTLKRR
YNSEYIEGGV FDECYCSSMA SWVNKYILPS SGPFVVPSGT CATGAVSIDI AVQSLITGKA
KIMLSGGHDD VTEECSMEFA NMQATANSTT DFACGRTAKE MSRPFTSTRH GFMDSQGSAV
QILMTAATAL EIGLPIYGII AYSGTSSDKV GRSFPAPGKG LITSVRESPR SIINPLLNIS
YRRRQLKKRL EEVDSWFSNQ LNTLITDFTG HSSKSLSLND LNEISITSPQ KISELNAKLV
FLNDHYSRLK KNARDYWSYD FWLKNPSISP IRGSLAAFGL TADDIDFVNC HGTSTAANDN
NESEVLASQF KKLGRTYGNV CPAVSQKGLM GHTKGGAAAF AINGVLQSIL TGVVPGSHNA
DNISNEFEDH FYVYHPSRSI KKPFIKACLM KSLGFGQIGA EILVLNPDYL FSSISEDKYL
EYKSKVSKRN MYANKIFFNT MTTTKLYLTE KQRLYDESNE VSILLNPNAR AEYSVEFDTF
RISAEQNTSN RITSIVTPSH VYATIKSLTA NAVEQDTRAP ASITHTQIPK SQPQPQPQPH
QAISTPTFTP RPNTEIIHIK SISVDDSEFT QTHFTELEIS YCKSRPSPRA SFAGKLAAKT
A
//
