ID A0A010ZXL8_9ACTN Unreviewed; 2312 AA.
AC A0A010ZXL8;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Polyketide synthase family protein {ECO:0000313|EMBL:EXG81967.1};
GN ORFNames=CryarDRAFT_3092 {ECO:0000313|EMBL:EXG81967.1};
OS Cryptosporangium arvum DSM 44712.
OC Bacteria; Actinomycetota; Actinomycetes; Cryptosporangiales;
OC Cryptosporangiaceae; Cryptosporangium.
OX NCBI_TaxID=927661 {ECO:0000313|EMBL:EXG81967.1, ECO:0000313|Proteomes:UP000021053};
RN [1] {ECO:0000313|EMBL:EXG81967.1, ECO:0000313|Proteomes:UP000021053}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44712 {ECO:0000313|EMBL:EXG81967.1,
RC ECO:0000313|Proteomes:UP000021053};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (JUL-2013) 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:EXG81967.1}.
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DR EMBL; JFBT01000001; EXG81967.1; -; Genomic_DNA.
DR PATRIC; fig|927661.3.peg.3052; -.
DR HOGENOM; CLU_000022_31_5_11; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000021053; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd05195; enoyl_red; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR020843; PKS_ER.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 3.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000021053};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..426
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1957..2035
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2312 AA; 245821 MW; 100E30C7106E51B0 CRC64;
MEPLAIVGIG CRLPGGVHGP DEFWELLMSG VDTVGEVPAD RWRTERFYDP DPETPGRMSV
RRAAFLTEPV DRLDAGFFDL TPREAAIVDP QQRLLLEVTW EALEDAGIPP SALAGRAVGT
YIGNAMVDAT HLQVSEPNLE MIGAHTATGA SLTLLSARLA HAFDWRGPCL SIDTACSSSL
VAFHYACGVV ASGECEVAIA GGVNVMLDPA SSIVLAKGQF LSPDGRCKAF DHRANGYARG
EGAAVVVVKR MADARRDGDR VYAAVLGTAV NQDGRTPGIT VPSRAAQRAA VAAACDTAGI
EAGSIGYFEA HGTGTPVGDP IEVAAIGDAL AGSTARHWIG SVKTNIGHLE GASGVAGLIK
AALCVERGLI PPNLHFERPN PAIPFDTLPL RVPTKPVEFD PAIGPRRAGV NSFGFGGTNA
HALVEQPPPG PSPEPDPATG PFVLPVSARS AGALRALVDG YAELLAADDA PALHQVCRGA
SRGRSHHPLR TSVVAADSAS AAVALRALEI PDKPRRAAGS GAVFVYTGMG PQWWGMGRAL
LQEEPVFAAT VRECDRVLAR FGISMDDELR RDQETSRLTE PLYAQVGNFV VQAGLTAVWR
SWGVEPSAVV GHSVGEVSAS YAAGVYSLED ALTIGVQRAR RTSAAGPGAM LAVGLGADDL
APYLVDGVSV AARNSPGTST LSGQRAPVAL VAERLRDAGV FVRELRVDIA YHSDVMDGIR
VPLLASLDGL RPRAATLPLL STVTGDWLDG TTMDAGYWWR NVREPVRFAE AIARAAATGP
AAFLEVGPHP VLAPAIREVV IDAGADVPVL ASQHRDRPGA RTLREALGGL YVAGGEPDWA
RIHPGERRPV DLPTYPWQRE RHWLESPYAR SARLGDEGWL MAGRKLPTPL PSWDTELSAA
EFPYLADHRI ADTVVFPGAG YIEAALAAFG DRTPCVLADI VLDRTLALPP KCVTTLRVTH
DPLTREVTMH ARRSGDDSGW SRHAGLRLAT LADPAPPPAV ATDPPVGWTE MAHEAVYAHL
AGAGLPYGPA FRGIERLWWR SGEVVARIDV GRVDHSGHRL HPALLDAALH AMLVGARPDG
TSRTFVPVRI DEVRFHRSPG RSLWVHGRGR TGPDSVVGDL TLITDDGAVV AELIGMRAQA
LSDSAATPGQ TTEELYYEQV WRPEPAPDDG TAEGSWTVVG ASPLAVGIAD GLAARGGVVR
RVVPEGDWST GLSAGTRGVI LVVDPDRADD RACGACTRPL ELIRALHEPT SLFLVTSGAQ
GRAGDGPPDP FSASVWGFGR AVNAEHPELR CRQIDADAPD DALIDELIHS GADDVLLRSG
HRSVLRFQRA EARSPLHHVT VGTADTPVRL RTGGSIEDIR IEACSRREPA PTEVELAVAY
TGLNFKDVLK ATGLLAREAM ENTHSGPAVG IECSGTVVRV GAQVTDLRPG DEVFAVSKGL
FSSYVTLDQV HVVRRPASLS LAESATLFPV VTAYVALVHL ANVRPGERVL IHSGAGGVGL
AAIRIAKWLG AEVFATAGTP ERRDLLRAEG VAGVATSRTT AFADEIRAWT GGEGVDVVVN
SIPGEILERS LELLRPLGRF VELGKADFAA DRALRLRPFN RSISFHAFDY DRLLLERPEI
GRRYMRDVVR LFDDGAIAAL PMTEVPLEAA ATAFRAMARR EHVGKLVVRI GDQQVRVPAS
SLPAVTLAPG TYVVTGGSSG FGLATARWLA DRGARHLLLL SRRGLASAEA ERTVAELRER
GVTVRIAPAD VTDRAQLHRT LEEARRTLPP LRGVVHAAVV YDNDLLADMS AEHFLDATAA
KADGAWNLHV ETAPDQLDLF ILFSSTAAQF GGSKVGPYAA ANEFLNTLAD HRRALGRPAV
AVGWGAVADV GVAARFDQIG DSLARRGFVG STADRLLAEL TTLLRTDPAR ASIGAIRWDR
WVRANAHLAT LPRYADVAPA DASEHSDAAL PDRLRAGTRE QRLALLPDLV EDLLGLLTGL
PKEQVAEQGV VSLDSMMSVE LRVLLRDRLG VSVPIVELLQ NLTAGRLVEV VADVLEGAAP
ETALPVVHEL TSSDGLTVYG HLSLPPGPGP HPAVLVCPPD PGGVLDAEGR YRRIPEHATL
VGAGFAVFSV DRRGALGHGD EYAARTDVGG LEVDDVIAAA QFLIRRDDID PDRLSIYGVS
RGAYAALLAL TRAPGLWHRG VLAMGFYDPG RYVAAERAAR PTTSRLIADA TWDALDVLAA
SADRLPLRVL DRVTAPLYVL HGAADEVTPV EHAYDLAERA EAAGGPVRLV VVPGLGHDID
HQHDAWSRLW PDLVTFLDDG VTTGRPGPYH QR
//
