ID A0A238Z4R4_9RHOB Unreviewed; 1875 AA.
AC A0A238Z4R4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Enediyne polyketide synthase {ECO:0000313|EMBL:SNR77823.1};
GN ORFNames=SAMN06265370_12320 {ECO:0000313|EMBL:SNR77823.1};
OS Puniceibacterium sediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Puniceibacterium.
OX NCBI_TaxID=1608407 {ECO:0000313|EMBL:SNR77823.1, ECO:0000313|Proteomes:UP000198417};
RN [1] {ECO:0000313|EMBL:SNR77823.1, ECO:0000313|Proteomes:UP000198417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29052 {ECO:0000313|EMBL:SNR77823.1,
RC ECO:0000313|Proteomes:UP000198417};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FZNN01000023; SNR77823.1; -; Genomic_DNA.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000198417; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
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; IPR029069; HotDog_dom_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; 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; 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; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 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 NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000198417};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..455
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 909..985
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1875 AA; 197120 MW; B107B7A921BCEB59 CRC64;
MTNRIAILST ACRYAEAPSP DALWQNVLDG RRSFRAIPPQ RLALGDYAVE HIGTEDSIPR
IYAGLISDWQ FRRDRLCIPK STFDTADLTH WLALETAMTA VGAVGGAEAL PRGRTAVILG
NTLTGEFSRA AQMRLRLPYL KRHLSQALQA GQIAPDLIDE VTSTFAANLA QDFPDPNEES
LAGALANTIA GRIANQLDLG GGAWTVDGAC AASLLAFSEA CSHIVQGDLD VAIVGGVDLS
LDPFELVGFA RTGALCRDEM RVFDKRSSGF WPGEGCGIAV LASEEAAQKL GGDPLAWVAG
WGCSTDGAGG LTRPTAPGQS RAIARAWARA GHAPAEAAYF EAHGTGTAIG DPTEITALAE
VIGQDGAAIP VGSIKANIGH CKAAAGIAGV IKTTQALKNG IIPPHISCAV PHPIFAESGG
RLCPAQVGEF RSDTRLAGVS AFGFGGINAH LVLAGPDSKI RHAKRVSVPA QPLAQEAELF
IFAAQSAEEL HQAMNALLKR APSLSHSEMA DAAAGCFRDA VPQAAFRAAI VADRPEALQE
ALTKALSIPP APVRSPPRIG FVFPGQAAPV RASGGAWTRR FPSLPHTLAT FPSDASVSTE
HAQPAIAASA LMGLDVLTQA GIMAEIAAGH SLGEITALHW AGALPRQEMS DLVQTRGQLM
ARHGEAGGTM LQVTASAQEI AALGRPDDLE VACLNGARDV VLAGPQETAV RWMQKARAAG
LSCELLKVSH AFHSAAMAQV ETPLAAALQD VPWSAPQMPV ISTVTGAPIE ASSDLSAILT
QQLCAPVRFS EVCAQLAQHC DLVIEVGPGK GLSRLARDAG LQVASPDVGA ETLFGLLDTL
ATVWRLGGRL DLGLLFADRA IRPLGPAPEL LRNPCGVSDK APPPSAVKPK IAAAALQDIN
ARPAHTSAAP TLDIVCKATA EALGLPLSLV KPEARLLEDL HLNSLSVGRI VKAAAQALGL
RQPALATDVA AETVYGLARL LDELLEFAPG EDTTPQSIEG VAPWVGEYRS VWQVCDWPKA
AAEAPEWCLF GPDPGGIPTA NGTKSGLVSL MDVALPDDTA AAHLLWSRVK AARAAGLRKL
LILHPGMAVS GFAGALLEDG VFDHITLVDA QGVDGPAREA GISTLLRTEA EPFAQYRCRA
AGGLDRAVLE FVPISQCRTR DDTAAGLGPC DTLLVTGGAK GIGAESALRL SKVSGAALLL
VGRSSGDDPA VTETLRRAKA QGCRARYLQA DVTDASEFRN ALETLPEEER PTAFLHAAGV
NDPAGFDQLD ATALSAALAP KLQGLETLLC ALDPQRIRLA IGFGSVIGAL GLAGETHYAL
ANAMMSARLM RWGRCHDLRT LALDWSVWAG AGMGERIGAV ERLARRGVEA IPLGTALDRL
CVLLYAPQSD EHLIVTGRFG QPRTLGFAAQ PSLQGRFLET AQIRFPGIEL VVDTRLARGS
DPWITDHVVE GTAVMPAVLM LEAMAQAAKA LTGHAPTGFR DLDLLGAVTL DGDEITLRTA
VLRRDDGSLL AAIRASDDGF SADRATVTLS FEPTLDRPEA FDLAANCRID GALLYRDLCF
NSGRFQRVEE IDHLTAFSLR AGLSNLSNAS AAPWFGPFES QDMVLGDAGA RDAGLHVLQA
CVPQRRVLPV TVAQIQIADP EARRVSVEAV ERASDGNTFV FDVLWRGPDG AIVEYWRGAR
FRAIAERSID RLAYPFFPAA MQRAAVLHAR RRDIRTAICN SADRQSRRQI VMGALDATEA
TRRGDGLQML DGPDALSLSH TASLTFGARG PGVLACDLVE TATRDDTPLV RDDSLIAEKL
HASGIANAFA AVWAARECAR KGGVPAAQPL LPLKGSEPGF QAFRCGAAQI LCHAVQNDGC
IALMLTPATA KESLA
//
