ID A0A1C4NGT8_9ACTN Unreviewed; 1177 AA.
AC A0A1C4NGT8;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Enediyne polyketide synthase {ECO:0000313|EMBL:SCD97384.1};
GN ORFNames=GA0115240_13336 {ECO:0000313|EMBL:SCD97384.1};
OS Streptomyces sp. DvalAA-14.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1839759 {ECO:0000313|EMBL:SCD97384.1, ECO:0000313|Proteomes:UP000199020};
RN [1] {ECO:0000313|EMBL:SCD97384.1, ECO:0000313|Proteomes:UP000199020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DvalAA-14 {ECO:0000313|EMBL:SCD97384.1,
RC ECO:0000313|Proteomes:UP000199020};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FMCH01000308; SCD97384.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4NGT8; -.
DR Proteomes; UP000199020; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd08953; KR_2_SDR_x; 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; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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 PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF21089; PKS_DH_N; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 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; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000199020}.
FT DOMAIN 168..244
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 142..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1177 AA; 122184 MW; F5EE068892A44BC6 CRC64;
MTGSVLAADT DVAELLERQV VQPVRFEQAL TALAADADLL VEVGPGRILR GLAAEICPDV
PVISMDTDSD SLTGTLQVLA GAYALGAAVS TEALFADRFT RPLPLDKVFQ FLASPTESAP
DGDFTAIPAT AATVTAGATA TAPARGGRAA EQPAGQAAGA ASAGQPGEST LDILLRLAAE
RAELPLEAVR ADSNAIDELH LSSITVGQIL AQTSRELGVT APLATSAMAT STLAELAAML
DELAATETAA DAAGSDTAPG VGPWVRAFAV DRTPAAAGPA LDTAAGSWTL FSSERHPLAE
ALAAELSARP LGSGVLLCLP EDTDEEHTPL MLAAVRAVLA QPGTRFVAVG HRRGAAGLAK
TLHLESPDVA TTLVTLPPTG DLSAEQIRHW VRRISADVAA TSGFSEVFYD RSGGRTVPVL
RPLQPAAPDG APAGAAEPGS QALTAGDVLL VTGGGKGITA ECALALARDS GASLALLGRS
DPATDPELAM NLERMRAAGV TFAYLRADVT SADEVKAAVS AATERLGTVT AVLHGSGRNE
PQGLVNLDES SFRRTLAPKI SGLEAVLAAT DPADLKLLIT FGSIIGRAGL RGEGDYATAN
DWLTDLTERV HEQHPHIRCL ALEWSVWSGA GMGERLGVLE SLMRDGIAPI SPEHGIAVLG
QLLADPAAPT SVVVMGRAEG LPTLTLPHRE LPLLRFLERV QVHYAGVELV ADADLSATDD
LYLPDHLLDG DLLFPAVLGM EAMTQAARAL TGRDTVPTLR DMEFLRPIVV PVDGSTTIRV
AVLADDDRTV RAVIRSSETG FKADHFSAVL DYGDRLPEVS PGIATEPLLA LDPHTELYGP
VLFQGGRFQQ LLGYRQLQAK GCVAEVSSHS GATWFGTFHP GDLLLSDPGA RDTMMHALQC
CVPDATLLPA GIERLHLADP AAVQGLDKLV LHATERSRTG DTYLYDLDVT DPEGRLLERW
TGLRLQAVRK QDGAGPWVPA LLGPYLQRRT EQFLPQELRV AVHADPDGPL EGVAARRAAT
AAAVRIALGA PAEVRYRPDG KPEATGIGGA GISASHGAGV TLAVSGAGQV GCDVEPVIGR
AAEDWAGLLG ADGAALADLL AQENGESPDL AATRVWCAIE CLRKTGHARV ELVAAGAAGN
GRWVMLRSGD STVATFATTL RSAGEPVVFA LCAEGSV
//