ID F3NC28_9ACTN Unreviewed; 1259 AA.
AC F3NC28;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE SubName: Full=Putative type-I PKS {ECO:0000313|EMBL:EGG48916.1};
GN ORFNames=SGM_6717 {ECO:0000313|EMBL:EGG48916.1};
OS Streptomyces griseoaurantiacus M045.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=996637 {ECO:0000313|EMBL:EGG48916.1, ECO:0000313|Proteomes:UP000003022};
RN [1] {ECO:0000313|EMBL:EGG48916.1, ECO:0000313|Proteomes:UP000003022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M045 {ECO:0000313|EMBL:EGG48916.1,
RC ECO:0000313|Proteomes:UP000003022};
RX PubMed=21551298; DOI=10.1128/JB.05053-11;
RA Li F., Jiang P., Zheng H., Wang S., Zhao G., Qin S., Liu Z.;
RT "Draft genome sequence of the marine bacterium Streptomyces
RT griseoaurantiacus M045, which produces novel manumycin-type antibiotics
RT with a pABA core component.";
RL J. Bacteriol. 193:3417-3418(2011).
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:EGG48916.1}.
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DR EMBL; AEYX01000005; EGG48916.1; -; Genomic_DNA.
DR RefSeq; WP_006138083.1; NZ_AEYX01000005.1.
DR AlphaFoldDB; F3NC28; -.
DR STRING; 996637.SGM_6717; -.
DR eggNOG; COG3321; Bacteria.
DR Proteomes; UP000003022; 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; cd08953; KR_2_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR036736; ACP-like_sf.
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; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 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; PF00550; PP-binding; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000003022};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..437
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1146..1221
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 474..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1224..1244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1259 AA; 134435 MW; D44808E80B9D1213 CRC64;
MSTHTDIAVV GLSVEVPDAP EQHAFWDIVR EGRSLTRPFP AGRRRELEEY VRYHQESALV
PDAAERVDFH EGSFLDRIDL FDHEFFGMTP KQAAVTDPHQ RLVLRTMYRA LEDAGYTGDR
LTGSRTGVYI GYAGNPGMTY LDYFCRVDPS LGQLGITGNI VTMLANRLSY LYDLRGPSMV
LDSACSASLV ALHQAKSALL LGDCEMAVVA GTRVVLAPLR HPHTRIGIES SDGVTRTFDE
RADGTGFGEG SGALVLKRLD RALADGDQVY AVIKGSAVNH DGHSEMMTAP DAGAQADLLD
AAWRDAGVDP RSIGYLEVHG TATKVGDPIE FEGLRRAFAA RTEDRRFCAV GTVKANVGHL
FEGSGVLGVI KAVLALRHRV IPPLANYERP NGSIDLAEGP VYVPTEAREW TAGDGPRRAG
VSAFGLGGTN AHVVLEEFTG ARADTEPAAG AAGAAGVVSA GATGAGSAAA ARTGSAAATG
TGSPTVTGTG SAGAAEARPS YLFTLSARTR LSLARLIRRY REALDAGRIE GGVRDVCWTA
NVSRAHHAHR FAVTVADLDG LRTALATAEA GEEPEAARTE AARAWTRGAE VDLSAAYEGQ
RPRTVHLPPY EFDETRAWVD FPDDWRERFA LAAPHRTHPV THEVRFVPAP LAESADPSVR
VLALAHPGTA GTVAEALPPG TVLRAPDDPA ADPERLAEEL VDEGYTHLVH ALALDESPAQ
DPAELSRRIE EQLTGLFHLA RELMRASAEL DLVVLTRRGL AVGPGEPGTV AEHAALAGFA
KAVAREYPYM TVTLLDLDEA VPAPVLRQEI LAAEPGVYAL RGKDKYRESF AELAEVPAVR
EEYLRPGGAY LITGGLGALG LEMARHFAAR APGLHLYLLG RTALPPEEEW DTLAAGSSHP
AAARISAVRA LTALGARVHP VAADAADEEA LSALLETIRA AHGRLDGIVH AAGVAGGDLI
ARREDAAFDS VVRPKLHGAF LLHHLTREDR PDFVLHMSSV AAVFPALGQG DYAAANFYLD
HLARALNTPE HRVVSVQWVA WREIGMAVAT NFQEDASFRS LRTRDGLALV DAALRGDLPG
FFGGGINYDS ELMSILPTYP LALSTEIEEK IATALADLAE RGKRNLARVR EAIEATEVRL
TGNPDGVYSE REWMVARCLA HTLGHSSIDV HADFRDLGLD SMMALTVGNS VSACIGRQFD
TVNLITDRTV VDVARLVESR YGADAQDGSG LPGEPGADGE GFGEDDEAWL DELLATPGE
//
