ID A0A0D6KA51_9CYAN Unreviewed; 1076 AA.
AC A0A0D6KA51;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Beta-ketoacyl synthase protein {ECO:0000313|EMBL:EKE96453.1};
GN ORFNames=FDUTEX481_07197 {ECO:0000313|EMBL:EKE96453.1};
OS Tolypothrix sp. PCC 7601.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1188 {ECO:0000313|EMBL:EKE96453.1, ECO:0000313|Proteomes:UP000032761};
RN [1] {ECO:0000313|EMBL:EKE96453.1, ECO:0000313|Proteomes:UP000032761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7601 / UTEX B 481 {ECO:0000313|Proteomes:UP000032761};
RX PubMed=25953173;
RA Yerrapragada S., Shukla A., Hallsworth-Pepin K., Choi K., Wollam A.,
RA Clifton S., Qin X., Muzny D., Raghuraman S., Ashki H., Uzman A.,
RA Highlander S.K., Fryszczyn B.G., Fox G.E., Tirumalai M.R., Liu Y., Kim S.,
RA Kehoe D.M., Weinstock G.M.;
RT "Extreme Sensory Complexity Encoded in the 10-Megabase Draft Genome
RT Sequence of the Chromatically Acclimating Cyanobacterium Tolypothrix sp.
RT PCC 7601.";
RL Genome Announc. 3:0-0(2015).
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:EKE96453.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGCR01000146; EKE96453.1; -; Genomic_DNA.
DR RefSeq; WP_052335497.1; NZ_JH930390.1.
DR AlphaFoldDB; A0A0D6KA51; -.
DR STRING; 1188.FDUTEX481_07197; -.
DR PATRIC; fig|1188.3.peg.10074; -.
DR HOGENOM; CLU_000022_16_6_3; -.
DR OrthoDB; 499075at2; -.
DR Proteomes; UP000032761; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 2.
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; 2.
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; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020806; PKS_PP-bd.
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; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 37..474
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1076 AA; 120587 MW; 769A3FD04C24C830 CRC64;
MNQNSQQDQE NFYSSQEGVK FPKHATNQTE ETEQRKSEAI AIIGIDCRFP GANNYEEFWL
NLEAGVNSIT EIPTQRWDTQ KYYSPNPQER NKTISKWSGL IEALDEFDAQ FFGISPREAK
MLEPQQRLML ELSWSCLEDA GYSPFQLSGS PVGVFIGACN YDSILYFNQD QEKIEGHLGT
GTWTCMIPNR ISHFFDFRGP SVPVDTACSS SLVALHLAMN ALKEKDCEIA LVGGISVMNL
PIGYLQMSQL GMLSPTGQCH SFDSHADGYV RGEGAGMILL KPLAKAIEDK DHIYGVIKGM
AVNHGGKSRT LTSPSIYAQA QVVRAAYTKA NVAPNTISYI EAHGTGTPLG DPIEINALKR
GFKQLYQQYK LPGFAKPYCG LGTVKTNIGH LEGAAGIAGV IKVLLAMKQK KLPKILNFQQ
LNPRIKLEDS PFYIVTETQE WQQLKTLAGE VVPRRAGVSS FGVGGVNAHV VLEEAPQPKT
QRVGVERPLH ILTLSAKNEQ ALEELVKKYQ GYLQSNQEAS TANICFTANS GRAHFEQKLA
VVAESNAELQ KQLEAFLKFN QTNGVVRGQA KGESPKVAFL FTGQGSQYVN MGWQLYQTQP
TFRKTLEECD QILLPYLKQP LLSVLYPQST ALAENSSLLN QTAYTQPALF AIEYALAQLW
QSWGIKPDVV MGHSVGEYVA ATVAGVFSLE EGLKLIVTRA RLMESMPGEF EAVAQEVTYS
QPQITIISHL PGQKATPKIS TPEYWIEHFR QPVHFGQSMQ TLYQSGYKLF LEIGPKPILL
EMDRQCLPED AGLWLPSLNP LQEDWQQILS SLGQLYIKGL KVDWSGFDKD YSRHKVVLPT
YPFQRQRYWL EASKNGHQKD TRENSLNLIA QLLNEIYPEQ LAQELNLSEL LTEQEKKLLP
KLLNILTKRS QEYGQLSKPY SEILQQLEKT PQTERHQLMI NYLQSVVGKL LGFHDSQSPD
SQLGFFDMGM NYSMMLELKD LLQTSLGCAI AVTTLSEHFN IQDLAKYLIT KIFMGELEEK
LEIDKYYENP NQGTLINGEI ELLCEDAIAN AMTEEIIATA LQDELKEIEF LLNQGM
//
