ID A9EAB7_9FLAO Unreviewed; 2025 AA.
AC A9EAB7;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Polyketide synthase of type I {ECO:0000313|EMBL:EDP94610.1};
GN ORFNames=KAOT1_04315 {ECO:0000313|EMBL:EDP94610.1};
OS Kordia algicida OT-1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Kordia.
OX NCBI_TaxID=391587 {ECO:0000313|EMBL:EDP94610.1, ECO:0000313|Proteomes:UP000002945};
RN [1] {ECO:0000313|EMBL:EDP94610.1, ECO:0000313|Proteomes:UP000002945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT-1 {ECO:0000313|EMBL:EDP94610.1,
RC ECO:0000313|Proteomes:UP000002945};
RX PubMed=21622754; DOI=10.1128/JB.05241-11;
RA Lee H.S., Kang S.G., Kwon K.K., Lee J.H., Kim S.J.;
RT "Genome sequence of the algicidal bacterium Kordia algicida OT-1.";
RL J. Bacteriol. 193:4031-4032(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:EDP94610.1}.
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DR EMBL; ABIB01000015; EDP94610.1; -; Genomic_DNA.
DR RefSeq; WP_007093434.1; NZ_DS544873.1.
DR STRING; 391587.KAOT1_04315; -.
DR eggNOG; COG3321; Bacteria.
DR eggNOG; COG4221; Bacteria.
DR HOGENOM; CLU_233497_0_0_10; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000002945; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR CDD; cd08953; KR_2_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 1.10.1240.100; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 2.
DR InterPro; IPR036736; ACP-like_sf.
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; 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; IPR020806; PKS_PP-bd.
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; PF21089; PKS_DH_N; 2.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF14765; PS-DH; 2.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002945};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 785..861
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 922..1342
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1940..2017
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2025 AA; 226254 MW; D2B10350F1CA918E CRC64;
MIDFIEYVVS ELKHKRLSKG NALSLIKQFS QKSSTQAVHK AIHPLLHTNT SDFYQQRYST
VLNGSEPFLA DHQVRLGEDN LMKILPGVAY LEMAHAALAN ALPNITDTHV IELKNVVWMQ
PFFVSEAKEI HIELLTENEE NIQFEIYSSE SNAQETIHCK GEINYVEKEE NKTLEVEKLT
DNMHRGELNT AEIYETYANL GLQYGDTHQV ISKIYQGNNE LIAKLELANA SKATQEKYTL
HHGMLDGALQ ASLGLVDDLA TLSSGSPMLP FALENIQVFT SCTEEMFVWI RYAEGSKSGD
TITKLDIDVC DADGIICAQL KGFTSKTFTV PSLKTIANSE EATVVYATQT WKETKGETAK
VAFDHNEIIF YNFAQEDVKT IQNNLSNASC SAFKVSSKKN TAEIYEEVSL QIFKKVQELI
QKKSQGKVHL QIVYNNTAEN EIFTGITGLL KTAALENPKF SGQIILTDQN DAKEITKQLQ
FNQENYIDTV VKYENTVRYV WQLEEISLPN TQENISFKEN GVYLITGGFG GLGTLFVEEI
LQQTNNATII LSGRSELTSE KEAKLKKLTE NGGNVAYRQL NLSDEKQTKS AIAAILKEFD
QLNGILHTAG MTADNFILKK TTEEFTNVLQ PKVIGTYNLN LATQNTDIDF IALFSSGVAA
LGNPGQGDYA LANGFLDHYA NYQNKQQNNT KYVAINWPLW KNGGMGLQAE MLENMKQQTG
VRPLETANGT TAFQHSLNLE TSSLFLLEGE AQKIRKLLFE KPAIETIKEI TEETPKATTT
ETTDNLVEKT IAYLRKEFSS VLKISLHKID TRAPLERYGI DSVVAMNLTG KLEKTFGTLS
KTLFFEYQTI DELGEYIAAN FQEKLQTLFS IEKTAVKSPK KQVSKPVQKV ETPTITRRQR
RKFKKLGANQ NAYSKSLESV NNEPIAIVGL SGRYPESINI EAYWNNLKNG KDCVTEVPKQ
RWDWRDFYNE DKANPGAHTS KWGGFITGVD EFDPRFFNIS PREASYIDPQ ERIFLQHAWT
AIEDAGYTRQ SLQIPMENDQ SAQIGVYVGV MYGEYNLSGS LASIANRVSY FLNLHGPSMT
LDTMCSSSLT AIHLACQDIK LGRTNMAIAG GVNVSIDANK YSMLSAGQFI SSDGHCQSFG
EGGDGYIPGE GVGAVILKRL SEAEKDGDHI YGIIKGTALN HGGKTNGYTV PNPNAQAAAI
SRALRESKTD PKHISYVEAH GTGTKLGDPI EIAALTKAYQ ISAEKSHCLV GSSKSNLGHC
ESAAGIAGFT KVLLQMKHKQ IVPSLHSKRL NPNIDFTKTP FEINQTLRDW EKPVVEGSTI
PRLAGLSSFG AGGSNAHIII QEYETKQNDY SLEISEFLVP LSARIERQLI QKATDLLAFI
QKNKETINLT ELAYTLQIGR EAMDERVGFL VTSVDDLIEK LTAFVNGDTE HGDIYRGQVQ
QNKETISLFN SDVDFQETIN KWIEQKKYAK VFDLWAKGLQ LDWSTFYGNE KIQRISLPTY
PFAKEKYWNA PEMRGKVLPE TQNISALHPL VHANTSNLDQ QRFTTTFTGK EFFVKDYQLK
LNGTGAKKAL PALASLEMAR AAAEHIKPAS KKAEAISLQG ISWGKPFLLN ENKQLDIILE
KEGENGVYFE ITSKQENEEI IHAQGLANYE TAEQSFQFDV AKLQNELQSN TREANEIYTA
FSVMGLYYGA SNQVIQKVYM SKNYLLSEIS LPKTIENSLT DFVLHPSILD SVMQASICLI
TDLKLSENYM FIPVATDSLT IYNAFTKKMF VLVQYDESQT SEDAVYINAD FCDENGIVYA
QLKGLELQQI KLDRTVKQAK KVTIDLEPFV ILESKIEKPT DVQLRELSTK IAIEEKIISP
KPTNVALANT QIIQKAAIQN DAPTIKKISL DDFDDAPKVE SAITPKQKEI KLIDLDVPKV
EAVKEKSVTI ETSNVSENTF SKEQLKQMLI NTLADALYLE PHEIDADKSF IDIGLDSIVG
VEWIKTINKE LNMELSSTKI YDYATVNALA KYIRSEMESM ENAIS
//
