GenomeNet

Database: UniProt
Entry: A9EAB4_9FLAO
LinkDB: A9EAB4_9FLAO
Original site: A9EAB4_9FLAO 
ID   A9EAB4_9FLAO            Unreviewed;      3274 AA.
AC   A9EAB4;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   SubName: Full=Polyketide synthase of type I {ECO:0000313|EMBL:EDP94609.1};
GN   ORFNames=KAOT1_04310 {ECO:0000313|EMBL:EDP94609.1};
OS   Kordia algicida OT-1.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Kordia.
OX   NCBI_TaxID=391587 {ECO:0000313|EMBL:EDP94609.1, ECO:0000313|Proteomes:UP000002945};
RN   [1] {ECO:0000313|EMBL:EDP94609.1, ECO:0000313|Proteomes:UP000002945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OT-1 {ECO:0000313|EMBL:EDP94609.1,
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC         NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35;
CC         Evidence={ECO:0000256|ARBA:ARBA00023693};
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000256|RuleBase:RU003707}.
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:EDP94609.1}.
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; ABIB01000015; EDP94609.1; -; Genomic_DNA.
DR   STRING; 391587.KAOT1_04310; -.
DR   eggNOG; COG3321; Bacteria.
DR   HOGENOM; CLU_000022_53_1_10; -.
DR   Proteomes; UP000002945; Unassembled WGS sequence.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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; cd06558; crotonase-like; 2.
DR   CDD; cd08953; KR_2_SDR_x; 1.
DR   CDD; cd00833; PKS; 2.
DR   Gene3D; 1.10.1240.100; -; 2.
DR   Gene3D; 3.40.47.10; -; 2.
DR   Gene3D; 6.20.390.20; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 3.
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; IPR036736; ACP-like_sf.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
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; IPR042104; PKS_dehydratase_sf.
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; PF00378; ECH_1; 2.
DR   Pfam; PF16197; KAsynt_C_assoc; 2.
DR   Pfam; PF00109; ketoacyl-synt; 2.
DR   Pfam; PF02801; Ketoacyl-synt_C; 2.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 3.
DR   Pfam; PF14765; PS-DH; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 2.
DR   SMART; SM00823; PKS_PP; 3.
DR   SMART; SM01294; PKS_PP_betabranch; 2.
DR   SUPFAM; SSF47336; ACP-like; 3.
DR   SUPFAM; SSF52096; ClpP/crotonase; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS50075; CARRIER; 3.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 3.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
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          475..551
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          611..1031
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2314..2388
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          2423..2500
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          2561..2984
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   COILED          244..292
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   3274 AA;  364748 MW;  C90C3ABF832BE2AE CRC64;
     MMKEQLKKIF LDLSSKKLSE KEALEKIRAI KAAQKHSDVS TLYASPTWKI VKNPHDNQAV
     NAHHVICLQI ADNAQKVLAK KLPQSTIHTV KASNFSEIAL SCFSIIKNIL ENKIQANSYV
     QIVLGTSVEE TLLQSLSALF KTATLENHNL IGQLIVSDQK NAVEKLAAQL IEETQQSTDA
     IIKYEGGKRA VKRLEEIQTQ QSNNSAYKEN GVYLITGGFG GVGIAFAKEI LQQLEKTTII
     LTGRSKLTAE KRQLLQQLSE KNKKVQYIQM DVANEQKVAE NVQNILKEYK KLHGIIHAAG
     INKDNFILKK SVAEFKEVLQ AKVAGTQNID EATKDVDLDF ITYFSSIAAW FGNPGQADYA
     VANAFMDEFA KQRNQLVQAG KRKGKTLSIN WPLWENGGME IDSEIKARLL EETGFIPLDD
     QTGTTIFQKA INTNQTHILG VKGSLEKIKD TLFNQVVKVQ QQEEEIISET LDEKELLRKT
     TAFVRDEFST IIKLPAREIE THVALEKYGI DSILAMNITS QLEKTFGRLS KTLFFEYQTI
     DELSEYLANA FTSVLTAKFS SNATKKQSVS NTKKTIVHSK SHQTKTTKKK IRTQSEQSFN
     VQFTPQNTNQ NEPIAIVGLS GRYPESENIQ EFWNNLQQGK DCIIEVPKSR WDWKKHYSKD
     RTEQNRHYSK WGGFIAGVDE FDPRFFNISP REAKNIDPQE RLFLQHSWMA MEDAGYTREA
     LHKASENNLP GQVGVYVGVM YGEYNLSGSL ASIANRVSYV LNLHGPSITL DTMCSSSLTS
     VHLACQDLKS GRTDMALAGG VNVSIDANKY QMLSTGQFIS SDGHCQSFGE GGDGYIPGEG
     VGVVMLKRLS DAEKDGDHIY GIIKGSALNH GGKTNGYSVP NPKAQASVIS RALREANVHP
     RHVSYIEAHG TGTKLGDPIE ITALNKAFGI DNENHFCQLG SAKSNIGHCE SAAGIAGITK
     VILQLQHKQI VPSLHSAKLN PHIDFEHTPF VVNQSLKTWE NPIVDGNIIP RIAGVSSFGA
     GGANAHILIE EYNSVKNVAT HTPNTEVAIV LSARTKPQLK QKIQELARFI ENQEHTPDLL
     AIAYTLQTGR EAMDERFATI VFSIEELTKT LNAYLGNALQ TSKYHQARTK DHKNDVLDFK
     SEANFDETCA TWLQNKNYGE LLAWWTKGID VQWNELYATQ KPQRISLPTY PFAKESYLLT
     PEERGRATKE TTKAIIHPLV HENTSNISET RFSSTFNGEE AYIKDFTIHK ENQTLHGLPF
     MASLEMAREA IAQAIPQQKE DNVLSITNVQ FGAFMQASSV NQIHIALLPE SESVASYEIY
     SQHDDEDIIY TQGKARYTDK KATLQVDINA LRQQMSKAVI SGTTIYENAV QYGTSYRGIK
     TVHFGNQQIL AHLQLPSEVV NDVKSYVLHP TILESAVKAV SGIAGNQNEI SATTIIPTEI
     TSVNIHASCT SEMFAWIRYS ENDSQAENEV KIDIDLCDTN GTICAQFVGI SFSTSVESTQ
     FEPTLETKET SVKAAATATL AETFETPKEL FFTVQTKPTI ALTATNAENT VSSLEKPSSI
     KLTKPTAIVV DKKNSATLKK GRVQLSVESS QQIIETTVPM LRLFNTGNGI YKLQLETSEL
     DKTFIVQFKS ALQRLAKEEN LKVLLIEGTQ TDFLHGESEV FNEALQQELF KEILSFNYPI
     IANVQGNASN VGFLLASLCD FIICNEQATY EFSNTNDKLT NLFNERFGAV LANNLLQPNK
     SFTGTQLKQN GFTMPIVASE KVTKTAADLA DNLAKKSQRT LRLLKQHLSR HISEKVEQLT
     AISTITENTA FEKVEISETK SFKVQYQKDG VCVVTIKNTK LKGIRTLNSE IGAFFSEVNN
     TKNHSTIVLK SEQESFIPQT AKDVEIIKLS EILLNCNYPI ITELQNSPNA KAWLVSLHTD
     EVIYSETGNY TAKELLANKT LAQKATLLFT ACYGELASKE LLLLGKSYNG KELKTVIPTI
     QTATNATELA KSWSTAKNTK TWKSAKIKAI KESKKELPTW KLATAKDEKA PKTGTVNLKS
     SVVKATVLEA GILEIRLEER GSKNMFTDDF MAGVNEVFEH IENTPNYKVV ILTGYDNYFA
     SGGTKEGLVA IQEGKSKFTD TKIFQLAMEC KIPVIAAMQG HAIGAGWAMG MYADFTLFSK
     ERKYLSPYMN YGFTPGAGAT YIFPEIMGYD LARETLFTAK EYSGLDFENR GVALPVLTKD
     EVVTYAVELA KMIAKNSRNT LIAFKQQLIQ NRVAEAEATK KLELAMHDET FVGDAATLQQ
     IQENFAYKQA TTNIDEVITT EKEVSNDIEE NTISDVVETI KKFLANELQL EENEIEEDAQ
     FVDIGLDSIT GVTWIRKIND YYKLSLEATQ IYTYTTLQQL GDFIQKELGG TIRTTKETKT
     VATPAPKEVE TIVYEEEVIE TVDGTAEIVE TIKKFLANEL QLEENEIEED AQFIDIGLDS
     ITGVTWIRKI NDHYKTSIEA TQIYTYPSLN SLSEFIKEEL QRLGLTETKK ITKKVVATTP
     KTVQTIPNSN NTFQFTERKL TSIRSKKAIK KSVAKTNNYT SQAIAVVGMA GQFPKAENVQ
     QFWQNIAQGE NCITEVPKER WDINEYYSEG TPTPGKTNSK WLGSLAGYDQ FDPLFFTISP
     IEAESMDPQQ RLFLQSCWHS IEDAGYNPQA LSGTKCGVFV GCATGDYQLP SREQQLSAQG
     FTGGTSSILA ARISYFLNLQ GPCIALDTAC SSSLVAIANA CDSLASGASD SALAGGVYVM
     TGPEMHVKTA QSGMLSKDGK CHTFDQEANG FVPGEAVGVV MLKRLEDAER DNDNIYGVIK
     GWGLNQDGRT NGITAPNSQS QTNLEQEVYD RYDINPEEIQ LIEAHGTGTK LGDPIEVAAL
     KNSFKKYTEK EQYCALGSVK SNIGHCLTAA GVAGFIKVMK AMEHKKLPPT IHYNQLNEHI
     SLEKSPFYVN DRLQDWEVGQ AEIRHAAISA FGFSGTNAHL VMSEYIPETV DKSQINVITQ
     NKKYLIPISA RNEEQLEIQA ENLLAYAKQN LTTIDLVEMA YTLQVGRDAM EARVGFMVTS
     VEELIDKVEA YLQGEEFIKD FYQGHIKENK EGLKLVSGDK EMKELIIQKW VSDKKLNKLL
     DLWTKGLDFD WNILYGNQKP KRQRLPIYPF AKESYWLEAT TINYNAEIPE EKSAKLHPLV
     HEKTEDLKAQ GLTDATQKDA TTETKRKKIK RINLPTYPFD QEKCWPETAP KAVETPKEST
     IVFKDLDAIE DVIERIDGEL LDTDEAVLIL KDLL
//
DBGET integrated database retrieval system