ID Q4ZNC9_PSEU2 Unreviewed; 2393 AA.
AC Q4ZNC9;
DT 07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2005, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE SubName: Full=Beta-ketoacyl synthase:Beta-ketoacyl synthase:Phosphopantetheine-binding protein {ECO:0000313|EMBL:AAY39343.1};
GN OrderedLocusNames=Psyr_4313 {ECO:0000313|EMBL:AAY39343.1};
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY39343.1, ECO:0000313|Proteomes:UP000000426};
RN [1] {ECO:0000313|EMBL:AAY39343.1, ECO:0000313|Proteomes:UP000000426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a {ECO:0000313|EMBL:AAY39343.1,
RC ECO:0000313|Proteomes:UP000000426};
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000256|ARBA:ARBA00008467}.
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DR EMBL; CP000075; AAY39343.1; -; Genomic_DNA.
DR RefSeq; WP_011268957.1; NC_007005.1.
DR RefSeq; YP_237381.1; NC_007005.1.
DR STRING; 205918.Psyr_4313; -.
DR KEGG; psb:Psyr_4313; -.
DR PATRIC; fig|205918.7.peg.4451; -.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000986_1_0_6; -.
DR OrthoDB; 9778690at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000000426; Chromosome.
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:UniProtKB-UniPathway.
DR CDD; cd08953; KR_2_SDR_x; 1.
DR CDD; cd00833; PKS; 2.
DR Gene3D; 1.10.1240.100; -; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 2.
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; 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; 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; 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; 2.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 2.
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; 2.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 667..1097
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1395..1469
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1501..1922
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 34..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2393 AA; 260197 MW; 03B93C524A418721 CRC64;
MNNSNEIANF QRYIIDQLKA GRITKEQAVQ ALAKTDATGG SMREEQSGPP GSTRYVPVWR
DAPLGRALDV AQAHEQHCVV VVTEHGHERL VDTLKARLDQ RLLARMTVVL APEEAAAKGT
LADQMSGLAS AMILDVFLSL KAQVTAILQH GKGRKSSADT LLQVFFLRPD SYAEDKVAHE
SVYVGVEAAI SAMLKTLNKE HPSITTQLVA LDEASLGQLS QNSLAEEQHS HAAYVRYLKN
VRYVQVFETL SDRSDGASLQ SFIKTDASYL IIGGVGGIGL HLADYILRQG QQARVVLTGR
RSEADLQSNT PYLQLVNTYG KSRVSYLTAN AASYSDLKSL LIKVVASHHL EGIFHCAGTL
NDSFLVNKTV EQFENTLEAK VSGSLHLIQA ANDVSQQTET GFDFILFCSS CAGQLGFVGQ
IDYAAGNGFI DGFSDARNKV GRNGFDRLLS VNWPLWENAG MGVDQQALKE LHVEYGLLPL
PVDVALNHVN TLLLAADTHH VLVTYGDPVK IDSQYVNAKP QRNLQTPALS QQTAQAASGK
GAVTSVETAY DPLVAHLKQL ISSVLKLETS KLDTFEPLQS YGLDSFSIMR INQALSEHFS
RLSKTLLYEV ESIHDLATTL SQLQPDAVQA WLGAVAPAAS QQAPQASARQ DAQPRPAVPR
AVDAQAGDAV AIIGINAQFP GAANIEAFWE LLRNGVNAVT EIPESRWSLE DFYATDKIEA
IRDGKSYCKQ GGFLEQAYDF DEQFFKLSPR EILAMDPQER LFMQSCWRAL EDSGYTKDKI
KQQYDGDVGV YVGITKTGFN LYGPALWNQD ERTIPTTSFS SVASRISYLF DLNGPSMPID
TMCSSSLVAI HEAVHSLKAG RCQMAIVGGV NLYLHPASYV QLCASSMLSQ KGQCHSFGDQ
ADGFVPGEGV ATLILKPLRQ AQADGDRIYA TIKGSAVNHG GAAKGYTVPN PKAQTAVIEK
ALNSANITAG ELSYIEAHGT GTELGDPIEL NALKACFSGN DLPESSCAIG SVKSNIGHLE
AAAGLAGVIK VVLQMQHRVL VPSLHAQTIN PNLEFDQSPF YLQRELIEWP SRNNRNRIAG
VSSFGAAGVN AHVILEEYTA PQEQVVGAPV GQEHVQALVF PFSSNTEQGL KRNCRRFLDF
LQAQAPEAST AMDIATFIRA TLRGLDNNLS LNQVDDSTPL VDAGLKPFDF YRLFEAVNTR
YGLNLSMLNW QGSVSIGRLV AVIQGGASSS TVPALRDVAF TLQTCRNAHQ HRVAICARDL
AGFIERLQRF LGEEDPQVNG SGLYAGVKTH RFEELSKQKA LAHDRVQIAF AHHESDALAQ
LWVNGSFEQW EGLYSDGLQP KKCRIPEYAF AANTHSFLDK VGSNARAVRH LDQPSEAGKV
SAEIISHVPV RLEVPAVAGF IRERLAHVLK MDEASINNEV SFVDYGLDSI LGVDLIHSLN
EQYRLGLKTT CIYDYPNVEA LSRHAHGLIT PVTIVDSSTQ FARPAPQLLN ELPATGQERN
QKPIAIIGMS GRFGGADDTE AFWNNIRDGK DSTESVNRWD LADYLNQEKY RDGVCQRGGF
LNEIDKFDAI FFNISGVEAT YMDPQQRLFL EEAWHALEDS GYAGSRLTPE VKDQFGIYVG
GWTGDYNEVF EASEAPAQAL WGNMGSMIAS RIAYYLDFKG PALTIDTACS SSLVAIHQAC
KDLRLGITNT AIAGGVFVQT TPRLYVQATQ AGMLSPTGTC SPFDENADGF VPGEAVGAII
LKRLDDALAD GDNIRAVIYG DGINQDGRTN GITAPSAVSQ EKLLKRVYKD FGITANDISM
VEAHGTGTNL GDPIEFNALC AAFTTDSAHK NYCALGSVKA NIGHTQFAAG ISSVIKSVLA
LEHSTIPPLI HHTKGNSRID LAGSPFYVAK SSQPWQARNG RRLATISAFG ASGTNAHVVL
GDLPQPVRHT AEKFGPQLIL LSANSDPQLV KLLQKLREHL ESDATVSLTN IAYTLACGRR
HFGKRVAILS RSVSELANAL GSLLSAAKPS MQIFTPSDLG QGNAQALLKQ AHVYIENGQV
NDASFQGSIC SLPASPFNSM SFWASSKDKA PAKQASVARP SPPASAPRAT ATRSKAASKY
CEFTLTVDDF FIADHLVMGQ KVLPGVMYIE LMKRSVCAVY GDKFKNAYQI ALNDIAWVQP
MVFTDATPRL PIIVEVTERG DNADLKVLSR DKKQLYAQAI CELSSGQQVL AEDQSFSHLK
AQGIRFDEID LSAAGLAQYR KVPAAQCYDL LRRHGITHKT RLQGIKALYF SPSTVIAQLQ
LPSILANKQS PFSVHPCLAD SALQAISILA VAREKAKQTR DQGGVQTRVP FAIDRFQQYR
EIPLNAWSVG HVLNDGKKEI WTIVIYDAQS NVCAVLDGYR QRILSGVPRL SEA
//
