ID A3D2I0_SHEB5 Unreviewed; 2693 AA.
AC A3D2I0;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Beta-ketoacyl synthase {ECO:0000313|EMBL:ABN60943.1};
GN OrderedLocusNames=Sbal_1425 {ECO:0000313|EMBL:ABN60943.1};
OS Shewanella baltica (strain OS155 / ATCC BAA-1091).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=325240 {ECO:0000313|EMBL:ABN60943.1, ECO:0000313|Proteomes:UP000001557};
RN [1] {ECO:0000313|EMBL:ABN60943.1, ECO:0000313|Proteomes:UP000001557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS155 / ATCC BAA-1091 {ECO:0000313|Proteomes:UP000001557};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I.,
RA Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS155.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000256|ARBA:ARBA00008467}.
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; CP000563; ABN60943.1; -; Genomic_DNA.
DR RefSeq; WP_011846330.1; NC_009052.1.
DR STRING; 325240.Sbal_1425; -.
DR KEGG; sbl:Sbal_1425; -.
DR HOGENOM; CLU_000022_30_2_6; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000001557; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR CDD; cd08953; KR_2_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 5.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
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; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR004432; Omega_3_polyunsat_FA_synth.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR NCBIfam; TIGR02813; omega_3_PfaA; 1.
DR PANTHER; PTHR43074; OMEGA-3 POLYUNSATURATED FATTY ACID SYNTHASE PFAB-RELATED; 1.
DR PANTHER; PTHR43074:SF1; PKS_AT DOMAIN-CONTAINING PROTEIN; 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; PF08659; KR; 1.
DR Pfam; PF00550; PP-binding; 5.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; ACP-like; 5.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS50075; CARRIER; 5.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 26..481
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1264..1344
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1365..1445
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1466..1546
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1568..1648
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1675..1755
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 2320..2363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2332..2346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2347..2361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2693 AA; 285553 MW; C0DE1A6BA85A6DB4 CRC64;
MSHTPSVPNS ATESKKDKRL NKRLKDMPVA IVGMASIFAN SRYLNKFWDL ISEKIDAITD
IPDTHWHAED YYDADKSKAD KSYCKRGGFL PEVDFNPMEF GLPPNILELT DTSQLLSLIV
AKEVLADANL PTDYDRDRIG ITLGVGGGQK ISQSLNSRLQ YPVLKKVFKS SGLSDEDSEM
LIKKFQDQYI HWEENSFPGS LGNVIAGRIA NRFDFGGMNC VVDAACAGSL AAMRMALTEL
TEGRSDMMIT GGVCTDNSPS MYMSFSKTPA FTTNETIQPF DIDSKGMMIG EGIGMVALKR
LEDAERDGDR IYAVIKGVGA SSDGKFKSIY APRPEGQAKA LERAYDDAGF APHSIGLVEA
HGTGTAAGDV AEFNGLKSVF AQGNDTNQHI ALGSVKSQVG HTKSTAGTAG VIKAALALHH
KVLPATINVS QPNPKLNIES SPFYLNTETR PWFQRADATP RRAGVSSFGF GGTNFHLVLE
EYKPEHSRDE QYRQRSVPQT LLFAAANKAA LLSELKAALS QSVNTNANKS SAASLNAIAQ
QYPLRTLAST DARLGFVAKD IAQLQAQLNQ SIAHLETNAI EVWQLPSGIS YRSHALVAKN
ESKKVAALFA GQGSQYLNMG RELACHFPEM RQQVMASDKV FAHHGQTPLS NILYPIPAFD
ADAVKAQEAA LTNTLFAQSA IGAISMAQYS LLTQAGFAPD MVAGHSFGEL SALCAAGVIS
NEDYVELAFA RGHAMAQVPS DTASKAADTG TQTDLGTMFA IILKQKNDID ALNSCLAQFD
GVKIANYNAP TQLVIAGGTE QTQLAAKAIS ELGFKAIALP VSGAFHTPLV GHAQKPFAKA
IDKAKFSAPS VALYANGTGQ LHPTDGKAIK AEFKQHMLQS VRFSEQLQAM YDAGARVFVE
FGPKNILQKL VENTLGEHLN ELCLVSMNPN PKGDSDSQLR LAAVQLAVAG VALTEVDPYQ
AITSQEIAER EAPSAMNIKL TATNHISAAT KAKMAKSLAT GSVTSQVQYV DRIVETVVEK
EVEKIVEKQV IVEKVVEKII EVEANQVAAV EMKQTSPSVV QGLSNHQQQA TAQLSPNTPN
ISSDALTAFF SAQSHVAQLH QQFLAIPQQY GDTFTTLMTE QAKMASQGIT IPESLQRSME
MFHQHQAQTL QSHAEFMQLQ SSSSQAALAM LNNAPINFTP AVASQPRVTA PAPAPVAAST
VAHNAAPVAA QAVATRPAVS TPIPPVVQTA PVAFAPAVTV QVAPAAPVLV MPEMTSVAPA
TSSLSAALVQ QTMMAVVADK TGYPTEMLEL GMDMEADLGI DSIKRVEILG TVQDELPGLP
ELSPEDLAEC RTLGEIVDYM NSKLPAAGQV VVSTTAPTAP AANGLSAALV QQTMMAVVAD
KTGYPTEMLE LGMDMEADLG IDSIKRVEIL GTVQDELPGL PELSPEDLAE CRTLGEIVDY
MNSKLPAAGQ VVVSTTAPTA PAANGLSAAL VQQTMMAVVA DKTGYPTEML ELSMDMEADL
GIDSIKRVEI LGTVQDELPG LPELSPEDLA ECRTLGEIVD YMNSKLPAVG SVIVATHVTT
AAPAASGLSA ALVQQTMMAV VADKTGYPTE MLELSMDMEA DLGIDSIKRV EILGTVQDEL
PGLPELNPED LAECRTLGEI VDYMNSKLPV VSAVAVAPAA NVEATPAQVP ANNGLSAEKV
QQTMMSVVAD KTGYPTEMLE LSMDMEADLG IDSIKRVEIL GTVQDELPGL PELNPEDLAE
CRTLGEIVSY MQGKLGQNTA ANVVNVAVAA EPAIDLPHDL PPHSEVVLKK LPAAAELAQK
ATQQSAQQAV TRTFAKDACI IISDDGHNAG VLAEKLHAQG LTVAVVRSPE SLVASASPLN
SHIASFTLAA IDDASISAVI NEIKSLGTVA GFIHLQPQHK TSADAKGLVL SCAAKASVEQ
AFLFAKHLQP FLTTAATANT DSSFISVSRI DGGFGYLNHS QIARSELNQA ALAGLTKTLS
HEWPSVHCRA LDIAPALDAK QLANAVIAEL FATDKLLEVG VSEAGATETL ARVTLVAGKA
DTRHSAANLT SADKILVTGG AKGVTFECAL SLAKRSKAHF ILAGRSSQQA IPAWAQGKNN
SELKAAAIAH IQSLGEKPTP KQVDALVWPV QSSLEIAAAL EAFSAVGASA EYLSLDVNNP
DAIASTIVPI TELSPITGII HGAGVLADKH IQDKTLDELA RVYGTKVTGI SNLLAALDLD
KVKLIALFSS AAGFYGNTGQ SDYAMSNDIL NKAALQLAQQ LPNAKVMSFD WGPWDGGMVN
PALKKMFMDR GVYVIPLKAG AELFASQLLS NTGAQLLVGT DMQGSAPHDD TSNKVQETEG
SNLKKPEADL TTDSSGPHAL PNAVNPSAVK LQRTLDPKAM IFIEDHCING NPVLPTVCAI
QWMREAAFDV LKQPVKVQSY KLLKGIIFDA VMLEKGALEN GAPITLELEL APIALTDKAA
KDTDECLSGQ FSALISFEGR PQYQAILVID DAVDDAANDY LATNSKATAF DAQSLAGLSA
ITTASSLYSD GTLFHGPRLQ GIESVVKFDD ASLVAKVSLP HFALADCGSF VPNLAPKGSQ
AFAEDLLLQA MLVWARLKYG AASLPSSIGE FISHAPFAFG DKGYLVLEVV KHSGRALEAN
IALYHQDGRL SCEMSNAKVT ISKNLNGAFL ANKVAANQTA ANKAIESVEA KVE
//
