ID D8AGW8_ECOMS Unreviewed; 1602 AA.
AC D8AGW8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Beta-ketoacyl synthase, N-terminal domain protein {ECO:0000313|EMBL:EFK17608.1};
DE Flags: Fragment;
GN ORFNames=HMPREF9530_05841 {ECO:0000313|EMBL:EFK17608.1};
OS Escherichia coli (strain MS 21-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=749527 {ECO:0000313|EMBL:EFK17608.1, ECO:0000313|Proteomes:UP000005688};
RN [1] {ECO:0000313|EMBL:EFK17608.1, ECO:0000313|Proteomes:UP000005688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS 21-1 {ECO:0000313|EMBL:EFK17608.1,
RC ECO:0000313|Proteomes:UP000005688};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
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}.
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:EFK17608.1}.
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DR EMBL; ADTR01000533; EFK17608.1; -; Genomic_DNA.
DR HOGENOM; CLU_000022_33_0_6; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000005688; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
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; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001227; Ac_transferase_dom_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; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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; PF08659; KR; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
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:ARBA00023098};
KW Transferase {ECO:0000256|ARBA:ARBA00023315}.
FT DOMAIN 26..449
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT NON_TER 1602
FT /evidence="ECO:0000313|EMBL:EFK17608.1"
SQ SEQUENCE 1602 AA; 174791 MW; 2F7256710CA4857C CRC64;
MDNLRFSSAP TADSIDASIV QHYPDCEPVA VIGYACHFPE SPDGETFWQN LLEGRECSRR
FTREELLAVG LDAAIIDDPH YVNIGTVLDN ADCFDATLFG YSRQEAESMD PQQRLFLQAV
WHALEHAGYA PGAVPHKTGV FASSRMSTYP GREALNVTEV AQVKGLQSLM GNDKDYIATR
AAYKLNLHGP ALSVQTACSS SLVAVHLACE SLRAGESDMA VAGGVALSFP QQAGYRYQPG
MIFSPDGHCR PFDASAEGTW AGNGLGCVVL RRLRDALLSG DPIISVILSS AVNNDGNRKV
GYTAPSVAGQ QAVIEEALML AAIDDRQVGY IETHGTGTPL GDAIEIEALR NVYAPRPQDQ
RCALGSVKSN MGHLDTAAGI AGLLKTVLAV SRGQIPPLLN FHTPNPALKL EESPFTIPVS
AQAWQDEMRY AGVSSFGIGG TNCHMIVASL PDALNARLPN TDSGRKSTAL LLSAASDSAL
RRLATDYAGA LRENADASSL AFTALHARRL DLPFRLAAPL NRETAEALSA WAGEKSGALV
YSGHGASGKQ VWLFTGQGSH WRTMGQTMYH HSTAFADTLD RCFSACSEML TPSLREAMFN
PDSAQLDNMA WAQPAIVAFE IAMAAHWRAE GLKPDFAIGH SVGEFAAAVV CGHYTIEQVM
PLVCRRGALM QQCASGAMVA VFADEDTLMP LARQFELDLA ANNGTQHTVF SGPEARLAVF
CATLSQHDIN YRRLSVTGAA HSALLEPILD RFQDACAGLH AEPGQIPIIS TLTADVIDES
TLNQADYWRR HMRQPVRFIQ SIQVAHQLGA RVFLEMGPDA QLVACGQREY RDNAYWIASA
RRNKEASDVL NQALLQLYAA GVALPWADLL AGDGQRIAAP CYPFDTERYW KERVSPACEP
ADAALSAGLE VASRAATALD LPRLEALKQC ATRLHAIYVD QLVQRCTGYA IENGVDAMTI
MRRGRLLPRY QQLLQRLLNN CVVDGDYRCT DGRYVRARPI EHQQRESLLT ELAGYCEGFQ
AIPDTIARAG DRLYEMMSGA EEPVAIIFPQ SASDGVEVLY QEFSFGRYFN QIAAGVLRGI
VQTRQPRQPL RILEVGGGTG GTTAWLLPEL NGVPALEYHF TDISALFTRR AQQKFADYDF
VKYSELDLEK EAQSQGFQAQ SYDLIVAANV IHATRHIGRT LDNLRPLLKP GGRLLMREIT
QPMRLFDFVF GPLVLPLQDL DAREGELFLT TAQWQQQCRH AGFSKVAWLP QDGSPNAGMS
EHIILATLPG QAVSAVTFTA PSEPVLGQAL TDNGDYLADW SDCAGQPEQF NARWQEAWRL
LSQRHGDALP VEPPPVAAPE WLGKVRLSWQ NEAFSRGQMR VEARHPAGEW LPLSPAAPLP
APQTHYQWRW TPLNVASIDH PLTFSFSAGT LARSDELAQY GIIHDPHASS RLMIVEESED
TLALAEKVIA ALTASAAGLI VVTRRAWRVE ENEALSASHH ALWALLRVAA NEQPERLLAA
IDLAENTPWE TLHQGLSAVS LSQRWLAARG DTLWLPSLSP NTGCAAELPA NVFTGDSRWH
LVTGAFGGLG RLAVNWLREK GARRIALLAP RVDESWLRDV EG
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