ID E5B1B5_ERWAM Unreviewed; 1726 AA.
AC E5B1B5;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Probable peptide synthetase protein {ECO:0000313|EMBL:CBX79266.1};
DE EC=5.1.1.11 {ECO:0000313|EMBL:CBX79266.1};
GN ORFNames=EAIL5_0446 {ECO:0000313|EMBL:CBX79266.1};
OS Erwinia amylovora ATCC BAA-2158.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=889211 {ECO:0000313|EMBL:CBX79266.1};
RN [1] {ECO:0000313|EMBL:CBX79266.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC BAA-2158 {ECO:0000313|EMBL:CBX79266.1};
RA Powney R., Smits T.H., Sawbridge T., Frey B., Blom J., Frey J.E.,
RA Plummer K.M., Beer S.V., Luck J., Duffy B., Rodoni B.;
RT "Genome Sequence of an Erwinia amylovora Strain with Pathogenicity
RT Restricted to Rubus Plants.";
RL J. Bacteriol. 193:785-786(2011).
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 ---------------------------------------------------------------------------
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; FR719186; CBX79266.1; -; Genomic_DNA.
DR UniPathway; UPA00094; -.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0047462; F:phenylalanine racemase (ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05274; KR_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
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 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; 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; 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; 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; 2.
DR SMART; SM00827; PKS_AT; 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; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 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 Isomerase {ECO:0000313|EMBL:CBX79266.1};
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 5..80
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 97..512
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1606..1680
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1726 AA; 185250 MW; 35EFA01D15DF81EE CRC64;
MNVQREYAGV LALILEQLAV VSGVPEVDED ERLGNIALDS VKIIHLVASL GLHLGVELDP
TLFWTCPTPA ELARHIAGNT AEQPVEMQEP EGKGITAEPL AITGLACRFP GARDANAYWD
LLIGGKGAVA TADAAHFQEI PDSPWHIDPN EIAGFLDEVS AFDFEQFGIS AHEASCMDPQ
QRVLLELSWA AIEQAGISPK KIKGQRVGVY VGAMWCDFAH HVVPDKMTAQ SATGMDTSIL
SARLSFVLGL TGPSLTVNTA CSSSLVALHL ACQAIRNNDC DFAIVAGVNL LLAAQSFAAM
RRFGGLSETG LCRTFDAAAD GYIRAEGCGV VVVRPLSRVL QDAGPVWGII RSSVVNNNGY
HASLTAPSVI AQQQLLRAAL VQAKLQPSDI QYVEAHGTGT AMGDPIEVSA ISAAYCQGAA
RSQPLLIGSV KTHIGHSEAA AGMAGLIKVL LAMRYRIIPA HLNYQTPNPS INWQKLGLQL
VTGALPWETA NPVAGVSSFG FGGTNAHIIV SETWHCRSDK GVNSAASKLM ADKSDFASLA
HSEEGRALLI FSGQGAHWQG MGRSYARLHP QFRKTVAQCD RCIQQLRGWS LAERLYDERE
TFADVRVAWP CHLVMQLAIS DVWLANGLQP GGVIGHSIGE IAAAHVAGLI SREDALHIIL
AQAEWAHRHP GSMALVKLDW AAAQTLLEQQ QSSACCAIQH DENATVITGS VQALRDIESH
CQRKDISFKW VNTAVSVHRQ IGDDDRQQLI ALLGDLPGSA ALLPFYSGIY GGELLGRLPA
DYWSDTIGRP LYWFDALRQA VSDSDGPLVE VAPHSVLSSS INNLLIKLGS RREVLFNGHR
SQPEGSSLPR ALQRYPHDDP WHGLHLLLLS GHSVEALSSR CVSIARWLDG KNAPGLRDCA
RALVHCTDDY RYRVALIVSS HKEAVAQLLD IAHRAGSVAS NADNIIPSSL VITDQAPFDE
QMCSWLRRFK TFCISYSCVM LAGQDRQIAS PMLEAAAQQL GCVALLAEWG VSFDHYDATG
HACCIAELIE RRVTRNEFIS AVASSNRVHA RPVVAGDRHS VHISLPSPGQ HASCADQTPL
PARAFLELVS RCYLAGKSVD HIPGGAHPPL TLPAMFYRSA GLPPSAETHA ITAQKPVTAY
RLVWQKKSAF STSHSAQQLL VFAQTGVQAQ LQARHPFSNA AWCSLSGGPL EDNAAVSEAA
HRDAADFAAL FAGRSIETVV FIWGDSHPLV GEDPSLNSAL MLLQYIQSMP GGRPTLLFVT
LGAQAVTDSK VYSPNAAMAW GLIRTAQREL ADVQCLLVDI DPPCAAGALS EYAIDALCMS
LGAKRDQSAW RAGQLFSPGL VELTDVTPAS PLAGPPPPGF HLITGGLGAL GLELLQALFN
RGERRFVLLG RTLPEHTDRV IVDLREAGAD ILLHSCDVTC LESLHTLVRQ SAHLLGPLTA
ITHAAGVLQA DSLATVSQVD FAAGLAAKKI GALNLHIISA EWPLKRFVLV SSVSSLFGFP
QFASYAVANA YLDGLIGYRQ THGLPALGVC YGPFLGKGLL EKQHPAMDFP RLAKISISEG
LEALSACSSV QGVLAIMRYS GPLALGRSVC TPAAERPQYA LQERHARLCA VIRRGVATLL
QQPGQQIPLD TPLSELGVSS LLGVEVRNRL QSELSVRMPA TVLWNYPTVS SLASYLETLL
WPECATPYPT AHPVQTNPLV GAIDDSEEAL MAQLLDELAI IKSTYI
//
