ID A0A0L6JMG5_9FIRM Unreviewed; 2625 AA.
AC A0A0L6JMG5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=6-deoxyerythronolide-B synthase, 3-oxoacyl-(Acyl-carrier-protein) reductase {ECO:0000313|EMBL:KNY26964.1};
DE EC=1.1.1.100 {ECO:0000313|EMBL:KNY26964.1};
DE EC=2.3.1.94 {ECO:0000313|EMBL:KNY26964.1};
GN ORFNames=Bccel_2229 {ECO:0000313|EMBL:KNY26964.1};
OS Pseudobacteroides cellulosolvens ATCC 35603 = DSM 2933.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Pseudobacteroides.
OX NCBI_TaxID=398512 {ECO:0000313|EMBL:KNY26964.1, ECO:0000313|Proteomes:UP000036923};
RN [1] {ECO:0000313|Proteomes:UP000036923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2933 {ECO:0000313|Proteomes:UP000036923};
RA Dassa B., Utturkar S.M., Klingeman D.M., Hurt R.A., Keller M., Xu J.,
RA Reddy Y.H.K., Borovok I., Grinberg I.R., Lamed R., Zhivin O., Bayer E.A.,
RA Brown S.D.;
RT "Near-Complete Genome Sequence of the Cellulolytic Bacterium Bacteroides
RT (Pseudobacteroides) cellulosolvens ATCC 35603.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004789}.
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:KNY26964.1}.
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DR EMBL; LGTC01000001; KNY26964.1; -; Genomic_DNA.
DR RefSeq; WP_036947309.1; NZ_LGTC01000001.1.
DR STRING; 398512.Bccel_2229; -.
DR PATRIC; fig|398512.5.peg.2324; -.
DR eggNOG; COG0304; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR OrthoDB; 9765680at2; -.
DR Proteomes; UP000036923; Unassembled WGS sequence.
DR GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0047879; F:erythronolide synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.40.47.10; -; 3.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 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; 3.10.129.110; 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; 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; IPR036291; NAD(P)-bd_dom_sf.
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 PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
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; SSF53901; Thiolase-like; 4.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 2.
DR PROSITE; PS52004; KS3_2; 2.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:KNY26964.1};
KW Oxidoreductase {ECO:0000313|EMBL:KNY26964.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036923};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KNY26964.1}.
FT DOMAIN 8..475
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 980..1492
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1593..1672
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1689..1768
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2625 AA; 292877 MW; A5B49AF715A13135 CRC64;
MSKYYYPEDR VAIIAMGGLL PDANKIETLW QNILDKKISI REIPERFYNK NIYYKPEFFG
KSNKFNKTYT NIAAVPDVLD NTALCRKYKI PPAVAEYMDP NQHATVYCVD QVIQEIKSNI
TKERTAVILN TSAPGHNFEN VVRRTFLQRV ESEFLNHPGL KSNPMLHQIE GVFNEMQEKL
LEGNLNITED STTGYLQNLT AGRISNIFDF QGPSFTVDSA CASALTAIAI SVSGLLNHEY
DLALTGGVEV TLTEVGLVAF SAINALSPDG SYPFDSRANG FVMGLGGGII ALKRLSDAIR
DGDQIYSVIS GYGQGSDGKG KYIAAPSADG QVRVIKNAVK MAGYSAETIE MIEAHGTGTS
VGDVSEITAL KNAFSDFGVS RKNYCGVGSI KSNIGHLRNA AGVAGVIKAS MALYNKFLPP
TANVREVNPN LKIEDSPFYI LTEGMNWNEQ VSHPRRANVS SFGFGGADYH FCLEEFRGEF
VNKSYSFNDK VCEKSDNVRN DSCECQKEAL LLSGNTFYEV KESFERFLSF GESETDFGKA
AYSNNVKAAA KMKIRVAICA STYDELKEKW SMVCQQMDGN KKMDDGLLLA KGIFIGIEEP
VASDTIAFMF PGQASQYPNM LKELYESYPI VKSFYTQVDN IWRANYGYSL MPLIFGDDED
QIFNQLRNTK NTHPAIFLSN MAVYKLLTEA GVKADYMIGH SLGEVTSFYA GEILDLKSAV
YMVGERGYCF DEIDQDKRGQ MLSVKANKSD VAAIIKENGL HVRIANMNSH VQTIVGGAAS
EIESFMKLLA QSKITYTLLN VSHAFHTELI KEAAEDFYNK IKDLKFNKPK SKIMACHLKE
FYSDIEDKLQ DMAGLLKDQI TSPVNFIDSI EKLYDEGVRV FIEAGPSNVL TNLAKNILDN
KDVKVIPVNF KGKNSSESFK QALAALFAIG VDVSMVPTEN MFKTSESICR PKEYACETNS
NLLRSVDSIT SITNNILSNN DSILYSGVSV GLPGTFKKAF SDDNFDLLFE GTNFIEKLTD
EEQNSILDLN VTRLLKTEEV TEFKKISSIN EIIKFAGKFG QMDMIEDYLM DEKMLKQTSL
AVCAGVAAGY EALKDAGIPL VREYIKTASG SLLPGRLVLP EEMRDNTAII YANGLFPLDN
VITQVSKYTA SKFGSEPKMD IINFYSSVIS KISDYSSRKL LTDWFNAHYS RLVGKYTEQD
IYEFNYNFMT ILSSQANNRF AQLIGATGPN LYVNTACSST ASSVSIAEDM LRTGRAGRAI
VIGADISSTE AVLPWIGAAF LSIGVLSDSH DLFEAAVPFD DRRNGMILGS GAVGLVIEKE
TDIEKRGMKG ICRILGTHMF NSAGHNSKVD TKRHCIELDR FLLKMESEHG INRADIASKT
VYCSHETYSP KNGGCGQMEK RSLEYAFGEK FKDIKVINTK GMTGHTMGAS LEEAISAKAL
QYQNIPPISN YKVEDPDLSG LNLSKGGSYR FQYVLRGVSA FGGNGNYHLL QKVSDGDDRV
FDKTIYENWI KRIADSNDAK LSSHGRILVA EAANANYVSK KEDLNSKSIN MLGIKEEGYH
DSFLESSYRK SLQKSVNNLE ESNGSIDNDT LVEHHGCVEE EVLKIYSEIT KYPVEMLDTE
MELEADLGID TVKQATIFSM LSERFGLKYD GSIALSNYPT IGHIVRLINS KTEGENKNDK
VEGKNTVVSI DSGSGDAILD IISEITMYPK EMLESEMEFE ADLGIDTIKQ ATIFSRVGEM
FKIDDPSILN PSRIRTIGSI IQLIESTFGI ESEKQSGVNE ENKKNYDQLD REDEEQPIAD
NLERQLCIQV PEVVEENINS KDFEIQKKNV LIIGDNEDTV QKATVFFEKY TDNLHCLNFM
YPMDTEDIEK KVKELAWKSI EVIIDLTHIG LNVDVSNLSE TDEDKYLTLS SQIRFAFYKS
LSEAVKKPEV RIIAAVAMDG SFGFANKSDV IPDPFYGAIC GFYKGLGKEW TECKVKVLDI
GGFGEKVLDN EALAKIIDEI EACGSSLETG YINNKRVVIK LDNLDRADLK NDLQINDGHF
LITGGGNGIT AEIIRKLSNE MTGKFTIIGR TSLPSDIDKI SKLDASSLEK KKIEIRDALL
EKGIKATPLE VQKEYNKILK SISVYTVMNE LKSKNCSVLY INCDVRDGDK LKAAIKSAAN
VHGPVNVVIH AAGVEKSNML DKKTEEEFNE VFSIKTKGLC NLYRFLDKEQ LKVIIGFSSI
SGRFGNEAQL DYCSANNFIT SFMSMVGKEN KKVQALSIAW SGWKDIGMAW RNEFVKTNSE
ELGIHLIEPD RGAHEFINVL TSRINAAEVV ISRGLSSFKD FTVIKESTFK TPFIDWITKK
DKKVDKVYKV LSVKRDPIIK NHLLGETPLM PAVGFMEICA EFHSLLHGRK NQYCFRDITL
TNPLKLHREN SQEISMIPRQ LGEEGSYKAT FYNYFQPKNM EGRFIELNRM EIYNSSGSYG
DLEYLKNIED GNMKEFTVRD LLAGQANSIK NGIGFGPLFM DDNCKKFNKA KFNDNSIVYS
ILLSEEQITN KQYNLDNLLI NPVFMDSLMQ ACGIHSAESS GRVHLPWKIQ EFGVVNVPRT
LGSYRVYGKL LNENDDMKTY DVIMYNENDD VNYYAKGVIV RRINS
//
