ID A0A0N0N2C5_9ACTN Unreviewed; 744 AA.
AC A0A0N0N2C5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=6-deoxyerythronolide-B synthase {ECO:0000313|EMBL:KPI16459.1};
DE EC=2.3.1.94 {ECO:0000313|EMBL:KPI16459.1};
DE Flags: Fragment;
GN ORFNames=OK074_8435 {ECO:0000313|EMBL:KPI16459.1};
OS Actinobacteria bacterium OK074.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592327 {ECO:0000313|EMBL:KPI16459.1, ECO:0000313|Proteomes:UP000037991};
RN [1] {ECO:0000313|EMBL:KPI16459.1, ECO:0000313|Proteomes:UP000037991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK074 {ECO:0000313|EMBL:KPI16459.1,
RC ECO:0000313|Proteomes:UP000037991};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:KPI16459.1}.
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DR EMBL; LJCV01000097; KPI16459.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0N2C5; -.
DR PATRIC; fig|1592327.3.peg.3158; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000037991; Unassembled WGS sequence.
DR GO; GO:0047879; F:erythronolide synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR CDD; cd08956; KR_3_FAS_SDR_x; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 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; IPR036736; ACP-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000313|EMBL:KPI16459.1};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000037991};
KW Transferase {ECO:0000313|EMBL:KPI16459.1}.
FT DOMAIN 666..741
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..51
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KPI16459.1"
SQ SEQUENCE 744 AA; 77132 MW; 30ECDDF18EA7554A CRC64;
PGQPARSSRR ARGPPDPPEW GGLWATQAAR GVTAREPPSP RAPPPAPPCP RHAHATIGSG
AEPAAFDLEL WPPADAEPRT PPAPDHLLRG LWHHGDDLFA EVELPAEYRA EGPRHGLHPA
LLDTALRAFA PDPSQLPDTW HHLVLHAEGA SSLRVRLTRT GDDTVSVAAA DDTGLPVATI
GAVRLRPADP ARLTDARAAR SGPLLRLDWP EVRCEAPKAK PRWALVGPDP LDARPALMKA
GVYTEAYDNL GALAKALDSG TAAPEAVLVA GVPDRADPTP VRQVRQAVEL LGEWLSDERF
AAVRLVFLTR GSLAAEDGAT APDPAAGALW GLVRCAQQAE PGRLVLADLD AKRASWRALP
AALASGEPQL ALVAGTLRVP RLTTVPAAPS GDPALAIDPT GTVLVTGGLR PAATAVVRHL
VTGHGVRHLL LAAPGEEAAA TTPLVAELAA LGAGTTVLDC DPADASALAA LPAAVPAGHP
LTAVVHVAGS GEDADLEREF KAALNLSVLT ERQVIDPAVP LLLLSSAVGT LGAVGRGGEA
ALGAFLDALA RRRRSAGLAG AASAWGSWTT ADGPVGGPLD GTVRLPRTAV LDLFDAACAL
GVTGAVLLRP DTRALAGRGG DDRLAAPLRG LAGPPARRRA GQRGSAGVLS TIRRRLAGLS
DAERDAVLVE LVRTDVAAVL DYPSPEAVEV TRAFRDIGLN SLTAFALRNR LRETTGLRLP
AALLFEADTP GRLATHLKEQ LLRR
//
