ID M3CD52_STRMB Unreviewed; 802 AA.
AC M3CD52;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=3-oxoacyl-ACP synthase {ECO:0000313|EMBL:EMF01992.1};
GN ORFNames=H340_03184 {ECO:0000313|EMBL:EMF01992.1};
OS Streptomyces mobaraensis NBRC 13819 = DSM 40847.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1223523 {ECO:0000313|EMBL:EMF01992.1, ECO:0000313|Proteomes:UP000011740};
RN [1] {ECO:0000313|EMBL:EMF01992.1, ECO:0000313|Proteomes:UP000011740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40847 {ECO:0000313|EMBL:EMF01992.1,
RC ECO:0000313|Proteomes:UP000011740};
RX PubMed=23558536;
RA Yang H., He T., Wu W., Zhu W., Lu B., Sun W.;
RT "Whole-Genome Shotgun Assembly and Analysis of the Genome of Streptomyces
RT mobaraensis DSM 40847, a Strain for Industrial Production of Microbial
RT Transglutaminase.";
RL Genome Announc. 1:E0014313-E0014313(2013).
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000256|ARBA:ARBA00008467,
CC ECO:0000256|RuleBase:RU003694}.
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:EMF01992.1}.
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; AORZ01000005; EMF01992.1; -; Genomic_DNA.
DR RefSeq; WP_004939247.1; NZ_CP072827.1.
DR AlphaFoldDB; M3CD52; -.
DR STRING; 1223523.H340_03184; -.
DR PATRIC; fig|1223523.3.peg.652; -.
DR eggNOG; COG0304; Bacteria.
DR Proteomes; UP000011740; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProt.
DR CDD; cd00834; KAS_I_II; 1.
DR Gene3D; 3.40.47.10; -; 3.
DR InterPro; IPR000794; Beta-ketoacyl_synthase.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR11712:SF320; BETA-KETOACYL SYNTHASE; 1.
DR PANTHER; PTHR11712; POLYKETIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 2.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS52004; KS3_2; 2.
PE 3: Inferred from homology;
KW Transferase {ECO:0000256|RuleBase:RU003694}.
FT DOMAIN 1..388
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 405..799
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 802 AA; 80332 MW; 26A6F6C0A6B5CE66 CRC64;
MRIVITGLGM ISAVGSTADE CWTAIRAARS GIGTVTEVDT TGLITTQGGQ SPVKEVPGVD
RCLTLALTAA TEAVEHGRLA EAGYAPERVG VVIGSSLGTS RSVGTFHQQW LREGLRKADV
RLLKGYALHS VADAVAEKLG LGGPRSLLSN ACAAGAVAIG YALELMWSGE ADAVLVGGVD
PLAELSFNGF NSLGALDSGG CSPYTRSEGL NLGEGAGFLL LEKADTAAAR GMSAVAEVAG
YGLSADAYHQ TAPDPGGEGA QRAMAAALHS AGHTVEDVDY INGHGTGTPT NDKVEPKAIK
TLFKTPPPVS STKSMIGHTL GAAGAVEAVV CALAVRDGVL PPTANTGGAE APSGLDIVPE
AAREQDVDVV VSNSFAFGGN NAALVIRHPE RVTTEPPAAA AAAAGRDVVI TGVAGIAGAA
TGNDELFAAL AEGTPVYQGE VELDGFGTRR AGTVDFKAIA AGINPAVLRR MDPTSRLAAA
VVAELHRAYG KPSRQEAAGT GLIFATGLAP ITPVQEFDSG VVLAGGPTGA NPKFFPNTVV
NAAAGHVAIL HRFKGITATV CSGGTSALSA LHYAYRLIAR GAAERIVVVV ADECPDALVA
GHVKVPGFLG SSDVRPFAGG GTVLSAGAVA IALESTDAAR ASGRRVLGRV AGFGLTGDDS
GIAGLRPDGA AWARSMTEAL RAADLSPEDI GLVASAAMGR PAVDDAEIAA LRAGGLAERP
VTATKSVFGE TYGSAPGLAL AAALRAMADG VLPGTAGVPD APEELPGLVP QGGRQGGVDH
ALISSFAYGG SYVSLVVSKG DV
//
