ID A0A0I9UTN6_9MYCO Unreviewed; 1489 AA.
AC A0A0I9UTN6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Polyketide synthase {ECO:0000313|EMBL:KLO34591.1};
GN ORFNames=ABH38_18515 {ECO:0000313|EMBL:KLO34591.1};
OS Mycobacterium haemophilum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=29311 {ECO:0000313|EMBL:KLO34591.1, ECO:0000313|Proteomes:UP000036334};
RN [1] {ECO:0000313|EMBL:KLO34591.1, ECO:0000313|Proteomes:UP000036334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UC1 {ECO:0000313|Proteomes:UP000036334};
RA Greninger A.L., Cunningham G., Miller S.;
RT "Genome sequence of Mycobacterium haemophilum.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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:KLO34591.1}.
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DR EMBL; LDPR01000024; KLO34591.1; -; Genomic_DNA.
DR RefSeq; WP_047316493.1; NZ_LDPT01000028.1.
DR STRING; 1202450.B586_03515; -.
DR PATRIC; fig|29311.18.peg.2595; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000036334; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
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; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation 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; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
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; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF51; PHENOLPHTHIOCEROL_PHTHIOCEROL POLYKETIDE SYNTHASE SUBUNIT E; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000036334};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..438
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 924..998
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1489 AA; 159375 MW; 0A8FE70C7925F5E5 CRC64;
MNTPDNAIAV VGMAGKFPGA NDVSAFWTNL RRGKESIVTL SEQELRDNGV SDKTLADPAY
VRRAPLLDGI DEFDADFFGL PPLAAQVLDP QHRLFLQCAW HALEDAGCDP AQFDGSIGVY
GTSSPSGYLL HNLLSQRDPH AVLAEGLNFD QFSLFLQNDK DFLATRISHA FNLRGPSIAV
QTACSSSLVA LHLACLSLLS GECDMALAGG SSLCIPHRVG YWNSPGSMVS AVGHCRPFDV
RADGTVFGSG VALVALKPLQ AAIDAGDRIH AVIRGSAINN DGSMKMGYAA PNPAAQADVI
AEAHAVAGID SSTVSYVETH GTGTPLGDPI EIQGLKTAFE VSQTPRPGPC VLGSVKSNIG
HLEVAAGIAG LIKTILCLKN KAIPATLHYT SPNPELRLDQ TPFVVQSKYG PWEWDGVRRA
GVSSFGVGGT NAHVILEEAP EVPAHAAPIG PQVILLSAQT AAALGESRAA LATVLEKSGG
PDLSDVAYTL ARRRKHDVTM AAVVRDREHA VTVLRAAEHD NVFVGESADA TESSSDRVVF
LFPGQGAQHV EMAKGLYDTE PVFAEHFDTC AAGFREAMGD LDLHSAIFSG TATDLERIDR
SQPALFTVEY ALAKLVDSYG VRAGAYIGYS TGEYIAATLA GVFDLETAIK TVSLRARLMH
ESPPGAMVAV ALGPDDITKY LAEYAAKGVE LSAVNDPGNC VVAGPKDQIR AFSQRLNEAG
IPVRRVRATH AFHTSSMNPM LAEFSEFLSR QQLRVPSTPL LSNLTGTWMS EQQVTDPESW
TRQISSTIRF ADELDVVLSQ PGRVLVEVGP GGSLTGSAMR HSKWSSEHRT VRLMRHPLQN
TDDRDTFLRA LGELWSAGVE VDWTPRRSAN LNSGPHLVSL PGYPFARQRY WVEPKHTVWT
QVPGTSNDAP IGARAEATVD GAHSGASQTE ATLQRIWSQC LGVSSVDRNA NFFDLGGDSL
MAISISMAAA NEGMTITPQD MYEHPTLASL TAAVDASFAS SGLAKPPEAA AHPAVPPNIA
YFVERGLRDI GRWCVPLILR LDPKVTPDDI RAVLTAVVNH HDALRLNLID NDGLWEQHIA
GPADFTRLST RSLPDDVAAD SAEERAAVSS ILDELIAENG ANQAYSDGPL AAVQITTSHG
GPHYLGLVVH QMVADDASRQ ILGTDIVTAF GQRLAGEEIA LEPITTGWRE WSLRCAALAT
HPAALDSRSF WIENANKVNL WPTDAIPNAP SIDATQPPGA NDLTKVSCTL SGEQTSQLDD
ARRRFRRSIQ AIVLAALGRT IAQAVGDGVV TVELEGEGRS VLRPDVDLRR TVGWFTTYYP
VPLTCAKGQG ALAELDAVHN TLKSVPHYGI GYGLLRYVYA PTGRVLGAQR TPDIHFRYAG
VIPELPSVDA PVQFDSDATL PVREPIPGLG HAIELRAYRS GGSLHLDWWY DTRRIPQETA
EALARSFPAT LSKLIQEGIA MQQDQHDESE IVGAPQAGAL VDLSSLDAG
//
