ID A0A1A3PD27_9MYCO Unreviewed; 1763 AA.
AC A0A1A3PD27;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OBK32123.1};
GN ORFNames=A5658_16985 {ECO:0000313|EMBL:OBK32123.1};
OS Mycobacterium sp. 1245111.1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834073 {ECO:0000313|EMBL:OBK32123.1, ECO:0000313|Proteomes:UP000092232};
RN [1] {ECO:0000313|EMBL:OBK32123.1, ECO:0000313|Proteomes:UP000092232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1245111.1 {ECO:0000313|EMBL:OBK32123.1,
RC ECO:0000313|Proteomes:UP000092232};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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:OBK32123.1}.
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DR EMBL; LZLV01000159; OBK32123.1; -; Genomic_DNA.
DR RefSeq; WP_067342548.1; NZ_LZLV01000159.1.
DR STRING; 1834073.A5658_16985; -.
DR OrthoDB; 9778690at2; -.
DR Proteomes; UP000092232; 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; 3.10.129.120; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
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; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020807; PKS_DH.
DR InterPro; IPR049551; PKS_DH_C.
DR InterPro; IPR049552; PKS_DH_N.
DR InterPro; IPR013968; PKS_KR.
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: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; PF21089; PKS_DH_N; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 33..462
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1645..1722
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1724..1763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1763 AA; 185920 MW; D7347697B9C324F8 CRC64;
MTAPPDRRAI ITEALRKIDD LTARLEIAEK ADLEPIAVVG MACRLPGGVN TPDDYWQLLH
EGRSGVIRVP EDRWDADAYF TDDHTRPGTI ANREGGFLTS WQPDQFDAEF FGISPREAIG
MDPQHRLLLE VAWEALENAG VTPKAARNSQ TGIYVGLTTS DYYWLSTAGG VRPEDFDPYL
VFGSASNFAA GRLSYFLGTH GPAVVLDTAC SSSLVAIHLA CQSLRRRETD YALAAGTNLI
LTPENSIACS RWGMLAPDGQ CKTFDASADG YVRSEGCGVV VLKRLSDAER DGDNVLALVR
GSAVNQDGPS SGQTVPSGPA QQAVMRAALA SARLEPSDID YIEAHGTGTA LGDPIELDAL
TAVFGQRDES APLVLGSVKT NLGHLENSAG IAGFIKTVLS LNHGFIPPHL HFTELTPNAG
AGASKFTIAA DGMPWPQVSR PRRAGVSSFG VSGTNAHVVI EQASGPEPAK NTAAQPEPTV
STLVISGKTP ARIAPIAEML ADWMSGAGAD VPLADVANTV NNYRGRYRSF AAVVARDPEQ
AVAGLRALAA GEPATGVVEA CEKPNGSGTV FLYSGQGSQW AGMGRQLLAE EPAFAAAVDE
LEPDFVAQVG FSLKDVLLAG EPVVGIDRIQ PVLVGMQLAL TALWRSYGVE PDAVIGHSMG
EVTAAVVSGA LSPADGLKVI ATRSKLMLRL SGQGAMALLE LGAEEAEKLA GQHPDVTVAV
YAAPQQTVIA GPPEQVDAAI AAVDAQGLLA RRIEVDVASH HPTVDPILAE LKDALADLKP
QTPRIPLIST VGQADPKFDA DYWVVNLRNP VRFSQAVAKA AQTHATFVEI SPHPLLTHGI
GETLASVASR DQFAVTAAMK RGDDETLSVH EQLATLGVTG DQTGRRRVDI PASPWLHASY
WVEKKPAAQR RTDVHPLLGA HVELPSGNEH VWQTDIDLQT LPWLADNTIG GQAVVSAAGF
AEMALAAVSQ AMGAATVSKL TIERPLVLDA QTRVTTQLSL SPDVNRVEIQ ARSAGGTWTR
YAVADVIDAG APTGQPGDGI EIALPDEVAD HPEYRIHPVL LDAALRQLAA AVPAESEDAS
YQAVSVEAIR VFAPIRGRAR VHTELADDRG RVVLTDDAGA VLAELTGVEL KPVDLASVPL
SLEQKIFDAA WSQSPAPAGD AVADGTWMVL AETDSETTEL ASQLVDKLTS STRWAVSAPL
GDESAVAAAF AKTADSKPVG IVVLLAKAPF NGEDTEATDA ALRRAHDLVL DISAAAHAAV
DGWKGTSPRL WLVTRDGLSV HDDEPGDPAI GALKGLIRNW RFPGEAARVL AGEPDLGATL
LDVGSGEVVD KVIHELAAST GDDVVALRED GRYVERMVRA SLDGERHEAV VRPDGSYIVT
GGLGGLGTVV TRWLVEQGAG RIVLNGRREP SDEQRAYLAG LGTDVVFVAG DIATAGTAER
LVAAAEETGK PLRGLVHGAG VTGDGLVSAL TREGLERVWT PKVAGALRLN TATATKEMDW
WVGFSSMATM LGLPGQLAYA TGNAWLDALM TWRRAAGRPA TAINWGQWSA VGMSSKLTYS
VLDPITPDEG IEALQTLVGG PLNRVGVGRL RLDRVLAATP EFRDLAYFER IAAEFGTHTV
EHRAASGEDS VSAAAPDWST LSADERLTEL QTRLQAILGR ELRMSPSSIN LDAPFPELGL
DSMMAMTVLK ETKKLVGLDV SANMLFNHPT IASLATYVTG LLAPADEPEE DSGGSAAEPE
RSVLDDLFDS VESASASTDG GLF
//
