ID A0A1I5Y0U1_9ACTN Unreviewed; 2551 AA.
AC A0A1I5Y0U1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=8-amino-7-oxononanoate synthase {ECO:0000313|EMBL:SFQ37819.1};
GN ORFNames=SAMN04489713_12922 {ECO:0000313|EMBL:SFQ37819.1};
OS Actinomadura madurae.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=1993 {ECO:0000313|EMBL:SFQ37819.1, ECO:0000313|Proteomes:UP000183413};
RN [1] {ECO:0000313|EMBL:SFQ37819.1, ECO:0000313|Proteomes:UP000183413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43067 {ECO:0000313|EMBL:SFQ37819.1,
RC ECO:0000313|Proteomes:UP000183413};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; FOVH01000029; SFQ37819.1; -; Genomic_DNA.
DR RefSeq; WP_075024805.1; NZ_FOVH01000029.1.
DR STRING; 1993.SAMN04489713_12922; -.
DR eggNOG; COG0318; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR InParanoid; A0A1I5Y0U1; -.
DR Proteomes; UP000183413; 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:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd05931; FAAL; 1.
DR CDD; cd06454; KBL_like; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major 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; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR040097; FAAL/FAAC.
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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
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; PF00155; Aminotran_1_2; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF01370; Epimerase; 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; 2.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 3.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000183413};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 685..762
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 778..1191
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 759..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1750..1784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2185..2214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1757..1784
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2196..2214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2551 AA; 269969 MW; 375903C4BBED92F2 CRC64;
MTRTHLIDGH WDGPEPETVA GILRHHLRRT PDRLAYRFLT GTGGQSESWT YRDLDARARA
VAGRLQREGL RNRPVLLLLP PGLEYVAGFL GCLYAGAIAV PAYPPDTGRT GQTLDRLAVI
ARNVRAGWAL VDEEQKRSLE TGAGSRGELG ATGIRWLAST DCGPDDADAY ADPGVSPGSL
AFLQYTSGST ATPKGVMVSN ENLVANLRTI HLTLEHDRDS ALVSWLPPYH DMGLIGGLLT
PLYGGLPAHL MAPRTFIQRP LLWLETISET RATTATSPNF GFDYCLRRIS AGQAAGLDLR
SWRLALNGAE PVRADTLDRF AERFAPCGFD RRALLPCYGL AEATLLVSGA AAGREPQVGT
LDAEALENGR AEPAAEGRRS VRSVGCGPAA DRVGVAIVDP ATRRRLPAGR VGEIWVSGPG
VARGYWRDSG ATRETFQARI EDGDGTAHLR TGDLGFERDG ELHVVGRLKD VVIVQGRNHY
PQDVELTVER ADGAVRAGCG AAFAVDVDGA EEMVVVFEVD GNRAGDTGEL LARLRAAIAR
DHDVSPHAIV LVGRASVGRT TSGKIQRQGC RRAFLSLALP VVAASVVRES GSAAATAAAP
DRARILGLIG SATGRTDVGR CSLADLGLDY TGLLDLAARL ERDLGLRVPM GELLTDPTVP
ALLRLLGADE DRAPAGHPAP GASGRSAADI EAWLVEKVAA RLGLPARTIG TTVPFATLGL
ASRTAVAIVE ELGAWLGRDL APSTVFERPT IRDVADLLGA EPEPGARPVP RSDEPGPAEP
VAVVGIGCRF PGAPDPDGYW RLLLDGRDAV AGVPAGRWDA AGVDAPARGG FLDQIDRFDA
RFFGISAREA ERMDPQQRLL LEVAWEAFED AGIAPDGAAG GDTGVFVGIS SHDYGDLQMN
DPASVDVYAA TGTAHSIAAN RLSYHFDLRG PSLAIDTACS SSLVAVHAAC RSLRAGECGM
ALAGGVNLLI NPVLSVAFAR GGMLSPDGAC RTFDDAAGGY VRGEGAGLVC LKPLSRARAD
GDRIYAVITG AAVGHGGRAN GLTAPKGSAQ RAVIERALAE AGTGGRGIDY VEAHGTGTAL
GDPVEWETLA AVYGAGRAAD APCPVGSVKA NIGHLEAAAG IAGLIKSALA VWHGELPPQL
HFTTPNRHLT WEGSGLTVLT GPAGRTRVPP SRIAVSSFGF GGANAHVIVG RADEARPAER
PGPERPVQAL CLSAHTPTAL ATLARRYRAH IAARPDVELA DLCHAANTGR AALGHRAAIT
ARSMTELGGA LTALASGEAS AGVLRGEPAG RGPRAAFLFS GQGTQYPGMG RGLYESSPVF
AEVIDRADEV LRPLIGGSLR DLVFTEDDPA RLKATRYCQP ALVAVEVALA RLWESIGVRP
AGVLGHSVGA FAAACVAGAL TLEDALTLAA TRGRLMDELP GSGAMIACAG DAAAIESAAA
ASPAVAVAAA NAPGHLVLSG PEEEIGRLTG DLQAKGVTVR RLAVSHAFHS PLMDGAAEPL
REAARAVAAR EPDIPWISDH TGEAMGRPDA GYWAGHLLGT VRFTDGVGAL RRLGCDAFVE
AGPHPALLGL VRAGLADAAG TVLSLPSLRR GGDDWQTFLR SAGRWYCAGG GVRWAGLDAG
RPRRRVPVPH AVFERSPYWL GQRREIEVNG NGYGHAGRTE GAAAPGAEAG RVLACVAQVS
GFPADQIPPH AHVGSELGLD SLMKGELERR LAPMYPGRVA ELRHTLPEDF TVAQLLDALG
IADAAPPARA YEPAVQAPPA APTPAPAPAP APAPAPAPAP VPEEPRPVVI QRRFEEWDEY
AEMLERLRLI ESSGPNAYER VHDGFNSGLI QMHGRRMVNF SAFNYLALSS HPRLRAAAKA
AIDRYGTSCS ATPLLCGETP LHHELEAEIA GFLGTEAAIV FAGGHATNVA TVGHLFGPED
LVLHDEWIHD STVRGTLLSG ARRRSFPHND WQALDRVLGA MRGRYRRAVV VIEGAYSQDG
DFPDLPRFIE VKRRHDAMLM IDEAHSLGVL GRTGRGIGEH FGVDPGDVDL WMGTLSKAIG
SLGGYIAARR PLIQFMKYTT PLYIFSTGIS PASAAAALEA FRVIRDEPER VARLRELAEH
FRSAARARGL DTGVSRETAV IPIIVGDWGR AMEISSALLD RGVNVMPIGH PAVPRDKCRL
RFFVNADHRE ADLDRSLDLL VDAMDPTSQN KRTPYEPSHV PRHRTSPRVE DRAETGGADV
LVTGASGFIG GHLTRRLTEI GHRVRVLVRE GSDRSAFADL PVEVEVGSLT DLDALLRATA
GVRHVYNCAG KSADWGPWEE FEQANVTGCR NLVDAAHHAG TVERFVHLST TDVYGYPVRP
CDERTEPKDI GLPYNRSKVL GERAVRRAAE KAGLPLTVIR PVSVYGPRSK DFVIEIANLL
KSRQMVYVRK GTAPAGLLYV GNAVDGMIAA CGSDAAAGKA YNLRDPETVT WREYIEALAA
GLGVRPPAVS LPRPLAAGVA GAAEKVYGTL RLKSRPVLTR HAVHLLERDQ SYPIDRARED
FGFKGEVAFE EGMARTIEWL ESPEGREHLG G
//
