ID A0A2U9T821_9GAMM Unreviewed; 2463 AA.
AC A0A2U9T821;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Thioester reductase {ECO:0000313|EMBL:AWV07722.1};
GN ORFNames=C9I47_2037 {ECO:0000313|EMBL:AWV07722.1};
OS Lysobacter maris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1605891 {ECO:0000313|EMBL:AWV07722.1, ECO:0000313|Proteomes:UP000249447};
RN [1] {ECO:0000313|EMBL:AWV07722.1, ECO:0000313|Proteomes:UP000249447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HZ9B {ECO:0000313|EMBL:AWV07722.1,
RC ECO:0000313|Proteomes:UP000249447};
RA Zhang X.-Q.;
RT "The complete genome of Lysobacter maris HZ9B, a marine bacterium
RT antagonistic against terrestrial plant pathogens.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000256|ARBA:ARBA00008467}.
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DR EMBL; CP029843; AWV07722.1; -; Genomic_DNA.
DR KEGG; lmb:C9I47_2037; -.
DR OrthoDB; 9030879at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000249447; Chromosome.
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:0008483; F:transaminase activity; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd12117; A_NRPS_Srf_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; 3.40.50.980; -; 2.
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; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR010071; AA_adenyl_domain.
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; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
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; IPR006162; Ppantetheine_attach_site.
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 NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 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 SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 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; PS00600; AA_TRANSFER_CLASS_3; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
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:UP000249447};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 731..809
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 831..1257
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1757..1839
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 865..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1709..1756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1841..1862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2420..2455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1726..1741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2463 AA; 260648 MW; 46AEC255CDE4B6A8 CRC64;
MNEPIAPVGA SPEASTLLEV LPGRAGSASS QRQRIEVPLA DTLRAALESI DAAGRADLLV
AALALSESRL TGADRILATR FDRDGGHQGD VEIVGEDDPD AWCRRVASQL QPMAPAQMRD
CIWAVATRDC DRSAAAAASL WGLSGDVLAV LEVGFQAPLS STAVETMAVA LTRVLEALLR
EPRVEAIDVA TAEECHWATP LGAGADPAAG GHRSVVSAFM AMVARYPDAT AVVDRTAALS
YGQLDARANA LAARLGDAGV APGAVVAIAM RRSIDAIVAV LGILKSGAAY LPLDDAYPSE
RLAFMLEDAA ASAVVVDADG DGGSIAQDLP RVVCEAFDPP AEGAAVPLEA PVATPAAGPD
DRRDRQSLAY VMYTSGSTGT PKGVEIPDGA ILRLVCDVDY IGLGPSTRML HAAPLGFDAS
TLEIWGPLLN GGCVVVHDER MPTASGLADA IERHAVTTAW LTAALFNTVV DDDPRHLAGL
EELFTGGEAL SVPHVRRMLA AAPGTRLRNG YGPTECTTFA CTHAIEPGLD ADAASIPIGR
PIAGTCLRVL SRQRRPLPLG VVGELYIGGA GLANGYLNRE SLTAERFVAD PFAAQPARLY
RTGDLVRARP DGAIEFVGRA DTQVKIRGYR IELGEIEAAL AKHPGVRACA VEARGDGATE
KRLIAYLQPA AAPVPAPELR CFLSRTLPEF MLPARFIALD TWPLTPNGKL DRRRLPEPDA
SRPDLANAYE PPLGTIETAI CDAFGTVLGI DGVGRHDNFF ELGGSSLLAV RLVEALSAAA
PAELAAITTI DLFRQPTPQR LAAALDRRCV RTASASAPEA RAARRSRPDD DDPIAIVAMA
GRFPGAADVE AFWDNLCEGR DTITSFDPSQ LDPSIPREER EDPGYVPARG VIEGVDRFDA
AFFGIGPREA ELMDPQQRLF LETCWECMER AGYVPDDAGG PVGVFAGMYN GSYFQRHVSP
RKDLIGTIGA FQVMLGNEKD YIATRTANKL NLTGPAVSVH TACSTSLVAI CQAVQAIRSG
QCEMALAGGA SVTCPPNSGY LYQEGAMLSP DGHTRTFDAD ARGTVFSDGV AAVLLKRLSA
ARADGNRVYA VVTGIGVNND GGHKASFTAP SSEGQAAVIA MAHDDAGVDA RSIGYVEAHG
TATPLGDPIE IEGLTRAFRR STDDVGFCRV GSLKSNVGHM VIAAGAASVI KTALSLSERK
IPASLHYQRA NPDIAFAGSP FVVNDALHPW QGDGGPLRAG VSSFGVGGTN AHVVLEQAPP
TPCSDPAKGP QTIVLSARSG DALQAACVRL AGFLEAAPDA NLADVAWTLA RGRKAFAHRV
ALTCTDIGDA IAQLRGRELE SAISRGKPVR ESGVVFMFPG QGATYPGMGR GLYDAEPEFR
KAIDQCAEVL SEPLGFDLRT RLFSDEADAL LPTAIMQPAT FAIEYALARV WMAQGLRPVA
MLGHSVGEFV AATLAGVFAL EDALRLVARR GALMQAQPAG GMLSIRMSAQ DVRTRMPDDL
QVAAENAPGT CVVAGPGDSI RGFAQALEGD GVVCRELRTS HAFHSAMMDP VVAPFEAEVA
SVPLSPPSLP IVSTVSAELL GDAEATSARY WSRHLRQPVR FAAALEAVAT MNPAQVLLEV
GPRRTLSGLA RQHPAIRERG GRALESLADS PGAELHSLRR AAGQLWAAGV DIDAAGFDRR
QRRARLRLPT YPFQRRRFWI EAAVAGTPSS DAGRASAHDA AESPAQTPPT AASAATETQV
PSPSAPRPPT APAAAAASAV PRALRLRARL SELIEDVAGF DLSDADPDDN FMELGLDSLM
LTQIALQLQK TFSVQVAFRQ LMGECSSLAS LASMLDAELP PEAEPAVPAE SPDTAMPAPP
AAAAAMPPMP AVPAPMPDAG APAGGGFVRE VIAQQMQLMT QQLALLGGQA PMAASAAVAA
PVEAAPAADT TAPPAPADAA DEETALSHTR YDVKKAFGAI ARIHSSADEL TGRQRARLDA
FIRRYTARTQ RSKEYTQAHR SHLADPRVVN GFRPLLKEIT YQIVVCRSQG ARVWDLDGNE
YVDVLNGFGM NLFGWQPDFV LDAVRQQLDL GYEIGPQHPL AGEVAKLVCE VTGSARAALC
NTGSEAVMGT IRIARTVTGR NTLVIFTGSY HGIFDEVIVR GTRKLKSIPA APGILRNTAE
NVLVLDYGTP ETLDIIRERA DDIAAVLVEP VQSRRPDFQP GEFLKELREV TAQAGSLLIF
DEVVTGFRAH ARGAQELFGI DADLVSYGKV VGGGFPIGVI AGKREYMDAL DGGYWQFGDD
SIPTVGVTYF AGTFVRHPLA LAAAKAVLEH VRDAGPSLQQ LLNARTTAMA EEMNAFCEEV
GAPISIKHYT SFWKVAFTED HPLQDLLFAM MRSRGVHILD NFPCFFTTAH SEADFAHVVD
AFRESVLELQ EAEFVPRHRE TEPAFDANNP PIPGARLGRD PDGKPAWFVP DPGTPGKFLK
VSA
//
