ID I3TNP9_TISMK Unreviewed; 922 AA.
AC I3TNP9;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=AMP-dependent synthetase and ligase {ECO:0000313|EMBL:AFK54387.1};
GN Name=ppsD {ECO:0000313|EMBL:AFK54387.1};
GN OrderedLocusNames=TMO_2549 {ECO:0000313|EMBL:AFK54387.1};
OS Tistrella mobilis (strain KA081020-065).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC Geminicoccaceae; Tistrella.
OX NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK54387.1, ECO:0000313|Proteomes:UP000005258};
RN [1] {ECO:0000313|EMBL:AFK54387.1, ECO:0000313|Proteomes:UP000005258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK54387.1,
RC ECO:0000313|Proteomes:UP000005258};
RX PubMed=22458477; DOI=10.1021/ja301735a;
RA Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT agents.";
RL J. Am. Chem. Soc. 134:8625-8632(2012).
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DR EMBL; CP003236; AFK54387.1; -; Genomic_DNA.
DR AlphaFoldDB; I3TNP9; -.
DR STRING; 1110502.TMO_2549; -.
DR KEGG; tmo:TMO_2549; -.
DR PATRIC; fig|1110502.3.peg.2614; -.
DR eggNOG; COG1020; Bacteria.
DR eggNOG; COG3208; Bacteria.
DR HOGENOM; CLU_319533_0_0_5; -.
DR Proteomes; UP000005258; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR036736; ACP-like_sf.
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; IPR042099; ANL_N_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR001031; Thioesterase.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:AFK54387.1};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005258}.
FT DOMAIN 579..648
FT /note="Polyketide synthase phosphopantetheine-binding"
FT /evidence="ECO:0000259|SMART:SM00823"
SQ SEQUENCE 922 AA; 95772 MW; DA7E6C8D33498863 CRC64;
MAAAPGDDMI GRPAATPEAL LVPIAPDRLE RPVFAVFADC AARNPRAPAV LGPGAATTYG
DLLGQALRIA AAIDGRRGAR GEGLGGEGLG GEGSGGEGPE PVAVAIPASA GCLAALLGAL
AAGRPYVPID PSFPAARNEL ILGHAGVRLV LTDRATAAGR PELMAAAMAA GATVLAIDDL
APPPAGWSPR GGPDDAAYVL YTSGSTGRPK GVWQTQRGLL HDVFQYRDVL DISAADRLTW
LYSPAVNGAI RDMYGALLAG AAVIPVDLRT EGVAAAGRRF AATRPTIFHA MPTVLRVLAD
GGAGPAALGG IRVAYLAGER ILAADLARVF ADAPADARIY VGIGSTENAT IYRHWLIDRE
TCPTNGVVPV GWPVADRSMR LVDAGGRPVP DGDIGEIEVE SRYMAAGYWR DPELTAATFL
TGGDVAPGAR RLRPGDLGRI RADGQLEFLG RADGQLKIRG HRVEPAEVEA ALRALPGVGD
AAVLPDRTPQ GETALAGVVV PAPGRLIDPA ALRSRLAAEL PPHLVPRRLL VMAELPRLAN
FKLDGRALAD CLADLPTVPL ASPAPALVSV GETGDPALAD AVDRAWAEMF GAAAPLAGMT
FTELGGDSLE LMRFATRVET LAGRPLPVTL LNGAITPADL RRALSGGMAG VTDRLLFFVP
GVMGMARHLI VLAARCAGMA TVRLVALPDL DAELSRRRGI EDLAAEVADR IAAHLTGAAG
PDGATPDFGL VGLSFGGRLA VAAAQILADR GLVAGMVVVG DIVASHDDAA SLLQAGRIPE
PSPGFRRRLV RGIGQPMSKL FFTLAQRPDH RALRLVAAFA RRAAPGRRNR IRVERALISA
IRRAMIVGWQ PGRLDCRLLL IVTSHTRSSY AGHGHLLGWD RVSSDVRLVE VAGDHAALAT
DEANLARIVA AIGDAWPDQP SA
//
