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Database: UniProt
Entry: I3TX49_TISMK
LinkDB: I3TX49_TISMK
Original site: I3TX49_TISMK 
ID   I3TX49_TISMK            Unreviewed;      1160 AA.
AC   I3TX49;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Amino acid adenylation domain protein {ECO:0000313|EMBL:AFK57337.1};
GN   OrderedLocusNames=TMO_c0727 {ECO:0000313|EMBL:AFK57337.1};
OS   Tistrella mobilis (strain KA081020-065).
OG   Plasmid pTM3 {ECO:0000313|EMBL:AFK57337.1,
OG   ECO:0000313|Proteomes:UP000005258}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC   Geminicoccaceae; Tistrella.
OX   NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK57337.1, ECO:0000313|Proteomes:UP000005258};
RN   [1] {ECO:0000313|EMBL:AFK57337.1, ECO:0000313|Proteomes:UP000005258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK57337.1,
RC   ECO:0000313|Proteomes:UP000005258};
RC   PLASMID=Plasmid pTM3 {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; CP003239; AFK57337.1; -; Genomic_DNA.
DR   AlphaFoldDB; I3TX49; -.
DR   KEGG; tmo:TMO_c0727; -.
DR   PATRIC; fig|1110502.3.peg.5603; -.
DR   HOGENOM; CLU_000022_2_17_5; -.
DR   Proteomes; UP000005258; Plasmid pTM3.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   CDD; cd05930; A_NRPS; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 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   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR013120; Far_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR010080; Thioester_reductase-like_dom.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   NCBIfam; TIGR01746; Thioester-redct; 1.
DR   PANTHER; PTHR44845:SF6; BETA-ALANINE-ACTIVATING ENZYME; 1.
DR   PANTHER; PTHR44845; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   PIRSF; PIRSF001617; Alpha-AR; 3.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Plasmid {ECO:0000313|EMBL:AFK57337.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005258}.
FT   DOMAIN          679..754
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1160 AA;  122609 MW;  14518DD73F26FFAA CRC64;
     MSAPDQALCR TRGAIPLDRL PALLAVLVHR WRALPQPRIA VADAGGLRIL ALEVTADARL
     GDLVPEGPTP DATEGPADAL LVPEPAGDLP AVALALRVEA DGRLRVVLDR RLCRPPFDEA
     RASDLAHALD RLIAAGADAA LGAVDLISPA RRYELLIERN GPRRPCPTAP AIPDAIRAIA
     RRDPQRVALV HETARLTFGE LDARADRLAA MLAARGVGRG DMLPLLMPNG LELPLAMLAA
     MKLGAPFVPM DDGWAPERIA ALLDALAPRL VIAADPAVVP PGVAALILDH AAILPAETPF
     DAVAVDGRDP IYGFYTSGTT GLPKCAINLH GGLLNRFGVM TRRFAADGRP PVVLQNSRHV
     FDSSIWQLLW PLTIGGRVII PRTRGVLDLE TTLRTIAAHE IEMTDFVPSI FNAMVDLMVA
     EPGLVRRLGS LRHLLIGGEE IDPRAVRRFR RMLPGIGIVN TYGPTEASIG MVFHHVGDAD
     DRSIPIGTPI DNTVAVVVDD HGFIAPPGMV GEIRIGGACL GGGYLGAPEK TAAAHVDNPF
     PELPGDRLYR TGDLGYWRRD GRLAYVGRRD DQVKIGGVRI ELGEIEGALA DHPDIRAGRV
     VVHEQGGRRE LVACLIGHGE VDTADLRRFL ATRLPRQALP ARLLVLDALP LNANGKVDRR
     ALARLANDRL EAAAAADAGF TDPTSAALAA RWRATLQLAP AGPEDGFFDL GGTSLTALVL
     AMDLTRHFGM RISVADIFTH PTLGALAALI DRRRRGEETG SAPVPAPEVR LADDIRPSAG
     AAAWTPPSGR VRVLLTGATG FVGAHLLPAL LARPDVDLVC LVRAEDDAAA ALRLGIAADR
     VTVLAGDLAL PQLGLGDAVW RRLAEGIDVI VNAGALVNLL HGYAAHAAAN VAGVETLLRL
     AVTGVPKHVH QVSTLSVFAR SPGHDAVTEA DAADPRALPQ DGYSRSKWAA ERLIDEARRR
     GITGSLHRLG EMLPARRSGL GNPQALVERL TAACLRLGLR FPTGLRFDYS PVDIVAAFVA
     ARLTEPAGTF HLYGPGTRFE DLLDEAEAAG IALTPVSYAA FHERLSRAAA SDVDAAALLA
     LLPDPAGDAG ADAFATADLV ADKDLMFGDA ASRAAMAAAG LAWPAVDAGL LAPWFARRRA
     ACPHPSGDVF SDESASEETA
//
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