ID L7F4J2_9ACTN Unreviewed; 1452 AA.
AC L7F4J2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Thaxtomin synthetase A {ECO:0000313|EMBL:ELP66034.1};
GN Name=txtA {ECO:0000313|EMBL:ELP66034.1};
GN ORFNames=STRTUCAR8_01752 {ECO:0000313|EMBL:ELP66034.1};
OS Streptomyces turgidiscabies Car8.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=698760 {ECO:0000313|EMBL:ELP66034.1, ECO:0000313|Proteomes:UP000010931};
RN [1] {ECO:0000313|EMBL:ELP66034.1, ECO:0000313|Proteomes:UP000010931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Car8 {ECO:0000313|EMBL:ELP66034.1,
RC ECO:0000313|Proteomes:UP000010931};
RX PubMed=21087627; DOI=10.1016/j.plasmid.2010.11.002;
RA Huguet-Tapia J.C., Badger J.H., Loria R., Pettis G.S.;
RT "Streptomyces turgidiscabies Car8 contains a modular pathogenicity island
RT that shares virulence genes with other actinobacterial plant pathogens.";
RL Plasmid 65:118-124(2011).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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:ELP66034.1}.
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DR EMBL; AEJB01000361; ELP66034.1; -; Genomic_DNA.
DR RefSeq; WP_006378967.1; NZ_AEJB01000361.1.
DR STRING; 85558.T45_09185; -.
DR PATRIC; fig|698760.3.peg.5285; -.
DR Proteomes; UP000010931; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0009403; P:toxin biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
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; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
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; PF00668; Condensation; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010931};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 929..1004
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 847..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1452 AA; 156985 MW; 314EE420391E0C92 CRC64;
MSHLTGGDRP EGALATTWPS LLEAWAADTP DAIALVTADT ALTYAQFNAR ANRLARWLKH
LGAGPERSVG LVLGRSADFF LCATAVLKCG AAYLPLDPSY PMERLSFMTR DAAPVALVTT
SDVPGELLDQ LSTRRLVSLD DEVAEDALRR LPDHDMEDGE RLEPLRPASP AYIIYTSGST
GIPKGVVVTH QGVASLIATQ RRRLAVTGVS RVLAFSSPSF DASFWEMSMA LLTGAALVVG
RPGRLLPDTE LAALIADQGV THLTLPPSVA GSLDPGMLPP GVTLVVAGEA CPAALVQRWR
PHRTMVNAYG PTESTVCATM SDPLADDMAP PVGRAVDGTR IHVLDDRLAP VVSGAVGEIF
IAGHSLARGY LKRPGLTAQR FVADPFGPAG SRMYRSGDLG RWTRSGELEF VGRADDQVKV
RGFRIEPGEI ESVLAGCRGV RQAAVVVRED RPGEPYLAAY VVPENEAADE TAEEELDGRL
AAWRRLYDDL YDRADTPDFG EDFSGWVSSY GGRPIEGMRE WRAQTVQQIR ELAPRRVLEI
GCGSGLLLSQ LAGDCESYWG TDISGALIER LRGQVAERPG LADRVVLHRL SAHELGGLPR
SGFDTVVLNS VIQYFPSGDY LFDVLREVSG LLAPGGAVFL GDVRNLRLLR TFHTGGLLAS
ASPADIPETV CAAIDRAMAQ ERELLVDPEF FATVVGALPG MTLESCTLKR GGYDNELSRY
RYEVVLRKHA GPADDPGPVV RLPWDGGTAS LAGVADWLRR GKPERVCVTG IPNGRVAGEH
AATLALFDRR PLPEVLSLGQ VPAGVAPEDL RQLGAELGYR VDCAWSSEND ALIDASFTLA
GTLVPRPAPR TDAKPDDFSP ARFTNRPAFA RPDSRTMASL PGQVAAQLPA FMVPEVFVPL
DRLPVTVNGK LDRAALPRPQ RAAPAAGRPP KTAREEVLAA IFADVLATAD VTADSDFFAT
GGNSLLATRL AAEVRHRLDT EMPLSWLFES PTVEALAARF DAEDEARPVP VPGEYASGST
APLSAQQLQM WDEYRQSLHR DMFNVPLSLR LTGAVDAEAL RAALADVVTR HVPLRTLVRD
DGSGPCAVIT EATADDIPWT QTRTTPKRLP EDLAHAARRH FDLETEIPLR AAHFTLGPNE
SVLLLVMHHI AADGWSFGPL QEDLVRAYRS RTEGHAPQWE PLSLGYLDYV AWQRRLLGSP
DDPSDVALRQ AEYWRKTLHG ADDRPVLETD SPAPSRQDFA GRSLDLPLEV GGHRVLTAAA
REHGVTVFMI LHAALVAMLA RKGAGGDITV TTAVAGRTDT QFEPLVGLFA NTLALRIDTS
GNPTFRELLY RVRVTDLAAY AHQDLLFEHL ADMPSPQVSL VLRTVAAPPS DLPGLTLAPG
PRPASESARY PVLWTVEHLA STADSGTLRS HIQYQSGLLR DDTVARIAQR YEVVLSLLLK
DPDLRVQDLP PQ
//
