ID C9ZDC1_STRSW Unreviewed; 1458 AA.
AC C9ZDC1;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Thaxtomin synthetase A {ECO:0000313|EMBL:CBG70279.1};
GN Name=txtA {ECO:0000313|EMBL:CBG70279.1};
GN OrderedLocusNames=SCAB_31791 {ECO:0000313|EMBL:CBG70279.1};
OS Streptomyces scabiei (strain 87.22).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG70279.1, ECO:0000313|Proteomes:UP000001444};
RN [1] {ECO:0000313|EMBL:CBG70279.1, ECO:0000313|Proteomes:UP000001444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=87.22 {ECO:0000313|EMBL:CBG70279.1,
RC ECO:0000313|Proteomes:UP000001444};
RX PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA Loria R.;
RT "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT cluster that contributes to plant-microbe interactions.";
RL Mol. Plant Microbe Interact. 23:161-175(2010).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR EMBL; FN554889; CBG70279.1; -; Genomic_DNA.
DR RefSeq; WP_010350605.1; NC_013929.1.
DR SMR; C9ZDC1; -.
DR STRING; 680198.SCAB_31791; -.
DR GeneID; 79930757; -.
DR KEGG; scb:SCAB_31791; -.
DR eggNOG; COG1020; Bacteria.
DR HOGENOM; CLU_000022_2_2_11; -.
DR Proteomes; UP000001444; Chromosome.
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; 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; 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:UP000001444};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 935..1010
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 851..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1458 AA; 157306 MW; 30944001D70E6253 CRC64;
MSHLTGEDLP EGALATTWPS LLEARVADTP DAIALVAGDT ALTYAQFNAR ANRLARWLKY
LGAGPERSVG LVLGRSADFF LCATAVLKCG AAYLPLDPNY PVERLSFMAR DAAPVVLVTT
SDVRGDLLGQ LPTGSLVVLD DEATEDVLRR LPDHDMEDGE RLEPLRPASP AYIIYTSGST
GIPKGVVVTH QGVASLIATQ RRRLAVTGAS RVLAFSSPSF DASFWEMSMA LLAGAALVVG
RPGRLLPDAE LAALIADHGV THVTLPPSVA GALGPDMLPP SVTLVVAGEA CPAALVQRWR
PHRTMVNAYG PTESTVCATM SDPLADDVAP PVGRAVDGTR IHVLDDRLAP VVPGAVGEIY
IAGHSLARGY LERPGLTAQR FVADPFGPAG SRMYRSGDLG RWTRSGDLEF VGRADDQVKV
RGFRIEPGEI ESVIAGCRGV RQAAVVLRED RPGEPYLAAY VIPENAAADE AAGEEPDGQL
DAWRRLYDDL YGRADTADFG EDFSGWVSSY GGRPIEGMRE WREQTVRQIR ELAPRRVLEI
GCGSGLLLSQ LAGDCESYWG TDISGALIER LRGQVAERPG LADRVVLHQL SAHELGSLPS
GGFDTVVLNS VIQYFPSGDY LFDLLREVSR LLVPGGAVFL GDVRNLRLLR TFHAGGLLAA
ATHTDTPQTV CAAIDRAMAQ EKELLVDPEF FTTAVGALPG MTLESCTLKR GGYDNELSRY
RYEVVLRKHA GPADDTGPTD DAGPVVRLRW DGEMASLADV ADRLRRGKPE RLCVTGIPNG
RVAGEHAATL ALFDRRPLHE VLSLGQAPAG VAPEDLRRLG AELGYRVDCT WSSEDDALID
ASFTRAGALV PRPAPRTDAE PDGFSPARFT NRPAFARPDS QTMASLPGQV AAKLPAFMVP
EVFVPLDRLP VTVNGKLDRG ALPRPRRAAH ASGRPPRTAR EEVLAAIFAD VLATADVTAD
SDFFAVGGNS LLATRLAAEV RRRLNTEMPL SWLFESPTVG ALAARFDAGD EARPLPVPSE
YASGSTAPLS AQQMQMWHEY RRSLCRDMFN VPLSQRLTGA VDAEALRAAL ADVVTRHVPL
RTLVQDDGSG PCAVITEATA DDIPWTETRT TPERLSEDLA HAARRHFDLE TEIPLRAVLF
TLGPDESVLL LVMHHIAADG WSFGPLLEDL VRAYRARTEG RAPQWEPLSF GYLDYVAWQR
RLLGATDDPS DVALRQAEYW RKTLHGADDR PVLETDSPAP AQQDFAGRSL DLPLEVGGHR
VLTAAAREHG VTVFMILHAA LVALLARRGA GGDVTVVTAV AGRTDTQFEP LVGLFANTLA
LRTDTSGNPT FRELLDRVRV TDLGAYAHQD LLFERLADVP PPQVSLVLRT VAAPPADLPG
LTISPGPRPA SESARYPVLW TVEHLASAAD GGTLRSHIQY QSGLLRDDTV VRLAQQYEVV
LSLLLKDPDL RVQDLPLQ
//
