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Database: UniProt
Entry: Q194Q9_STRAA
LinkDB: Q194Q9_STRAA
Original site: Q194Q9_STRAA 
ID   Q194Q9_STRAA            Unreviewed;       514 AA.
AC   Q194Q9;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Acyl CoA ligase {ECO:0000313|EMBL:CAK50779.1};
GN   Name=mtmL {ECO:0000313|EMBL:CAK50779.1};
OS   Streptomyces argillaceus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=41951 {ECO:0000313|EMBL:CAK50779.1};
RN   [1] {ECO:0000313|EMBL:CAK50779.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 12956 {ECO:0000313|EMBL:CAK50779.1};
RX   PubMed=8807845; DOI=10.1016/S1074-5521(96)90262-8;
RA   Blanco G., Fu H., Mendez C., Khosla C., Salas J.A.;
RT   "Deciphering the biosynthetic origin of the aglycone of the aureolic acid
RT   group of anti-tumor agents.";
RL   Chem. Biol. 3:193-196(1996).
RN   [2] {ECO:0000313|EMBL:CAK50779.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 12956 {ECO:0000313|EMBL:CAK50779.1};
RX   PubMed=8654997; DOI=10.1016/0378-1119(96)00029-7;
RA   Lombo F., Blanco G., Fernandez E., Mendez C., Salas J.A.;
RT   "Characterization of Streptomyces argillaceus genes encoding a polyketide
RT   synthase involved in the biosynthesis of the antitumor mithramycin.";
RL   Gene 172:87-91(1996).
RN   [3] {ECO:0000313|EMBL:CAK50779.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 12956 {ECO:0000313|EMBL:CAK50779.1};
RX   PubMed=8757400; DOI=10.1007/s004380050218;
RA   Fernandez E., Lombo F., Mendez C., Salas J.A.;
RT   "An ABC transporter is essential for resistance to the antitumor agent
RT   mithramycin in the producer Streptomyces argillaceus.";
RL   Mol. Gen. Genet. 251:692-698(1996).
RN   [4] {ECO:0000313|EMBL:CAK50779.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 12956 {ECO:0000313|EMBL:CAK50779.1};
RX   PubMed=9375253; DOI=10.1016/S1074-5521(97)90313-6;
RA   Kantola J., Blanco G., Hautala A., Kunnari T., Hakala J., Mendez C.,
RA   Ylihonko K., Mantsala P., Salas J.;
RT   "Folding of the polyketide chain is not dictated by minimal polyketide
RT   synthase in the biosynthesis of mithramycin and anthracycline.";
RL   Chem. Biol. 4:751-755(1997).
RN   [5] {ECO:0000313|EMBL:CAK50779.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 12956 {ECO:0000313|EMBL:CAK50779.1};
RX   PubMed=9150235;
RA   Lombo F., Siems K., Brana A.F., Mendez C., Bindseil K., Salas J.A.;
RT   "Cloning and insertional inactivation of Streptomyces argillaceus genes
RT   involved in the earliest steps of biosynthesis of the sugar moieties of the
RT   antitumor polyketide mithramycin.";
RL   J. Bacteriol. 179:3354-3357(1997).
RN   [6] {ECO:0000313|EMBL:CAK50779.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 12956 {ECO:0000313|EMBL:CAK50779.1};
RX   PubMed=9733697;
RA   Fernandez E., Weissbach U., Reillo C.S., Brana A.F., Mendez C., Rohr J.,
RA   Salas J.A.;
RT   "Identification of two genes from Streptomyces argillaceus encoding
RT   glycosyltransferases involved in transfer of a disaccharide during
RT   biosynthesis of the antitumor drug mithramycin.";
RL   J. Bacteriol. 180:4929-4937(1998).
RN   [7] {ECO:0000313|EMBL:CAK50779.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 12956 {ECO:0000313|EMBL:CAK50779.1};
RX   PubMed=9889148; DOI=10.1016/S1074-5521(99)80017-9;
RA   Prado L., Fernandez E., Weissbach U., Blanco G., Quiros L.M., Brana A.F.,
RA   Mendez C., Rohr J., Salas J.A.;
RT   "Oxidative cleavage of premithramycin B is one of the last steps in the
RT   biosynthesis of the antitumor drug mithramycin.";
RL   Chem. Biol. 6:19-30(1999).
RN   [8] {ECO:0000313|EMBL:CAK50779.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 12956 {ECO:0000313|EMBL:CAK50779.1};
RX   PubMed=9917296; DOI=10.1021/np980355k;
RA   Wohlert S.E., Kunzel E., Machinek R., Mendez C., Salas J.A., Rohr J.;
RT   "The structure of mithramycin reinvestigated.";
RL   J. Nat. Prod. 62:119-121(1999).
RN   [9] {ECO:0000313|EMBL:CAK50779.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 12956 {ECO:0000313|EMBL:CAK50779.1};
RX   PubMed=10102355; DOI=10.1007/s004380050960;
RA   Prado L., Lombo F., Brana A.F., Mendez C., Rohr J., Salas J.A.;
RT   "Analysis of two chromosomal regions adjacent to genes for a type II
RT   polyketide synthase involved in the biosynthesis of the antitumor
RT   polyketide mithramycin in Streptomyces argillaceus.";
RL   Mol. Gen. Genet. 261:216-225(1999).
RN   [10] {ECO:0000313|EMBL:CAK50779.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 12956 {ECO:0000313|EMBL:CAK50779.1};
RX   PubMed=10760873;
RX   DOI=10.1002/(SICI)1521-3773(20000218)39:4<796::AID-ANIE796>3.0.CO;2-N;
RA   Lombo F., Kunzel E., Prado L., Brana A.F., Bindseil K.U., Frevert J.,
RA   Bearden D., Mendez C., Salas J.A., Rohr J.;
RT   "The Novel Hybrid Antitumor Compound Premithramycinone H Provides Indirect
RT   Evidence for a Tricyclic Intermediate of the Biosynthesis of the Aureolic
RT   Acid Antibiotic Mithramycin.";
RL   Angew. Chem. Int. Ed. 39:796-799(2000).
RN   [11] {ECO:0000313|EMBL:CAK50779.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 12956 {ECO:0000313|EMBL:CAK50779.1};
RX   PubMed=10779713; DOI=10.1111/j.1574-6968.2000.tb09082.x;
RA   Garcia-Bernardo J., Brana A.F., Mendez C., Salas J.A.;
RT   "Insertional inactivation of mtrX and mtrY genes from the mithramycin gene
RT   cluster affects production and growth of the producer organism Streptomyces
RT   argillaceus.";
RL   FEMS Microbiol. Lett. 186:61-65(2000).
RN   [12] {ECO:0000313|EMBL:CAK50779.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 12956 {ECO:0000313|EMBL:CAK50779.1};
RX   PubMed=10652287; DOI=10.1074/jbc.275.5.3065;
RA   Lozano M.J., Remsing L.L., Quiros L.M., Brana A.F., Fernandez E.,
RA   Sanchez C., Mendez C., Rohr J., Salas J.A.;
RT   "Characterization of two polyketide methyltransferases involved in the
RT   biosynthesis of the antitumor drug mithramycin by Streptomyces
RT   argillaceus.";
RL   J. Biol. Chem. 275:3065-3074(2000).
RN   [13] {ECO:0000313|EMBL:CAK50779.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 12956 {ECO:0000313|EMBL:CAK50779.1};
RX   PubMed=10660060; DOI=10.1007/PL00008667;
RA   Blanco G., Fernandez E., Fernandez M.J., Brana A.F., Weissbach U.,
RA   Kunzel E., Rohr J., Mendez C., Salas J.A.;
RT   "Characterization of two glycosyltransferases involved in early
RT   glycosylation steps during biosynthesis of the antitumor polyketide
RT   mithramycin by Streptomyces argillaceus.";
RL   Mol. Gen. Genet. 262:991-1000(2000).
RN   [14] {ECO:0000313|EMBL:CAK50779.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 12956 {ECO:0000313|EMBL:CAK50779.1};
RX   PubMed=11254130; DOI=10.1007/s004380000372;
RA   Gonzalez A., Remsing L.L., Lombo F., Fernandez M.J., Prado L., Brana A.F.,
RA   Kunzel E., Rohr J., Mendez C., Salas J.A.;
RT   "The mtmVUC genes of the mithramycin gene cluster in Streptomyces
RT   argillaceus are involved in the biosynthesis of the sugar moieties.";
RL   Mol. Gen. Genet. 264:827-835(2001).
RN   [15] {ECO:0000313|EMBL:CAK50779.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 12956 {ECO:0000313|EMBL:CAK50779.1};
RX   PubMed=11853433; DOI=10.1021/ja0105156;
RA   Remsing L.L., Garcia-Bernardo J., Gonzalez A., Kunzel E., Rix U.,
RA   Brana A.F., Bearden D.W., Mendez C., Salas J.A., Rohr J.;
RT   "Ketopremithramycins and ketomithramycins, four new aureolic acid-type
RT   compounds obtained upon inactivation of two genes involved in the
RT   biosynthesis of the deoxysugar moieties of the antitumor drug mithramycin
RT   by Streptomyces argillaceus, reveal novel insights into post-PKS tailoring
RT   steps of the mithramycin biosynthetic pathway.";
RL   J. Am. Chem. Soc. 124:1606-1614(2002).
RN   [16] {ECO:0000313|EMBL:CAK50779.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 12956 {ECO:0000313|EMBL:CAK50779.1};
RX   PubMed=12022840; DOI=10.1021/ja017385l;
RA   Trefzer A., Blanco G., Remsing L., Kunzel E., Rix U., Lipata F.,
RA   Brana A.F., Mendez C., Rohr J., Bechthold A., Salas J.A.;
RT   "Rationally designed glycosylated premithramycins: hybrid aromatic
RT   polyketides using genes from three different biosynthetic pathways.";
RL   J. Am. Chem. Soc. 124:6056-6062(2002).
RN   [17] {ECO:0000313|EMBL:CAK50779.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 12956 {ECO:0000313|EMBL:CAK50779.1};
RX   PubMed=12733914; DOI=10.1021/ja034162h;
RA   Remsing L.L., Gonzalez A.M., Nur-e-Alam M., Fernandez-Lozano M.J.,
RA   Brana A.F., Rix U., Oliveira M.A., Mendez C., Salas J.A., Rohr J.;
RT   "Mithramycin SK, a novel antitumor drug with improved therapeutic index,
RT   mithramycin SA, and demycarosyl-mithramycin SK: three new products
RT   generated in the mithramycin producer Streptomyces argillaceus through
RT   combinatorial biosynthesis.";
RL   J. Am. Chem. Soc. 125:5745-5753(2003).
RN   [18] {ECO:0000313|EMBL:CAK50779.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 12956 {ECO:0000313|EMBL:CAK50779.1};
RX   PubMed=12813091; DOI=10.1128/JB.185.13.3962-3965.2003;
RA   Rodriguez D., Quiros L.M., Brana A.F., Salas J.A.;
RT   "Purification and characterization of a monooxygenase involved in the
RT   biosynthetic pathway of the antitumor drug mithramycin.";
RL   J. Bacteriol. 185:3962-3965(2003).
RN   [19] {ECO:0000313|EMBL:CAK50779.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 12956 {ECO:0000313|EMBL:CAK50779.1};
RX   PubMed=14660589; DOI=10.1074/jbc.M312351200;
RA   Rodriguez D., Quiros L.M., Salas J.A.;
RT   "MtmMII-mediated C-methylation during biosynthesis of the antitumor drug
RT   mithramycin is essential for biological activity and DNA-drug
RT   interaction.";
RL   J. Biol. Chem. 279:8149-8158(2004).
RN   [20] {ECO:0000313|EMBL:CAK50779.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 12956 {ECO:0000313|EMBL:CAK50779.1};
RX   PubMed=15712316; DOI=10.1002/cbic.200400309;
RA   Nur-e-Alam M., Mendez C., Salas J.A., Rohr J.;
RT   "Elucidation of the glycosylation sequence of mithramycin biosynthesis:
RT   isolation of 3A-deolivosylpremithramycin B and its conversion to
RT   premithramycin B by glycosyltransferase MtmGII.";
RL   ChemBioChem 6:632-636(2005).
RN   [21] {ECO:0000313|EMBL:CAK50779.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 12956 {ECO:0000313|EMBL:CAK50779.1};
RA   Lombo F.;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [22] {ECO:0000313|EMBL:CAK50779.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 12956 {ECO:0000313|EMBL:CAK50779.1};
RA   Rohr J.;
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; X89899; CAK50779.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q194Q9; -.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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   PANTHER; PTHR43767; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   PANTHER; PTHR43767:SF1; NONRIBOSOMAL PEPTIDE SYNTHASE PES1 (EUROFUNG)-RELATED; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:CAK50779.1}.
FT   DOMAIN          19..378
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   DOMAIN          427..502
FT                   /note="AMP-binding enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13193"
FT   REGION          324..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          495..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   514 AA;  54171 MW;  A88F7539276BBBAD CRC64;
     MSELPPGPAV PLDGLLRLAA ERHPEQVAVR DERGAVDYAG LDARADRFAR ALLRLTGGRP
     TAVGVASVLD PVFAAAFYGT SRSGNRVVLV NPLVREPVLE HVFRTAGIEI ALVSAETRSP
     GGRRAALPDL REVYVVDADR TGPPPPGTRP LDDLLTEDGT AALPDPAGVD LDSVVCVQFT
     SGTTGPPKGV RLTHRNLVAN AAQAAHALGL DAGSVCLNHL PLYHVMHLDS AVYAGATQVL
     CHDPDPVASV AAAAEAGATH YFGLPVRLAR LAADPRLASV VPGPELGLVR SGGSRLAPAV
     AARLRERLGV PVIQGYGLAE LSPLSHNDRP ERSKPGSVGP AVPGTECRIV DLETGAALDP
     GRPGEVLLRG PQLMAGYLGL PDAPDIDAAG WFHTGDVGYQ DEDGWLFLVD RIKDVFKVDN
     ELVSPSEIEQ VLLQDPDVAD CVVADLPDEF SGAVVWAGVV PAGDGPVDLN PIVARANALL
     SDHQRIRRAE RLTAVPRSPN GKTERTRLRE RLRA
//
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