ID   A0R0U9_MYCS2            Unreviewed;      1169 AA.
AC   A0R0U9;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 134.
DE   RecName: Full=Phenyloxazoline synthase MbtB {ECO:0000256|ARBA:ARBA00016743};
DE   AltName: Full=Mycobactin synthetase protein B {ECO:0000256|ARBA:ARBA00033440};
GN   OrderedLocusNames=MSMEG_4515 {ECO:0000313|EMBL:ABK71954.1};
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196 {ECO:0000313|EMBL:ABK71954.1, ECO:0000313|Proteomes:UP000000757};
RN   [1] {ECO:0000313|EMBL:ABK71954.1, ECO:0000313|Proteomes:UP000000757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000000757};
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
CC   -!- PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005102}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       MbtB subfamily. {ECO:0000256|ARBA:ARBA00007380}.
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DR   EMBL; CP000480; ABK71954.1; -; Genomic_DNA.
DR   RefSeq; WP_011729889.1; NZ_SIJM01000026.1.
DR   RefSeq; YP_888787.1; NC_008596.1.
DR   AlphaFoldDB; A0R0U9; -.
DR   STRING; 246196.MSMEG_4515; -.
DR   PaxDb; 246196-MSMEI_4403; -.
DR   GeneID; 66735843; -.
DR   KEGG; msm:MSMEG_4515; -.
DR   PATRIC; fig|246196.19.peg.4418; -.
DR   eggNOG; COG1020; Bacteria.
DR   OrthoDB; 2472181at2; -.
DR   UniPathway; UPA00011; -.
DR   Proteomes; UP000000757; 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:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd19535; Cyc_NRPS; 1.
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; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 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; IPR042099; ANL_N_sf.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   PANTHER; PTHR45527:SF10; PHENYLOXAZOLINE SYNTHASE MBTB; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   3: Inferred from homology;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000757}.
FT   DOMAIN          6..79
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1059..1135
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          82..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1169 AA;  125346 MW;  D99BB41DE88009F1 CRC64;
     MGDVAGANSQ TIRAAVADLL GIGSEAVDPD ADLIGQGLDS IRMMSLAGRW RQQGIDIDFA
     TLAANPTVSD WARLIAARSA DSKASSAHAN SRPSEAGEQA GAPFPLAPMQ HAMWVGREDD
     QQLGGVAGHL YVEFDGTGVD PERLRRAATA LAERHPMLRV EFLPDGTQRI GAPANEFPVT
     VEDLRTATPD EVARRLSEIQ RAKSHQQLQG EVFELTLSLL PSGATRLHVD LDMQAGDAMS
     YRTLMADLAA LYNSGTSLPA LGYTYREYRL ETPEGGPAHD ADQKWWAERI PDLPDPPRLP
     LIPVAEQADP HHTTRRHHWL DPQTRDALFA AARKRGITPA MALAASFAEV LAGWSADQRF
     LLNVPLFGRE QRHPDVDKII GDFTSSLLLD IDLTDTTTPT QRAKVVQDTF RAAAGHANYP
     GLSVLRDLGR HRGTQVIAPV VYTSALGLGE LFATEVTDAF GKPVWINSQG PQVLLDAQVT
     EFDGGVLVNW DVREDAFRPG VIDAMFARHI AELRRLATDD TAWDIPSPPL LPQSQRDVRD
     AVNARSAAPS GRALHDGFFE QAAMRPGAVA LIGSNGPLTY AELREQALAV ATALRVAGVR
     RGESVAVMGP KGPDQIPALL GILAAGAVYV PVGVDQPTDR AERMLADAGV RMALFCGDGT
     PTWLPALTVT EAVLVGRRHE TVEPVSAAPD DLAYVLFTSG STGEPKGVEV THDAAMNTVE
     TLNTYFGTGP GDSVLALTHL ESDLSVLDVF GTLAAGGSIV MVDEADRRNP DHWVAQINAH
     GVTTLNFLPG SLEMLVETAW STRTPMPSLR AVPTGGDWVR TTMVRKLQQL SPGVVLTGLG
     GATETAIHAT LFEAKELPEH WTAVPYGAPF PNNACRVVNA AGQDCPDWVP GELWIGGRGI
     ARGYRGKPDL TAEKFVTWCG RRWYRTGDLA RYWPDGTLEF VGRADHRVKL SGYRIELGEV
     EAALQRLPGV HAAVADIVDT PAGDLLAAVV GLDDTSVTDA DLRAGLAELL PPHMVPRHFE
     LTGKVPFTVG GKTDRRAVAR LLAEAVEQAQ AGGRGTARRP ETSLERALAA ILGELLSVAD
     VGADEDFFEL GGDSVLATAA VARIRDWLDT PTVMVPDIFA TRTVEKLASR LVAREADGSR
     LEQVAELYLE VAAMDDAAVM SALDTAATS
//