ID   MBTM_MYCSS              Reviewed;         521 AA.
AC   Q1BBA2;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Medium/long-chain-fatty-acid--[acyl-carrier-protein] ligase MbtM {ECO:0000250|UniProtKB:A0QUA1};
DE            EC=6.2.1.20 {ECO:0000250|UniProtKB:A0QUA1};
DE            EC=6.2.1.47 {ECO:0000250|UniProtKB:A0QUA1};
DE   AltName: Full=Fatty acyl-[acyl-carrier-protein] synthetase {ECO:0000250|UniProtKB:A0QUA1};
DE            Short=Fatty acyl-ACP synthetase {ECO:0000250|UniProtKB:A0QUA1};
DE   AltName: Full=Mycobactin synthetase protein M {ECO:0000250|UniProtKB:A0QUA1};
GN   Name=mbtM; OrderedLocusNames=Mmcs_1723;
OS   Mycobacterium sp. (strain MCS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=164756;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Miller C.D., Hughes J.E., Anderson A.J., Sims R.C., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. MCS.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Activates lipidic moieties required for mycobactin
CC       biosynthesis. Converts medium- to long-chain aliphatic fatty acids into
CC       acyl adenylate, which is further transferred on to the
CC       phosphopantetheine arm of the carrier protein MbtL.
CC       {ECO:0000250|UniProtKB:A0QUA1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain fatty acid + ATP + holo-[ACP] = a long-chain
CC         fatty acyl-[ACP] + AMP + diphosphate; Xref=Rhea:RHEA:45588,
CC         Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:12682, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57560, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:133243, ChEBI:CHEBI:456215; EC=6.2.1.20;
CC         Evidence={ECO:0000250|UniProtKB:A0QUA1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a medium chain fatty acid + ATP + holo-[ACP] = a medium-chain
CC         fatty acyl-[ACP] + AMP + diphosphate; Xref=Rhea:RHEA:50460,
CC         Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:12681, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:59558, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:133242, ChEBI:CHEBI:456215; EC=6.2.1.47;
CC         Evidence={ECO:0000250|UniProtKB:A0QUA1};
CC   -!- PATHWAY: Siderophore biosynthesis; mycobactin biosynthesis.
CC       {ECO:0000250|UniProtKB:A0QUA1}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; CP000384; ABG07832.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1BBA2; -.
DR   SMR; Q1BBA2; -.
DR   PRIDE; Q1BBA2; -.
DR   KEGG; mmc:Mmcs_1723; -.
DR   HOGENOM; CLU_000022_23_7_11; -.
DR   OMA; SSCEPRH; -.
DR   BioCyc; MSP164756:G1G6O-1764-MON; -.
DR   UniPathway; UPA00011; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008922; F:long-chain fatty acid [acyl-carrier-protein] ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR   CDD; cd05931; FAAL; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 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.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR040097; FAAL/FAAC.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding.
FT   CHAIN           1..521
FT                   /note="Medium/long-chain-fatty-acid--[acyl-carrier-protein]
FT                   ligase MbtM"
FT                   /id="PRO_0000278305"
SQ   SEQUENCE   521 AA;  55020 MW;  38D49A58728ED852 CRC64;
     MASALADAMT SSGRDLVVLD HGGWRRHPWA EVHQRAENIA ARITEDAATV VVLVGEPTVE
     FIAAIPGTLY AGAALSILPG PVRGADLGQW ARNTMQRCAS IGVRLVFSHG EHLDALRATP
     ASIPTCDVTE TGHARRDSSF TPPDHGEFAV LQGTAGSTGI PRTAQLSPEA VLANLRGLVA
     CIDITPADTG CSWLPLYHDM GLAFLLTNAL GGAELWQAPT TAFSASPFSW LQWMTESTAT
     LTAAPNMAYG LIGKYGSRLT DFDLGALRFA LNGGEPVDCQ GYRRFATEMA RFGLDPSALV
     PAYGLAESSC AVTVPILGSG LQVDEVQVSS DDGRFIRTHA VVGEPIPGMQ VRIAPTDGSG
     EQVDGRDFGE IEVRGTSLMS GYLGEPPLEA GSWFPTGDLG YFVDSGLVVC GRAKELITVA
     GRNIFPAEVE RVAAQVQGVR EGAVVAVGTD ESAVRPGLVI AAEFRGTDEP AARTELVQRV
     ASECGVVPSN VVFLEPGALP RTSSGKLRRL EVKRSMEDVN R