FAA32_MYCMM
ID FAA32_MYCMM Reviewed; 629 AA.
AC B2HMK0;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Long-chain-fatty-acid--AMP ligase FadD32;
DE Short=FAAL;
DE EC=6.2.1.20 {ECO:0000250|UniProtKB:O53580};
DE AltName: Full=Acyl-AMP synthetase;
GN Name=fadD32; OrderedLocusNames=MMAR_5365;
OS Mycobacterium marinum (strain ATCC BAA-535 / M).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=216594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-535 / M;
RX PubMed=18403782; DOI=10.1101/gr.075069.107;
RA Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT "Insights from the complete genome sequence of Mycobacterium marinum on the
RT evolution of Mycobacterium tuberculosis.";
RL Genome Res. 18:729-741(2008).
RN [2] {ECO:0007744|PDB:5EY9}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH ALKYL ADENYLATE
RP INHIBITOR AMPC12, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=26900152; DOI=10.1074/jbc.m115.712612;
RA Guillet V., Galandrin S., Maveyraud L., Ladeveze S., Mariaule V., Bon C.,
RA Eynard N., Daffe M., Marrakchi H., Mourey L.;
RT "Insight into structure-function relationships and inhibition of the fatty
RT acyl-AMP ligase (FadD32) orthologs from Mycobacteria.";
RL J. Biol. Chem. 291:7973-7989(2016).
CC -!- FUNCTION: Involved in the biosynthesis of mycolic acids (By
CC similarity). Catalyzes the activation of long-chain fatty acids as
CC acyl-adenylates (acyl-AMP), which are then transferred to the
CC phosphopantetheine arm of the polyketide synthase Pks13 for further
CC chain extension (By similarity). Can use dodecanoate (C12) and
CC tetradecanoate (C14) (PubMed:26900152). {ECO:0000250|UniProtKB:O53580,
CC ECO:0000269|PubMed:26900152}.
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:O53580};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45589;
CC Evidence={ECO:0000250|UniProtKB:O53580};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dodecanoate + H(+) = diphosphate + dodecanoyl-AMP;
CC Xref=Rhea:RHEA:43712, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83623;
CC Evidence={ECO:0000269|PubMed:26900152};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43713;
CC Evidence={ECO:0000269|PubMed:26900152};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + tetradecanoate = diphosphate + tetradecanoyl-AMP;
CC Xref=Rhea:RHEA:43704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:33019, ChEBI:CHEBI:83626;
CC Evidence={ECO:0000269|PubMed:26900152};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43705;
CC Evidence={ECO:0000269|PubMed:26900152};
CC -!- ACTIVITY REGULATION: The acyl-AMP ligase activity is inhibited by the
CC alkylphosphate esters of AMP, adenosine 50-dodecylphosphate (AMPC12)
CC and eicosyl-AMP (AMPC20). {ECO:0000269|PubMed:26900152}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=103.2 uM for dodecanoate {ECO:0000269|PubMed:26900152};
CC KM=5.76 uM for tetradecanoate {ECO:0000269|PubMed:26900152};
CC KM=902 uM for ATP {ECO:0000269|PubMed:26900152};
CC Note=kcat is 1.51 min(-1) with dodecanoate as substrate
CC (PubMed:26900152). kcat is 0.69 min(-1) with tetradecanoate as
CC substrate (PubMed:26900152). {ECO:0000269|PubMed:26900152};
CC -!- PATHWAY: Lipid metabolism; mycolic acid biosynthesis.
CC {ECO:0000250|UniProtKB:O53580}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:26900152}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; CP000854; ACC43769.1; -; Genomic_DNA.
DR RefSeq; WP_012396868.1; NC_010612.1.
DR PDB; 5EY9; X-ray; 2.50 A; A/B=1-629.
DR PDBsum; 5EY9; -.
DR AlphaFoldDB; B2HMK0; -.
DR SMR; B2HMK0; -.
DR STRING; 216594.MMAR_5365; -.
DR EnsemblBacteria; ACC43769; ACC43769; MMAR_5365.
DR GeneID; 64258647; -.
DR KEGG; mmi:MMAR_5365; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_23_7_11; -.
DR OMA; NGRNIWP; -.
DR OrthoDB; 572620at2; -.
DR UniPathway; UPA00915; -.
DR Proteomes; UP000001190; Chromosome.
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:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
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; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR040097; FAAL/FAAC.
DR Pfam; PF00501; AMP-binding; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..629
FT /note="Long-chain-fatty-acid--AMP ligase FadD32"
FT /id="PRO_0000406636"
FT BINDING 186..191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A0R618"
FT BINDING 341
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A0R618"
FT BINDING 345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A0R618"
FT BINDING 468
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A0R618"
FT BINDING 482
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A0R618"
FT HELIX 21..31
FT /evidence="ECO:0007829|PDB:5EY9"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:5EY9"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:5EY9"
FT HELIX 56..73
FT /evidence="ECO:0007829|PDB:5EY9"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:5EY9"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:5EY9"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:5EY9"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:5EY9"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:5EY9"
FT HELIX 135..146
FT /evidence="ECO:0007829|PDB:5EY9"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:5EY9"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:5EY9"
FT HELIX 164..169
FT /evidence="ECO:0007829|PDB:5EY9"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:5EY9"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:5EY9"
FT HELIX 202..214
FT /evidence="ECO:0007829|PDB:5EY9"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:5EY9"
FT HELIX 231..238
FT /evidence="ECO:0007829|PDB:5EY9"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:5EY9"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:5EY9"
FT HELIX 252..257
FT /evidence="ECO:0007829|PDB:5EY9"
FT HELIX 260..266
FT /evidence="ECO:0007829|PDB:5EY9"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:5EY9"
FT HELIX 282..291
FT /evidence="ECO:0007829|PDB:5EY9"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:5EY9"
FT HELIX 318..328
FT /evidence="ECO:0007829|PDB:5EY9"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:5EY9"
FT STRAND 337..343
FT /evidence="ECO:0007829|PDB:5EY9"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:5EY9"
FT STRAND 348..353
FT /evidence="ECO:0007829|PDB:5EY9"
FT STRAND 362..366
FT /evidence="ECO:0007829|PDB:5EY9"
FT HELIX 367..371
FT /evidence="ECO:0007829|PDB:5EY9"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:5EY9"
FT STRAND 398..404
FT /evidence="ECO:0007829|PDB:5EY9"
FT TURN 405..408
FT /evidence="ECO:0007829|PDB:5EY9"
FT STRAND 417..423
FT /evidence="ECO:0007829|PDB:5EY9"
FT HELIX 434..441
FT /evidence="ECO:0007829|PDB:5EY9"
FT TURN 453..456
FT /evidence="ECO:0007829|PDB:5EY9"
FT STRAND 462..473
FT /evidence="ECO:0007829|PDB:5EY9"
FT STRAND 476..482
FT /evidence="ECO:0007829|PDB:5EY9"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:5EY9"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:5EY9"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:5EY9"
FT HELIX 496..505
FT /evidence="ECO:0007829|PDB:5EY9"
FT STRAND 510..521
FT /evidence="ECO:0007829|PDB:5EY9"
FT HELIX 522..524
FT /evidence="ECO:0007829|PDB:5EY9"
FT HELIX 527..531
FT /evidence="ECO:0007829|PDB:5EY9"
FT TURN 533..535
FT /evidence="ECO:0007829|PDB:5EY9"
FT STRAND 546..554
FT /evidence="ECO:0007829|PDB:5EY9"
FT HELIX 563..578
FT /evidence="ECO:0007829|PDB:5EY9"
FT STRAND 582..588
FT /evidence="ECO:0007829|PDB:5EY9"
FT HELIX 603..611
FT /evidence="ECO:0007829|PDB:5EY9"
FT TURN 612..616
FT /evidence="ECO:0007829|PDB:5EY9"
SQ SEQUENCE 629 AA; 68891 MW; 4D64231BBA802073 CRC64;
MAYHNPFIVN GKIRFPENTN LVRHVEKWAR VRGDKLAYRF LDFSTERDGV ERDILWSEFS
ARNRAVGARL QQVTQPGDRI AILCPQNLDY LISFFGALYS GRIAVPLFDP AEPGHVGRLH
AVLDDCTPST ILTTTDSAEG VRKFIRSRSA KERPRVIAVD AVPTEVASTW QQPEANELTT
AYLQYTSGST RVPSGVQITH LNLPTNVLQV LNALEGQEGD RGVSWLPFFH DMGLITVLLA
SVLGHSFTFM TPAAFVRRPG RWIRELARKP GETGGTFSAA PNFAFEHAAM RGVPRDDEPP
LDLSNVKGIL NGSEPVSPAS MRKFFKAFEP YGLRETAVKP SYGLAEATLF VSTTPMDEVP
TVIHVDRDEL NKQRFVEVAA DAPNAVAQVS AGKVGVDEWA VIVDTETASE LPDGQIGEIW
LHGNNLGIGY WGKEEESAQT FRNILKSRVP ESHAEGAPDD GLWVRTGDYG TYFKGHLYIA
GRIKDLVIID GRNHYPQDLE YTAQESTKAL RVGYVAAFSV PANQLPQKVF DDPHAGLSFD
PEDTSEQLVI VGERAAGTHK LEYQPIADDI RAAIAVGHGV TVRDVLLVSA GTIPRTSSGK
IGRRACRTAY IDGSLRSGVS SPTVFATGS
