FAC15_MYCTU
ID FAC15_MYCTU Reviewed; 600 AA.
AC O53521; L0T8V6;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase FadD15;
DE Short=FACL;
DE EC=6.2.1.3 {ECO:0000269|PubMed:15042094, ECO:0000269|PubMed:19182784};
DE AltName: Full=Acyl-CoA synthetase;
DE AltName: Full=FACL15 {ECO:0000303|PubMed:19182784};
GN Name=fadD15; OrderedLocusNames=Rv2187;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION AS AN ACYL-COA SYNTHETASE, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15042094; DOI=10.1038/nature02384;
RA Trivedi O.A., Arora P., Sridharan V., Tickoo R., Mohanty D., Gokhale R.S.;
RT "Enzymic activation and transfer of fatty acids as acyl-adenylates in
RT mycobacteria.";
RL Nature 428:441-445(2004).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=19182784; DOI=10.1038/nchembio.143;
RA Arora P., Goyal A., Natarajan V.T., Rajakumara E., Verma P., Gupta R.,
RA Yousuf M., Trivedi O.A., Mohanty D., Tyagi A., Sankaranarayanan R.,
RA Gokhale R.S.;
RT "Mechanistic and functional insights into fatty acid activation in
RT Mycobacterium tuberculosis.";
RL Nat. Chem. Biol. 5:166-173(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Catalyzes the activation of long-chain fatty acids as acyl-
CC coenzyme A (acyl-CoA), which are then transferred to the
CC multifunctional polyketide synthase (PKS) type III for further chain
CC extension. {ECO:0000269|PubMed:15042094, ECO:0000269|PubMed:19182784}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC Evidence={ECO:0000269|PubMed:15042094, ECO:0000269|PubMed:19182784};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000269|PubMed:19182784};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + dodecanoate = AMP + diphosphate + dodecanoyl-CoA;
CC Xref=Rhea:RHEA:33623, ChEBI:CHEBI:18262, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:19182784};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33624;
CC Evidence={ECO:0000269|PubMed:19182784};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-
CC CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:19182784};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC Evidence={ECO:0000269|PubMed:19182784};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP44964.1; -; Genomic_DNA.
DR PIR; E70937; E70937.
DR RefSeq; NP_216703.1; NC_000962.3.
DR RefSeq; WP_003906768.1; NZ_NVQJ01000008.1.
DR AlphaFoldDB; O53521; -.
DR SMR; O53521; -.
DR STRING; 83332.Rv2187; -.
DR SwissLipids; SLP:000000981; -.
DR PaxDb; O53521; -.
DR PRIDE; O53521; -.
DR DNASU; 887456; -.
DR GeneID; 887456; -.
DR KEGG; mtu:Rv2187; -.
DR TubercuList; Rv2187; -.
DR eggNOG; COG1022; Bacteria.
DR InParanoid; O53521; -.
DR OMA; PRIWTKF; -.
DR PhylomeDB; O53521; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016405; F:CoA-ligase activity; IBA:GO_Central.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:MTBBASE.
DR GO; GO:0071766; P:Actinobacterium-type cell wall biogenesis; IDA:UniProtKB.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008610; P:lipid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:MTBBASE.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
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 Pfam; PF00501; AMP-binding; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..600
FT /note="Long-chain-fatty-acid--CoA ligase FadD15"
FT /id="PRO_0000406784"
SQ SEQUENCE 600 AA; 64035 MW; DCA7C09033C3CEBA CRC64;
MREISVPAPF TVGEHDNVAA MVFEHERDDP DYVIYQRLID GVWTDVTCAE AANQIRAAAL
GLISLGVQAG DRVVIFSATR YEWAILDFAI LAVGAVTVPT YETSSAEQVR WVLQDSEAVV
LFAETDSHAT MVAELSGSVP ALREVLQIAG SGPNALDRLT EAGASVDPAE LTARLAALRS
TDPATLIYTS GTTGRPKGCQ LTQSNLVHEI KGARAYHPTL LRKGERLLVF LPLAHVLARA
ISMAAFHSKV TVGFTSDIKN LLPMLAVFKP TVVVSVPRVF EKVYNTAEQN AANAGKGRIF
AIAAQTAVDW SEACDRGGPG LLLRAKHAVF DRLVYRKLRA ALGGNCRAAV SGGAPLGARL
GHFYRGAGLT IYEGYGLSGT SGGVAISQFN DLKIGTVGKP VPGNSLRIAD DGELLVRGGV
VFSGYWRNEQ ATTEAFTDGW FKTGDLGAVD EDGFLTITGR KKEIIVTAGG KNVAPAVLED
QLRAHPLISQ AVVVGDAKPF IGALITIDPE AFEGWKQRNS KTAGASVGDL ATDPDLIAEI
DAAVKQANLA VSHAESIRKF RILPVDFTED TGELTPTMKV KRKVVAEKFA SDIEAIYNKE
