FAC17_MYCTU
ID FAC17_MYCTU Reviewed; 502 AA.
AC O53551; L0TCQ9;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Medium/long-chain-fatty-acid--CoA ligase FadD17;
DE Short=FACL;
DE EC=6.2.1.2 {ECO:0000269|PubMed:19182784};
DE EC=6.2.1.3 {ECO:0000269|PubMed:15042094, ECO:0000269|PubMed:19182784};
DE AltName: Full=Acyl-CoA synthetase;
DE AltName: Full=FACL17 {ECO:0000303|PubMed:19182784};
DE AltName: Full=Steroid-24-oyl-CoA synthetase {ECO:0000303|PubMed:24244004};
GN Name=fadD17; OrderedLocusNames=Rv3506;
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).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24244004; DOI=10.1128/jb.01012-13;
RA Casabon I., Swain K., Crowe A.M., Eltis L.D., Mohn W.W.;
RT "Actinobacterial acyl coenzyme A synthetases involved in steroid side-chain
RT catabolism.";
RL J. Bacteriol. 196:579-587(2014).
CC -!- FUNCTION: Catalyzes the activation of medium/long-chain fatty acids as
CC acyl-coenzyme A (acyl-CoA), which are then transferred to the
CC multifunctional polyketide synthase (PKS) type III for further chain
CC extension (PubMed:15042094, PubMed:19182784). Also involved in steroid
CC side-chain degradation. Activates cholesterol metabolites with a C5
CC side chain, including cholate and chenodeoxycholate (PubMed:24244004).
CC {ECO:0000269|PubMed:15042094, ECO:0000269|PubMed:19182784,
CC ECO:0000269|PubMed:24244004}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty
CC acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2;
CC Evidence={ECO:0000269|PubMed:19182784};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341;
CC Evidence={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 + hexanoate = AMP + diphosphate + hexanoyl-CoA;
CC Xref=Rhea:RHEA:43740, ChEBI:CHEBI:17120, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:19182784};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43741;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cholate + CoA = AMP + choloyl-CoA + diphosphate;
CC Xref=Rhea:RHEA:23532, ChEBI:CHEBI:29747, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57373,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:24244004};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23533;
CC Evidence={ECO:0000269|PubMed:24244004};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + chenodeoxycholate + CoA = AMP + chenodeoxycholoyl-CoA +
CC diphosphate; Xref=Rhea:RHEA:43764, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:36234, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:62989, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:24244004};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43765;
CC Evidence={ECO:0000269|PubMed:24244004};
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; CCP46328.1; -; Genomic_DNA.
DR PIR; D70806; D70806.
DR RefSeq; NP_218023.1; NC_000962.3.
DR RefSeq; WP_003901655.1; NZ_NVQJ01000042.1.
DR AlphaFoldDB; O53551; -.
DR SMR; O53551; -.
DR STRING; 83332.Rv3506; -.
DR ChEMBL; CHEMBL5783; -.
DR SwissLipids; SLP:000000982; -.
DR PaxDb; O53551; -.
DR DNASU; 888251; -.
DR GeneID; 888251; -.
DR KEGG; mtu:Rv3506; -.
DR TubercuList; Rv3506; -.
DR eggNOG; COG0318; Bacteria.
DR OMA; NAIMAGW; -.
DR PhylomeDB; O53551; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:O53551; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047760; F:butyrate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; IBA:GO_Central.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:MTBBASE.
DR GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0071766; P:Actinobacterium-type cell wall biogenesis; IDA:UniProtKB.
DR GO; GO:0008610; P:lipid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IDA:MTBBASE.
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; IPR030310; FadD17/FadD6-like.
DR PANTHER; PTHR43107:SF15; PTHR43107:SF15; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 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..502
FT /note="Medium/long-chain-fatty-acid--CoA ligase FadD17"
FT /id="PRO_0000406787"
SQ SEQUENCE 502 AA; 53739 MW; 0AF9A7B3B9C83A4D CRC64;
MTPTHPTVTE LLLPLSEIDD RGVYFEDSFT SWRDHIRHGA AIAAALRERL DPARPPHVGV
LLQNTPFFSA TLVAGALSGI VPVGLNPVRR GAALAGDIAK ADCQLVLTGS GSAEVPADVE
HINVDSPEWT DEVAAHRDTE VRFRSADLAD LFMLIFTSGT SGDPKAVKCS HRKVAIAGVT
ITQRFSLGRD DVCYVSMPLF HSNAVLVGWA VAAACQGSMA LRRKFSASQF LADVRRYGAT
YANYVGKPLS YVLATPELPD DADNPLRAVY GNEGVPGDID RFGRRFGCVV MDGFGSTEGG
VAITRTLDTP AGALGPLPGG IQIVDPDTGE PCPTGVVGEL VNTAGPGGFE GYYNDEAAEA
ERMAGGVYHS GDLAYRDDAG YAYFAGRLGD WMRVDGENLG TAPIERVLMR YPDATEVAVY
PVPDPVVGDQ VMAALVLAPG TKFDADKFRA FLTEQPDLGH KQWPSYVRVS AGLPRTMTFK
VIKRQLSAEG VACADPVWPI RR
