LCFCS_THET8
ID LCFCS_THET8 Reviewed; 541 AA.
AC Q5SKN9; Q6L8F0;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Long-chain-fatty-acid--CoA ligase;
DE EC=6.2.1.3;
DE AltName: Full=Long-chain fatty acyl-CoA synthetase;
DE Short=LC-FACS;
GN OrderedLocusNames=TTHA0604;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Inoue Y., Shibata T., Miki K., Yokoyama S., Kuramitsu S.;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH
RP ATP ANALOG OR MYRISTOYL-AMP INTERMEDIATE AND MAGNESIUM, FUNCTION, CATALYTIC
RP ACTIVITY, SUBSTRATE SPECIFICITY, CATALYTIC MECHANISM, SUBUNIT, AND
RP COFACTOR.
RX PubMed=15145952; DOI=10.1074/jbc.m400100200;
RA Hisanaga Y., Ago H., Nakagawa N., Hamada K., Ida K., Yamamoto M., Hori T.,
RA Arii Y., Sugahara M., Kuramitsu S., Yokoyama S., Miyano M.;
RT "Structural basis of the substrate-specific two-step catalysis of long
RT chain fatty acyl-CoA synthetase dimer.";
RL J. Biol. Chem. 279:31717-31726(2004).
CC -!- FUNCTION: Catalyzes the esterification of a number of long chain fatty
CC acids with CoA, resulting in the formation of long-chain fatty acyl-
CC CoA. Myristate (C14) is the most efficiently processed fatty acid,
CC followed by palmitate (C16). Also catalyzes the esterification of
CC stearate (C18) and laurate (C12), but at lower efficiency. Does not
CC catalyze the esterification of the unsaturated fatty acids mysteroleic
CC and palmitoleic acids in vitro. {ECO:0000269|PubMed:15145952}.
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:15145952};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15145952};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC -!- SUBUNIT: Forms a domain swapped homodimer.
CC {ECO:0000269|PubMed:15145952}.
CC -!- MISCELLANEOUS: Upon ATP binding, the fatty acid-binding tunnel gated by
CC the aromatic residue Trp-234 opens to the ATP-binding site. The
CC acylation reaction proceeds in two steps, via the formation of a fatty
CC acyl-AMP intermediate, and is proposed to follow a unidirectional Bi
CC Uni Uni Bi ping-pong mechanism.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AB126656; BAD20228.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD70427.1; -; Genomic_DNA.
DR RefSeq; YP_143870.1; NC_006461.1.
DR PDB; 1ULT; X-ray; 2.55 A; A/B=1-541.
DR PDB; 1V25; X-ray; 2.30 A; A/B=1-541.
DR PDB; 1V26; X-ray; 2.50 A; A/B=1-541.
DR PDBsum; 1ULT; -.
DR PDBsum; 1V25; -.
DR PDBsum; 1V26; -.
DR AlphaFoldDB; Q5SKN9; -.
DR SMR; Q5SKN9; -.
DR STRING; 300852.55771986; -.
DR EnsemblBacteria; BAD70427; BAD70427; BAD70427.
DR KEGG; ttj:TTHA0604; -.
DR PATRIC; fig|300852.9.peg.602; -.
DR eggNOG; COG0318; Bacteria.
DR HOGENOM; CLU_000022_59_5_0; -.
DR OMA; FAIPSMG; -.
DR PhylomeDB; Q5SKN9; -.
DR UniPathway; UPA00199; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 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 3D-structure; ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Magnesium; Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..541
FT /note="Long-chain-fatty-acid--CoA ligase"
FT /id="PRO_0000419182"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:15145952"
FT BINDING 234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15145952"
FT BINDING 323
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15145952"
FT BINDING 327
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15145952"
FT BINDING 328
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:15145952"
FT BINDING 418
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15145952"
FT BINDING 435
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15145952"
FT BINDING 439
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15145952"
FT BINDING 444
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:15145952"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:1V25"
FT HELIX 50..66
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:1V25"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:1V25"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:1V25"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:1V25"
FT HELIX 130..136
FT /evidence="ECO:0007829|PDB:1V25"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:1V25"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 177..184
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:1V25"
FT HELIX 198..207
FT /evidence="ECO:0007829|PDB:1V25"
FT TURN 211..214
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:1V25"
FT HELIX 231..234
FT /evidence="ECO:0007829|PDB:1V25"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:1V25"
FT HELIX 256..265
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:1V25"
FT HELIX 275..288
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:1V25"
FT HELIX 307..315
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 319..325
FT /evidence="ECO:0007829|PDB:1V25"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 330..335
FT /evidence="ECO:0007829|PDB:1V25"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:1V25"
FT HELIX 347..354
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 365..369
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 384..390
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 393..396
FT /evidence="ECO:0007829|PDB:1V25"
FT HELIX 401..405
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 414..422
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 428..435
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 437..440
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 443..446
FT /evidence="ECO:0007829|PDB:1V25"
FT HELIX 447..451
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 465..469
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 471..479
FT /evidence="ECO:0007829|PDB:1V25"
FT HELIX 495..499
FT /evidence="ECO:0007829|PDB:1V25"
FT TURN 504..506
FT /evidence="ECO:0007829|PDB:1V25"
FT STRAND 509..513
FT /evidence="ECO:0007829|PDB:1ULT"
FT HELIX 530..533
FT /evidence="ECO:0007829|PDB:1V25"
FT TURN 535..538
FT /evidence="ECO:0007829|PDB:1V26"
SQ SEQUENCE 541 AA; 59571 MW; 5243A09836304D42 CRC64;
MEGERMNAFP STMMDEELNL WDFLERAAAL FGRKEVVSRL HTGEVHRTTY AEVYQRARRL
MGGLRALGVG VGDRVATLGF NHFRHLEAYF AVPGMGAVLH TANPRLSPKE IAYILNHAED
KVLLFDPNLL PLVEAIRGEL KTVQHFVVMD EKAPEGYLAY EEALGEEADP VRVPERAACG
MAYTTGTTGL PKGVVYSHRA LVLHSLAASL VDGTALSEKD VVLPVVPMFH VNAWCLPYAA
TLVGAKQVLP GPRLDPASLV ELFDGEGVTF TAGVPTVWLA LADYLESTGH RLKTLRRLVV
GGSAAPRSLI ARFERMGVEV RQGYGLTETS PVVVQNFVKS HLESLSEEEK LTLKAKTGLP
IPLVRLRVAD EEGRPVPKDG KALGEVQLKG PWITGGYYGN EEATRSALTP DGFFRTGDIA
VWDEEGYVEI KDRLKDLIKS GGEWISSVDL ENALMGHPKV KEAAVVAIPH PKWQERPLAV
VVPRGEKPTP EELNEHLLKA GFAKWQLPDA YVFAEEIPRT SAGKFLKRAL REQYKNYYGG
A
