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Q5SKN9 (LCFCS_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Long-chain-fatty-acid--CoA ligase

EC=6.2.1.3
Alternative name(s):
Long-chain fatty acyl-CoA synthetase
Short name=LC-FACS
Gene names
Ordered Locus Names:TTHA0604
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length541 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the esterification of a number of long chain fatty acids with CoA, resulting in the formation of long-chain fatty acyl-CoA. Myristate (C14) is the most efficiently processed fatty acid, followed by palmitate (C16). Also catalyzes the esterification of stearate (C18) and laurate (C12), but at lower efficiency. Does not catalyze the esterification of the unsaturated fatty acids mysteroleic and palmitoleic acids in vitro. Ref.3

Catalytic activity

ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA. Ref.3

Pathway

Lipid metabolism; fatty acid metabolism.

Subunit structure

Forms a domain swapped homodimer. Ref.3

Miscellaneous

Upon ATP binding, the fatty acid-binding tunnel gated by the aromatic residue Trp-234 opens to the ATP-binding site. The acylation reaction proceeds in two steps, via the formation of a fatty acyl-AMP intermediate, and is proposed to follow a unidirectional Bi Uni Uni Bi ping-pong mechanism.

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 541541Long-chain-fatty-acid--CoA ligase
PRO_0000419182

Sites

Metal binding1841Magnesium
Metal binding3281Magnesium
Binding site2341ATP
Binding site3231ATP; via carbonyl oxygen
Binding site3271ATP
Binding site4181ATP
Binding site4351ATP
Binding site4391ATP
Binding site4441ATP

Secondary structure

.................................................................................................. 541
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5SKN9 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 5243A09836304D42

FASTA54159,571
        10         20         30         40         50         60 
MEGERMNAFP STMMDEELNL WDFLERAAAL FGRKEVVSRL HTGEVHRTTY AEVYQRARRL 

        70         80         90        100        110        120 
MGGLRALGVG VGDRVATLGF NHFRHLEAYF AVPGMGAVLH TANPRLSPKE IAYILNHAED 

       130        140        150        160        170        180 
KVLLFDPNLL PLVEAIRGEL KTVQHFVVMD EKAPEGYLAY EEALGEEADP VRVPERAACG 

       190        200        210        220        230        240 
MAYTTGTTGL PKGVVYSHRA LVLHSLAASL VDGTALSEKD VVLPVVPMFH VNAWCLPYAA 

       250        260        270        280        290        300 
TLVGAKQVLP GPRLDPASLV ELFDGEGVTF TAGVPTVWLA LADYLESTGH RLKTLRRLVV 

       310        320        330        340        350        360 
GGSAAPRSLI ARFERMGVEV RQGYGLTETS PVVVQNFVKS HLESLSEEEK LTLKAKTGLP 

       370        380        390        400        410        420 
IPLVRLRVAD EEGRPVPKDG KALGEVQLKG PWITGGYYGN EEATRSALTP DGFFRTGDIA 

       430        440        450        460        470        480 
VWDEEGYVEI KDRLKDLIKS GGEWISSVDL ENALMGHPKV KEAAVVAIPH PKWQERPLAV 

       490        500        510        520        530        540 
VVPRGEKPTP EELNEHLLKA GFAKWQLPDA YVFAEEIPRT SAGKFLKRAL REQYKNYYGG 


A 

« Hide

References

« Hide 'large scale' references
[1]Masui R., Inoue Y., Shibata T., Miki K., Yokoyama S., Kuramitsu S.
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: HB8 / ATCC 27634 / DSM 579.
[2]"Complete genome sequence of Thermus thermophilus HB8."
Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HB8 / ATCC 27634 / DSM 579.
[3]"Structural basis of the substrate-specific two-step catalysis of long chain fatty acyl-CoA synthetase dimer."
Hisanaga Y., Ago H., Nakagawa N., Hamada K., Ida K., Yamamoto M., Hori T., Arii Y., Sugahara M., Kuramitsu S., Yokoyama S., Miyano M.
J. Biol. Chem. 279:31717-31726(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH ATP ANALOG OR MYRISTOYL-AMP INTERMEDIATE AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, CATALYTIC MECHANISM, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB126656 Genomic DNA. Translation: BAD20228.1.
AP008226 Genomic DNA. Translation: BAD70427.1.
RefSeqYP_143870.1. NC_006461.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ULTX-ray2.55A/B1-541[»]
1V25X-ray2.30A/B1-541[»]
1V26X-ray2.50A/B1-541[»]
ProteinModelPortalQ5SKN9.
SMRQ5SKN9. Positions 8-540.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300852.TTHA0604.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD70427; BAD70427; BAD70427.
GeneID3169318.
KEGGttj:TTHA0604.
PATRIC23956183. VBITheThe93045_0602.

Phylogenomic databases

eggNOGCOG0318.
HOGENOMHOG000229980.
KOK00666.
OMANAWGTPF.
OrthoDBEOG6JMMQ5.
PhylomeDBQ5SKN9.

Enzyme and pathway databases

BioCycTTHE300852:GH8R-629-MONOMER.
UniPathwayUPA00199.

Family and domain databases

InterProIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLCFCS_THET8
AccessionPrimary (citable) accession number: Q5SKN9
Secondary accession number(s): Q6L8F0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: December 21, 2004
Last modified: July 9, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways