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Protein

Long-chain-fatty-acid--CoA ligase

Gene

TTHA0604

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.1 Publication

Cofactori

Mg2+1 Publication

Pathwayi: fatty acid metabolism

This protein is involved in the pathway fatty acid metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid metabolism and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi184Magnesium1 Publication1
Binding sitei234ATP1 Publication1
Binding sitei323ATP; via carbonyl oxygen1 Publication1
Binding sitei327ATP1 Publication1
Metal bindingi328Magnesium1 Publication1
Binding sitei418ATP1 Publication1
Binding sitei435ATP1 Publication1
Binding sitei439ATP1 Publication1
Binding sitei444ATP1 Publication1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-615-MONOMER.
UniPathwayiUPA00199.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Ordered Locus Names:TTHA0604
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004191821 – 541Long-chain-fatty-acid--CoA ligaseAdd BLAST541

Interactioni

Subunit structurei

Forms a domain swapped homodimer.1 Publication

Protein-protein interaction databases

STRINGi300852.TTHA0604.

Structurei

Secondary structure

1541
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi21 – 30Combined sources10
Beta strandi35 – 39Combined sources5
Beta strandi45 – 49Combined sources5
Helixi50 – 66Combined sources17
Beta strandi74 – 78Combined sources5
Helixi83 – 94Combined sources12
Beta strandi98 – 101Combined sources4
Helixi108 – 118Combined sources11
Beta strandi121 – 125Combined sources5
Helixi127 – 129Combined sources3
Helixi130 – 136Combined sources7
Helixi137 – 139Combined sources3
Beta strandi145 – 151Combined sources7
Helixi160 – 163Combined sources4
Beta strandi177 – 184Combined sources8
Beta strandi186 – 190Combined sources5
Beta strandi192 – 197Combined sources6
Helixi198 – 207Combined sources10
Turni211 – 214Combined sources4
Beta strandi221 – 224Combined sources4
Helixi231 – 234Combined sources4
Helixi236 – 243Combined sources8
Beta strandi246 – 249Combined sources4
Helixi256 – 265Combined sources10
Beta strandi270 – 273Combined sources4
Helixi275 – 288Combined sources14
Beta strandi297 – 300Combined sources4
Helixi307 – 315Combined sources9
Beta strandi319 – 325Combined sources7
Helixi327 – 329Combined sources3
Beta strandi330 – 335Combined sources6
Helixi340 – 342Combined sources3
Helixi347 – 354Combined sources8
Beta strandi358 – 360Combined sources3
Beta strandi365 – 369Combined sources5
Beta strandi378 – 380Combined sources3
Beta strandi384 – 390Combined sources7
Beta strandi393 – 396Combined sources4
Helixi401 – 405Combined sources5
Beta strandi414 – 422Combined sources9
Beta strandi428 – 435Combined sources8
Beta strandi437 – 440Combined sources4
Beta strandi443 – 446Combined sources4
Helixi447 – 451Combined sources5
Beta strandi465 – 469Combined sources5
Beta strandi471 – 479Combined sources9
Helixi495 – 499Combined sources5
Turni504 – 506Combined sources3
Beta strandi509 – 513Combined sources5
Helixi530 – 533Combined sources4
Turni535 – 538Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ULTX-ray2.55A/B1-541[»]
1V25X-ray2.30A/B1-541[»]
1V26X-ray2.50A/B1-541[»]
ProteinModelPortaliQ5SKN9.
SMRiQ5SKN9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CEY. Bacteria.
COG0318. LUCA.
HOGENOMiHOG000229980.
KOiK00666.
OMAiHIVLMEP.
PhylomeDBiQ5SKN9.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5SKN9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGERMNAFP STMMDEELNL WDFLERAAAL FGRKEVVSRL HTGEVHRTTY
60 70 80 90 100
AEVYQRARRL MGGLRALGVG VGDRVATLGF NHFRHLEAYF AVPGMGAVLH
110 120 130 140 150
TANPRLSPKE IAYILNHAED KVLLFDPNLL PLVEAIRGEL KTVQHFVVMD
160 170 180 190 200
EKAPEGYLAY EEALGEEADP VRVPERAACG MAYTTGTTGL PKGVVYSHRA
210 220 230 240 250
LVLHSLAASL VDGTALSEKD VVLPVVPMFH VNAWCLPYAA TLVGAKQVLP
260 270 280 290 300
GPRLDPASLV ELFDGEGVTF TAGVPTVWLA LADYLESTGH RLKTLRRLVV
310 320 330 340 350
GGSAAPRSLI ARFERMGVEV RQGYGLTETS PVVVQNFVKS HLESLSEEEK
360 370 380 390 400
LTLKAKTGLP IPLVRLRVAD EEGRPVPKDG KALGEVQLKG PWITGGYYGN
410 420 430 440 450
EEATRSALTP DGFFRTGDIA VWDEEGYVEI KDRLKDLIKS GGEWISSVDL
460 470 480 490 500
ENALMGHPKV KEAAVVAIPH PKWQERPLAV VVPRGEKPTP EELNEHLLKA
510 520 530 540
GFAKWQLPDA YVFAEEIPRT SAGKFLKRAL REQYKNYYGG A
Length:541
Mass (Da):59,571
Last modified:December 21, 2004 - v1
Checksum:i5243A09836304D42
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB126656 Genomic DNA. Translation: BAD20228.1.
AP008226 Genomic DNA. Translation: BAD70427.1.
RefSeqiWP_011228062.1. NC_006461.1.
YP_143870.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70427; BAD70427; BAD70427.
GeneIDi3169318.
KEGGittj:TTHA0604.
PATRICi23956183. VBITheThe93045_0602.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB126656 Genomic DNA. Translation: BAD20228.1.
AP008226 Genomic DNA. Translation: BAD70427.1.
RefSeqiWP_011228062.1. NC_006461.1.
YP_143870.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ULTX-ray2.55A/B1-541[»]
1V25X-ray2.30A/B1-541[»]
1V26X-ray2.50A/B1-541[»]
ProteinModelPortaliQ5SKN9.
SMRiQ5SKN9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA0604.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70427; BAD70427; BAD70427.
GeneIDi3169318.
KEGGittj:TTHA0604.
PATRICi23956183. VBITheThe93045_0602.

Phylogenomic databases

eggNOGiENOG4105CEY. Bacteria.
COG0318. LUCA.
HOGENOMiHOG000229980.
KOiK00666.
OMAiHIVLMEP.
PhylomeDBiQ5SKN9.

Enzyme and pathway databases

UniPathwayiUPA00199.
BioCyciTTHE300852:GH8R-615-MONOMER.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLCFCS_THET8
AccessioniPrimary (citable) accession number: Q5SKN9
Secondary accession number(s): Q6L8F0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: December 21, 2004
Last modified: November 2, 2016
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.