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Q5SKN9

- LCFCS_THET8

UniProt

Q5SKN9 - LCFCS_THET8

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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: 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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi184 – 1841Magnesium
Binding sitei234 – 2341ATP
Binding sitei323 – 3231ATP; via carbonyl oxygen
Binding sitei327 – 3271ATP
Metal bindingi328 – 3281Magnesium
Binding sitei418 – 4181ATP
Binding sitei435 – 4351ATP
Binding sitei439 – 4391ATP
Binding sitei444 – 4441ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. long-chain fatty acid-CoA ligase activity Source: UniProtKB-EC
  3. metal ion binding Source: UniProtKB-KW
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-629-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
ProteomesiUP000000532: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 541541Long-chain-fatty-acid--CoA ligasePRO_0000419182Add
BLAST

Interactioni

Subunit structurei

Forms a domain swapped homodimer.1 Publication

Protein-protein interaction databases

STRINGi300852.TTHA0604.

Structurei

Secondary structure

1
541
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi21 – 3010Combined sources
Beta strandi35 – 395Combined sources
Beta strandi45 – 495Combined sources
Helixi50 – 6617Combined sources
Beta strandi74 – 785Combined sources
Helixi83 – 9412Combined sources
Beta strandi98 – 1014Combined sources
Helixi108 – 11811Combined sources
Beta strandi121 – 1255Combined sources
Helixi127 – 1293Combined sources
Helixi130 – 1367Combined sources
Helixi137 – 1393Combined sources
Beta strandi145 – 1517Combined sources
Helixi160 – 1634Combined sources
Beta strandi177 – 1848Combined sources
Beta strandi186 – 1905Combined sources
Beta strandi192 – 1976Combined sources
Helixi198 – 20710Combined sources
Turni211 – 2144Combined sources
Beta strandi221 – 2244Combined sources
Helixi231 – 2344Combined sources
Helixi236 – 2438Combined sources
Beta strandi246 – 2494Combined sources
Helixi256 – 26510Combined sources
Beta strandi270 – 2734Combined sources
Helixi275 – 28814Combined sources
Beta strandi297 – 3004Combined sources
Helixi307 – 3159Combined sources
Beta strandi319 – 3257Combined sources
Helixi327 – 3293Combined sources
Beta strandi330 – 3356Combined sources
Helixi340 – 3423Combined sources
Helixi347 – 3548Combined sources
Beta strandi358 – 3603Combined sources
Beta strandi365 – 3695Combined sources
Beta strandi378 – 3803Combined sources
Beta strandi384 – 3907Combined sources
Beta strandi393 – 3964Combined sources
Helixi401 – 4055Combined sources
Beta strandi414 – 4229Combined sources
Beta strandi428 – 4358Combined sources
Beta strandi437 – 4404Combined sources
Beta strandi443 – 4464Combined sources
Helixi447 – 4515Combined sources
Beta strandi465 – 4695Combined sources
Beta strandi471 – 4799Combined sources
Helixi490 – 4989Combined sources
Turni499 – 5013Combined sources
Turni504 – 5063Combined sources
Beta strandi509 – 5135Combined sources
Helixi530 – 5334Combined sources
Turni535 – 5384Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ULTX-ray2.55A/B1-541[»]
1V25X-ray2.30A/B1-541[»]
1V26X-ray2.50A/B1-541[»]
ProteinModelPortaliQ5SKN9.
SMRiQ5SKN9. Positions 8-540.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0318.
HOGENOMiHOG000229980.
KOiK00666.
OMAiNAWGTPF.
OrthoDBiEOG6JMMQ5.
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 .
RefSeqi WP_011228062.1. NC_006461.1.
YP_143870.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ULT X-ray 2.55 A/B 1-541 [» ]
1V25 X-ray 2.30 A/B 1-541 [» ]
1V26 X-ray 2.50 A/B 1-541 [» ]
ProteinModelPortali Q5SKN9.
SMRi Q5SKN9. Positions 8-540.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 300852.TTHA0604.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD70427 ; BAD70427 ; BAD70427 .
GeneIDi 3169318.
KEGGi ttj:TTHA0604.
PATRICi 23956183. VBITheThe93045_0602.

Phylogenomic databases

eggNOGi COG0318.
HOGENOMi HOG000229980.
KOi K00666.
OMAi NAWGTPF.
OrthoDBi EOG6JMMQ5.
PhylomeDBi Q5SKN9.

Enzyme and pathway databases

UniPathwayi UPA00199 .
BioCyci TTHE300852:GH8R-629-MONOMER.

Family and domain databases

InterProi IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view ]
PROSITEi PS00455. AMP_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

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 26, 2014
This is version 55 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

External Data

Dasty 3