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Q5SKN9

- LCFCS_THET8

UniProt

Q5SKN9 - LCFCS_THET8

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
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    • History
      Entry version 54 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
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    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

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

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    MEGERMNAFP STMMDEELNL WDFLERAAAL FGRKEVVSRL HTGEVHRTTY    50
    AEVYQRARRL MGGLRALGVG VGDRVATLGF NHFRHLEAYF AVPGMGAVLH 100
    TANPRLSPKE IAYILNHAED KVLLFDPNLL PLVEAIRGEL KTVQHFVVMD 150
    EKAPEGYLAY EEALGEEADP VRVPERAACG MAYTTGTTGL PKGVVYSHRA 200
    LVLHSLAASL VDGTALSEKD VVLPVVPMFH VNAWCLPYAA TLVGAKQVLP 250
    GPRLDPASLV ELFDGEGVTF TAGVPTVWLA LADYLESTGH RLKTLRRLVV 300
    GGSAAPRSLI ARFERMGVEV RQGYGLTETS PVVVQNFVKS HLESLSEEEK 350
    LTLKAKTGLP IPLVRLRVAD EEGRPVPKDG KALGEVQLKG PWITGGYYGN 400
    EEATRSALTP DGFFRTGDIA VWDEEGYVEI KDRLKDLIKS GGEWISSVDL 450
    ENALMGHPKV KEAAVVAIPH PKWQERPLAV VVPRGEKPTP EELNEHLLKA 500
    GFAKWQLPDA YVFAEEIPRT SAGKFLKRAL REQYKNYYGG A 541
    Length:541
    Mass (Da):59,571
    Last modified:December 21, 2004 - v1
    Checksum:i5243A09836304D42
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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

    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: October 1, 2014
    This is version 54 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