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P00469

- TYSY_LACCA

UniProt

P00469 - TYSY_LACCA

Protein

Thymidylate synthase

Gene

thyA

Organism
Lactobacillus casei
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    • Comment

    Functioni

    Provides the sole de novo source of dTMP for DNA biosynthesis.

    Catalytic activityi

    5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei198 – 1981

    GO - Molecular functioni

    1. thymidylate synthase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. dTMP biosynthetic process Source: UniProtKB-HAMAP
    2. dTTP biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Methyltransferase, Transferase

    Keywords - Biological processi

    Nucleotide biosynthesis

    Enzyme and pathway databases

    SABIO-RKP00469.
    UniPathwayiUPA00575.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thymidylate synthaseUniRule annotation (EC:2.1.1.45UniRule annotation)
    Short name:
    TSUniRule annotation
    Short name:
    TSaseUniRule annotation
    Gene namesi
    Name:thyAUniRule annotation
    OrganismiLactobacillus casei
    Taxonomic identifieri1582 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 316316Thymidylate synthasePRO_0000140967Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    Secondary structure

    1
    316
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 1613
    Beta strandi18 – 225
    Turni23 – 253
    Beta strandi26 – 338
    Beta strandi35 – 395
    Helixi40 – 423
    Beta strandi48 – 503
    Helixi54 – 6512
    Helixi71 – 755
    Turni76 – 783
    Helixi83 – 908
    Beta strandi93 – 953
    Beta strandi98 – 1003
    Helixi101 – 1033
    Helixi104 – 1107
    Helixi112 – 13120
    Helixi133 – 1397
    Beta strandi143 – 1453
    Helixi146 – 1516
    Beta strandi152 – 1543
    Beta strandi156 – 1583
    Helixi163 – 17311
    Beta strandi174 – 1763
    Beta strandi181 – 1833
    Turni187 – 1926
    Beta strandi193 – 1953
    Beta strandi198 – 20710
    Beta strandi210 – 22112
    Turni222 – 2243
    Helixi225 – 24420
    Beta strandi247 – 26115
    Helixi262 – 2643
    Helixi265 – 2717
    Beta strandi281 – 2844
    Helixi291 – 2933
    Helixi296 – 2983
    Beta strandi299 – 3024

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BO7X-ray2.40A1-316[»]
    1BO8X-ray2.40A1-316[»]
    1BP0X-ray2.40A1-316[»]
    1BP6X-ray2.40A1-316[»]
    1BPJX-ray2.40A1-316[»]
    1JMFX-ray2.50A1-316[»]
    1JMGX-ray2.20A1-316[»]
    1JMHX-ray2.50A1-316[»]
    1JMIX-ray2.50A1-316[»]
    1LCAX-ray2.50A1-316[»]
    1LCBX-ray2.50A1-316[»]
    1LCEX-ray2.50A1-316[»]
    1NJAX-ray2.50A1-316[»]
    1NJBX-ray2.74A1-316[»]
    1NJCX-ray2.50A1-316[»]
    1NJDX-ray2.20A1-316[»]
    1NJEX-ray2.30A1-316[»]
    1TDAX-ray3.09A1-315[»]
    1TDBX-ray2.65A1-315[»]
    1TDCX-ray2.65A1-315[»]
    1THYX-ray2.90A1-316[»]
    1TSLX-ray2.50A1-316[»]
    1TSMX-ray3.00A1-316[»]
    1TSVX-ray2.90A1-316[»]
    1TSWX-ray2.50A1-316[»]
    1TSXX-ray2.50A1-316[»]
    1TSYX-ray2.20A1-316[»]
    1TSZX-ray2.75A1-316[»]
    1TVUX-ray2.50A1-316[»]
    1TVVX-ray2.30A1-316[»]
    1TVWX-ray2.50A1-316[»]
    1VZAX-ray2.50A1-316[»]
    1VZBX-ray2.50A1-316[»]
    1VZCX-ray2.50A1-316[»]
    1VZDX-ray2.50A1-316[»]
    1VZEX-ray2.30A1-316[»]
    2G86X-ray2.40A1-316[»]
    2G89X-ray2.50A1-316[»]
    2G8AX-ray2.40A1-316[»]
    2G8DX-ray2.40A1-316[»]
    2TDDX-ray2.70A1-315[»]
    2TDMX-ray2.55A1-316[»]
    3BNZX-ray2.60A1-316[»]
    3BYXX-ray2.40A1-316[»]
    3BZ0X-ray2.70A1-316[»]
    3C06X-ray2.60A1-316[»]
    3C0AX-ray2.40A1-316[»]
    3IJZX-ray2.21A1-316[»]
    3IK0X-ray2.10A1-316[»]
    3IK1X-ray2.25A1-316[»]
    4TMSX-ray2.35A1-316[»]
    ProteinModelPortaliP00469.
    SMRiP00469. Positions 1-316.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00469.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the thymidylate synthase family. Bacterial-type ThyA subfamily.UniRule annotation

    Family and domain databases

    Gene3Di3.30.572.10. 2 hits.
    HAMAPiMF_00008. Thymidy_synth_bact.
    InterProiIPR023451. Thymidate_synth/dCMP_Mease.
    IPR000398. Thymidylate_synthase.
    IPR020940. Thymidylate_synthase_AS.
    [Graphical view]
    PfamiPF00303. Thymidylat_synt. 1 hit.
    [Graphical view]
    PRINTSiPR00108. THYMDSNTHASE.
    SUPFAMiSSF55831. SSF55831. 1 hit.
    TIGRFAMsiTIGR03284. thym_sym. 1 hit.
    PROSITEiPS00091. THYMIDYLATE_SYNTHASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P00469-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLEQPYLDLA KKVLDEGHFK PDRTHTGTYS IFGHQMRFDL SKGFPLLTTK    50
    KVPFGLIKSE LLWFLHGDTN IRFLLQHRNH IWDEWAFEKW VKSDEYHGPD 100
    MTDFGHRSQK DPEFAAVYHE EMAKFDDRVL HDDAFAAKYG DLGLVYGSQW 150
    RAWHTSKGDT IDQLGDVIEQ IKTHPYSRRL IVSAWNPEDV PTMALPPCHT 200
    LYQFYVNDGK LSLQLYQRSA DIFLGVPFNI ASYALLTHLV AHECGLEVGE 250
    FIHTFGDAHL YVNHLDQIKE QLSRTPRPAP TLQLNPDKHD IFDFDMKDIK 300
    LLNYDPYPAI KAPVAV 316
    Length:316
    Mass (Da):36,580
    Last modified:July 21, 1986 - v1
    Checksum:i4C391722044FF0A5
    GO

    Sequence cautioni

    The sequence AAA25255.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19653 Genomic DNA. Translation: AAA25255.1. Different initiation.
    PIRiA29817. SYLBT.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M19653 Genomic DNA. Translation: AAA25255.1 . Different initiation.
    PIRi A29817. SYLBT.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BO7 X-ray 2.40 A 1-316 [» ]
    1BO8 X-ray 2.40 A 1-316 [» ]
    1BP0 X-ray 2.40 A 1-316 [» ]
    1BP6 X-ray 2.40 A 1-316 [» ]
    1BPJ X-ray 2.40 A 1-316 [» ]
    1JMF X-ray 2.50 A 1-316 [» ]
    1JMG X-ray 2.20 A 1-316 [» ]
    1JMH X-ray 2.50 A 1-316 [» ]
    1JMI X-ray 2.50 A 1-316 [» ]
    1LCA X-ray 2.50 A 1-316 [» ]
    1LCB X-ray 2.50 A 1-316 [» ]
    1LCE X-ray 2.50 A 1-316 [» ]
    1NJA X-ray 2.50 A 1-316 [» ]
    1NJB X-ray 2.74 A 1-316 [» ]
    1NJC X-ray 2.50 A 1-316 [» ]
    1NJD X-ray 2.20 A 1-316 [» ]
    1NJE X-ray 2.30 A 1-316 [» ]
    1TDA X-ray 3.09 A 1-315 [» ]
    1TDB X-ray 2.65 A 1-315 [» ]
    1TDC X-ray 2.65 A 1-315 [» ]
    1THY X-ray 2.90 A 1-316 [» ]
    1TSL X-ray 2.50 A 1-316 [» ]
    1TSM X-ray 3.00 A 1-316 [» ]
    1TSV X-ray 2.90 A 1-316 [» ]
    1TSW X-ray 2.50 A 1-316 [» ]
    1TSX X-ray 2.50 A 1-316 [» ]
    1TSY X-ray 2.20 A 1-316 [» ]
    1TSZ X-ray 2.75 A 1-316 [» ]
    1TVU X-ray 2.50 A 1-316 [» ]
    1TVV X-ray 2.30 A 1-316 [» ]
    1TVW X-ray 2.50 A 1-316 [» ]
    1VZA X-ray 2.50 A 1-316 [» ]
    1VZB X-ray 2.50 A 1-316 [» ]
    1VZC X-ray 2.50 A 1-316 [» ]
    1VZD X-ray 2.50 A 1-316 [» ]
    1VZE X-ray 2.30 A 1-316 [» ]
    2G86 X-ray 2.40 A 1-316 [» ]
    2G89 X-ray 2.50 A 1-316 [» ]
    2G8A X-ray 2.40 A 1-316 [» ]
    2G8D X-ray 2.40 A 1-316 [» ]
    2TDD X-ray 2.70 A 1-315 [» ]
    2TDM X-ray 2.55 A 1-316 [» ]
    3BNZ X-ray 2.60 A 1-316 [» ]
    3BYX X-ray 2.40 A 1-316 [» ]
    3BZ0 X-ray 2.70 A 1-316 [» ]
    3C06 X-ray 2.60 A 1-316 [» ]
    3C0A X-ray 2.40 A 1-316 [» ]
    3IJZ X-ray 2.21 A 1-316 [» ]
    3IK0 X-ray 2.10 A 1-316 [» ]
    3IK1 X-ray 2.25 A 1-316 [» ]
    4TMS X-ray 2.35 A 1-316 [» ]
    ProteinModelPortali P00469.
    SMRi P00469. Positions 1-316.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P00469.
    ChEMBLi CHEMBL5328.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00575 .
    SABIO-RK P00469.

    Miscellaneous databases

    EvolutionaryTracei P00469.

    Family and domain databases

    Gene3Di 3.30.572.10. 2 hits.
    HAMAPi MF_00008. Thymidy_synth_bact.
    InterProi IPR023451. Thymidate_synth/dCMP_Mease.
    IPR000398. Thymidylate_synthase.
    IPR020940. Thymidylate_synthase_AS.
    [Graphical view ]
    Pfami PF00303. Thymidylat_synt. 1 hit.
    [Graphical view ]
    PRINTSi PR00108. THYMDSNTHASE.
    SUPFAMi SSF55831. SSF55831. 1 hit.
    TIGRFAMsi TIGR03284. thym_sym. 1 hit.
    PROSITEi PS00091. THYMIDYLATE_SYNTHASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, sequencing, and expression of the Lactobacillus casei thymidylate synthase gene."
      Pinter K., Davisson V.J., Santi D.V.
      DNA 7:235-241(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The primary structure of Lactobacillus casei thymidylate synthetase. III. The use of 2-(2-nitrophenylsulfenyl)-3-methyl-3-bromoindolenine and limited tryptic peptides to establish the complete amino acid sequence of the enzyme."
      Maley G.F., Bellisario R.L., Guarino D.U., Maley F.
      J. Biol. Chem. 254:1301-1304(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.
    3. "Plastic adaptation toward mutations in proteins: structural comparison of thymidylate synthases."
      Perry K.M., Fauman E.B., Finer-Moore J.S., Montfort W.R., Maley G.F., Maley F., Stroud R.M.
      Proteins 8:315-333(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
    4. "Refined structures of substrate-bound and phosphate-bound thymidylate synthase from Lactobacillus casei."
      Finer-Moore J.S., Fauman E.B., Foster P.G., Perry K.M., Santi D.V., Stroud R.M.
      J. Mol. Biol. 232:1101-1116(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS).
    5. "Role of the conserved tryptophan 82 of Lactobacillus casei thymidylate synthase."
      Kealey J.T., Eckstein J., Santi D.V.
      Chem. Biol. 2:609-614(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-82.

    Entry informationi

    Entry nameiTYSY_LACCA
    AccessioniPrimary (citable) accession number: P00469
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    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