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P00469

- TYSY_LACCA

UniProt

P00469 - TYSY_LACCA

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Protein
Thymidylate synthase
Gene
thyA
Organism
Lactobacillus casei
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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

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
Complete GO annotation...

GO - Biological processi

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

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Nucleotide biosynthesis

Enzyme and pathway databases

SABIO-RKP00469.
UniPathwayiUPA00575.

Names & Taxonomyi

Protein namesi
Recommended name:
Thymidylate synthase (EC:2.1.1.45)
Short name:
TS
Short name:
TSase
Gene namesi
Name:thyA
OrganismiLactobacillus casei
Taxonomic identifieri1582 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 316316Thymidylate synthaseUniRule annotation
PRO_0000140967Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP00469.

Family & Domainsi

Sequence similaritiesi

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...

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: June 11, 2014
This is version 110 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

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