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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.

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
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 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-HAMAP
Complete GO annotation...

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 – 1613Combined sources
Beta strandi18 – 225Combined sources
Turni23 – 253Combined sources
Beta strandi26 – 338Combined sources
Beta strandi35 – 395Combined sources
Helixi40 – 423Combined sources
Beta strandi48 – 503Combined sources
Helixi54 – 6512Combined sources
Helixi71 – 755Combined sources
Turni76 – 783Combined sources
Helixi83 – 908Combined sources
Beta strandi93 – 953Combined sources
Beta strandi98 – 1003Combined sources
Helixi101 – 1033Combined sources
Helixi104 – 1107Combined sources
Helixi112 – 13120Combined sources
Helixi133 – 1397Combined sources
Beta strandi143 – 1453Combined sources
Helixi146 – 1516Combined sources
Beta strandi152 – 1543Combined sources
Beta strandi156 – 1583Combined sources
Helixi163 – 17311Combined sources
Beta strandi174 – 1763Combined sources
Beta strandi181 – 1833Combined sources
Turni187 – 1926Combined sources
Beta strandi193 – 1953Combined sources
Beta strandi198 – 20710Combined sources
Beta strandi210 – 22112Combined sources
Turni222 – 2243Combined sources
Helixi225 – 24420Combined sources
Beta strandi247 – 26115Combined sources
Helixi262 – 2643Combined sources
Helixi265 – 2717Combined sources
Beta strandi281 – 2844Combined sources
Helixi291 – 2933Combined sources
Helixi296 – 2983Combined sources
Beta strandi299 – 3024Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MLEQPYLDLA KKVLDEGHFK PDRTHTGTYS IFGHQMRFDL SKGFPLLTTK
60 70 80 90 100
KVPFGLIKSE LLWFLHGDTN IRFLLQHRNH IWDEWAFEKW VKSDEYHGPD
110 120 130 140 150
MTDFGHRSQK DPEFAAVYHE EMAKFDDRVL HDDAFAAKYG DLGLVYGSQW
160 170 180 190 200
RAWHTSKGDT IDQLGDVIEQ IKTHPYSRRL IVSAWNPEDV PTMALPPCHT
210 220 230 240 250
LYQFYVNDGK LSLQLYQRSA DIFLGVPFNI ASYALLTHLV AHECGLEVGE
260 270 280 290 300
FIHTFGDAHL YVNHLDQIKE QLSRTPRPAP TLQLNPDKHD IFDFDMKDIK
310
LLNYDPYPAI KAPVAV
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. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19653 Genomic DNA. Translation: AAA25255.1. Different initiation.
PIRiA29817. SYLBT.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19653 Genomic DNA. Translation: AAA25255.1 . Different initiation.
PIRi A29817. SYLBT.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 113 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