Thymidylate synthase - Lactobacillus casei

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P00469 (TYSY_LACCA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 106. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Thymidylate synthase
Short name=TS
Short name=TSase
EC=2.1.1.45

Gene names

Name:

thyA

Organism

Lactobacillus casei

Taxonomic identifier

Taxonomic lineage

Bacteria › Firmicutes › Bacilli › Lactobacillales › Lactobacillaceae › Lactobacillus ›

Protein attributes

Sequence length	316 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Provides the sole de novo source of dTMP for DNA biosynthesis. HAMAP-Rule MF_00008
Catalytic activity	5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP. HAMAP-Rule MF_00008
Pathway	Pyrimidine metabolism; dTTP biosynthesis. HAMAP-Rule MF_00008
Subunit structure	Homodimer.
Subcellular location	Cytoplasm HAMAP-Rule MF_00008.
Sequence similarities	Belongs to the thymidylate synthase family. Bacterial-type ThyA subfamily.
Sequence caution	The sequence AAA25255.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Nucleotide biosynthesis
Cellular component	Cytoplasm
Molecular function	Methyltransferase Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	dTMP biosynthetic process Inferred from electronic annotation. Source: HAMAP dTTP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	thymidylate synthase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

316

Thymidylate synthase HAMAP-Rule MF_00008

PRO_0000140967

Sites

Active site

1

Secondary structure

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316

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P00469 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 4C391722044FF0A5
Show »

316

36,580

        10         20         30         40         50         60 
MLEQPYLDLA KKVLDEGHFK PDRTHTGTYS IFGHQMRFDL SKGFPLLTTK KVPFGLIKSE 

        70         80         90        100        110        120 
LLWFLHGDTN IRFLLQHRNH IWDEWAFEKW VKSDEYHGPD MTDFGHRSQK DPEFAAVYHE 

       130        140        150        160        170        180 
EMAKFDDRVL HDDAFAAKYG DLGLVYGSQW RAWHTSKGDT IDQLGDVIEQ IKTHPYSRRL 

       190        200        210        220        230        240 
IVSAWNPEDV PTMALPPCHT LYQFYVNDGK LSLQLYQRSA DIFLGVPFNI ASYALLTHLV 

       250        260        270        280        290        300 
AHECGLEVGE FIHTFGDAHL YVNHLDQIKE QLSRTPRPAP TLQLNPDKHD IFDFDMKDIK 

       310 
LLNYDPYPAI KAPVAV

References

[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M19653 Genomic DNA. Translation: AAA25255.1. Different initiation.

PIR

SYLBT. A29817.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

SMR

P00469. Positions 1-316.

ModBase

Protocols and materials databases

StructuralBiologyKnowledgebase

Enzyme and pathway databases

SABIO-RK

UniPathway

Family and domain databases

Gene3D

3.30.572.10. 2 hits.

HAMAP

MF_00008. Thymidy_synth_bact.

InterPro

IPR023451. Thymidate_synth/dCMP_Mease.
IPR000398. Thymidylate_synthase.
IPR020940. Thymidylate_synthase_AS.
[Graphical view]

Pfam

PF00303. Thymidylat_synt. 1 hit.
[Graphical view]

PRINTS

PR00108. THYMDSNTHASE.

SUPFAM

SSF55831. Thymidylat_synth_C. 1 hit.

TIGRFAMs

TIGR03284. thym_sym. 1 hit.

PROSITE

PS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]

ProtoNet

Other

BindingDB

ChEMBL

EvolutionaryTrace

Entry information

Entry name

TYSY_LACCA

Accession

Primary (citable) accession number: P00469

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents