Thymidylate synthase - Lactobacillus casei

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Reviewed, UniProtKB/Swiss-Prot P00469 (TYSY_LACCA)

Last modified June 10, 2008. Version 79. History...

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Names and origin · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

Thymidylate synthase
Also known as:
     EC 2.1.1.45
     TS
     TSase

Gene names

Name:

thyA

Organism

Lactobacillus casei

Taxonomic identifier

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein existence

Evidence at protein level.

General annotation (Comments)

Function	Provides the sole de novo source of dTMP for DNA biosynthesis.
Catalytic activity	5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP.
Pathway	Pyrimidine metabolism; dTTP biosynthesis.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the thymidylate synthase family.

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
Cellular component	cytoplasm Inferred from electronic annotation. Source: HAMAP
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

Molecule processing

Chain

316

Thymidylate synthase

Sites

Active site

1

Secondary structure

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316

Helix Strand Turn

Sequences

Sequence

Length

Mass (Da)

Tools

P00469-1 [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: 2840247] [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: 105005] [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: 2128651] [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: 8371269] [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: 9383465] [Abstract] Cited for: MUTAGENESIS OF TYR-82.

Cross-references

Sequence databases

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

PIR

SYLBT. A29817.

3D structure databases

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	[»]
4TMS	X-ray	2.35	A	1-316	[»]

ModBase

Family and domain databases

HAMAP

MF_00008.
[Family] [Alignment] [Tree]

InterPro

IPR000398. Thymidylat_synth_C.
[Graphical view]

Gene3D

G3DSA:3.30.572.10. Thymidylat_synth_C. 1 hit.

PANTHER

PTHR11549:SF2. Thymidylat_synth_C. 1 hit.

Pfam

PF00303. Thymidylat_synt. 1 hit.
[Graphical view]

PRINTS

PR00108. THYMDSNTHASE.

ProDom

PD001180. Thymidylat_synth. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR03284. thym_sym. 1 hit.

PROSITE

PS00091. THYMIDYLATE_SYNTHASE. 1 hit.
[Graphical view]

BLOCKS

Other Resources

LinkHub

ProtoNet

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:	June 10, 2008
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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

Names and origin · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents