Reviewed, UniProtKB/Swiss-Prot P00469 (TYSY_LACCA)

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

1582 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	316 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Provides the sole de novo source of dTMP for DNA biosynthesis. HAMAP MF_00008
Catalytic activity	5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP. HAMAP MF_00008
Pathway	Pyrimidine metabolism; dTTP biosynthesis. HAMAP MF_00008
Subunit structure	Homodimer. HAMAP MF_00008
Subcellular location	Cytoplasm. HAMAP MF_00008
Sequence similarities	Belongs to the thymidylate synthase family. Bacterial-type thyA subfamily.

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: 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

1 – 316

316

Thymidylate synthase HAMAP MF_00008

PRO_0000140967

Sites

Active site

198

1

HAMAP MF_00008

Secondary structure

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316

Helix Strand Turn

Details...

Helix

4 – 14

11

Beta strand

18 – 20

3

Beta strand

28 – 39

12

Beta strand

48 – 50

3

Helix

54 – 65

12

Helix

72 – 75

4

Turn

76 – 78

3

Helix

83 – 91

9

Helix

104 – 110

7

Helix

114 – 131

18

Helix

133 – 139

7

Beta strand

143 – 145

3

Helix

146 – 151

6

Helix

163 – 173

11

Beta strand

181 – 183

3

Turn

187 – 192

6

Beta strand

198 – 207

10

Beta strand

210 – 221

12

Turn

222 – 225

4

Helix

226 – 243

18

Beta strand

247 – 261

15

Helix

262 – 264

3

Helix

265 – 271

7

Beta strand

281 – 284

4

Helix

291 – 293

3

Helix

296 – 298

3

Beta strand

299 – 302

4

Sequences

	Sequence		Length	Mass (Da)
	P00469-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 4C391722044FF0A5	FASTA	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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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

PIR

SYLBT. A29817.

3D structure databases

PDBPDBe

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	[»]
4TMS	X-ray	2.35	A	1-316	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

2.1.1.45. 610.

Family and domain databases

HAMAP

MF_00008.
[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]

ProtoNet

Search...

Other Resources

BindingDB

P00469.

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 16, 2009
This is version 84 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)