P0CI79 (TYSY1_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thymidylate synthase 1
Short name=TS 1
Short name=TSase 1
EC=2.1.1.45

Alternative name(s):
Thymidylate synthase A
Short name=TS A
Short name=TSase A

Gene names

Name:	thyA1
Ordered Locus Names:	BSU17680

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	279 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 By similarity.
Miscellaneous	B.subtilis strain 168 possesses two thymidylate synthases, a major form ThyA and a minor form ThyB. HAMAP-Rule MF_00008
Sequence similarities	Belongs to the thymidylate synthase family. Bacterial-type ThyA subfamily.
Biophysicochemical properties	Temperature dependence: Thermostable. Active at 46 degrees Celsius. HAMAP-Rule MF_00008

Ontologies

Keywords
Biological process	Nucleotide biosynthesis
Cellular component	Cytoplasm
Molecular function	Methyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
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

1 – 279

279

Thymidylate synthase 1 HAMAP-Rule MF_00008

PRO_0000140931

Sites

Active site

161

1

By similarity

Natural variations

Natural variant

84 – 85

2

ND → TE in strain: ATCC 6633.

Natural variant

88

1

M → K in strain: ATCC 6633.

Natural variant

118

1

S → N in strain: ATCC 6633.

Natural variant

155

1

A → S in strain: ATCC 6633.

Natural variant

171

1

H → Q in strain: ATCC 6633.

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

279

Helix Strand Turn

Details...

Helix

4 – 18

15

Helix

22 – 24

3

Turn

32 – 34

3

Beta strand

40 – 50

11

Beta strand

52 – 54

3

Beta strand

59 – 61

3

Helix

65 – 76

12

Helix

83 – 87

5

Turn

88 – 90

3

Helix

95 – 97

3

Beta strand

100 – 103

4

Beta strand

105 – 107

3

Helix

109 – 113

5

Beta strand

117 – 119

3

Beta strand

122 – 124

3

Helix

126 – 136

11

Beta strand

144 – 147

4

Turn

150 – 152

3

Helix

153 – 155

3

Beta strand

156 – 158

3

Beta strand

161 – 170

10

Beta strand

173 – 184

12

Turn

185 – 188

4

Helix

189 – 207

19

Beta strand

210 – 224

15

Helix

225 – 227

3

Helix

228 – 236

9

Beta strand

244 – 247

4

Helix

254 – 256

3

Helix

259 – 261

3

Beta strand

262 – 266

5

Sequences

	Sequence		Length	Mass (Da)
	P0CI79 [UniParc]. Last modified January 11, 2011. Version 1. Checksum: CC0B127AAF7912BD	FASTA	279	32,807
	10 20 30 40 50 60 MTQFDKQYNS IIKDIINNGI SDEEFDVRTK WDSDGTPAHT LSVISKQMRF DNSEVPILTT 70 80 90 100 110 120 KKVAWKTAIK ELLWIWQLKS NDVNDLNMMG VHIWDQWKQE DGTIGHAYGF QLGKKNRSLN 130 140 150 160 170 180 GEKVDQVDYL LHQLKNNPSS RRHITMLWNP DELDAMALTP CVYETQWYVK HGKLHLEVRA 190 200 210 220 230 240 RSNDMALGNP FNVFQYNVLQ RMIAQVTGYE LGEYIFNIGD CHVYTRHIDN LKIQMEREQF 250 260 270 EAPELWINPE VKDFYDFTID DFKLINYKHG DKLLFEVAV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The thyA gene from Bacillus subtilis exhibits similarity with the phage phi 3T thymidylate synthase gene." Tam N.H., Borriss R. Microbiology 141:291-297(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"Genes encoding thymidylate synthases A and B in the genus Bacillus are members of two distinct families." Tam N.H., Borriss R. Mol. Gen. Genet. 258:427-430(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 49-279. Strain: ATCC 6633 / NCIMB 8054 / CCM1999.
[4]	"Crystal structures of a unique thermal-stable thymidylate synthase from Bacillus subtilis." Stout T.J., Schellenberger U., Santi D.V., Stroud R.M. Biochemistry 37:14736-14747(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[5]	"Crystal structure of thymidylate synthase A from Bacillus subtilis." Fox K.M., Maley F., Garibian A., Changchien L.M., van Roey P. Protein Sci. 8:538-544(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X78560 Genomic DNA. Translation: CAA55307.1.
AL009126 Genomic DNA. Translation: CAB13652.1.
AF004102 Genomic DNA. Translation: AAC26324.1.

PIR

I40494.

RefSeq

NP_389651.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B02	X-ray	2.50	A	1-279	[»]
1BKO	X-ray	2.75	A/B/C/D	2-279	[»]
1BKP	X-ray	1.70	A/B	2-279	[»]
1BSF	X-ray	2.20	A/B	2-279	[»]
1BSP	X-ray	2.50	A/B	2-279	[»]

ProteinModelPortal

P0CI79.

SMR

P0CI79. Positions 2-279.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB13652; CAB13652; BSU17680.

GeneID

939555.

KEGG

bsu:BSU17680.

PATRIC

18975359. VBIBacSub10457_1871.

Organism-specific databases

GenoList

BSU17680. [Micado]

Phylogenomic databases

HOGENOM

HOG000257898.

KO

K00560.

OMA

TIGHAYG.

Enzyme and pathway databases

UniPathway

UPA00575.

Family and domain databases

Gene3D

3.30.572.10. 1 hit.

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

Search...

Other

EvolutionaryTrace

P0CI79.

Entry information

Entry name

TYSY1_BACSU

Accession

Primary (citable) accession number: P0CI79
Secondary accession number(s): O30395, O30396, P42326

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2011
Last sequence update:	January 11, 2011
Last modified:	May 1, 2013
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program