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P0CI79

- TYSY1_BACSU

UniProt

P0CI79 - TYSY1_BACSU

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Protein
Thymidylate synthase 1
Gene
thyA1, BSU17680
Organism
Bacillus subtilis (strain 168)
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.UniRule annotation

Catalytic activityi

5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP.UniRule annotation

Temperature dependencei

Thermostable. Active at 46 degrees Celsius.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei161 – 1611 By similarity

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

UniPathwayiUPA00575.

Names & Taxonomyi

Protein namesi
Recommended name:
Thymidylate synthase 1 (EC:2.1.1.45)
Short name:
TS 1
Short name:
TSase 1
Alternative name(s):
Thymidylate synthase A
Short name:
TS A
Short name:
TSase A
Gene namesi
Name:thyA1
Ordered Locus Names:BSU17680
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU17680. [Micado]

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 279279Thymidylate synthase 1UniRule annotation
PRO_0000140931Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1815
Helixi22 – 243
Turni32 – 343
Beta strandi40 – 5011
Beta strandi52 – 543
Beta strandi59 – 613
Helixi65 – 7612
Helixi83 – 875
Turni88 – 903
Helixi95 – 973
Beta strandi100 – 1034
Beta strandi105 – 1073
Helixi109 – 1135
Beta strandi117 – 1193
Beta strandi122 – 1243
Helixi126 – 13611
Beta strandi144 – 1474
Turni150 – 1523
Helixi153 – 1553
Beta strandi156 – 1583
Beta strandi161 – 17010
Beta strandi173 – 18412
Turni185 – 1884
Helixi189 – 20719
Beta strandi210 – 22415
Helixi225 – 2273
Helixi228 – 2369
Beta strandi244 – 2474
Helixi254 – 2563
Helixi259 – 2613
Beta strandi262 – 2665

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B02X-ray2.50A1-279[»]
1BKOX-ray2.75A/B/C/D2-279[»]
1BKPX-ray1.70A/B2-279[»]
1BSFX-ray2.20A/B2-279[»]
1BSPX-ray2.50A/B2-279[»]
ProteinModelPortaliP0CI79.
SMRiP0CI79. Positions 2-279.

Miscellaneous databases

EvolutionaryTraceiP0CI79.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000257898.
KOiK00560.
OMAiTIGHAYG.
OrthoDBiEOG6K6V53.
PhylomeDBiP0CI79.

Family and domain databases

Gene3Di3.30.572.10. 1 hit.
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.

P0CI79-1 [UniParc]FASTAAdd to Basket

« Hide

MTQFDKQYNS IIKDIINNGI SDEEFDVRTK WDSDGTPAHT LSVISKQMRF    50
DNSEVPILTT KKVAWKTAIK ELLWIWQLKS NDVNDLNMMG VHIWDQWKQE 100
DGTIGHAYGF QLGKKNRSLN GEKVDQVDYL LHQLKNNPSS RRHITMLWNP 150
DELDAMALTP CVYETQWYVK HGKLHLEVRA RSNDMALGNP FNVFQYNVLQ 200
RMIAQVTGYE LGEYIFNIGD CHVYTRHIDN LKIQMEREQF EAPELWINPE 250
VKDFYDFTID DFKLINYKHG DKLLFEVAV 279
Length:279
Mass (Da):32,807
Last modified:January 11, 2011 - v1
Checksum:iCC0B127AAF7912BD
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti84 – 852ND → TE in strain: ATCC 6633.
Natural varianti88 – 881M → K in strain: ATCC 6633.
Natural varianti118 – 1181S → N in strain: ATCC 6633.
Natural varianti155 – 1551A → S in strain: ATCC 6633.
Natural varianti171 – 1711H → Q in strain: ATCC 6633.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X78560 Genomic DNA. Translation: CAA55307.1.
AL009126 Genomic DNA. Translation: CAB13652.1.
AF004102 Genomic DNA. Translation: AAC26324.1.
PIRiI40494.
RefSeqiNP_389651.1. NC_000964.3.
WP_003244896.1. NZ_CM000487.1.

Genome annotation databases

EnsemblBacteriaiCAB13652; CAB13652; BSU17680.
GeneIDi939555.
KEGGibsu:BSU17680.
PATRICi18975359. VBIBacSub10457_1871.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X78560 Genomic DNA. Translation: CAA55307.1 .
AL009126 Genomic DNA. Translation: CAB13652.1 .
AF004102 Genomic DNA. Translation: AAC26324.1 .
PIRi I40494.
RefSeqi NP_389651.1. NC_000964.3.
WP_003244896.1. NZ_CM000487.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P0CI79.
SMRi P0CI79. Positions 2-279.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB13652 ; CAB13652 ; BSU17680 .
GeneIDi 939555.
KEGGi bsu:BSU17680.
PATRICi 18975359. VBIBacSub10457_1871.

Organism-specific databases

GenoListi BSU17680. [Micado ]

Phylogenomic databases

HOGENOMi HOG000257898.
KOi K00560.
OMAi TIGHAYG.
OrthoDBi EOG6K6V53.
PhylomeDBi P0CI79.

Enzyme and pathway databases

UniPathwayi UPA00575 .

Miscellaneous databases

EvolutionaryTracei P0CI79.

Family and domain databases

Gene3Di 3.30.572.10. 1 hit.
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

« Hide 'large scale' publications
  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).

Entry informationi

Entry nameiTYSY1_BACSU
AccessioniPrimary (citable) accession number: P0CI79
Secondary accession number(s): O30395, O30396, P42326
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: January 11, 2011
Last modified: September 3, 2014
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

B.subtilis strain 168 possesses two thymidylate synthases, a major form ThyA and a minor form ThyB.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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