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P04990

- THRC_BACSU

UniProt

P04990 - THRC_BACSU

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Protein

Threonine synthase

Gene

thrC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.By similarity

Catalytic activityi

O-phospho-L-homoserine + H2O = L-threonine + phosphate.

Cofactori

Pyridoxal phosphate.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei85 – 851Pyridoxal phosphateBy similarity
Binding sitei314 – 3141Pyridoxal phosphateBy similarity

GO - Molecular functioni

  1. pyridoxal phosphate binding Source: InterPro
  2. threonine synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. threonine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Threonine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciBSUB:BSU32250-MONOMER.
UniPathwayiUPA00050; UER00065.

Names & Taxonomyi

Protein namesi
Recommended name:
Threonine synthase (EC:4.2.3.1)
Short name:
TS
Gene namesi
Name:thrC
Ordered Locus Names:BSU32250
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU32250. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 352352Threonine synthasePRO_0000185626Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591N6-(pyridoxal phosphate)lysineBy similarity

Proteomic databases

PaxDbiP04990.

Interactioni

Protein-protein interaction databases

IntActiP04990. 1 interaction.
MINTiMINT-8366482.
STRINGi224308.BSU32250.

Structurei

3D structure databases

ProteinModelPortaliP04990.
SMRiP04990. Positions 2-325.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni185 – 1895Pyridoxal phosphate bindingBy similarity

Sequence similaritiesi

Belongs to the threonine synthase family.Curated

Phylogenomic databases

eggNOGiCOG0498.
HOGENOMiHOG000076503.
InParanoidiP04990.
KOiK01733.
OMAiGITHMAM.
OrthoDBiEOG6HMX9M.
PhylomeDBiP04990.

Family and domain databases

InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR026260. Thr_Synthase_bac/arc.
IPR004450. Thr_synthase_like.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
PIRSFiPIRSF038945. Thr_synthase. 1 hit.
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR00260. thrC. 1 hit.
PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04990-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MWKGLIHQYK EFLPVTDQTP ALTLHEGNTP LIHLPKLSEQ LGIELHVKTE
60 70 80 90 100
GVNPTGSFKD RGMVMAVAKA KEEGNDTIMC ASTGNTSAAA AAYAARANMK
110 120 130 140 150
CIVIIPNGKI AFGKLAQAVM YGAEIIAIDG NFDDALKIVR SICEKSPIAL
160 170 180 190 200
VNSVNPYRIE GQKTAAFEVC EQLGEAPDVL AIPVGNAGNI TAYWKGFKEY
210 220 230 240 250
HEKNGTGLPK MRGFEAEGAA AIVRNEVIEN PETIATAIRI GNPASWDKAV
260 270 280 290 300
KAAEESNGKI DEVTDDEILH AYQLIARVEG VFAEPGSCAS IAGVLKQVKS
310 320 330 340 350
GEIPKGSKVV AVLTGNGLKD PNTAVDISEI KPVTLPTDED SILEYVKGAA

RV
Length:352
Mass (Da):37,464
Last modified:August 13, 1987 - v1
Checksum:iF478003AA330C6A0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04603 Genomic DNA. Translation: CAA28270.1.
AL009126 Genomic DNA. Translation: CAB15215.1.
M23217 Genomic DNA. Translation: AAA50610.1.
PIRiA25364.
RefSeqiNP_391105.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB15215; CAB15215; BSU32250.
GeneIDi936660.
KEGGibsu:BSU32250.
PATRICi18978422. VBIBacSub10457_3374.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X04603 Genomic DNA. Translation: CAA28270.1 .
AL009126 Genomic DNA. Translation: CAB15215.1 .
M23217 Genomic DNA. Translation: AAA50610.1 .
PIRi A25364.
RefSeqi NP_391105.1. NC_000964.3.

3D structure databases

ProteinModelPortali P04990.
SMRi P04990. Positions 2-325.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P04990. 1 interaction.
MINTi MINT-8366482.
STRINGi 224308.BSU32250.

Proteomic databases

PaxDbi P04990.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB15215 ; CAB15215 ; BSU32250 .
GeneIDi 936660.
KEGGi bsu:BSU32250.
PATRICi 18978422. VBIBacSub10457_3374.

Organism-specific databases

GenoListi BSU32250. [Micado ]

Phylogenomic databases

eggNOGi COG0498.
HOGENOMi HOG000076503.
InParanoidi P04990.
KOi K01733.
OMAi GITHMAM.
OrthoDBi EOG6HMX9M.
PhylomeDBi P04990.

Enzyme and pathway databases

UniPathwayi UPA00050 ; UER00065 .
BioCyci BSUB:BSU32250-MONOMER.

Family and domain databases

InterProi IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR026260. Thr_Synthase_bac/arc.
IPR004450. Thr_synthase_like.
IPR001926. TrpB-like_PLP-dep.
[Graphical view ]
Pfami PF00291. PALP. 1 hit.
[Graphical view ]
PIRSFi PIRSF038945. Thr_synthase. 1 hit.
SUPFAMi SSF53686. SSF53686. 1 hit.
TIGRFAMsi TIGR00260. thrC. 1 hit.
PROSITEi PS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Evolution of biosynthetic pathways: a common ancestor for threonine synthase, threonine dehydratase and D-serine dehydratase."
    Parsot C.
    EMBO J. 5:3013-3019(1986) [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. "Cloning and nucleotide sequence of the Bacillus subtilis hom gene coding for homoserine dehydrogenase. Structural and evolutionary relationships with Escherichia coli aspartokinases-homoserine dehydrogenases I and II."
    Parsot C., Cohen G.N.
    J. Biol. Chem. 263:14654-14660(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35.
    Strain: 168.

Entry informationi

Entry nameiTHRC_BACSU
AccessioniPrimary (citable) accession number: P04990
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: October 29, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3