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P27735

- THRC_SERMA

UniProt

P27735 - THRC_SERMA

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Protein
Threonine synthase
Gene
thrC
Organism
Serratia marcescens
Status
Reviewed - Annotation score: 2 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

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

UniPathwayiUPA00050; UER00065.

Names & Taxonomyi

Protein namesi
Recommended name:
Threonine synthase (EC:4.2.3.1)
Short name:
TS
Gene namesi
Name:thrC
OrganismiSerratia marcescens
Taxonomic identifieri615 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 429429Threonine synthase
PRO_0000185640Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei107 – 1071N6-(pyridoxal phosphate)lysine By similarity

Proteomic databases

PRIDEiP27735.

Structurei

3D structure databases

ProteinModelPortaliP27735.
SMRiP27735. Positions 1-425.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.90.1380.10. 1 hit.
InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR029144. Thr_synth_N.
IPR004450. Thr_synthase_like.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
PF14821. Thr_synth_N. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR00260. thrC. 1 hit.
PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P27735-1 [UniParc]FASTAAdd to Basket

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MKLYNLKDHN EQVSFAQAIK QGLGKQQGLF FPLDLPEFEL TEIDHLLEQD    50
FVTRSSRILS AFIGEEVPET ALKKRVQAAF EFPAPVAKVT DDVSCLELFH 100
GPTLAFKDFG GRFMAQMLAE VAGEQPVTIL TATSGDTGAA VAHAFYGLKN 150
VRVVILYPQG KISPLQEKLF CTLGGNIHTV AIDGDFDACQ ALVKQAFDDQ 200
ELKDALHLNS ANSINISRLL AQICYYFEAV AQLPQEARNQ LVISVPSGNF 250
GDLTAGLLAK SLGLPVKRFI AATNANDTVP RFLTSGQWQP HATVATLSNA 300
MDVSQPNNWP RVEELFRRKV WQLKELGHAA VSDETTKDTM RELAELGYIS 350
EPHAAIAYRA LRDQLQEGEF GLFLGTAHPA KFKESVEAIL GQELPLPKAL 400
ALRAELPLLS HTLPASFGEL RKFLMGLPA 429
Length:429
Mass (Da):47,094
Last modified:August 1, 1992 - v1
Checksum:iB47262DE94848015
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D10387 Genomic DNA. Translation: BAA01222.1.
X60821 Genomic DNA. Translation: CAA43214.1.
PIRiD47057. S16043.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D10387 Genomic DNA. Translation: BAA01222.1 .
X60821 Genomic DNA. Translation: CAA43214.1 .
PIRi D47057. S16043.

3D structure databases

ProteinModelPortali P27735.
SMRi P27735. Positions 1-425.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P27735.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00050 ; UER00065 .

Family and domain databases

Gene3Di 3.90.1380.10. 1 hit.
InterProi IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR029144. Thr_synth_N.
IPR004450. Thr_synthase_like.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view ]
Pfami PF00291. PALP. 1 hit.
PF14821. Thr_synth_N. 1 hit.
[Graphical view ]
SUPFAMi SSF53686. SSF53686. 1 hit.
TIGRFAMsi TIGR00260. thrC. 1 hit.
PROSITEi PS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Nucleotide sequence of the Serratia marcescens threonine operon and analysis of the threonine operon mutations which alter feedback inhibition of both aspartokinase I and homoserine dehydrogenase I."
    Omori K., Suzuki S., Komatsubara S.
    J. Bacteriol. 175:785-794(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Sr41.

Entry informationi

Entry nameiTHRC_SERMA
AccessioniPrimary (citable) accession number: P27735
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: June 11, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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