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Reviewed, UniProtKB/Swiss-Prot Q4L7U4 (THD1_STAHJ)

Last modified June 16, 2009. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Threonine dehydratase biosynthetic
    EC=4.3.1.19
Alternative name(s):
    Threonine deaminase
Gene names
Name: ilvA
Ordered Locus Names: SH0972
OrganismStaphylococcus haemolyticus (strain JCSC1435) [Complete proteome] [HAMAP]
Taxonomic identifier279808 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length422 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the formation of alpha-ketobutyrate from threonine in a two-step reaction. The first step is a dehydration of threonine, followed by rehydration and liberation of ammonia By similarity.

Catalytic activity

L-threonine = 2-oxobutanoate + NH3.

Cofactor

Pyridoxal phosphate By similarity.

Pathway

Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from L-threonine: step 1/1.

Sequence similarities

Belongs to the serine/threonine dehydratase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 422422Threonine dehydratase biosynthetic
PRO_0000234314

Amino acid modifications

Modified residue561N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4L7U4-1 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: 6CA7388A563960E0

FASTA42246,986
        10         20         30         40         50         60 
MTVKTTLNAK DVDNAYLRIK DVVKETPLQF DLYLSQKYDC NVYLKREDLQ WVRSFKLRGA 

        70         80         90        100        110        120 
YNAISVLTSE AKEKGITCAS AGNHAQGVAY TAKALNLKAV IFMPVTTPLQ KVNQVKFFGS 

       130        140        150        160        170        180 
KNVKIILTGD TFDDCLKEAL IYTEQNHMTF IDPFNNVDTI AGQGTLAKEI LNQSSNDSIT 

       190        200        210        220        230        240 
FDYLFAAIGG GGLISGISTY MNQYSPQTKI IGVEPSGASS MYESVVVQNK IVTLDHIDKF 

       250        260        270        280        290        300 
VDGASVARVG DITYDIAKKF VDDYIQVDEG AVCSTILDMY SKQAIVAEPA GALSVSALEQ 

       310        320        330        340        350        360 
YKEKIKGKTV VCVVSGGNND INRMKEIEER SLLYEEMKHY FILNFPQRPG ALKEFVNDVL 

       370        380        390        400        410        420 
GPQDDITKFE YLKKTSQNTG TVIIGIQLKN HDDLNQLKIN VHDFDPSNIY INENKMLYSL 


LI 

« Hide

References

[1]"Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
J. Bacteriol. 187:7292-7308(2005) [PubMed: 16237012] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AP006716 Genomic DNA. Translation: BAE04281.1.
RefSeqYP_252887.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3482161.
GenomeReviewsGene locus SH0972 in contig AP006716_GR.
KEGGsha:SH0972.
NMPDRfig|279808.3.peg.1404.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ4L7U4.
OMAQ4L7U4. IFMPTTT.

Enzyme and pathway databases

BioCycSHAE279808:SH0972-MON.

Family and domain databases

InterProIPR001926. PyrdxlP-dep_enz_bsu.
IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR001721. Thr_deHydtase_C.
IPR011820. Threonine_deHydtase.
[Graphical view]
PfamPF00291. PALP. 1 hit.
PF00585. Thr_dehydrat_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR02079. THD1. 1 hit.
PROSITEPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTHD1_STAHJ
AccessionPrimary (citable) accession number: Q4L7U4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: August 2, 2005
Last modified: June 16, 2009
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents