Reviewed, UniProtKB/Swiss-Prot Q3V7T5 (THD1_STAAR)

Names and origin

Protein names

Recommended name:
    Threonine dehydratase biosynthetic
    EC=4.3.1.19
Alternative name(s):
    Threonine deaminase

Gene names

Name:	ilvA
Ordered Locus Names:	SAR2148

Organism

Staphylococcus aureus (strain MRSA252) [Complete proteome] [HAMAP]

Taxonomic identifier

282458 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	422 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred 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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Isoleucine biosynthesis
Ligand	Pyridoxal phosphate
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	isoleucine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-threonine ammonia-lyase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 422	422	Threonine dehydratase biosynthetic		PRO_0000234309
Amino acid modifications
	Modified residue	56	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3V7T5-1 [UniParc]. Last modified October 11, 2005. Version 1. Checksum: 14D14766F96CA9BB	FASTA	422	46,948
	10 20 30 40 50 60 MTVKTTVSTK DIDEAFLRLK DIVKETPLQL DHYLSQKYDC KVYLKREDLQ WVRSFKLRGA 70 80 90 100 110 120 YNAISVLSDE AKSKGITCAS AGNHAQGVAY TAKKLNLNAV IFMPVTTPLQ KVNQVKFFGN 130 140 150 160 170 180 SNVEVVLTGD TFDHCLAEAL TYTSEHQMNF IDPFNNVHTI SGQGTLAKEM LEQAKSDNVN 190 200 210 220 230 240 FDYLFAAIGG GGLISGISTY FKSYSPNTKI IGVEPSGASS MYESVVVNNQ VITLPNIDKF 250 260 270 280 290 300 VDGASVARVG DITFEIAKKN VDNYVQVDEG AVCSTILDMY SKQAIVAEPA GALSVSALEN 310 320 330 340 350 360 YKDHIKGKTV VCVISGGNND INRMKEIEER SLLYEEMKHY FILNFPQRPG ALREFVNDVL 370 380 390 400 410 420 GPQDDITKFE YLKKSSQNTG TVIIGIQLKD HDDLIQLKQR VNHFDPSNIY INENKMLYSL LI

References

[1]

"Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance." Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C. , Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004) [PubMed: 15213324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX571856 Genomic DNA. Translation: CAG41129.1.
RefSeq	YP_041510.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2859662.
GenomeReviews	Gene locus SAR2148 in contig BX571856_GR.
KEGG	sar:SAR2148.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q3V7T5.
OMA	Q3V7T5. IFMPTTT.
Enzyme and pathway databases
BioCyc	SAUR282458:SAR2148-MON.
Family and domain databases
InterPro	IPR001926. PyrdxlP-dep_enz_bsu. IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS. IPR001721. Thr_deHydtase_C. IPR011820. Threonine_deHydtase. [Graphical view]
Pfam	PF00291. PALP. 1 hit. PF00585. Thr_dehydrat_C. 1 hit. [Graphical view]
TIGRFAMs	TIGR02079. THD1. 1 hit.
PROSITE	PS00165. DEHYDRATASE_SER_THR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

THD1_STAAR

Accession

Primary (citable) accession number: Q3V7T5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	October 11, 2005
Last modified:	June 16, 2009
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)