Q2FF63 (ILVA_STAA3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
L-threonine dehydratase biosynthetic IlvA
EC=4.3.1.19

Alternative name(s):
Threonine deaminase

Gene names

Name:	ilvA
Ordered Locus Names:	SAUSA300_2014

Organism

Staphylococcus aureus (strain USA300) [Complete proteome] [HAMAP]

Taxonomic identifier

367830 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › Staphylococcus aureus › Staphylococcus aureus subsp. aureus

Protein attributes

Sequence length	422 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA 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.
Subunit structure	Homotetramer By similarity.
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-UniPathway threonine metabolic process Inferred from sequence or structural similarity. Source: UniProtKB
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	L-threonine dehydratase biosynthetic IlvA		PRO_0000234304
Regions
	Region	190 – 193	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	83	1	Pyridoxal phosphate By similarity
	Binding site	315	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	56	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2FF63 [UniParc]. Last modified March 21, 2006. Version 1. Checksum: A1A085175DA56D90	FASTA	422	46,937
	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 FKTYSPTTKI IGVEPSGASS MYESVVVNNQ VVTLPNIDKF 250 260 270 280 290 300 VDGASVARVG DITFEIAKEN VDDYVQVDEG 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 genome sequence of USA300, an epidemic clone of community-acquired meticillin-resistant Staphylococcus aureus." Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G., Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F., Perdreau-Remington F. Lancet 367:731-739(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: USA300.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000255 Genomic DNA. Translation: ABD20804.1.
RefSeq	YP_494665.1. NC_007793.1.
3D structure databases
ProteinModelPortal	Q2FF63.
SMR	Q2FF63. Positions 9-421.
ModBase	Search...
Protein-protein interaction databases
STRING	451515.SAUSA300_2014.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABD20804; ABD20804; SAUSA300_2014.
GeneID	3915391.
KEGG	saa:SAUSA300_2014.
PATRIC	19593533. VBIStaAur129981_2157.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1171.
HOGENOM	HOG000046973.
KO	K01754.
OMA	DILMAHN.
ProtClustDB	PRK08639.
Enzyme and pathway databases
BioCyc	SAUR451515:GH3C-2028-MONOMER.
UniPathway	UPA00047; UER00054.
Family and domain databases
InterPro	IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS. IPR001721. Thr_deHydtase_C_reg_dom. IPR011820. Threonine_deHydtase_mt/plastid. IPR001926. Trp_syn_b_sub_like_PLP_eny_SF. [Graphical view]
Pfam	PF00291. PALP. 1 hit. PF00585. Thr_dehydrat_C. 1 hit. [Graphical view]
SUPFAM	SSF53686. PyrdxlP-dep_enz_bsu. 1 hit.
TIGRFAMs	TIGR02079. THD1. 1 hit.
PROSITE	PS00165. DEHYDRATASE_SER_THR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ILVA_STAA3

Accession

Primary (citable) accession number: Q2FF63

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	March 21, 2006
Last modified:	May 1, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program