P46493 (ILVA_HAEIN) 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:	HI_0738.1

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › Haemophilus influenzae

Protein attributes

Sequence length	513 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 Reference 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 – 513	513	L-threonine dehydratase biosynthetic IlvA		PRO_0000185574
Regions
	Region	190 – 193	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	90	1	Pyridoxal phosphate By similarity
	Binding site	316	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	63	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P46493 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: DF42CA8B6FDE4CD7	FASTA	513	56,663
	10 20 30 40 50 60 MKNLLTNPQP SQSDYINAIV KLGSRVYEAA QVTPLQKMGK LSERLHNNIW IKREDRQPVN 70 80 90 100 110 120 SFKLRGAYAM ISSLSAEQKA AGVIAASAGN HAQGVALSAK QLGLKALIVM PQNTPSIKVD 130 140 150 160 170 180 AVRGFGGEVL LHGANFDEAK AKAIELSKEK NMTFIPPFDH PLVIAGQGTL AMEMLQQVAD 190 200 210 220 230 240 LDYVFVQVGG GGLAAGVAIL LKQFMPEIKI IGVESKDSAC LKAALDKGEP TDLTHIGLFA 250 260 270 280 290 300 DGVAVKRIGD ETFRLCQQYL DDMVLVDSDE VCAAMKDLFE NVRAVAEPSG ALGLAGLKKY 310 320 330 340 350 360 VKQNHIEGKN MAAILSGANL NFHTLRYVSE RCEIGENREA LLAVTMPEQP GSFLKFAYVL 370 380 390 400 410 420 GNRAVTEFSY RYADDKRACV FVGVRTTNEQ EKADIIADLT KNGFDVEDMS DDDIAKTHVR 430 440 450 460 470 480 YLMGGRAAND NERLYTFEFP EQKGALLKFL ETLQNRWNIS LFHYRAHGAD YGNILAGFQI 490 500 510 EQREQAEFEQ GLAQLNYVFE DVTKSKSYRY FLR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[2]	Koonin E.V., Rudd K.E. Submitted (SEP-1995) to UniProtKB Cited for: IDENTIFICATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L42023 Genomic DNA. Translation: AAC22398.1.
RefSeq	NP_438898.1. NC_000907.1.
3D structure databases
ProteinModelPortal	P46493.
SMR	P46493. Positions 10-512.
ModBase	Search...
Protein-protein interaction databases
STRING	71421.HI0738.1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC22398; AAC22398; HI_0738.1.
GeneID	950764.
KEGG	hin:HI0738.1.
PATRIC	20190119. VBIHaeInf48452_0775.
Phylogenomic databases
eggNOG	COG1171.
KO	K01754.
OMA	AAYYKAV.
ProtClustDB	PRK09224.
Enzyme and pathway databases
UniPathway	UPA00047; UER00054.
Family and domain databases
InterPro	IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS. IPR005787. Thr_deHydtase_biosynth. IPR001721. Thr_deHydtase_C_reg_dom. IPR001926. Trp_syn_b_sub_like_PLP_eny_SF. [Graphical view]
Pfam	PF00291. PALP. 1 hit. PF00585. Thr_dehydrat_C. 2 hits. [Graphical view]
SUPFAM	SSF53686. PyrdxlP-dep_enz_bsu. 1 hit.
TIGRFAMs	TIGR01124. ilvA_2Cterm. 1 hit.
PROSITE	PS00165. DEHYDRATASE_SER_THR. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ILVA_HAEIN

Accession

Primary (citable) accession number: P46493

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program