Reviewed, UniProtKB/Swiss-Prot P43902 (TYRA_HAEIN)

Names and origin

Protein names

Recommended name:
    T-protein
Including the following 2 domains:
    1- Recommended name:
            Chorismate mutase
                Short name=CM
              EC=5.4.99.5
    2- Recommended name:
            Prephenate dehydrogenase
                Short name=PDH
              EC=1.3.1.12

Gene names

Name:	tyrA
Ordered Locus Names:	HI1290

Organism

Haemophilus influenzae [Complete proteome] [HAMAP]

Taxonomic identifier

727 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Chorismate = prephenate. Prephenate + NAD+ = 4-hydroxyphenylpyruvate + CO2 + NADH.
Pathway	Amino-acid biosynthesis; L-tyrosine biosynthesis; L-tyrosine from prephenate: step 1/2. Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1.
Subcellular location	Cytoplasm.
Sequence similarities	Contains 1 chorismate mutase domain. Contains 1 prephenate/arogenate dehydrogenase domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Tyrosine biosynthesis
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Isomerase Oxidoreductase
Technical term	3D-structure Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tyrosine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	binding Inferred from electronic annotation. Source: InterPro chorismate mutase activity Inferred from electronic annotation. Source: EC prephenate dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: InterPro prephenate dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 377	377	T-protein		PRO_0000119197
Regions
	Domain	1 – 92	92	Chorismate mutase
	Domain	101 – 364	264	Prephenate/arogenate dehydrogenase

Sequences

	Sequence		Length	Mass (Da)
	P43902-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 319722CFDFDE5791	FASTA	377	43,022
	10 20 30 40 50 60 MSFMEALKDL RSEIDSLDRE LIQLFAKRLE LVSQVGKVKH QHGLPIYAPE REIAMLQARR 70 80 90 100 110 120 LEAEKAGISA DLIEDVLRRF MRESYANENQ FGFKTINSDI HKIVIVGGYG KLGGLFARYL 130 140 150 160 170 180 RASGYPISIL DREDWAVAES ILANADVVIV SVPINLTLET IERLKPYLTE NMLLADLTSV 190 200 210 220 230 240 KREPLAKMLE VHTGAVLGLH PMFGADIASM AKQVVVRCDG RFPERYEWLL EQIQIWGAKI 250 260 270 280 290 300 YQTNATEHDH NMTYIQALRH FSTFANGLHL SKQPINLANL LALSSPIYRL ELAMIGRLFA 310 320 330 340 350 360 QDAELYADII MDKSENLAVI ETLKQTYDEA LTFFENNDRQ GFIDAFHKVR DWFGDYSEQF 370 LKESRQLLQQ ANDLKQG

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: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L42023 Genomic DNA. Translation: AAC22939.1.

PIR

H64114.

RefSeq

NP_439442.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PV7	X-ray	2.00	A/B	81-377	[»]

ModBase

Search...

Genome annotation databases

GeneID

950220.

GenomeReviews

Gene locus HI1290 in contig L42023_GR.

KEGG

hin:HI1290.

NMPDR

fig|71421.1.peg.1230.

TIGR

HI1290.

Phylogenomic databases

HOGENOM

P43902.

OMA

P43902. RTMRESY.

Enzyme and pathway databases

BioCyc

HINF71421:HI_1290-MON.

BRENDA

1.3.1.12. 109.
5.4.99.5. 109.

Family and domain databases

InterPro

IPR008244. Chor_mut/prephenate_DH_T.
IPR002701. Chorismate_mut.
IPR011277. CM_T.
IPR016040. NAD(P)-bd_dom.
IPR003099. Prephen_DH.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

Pfam

PF01817. CM_2. 1 hit.
PF02153. PDH. 1 hit.
[Graphical view]

PIRSF

PIRSF001499. Chor_mut_pdh_Tpr. 1 hit.

TIGRFAMs

TIGR01799. CM_T. 1 hit.

PROSITE

PS51168. CHORISMATE_MUT_2. 1 hit.
PS51176. PDH_ADH. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

TYRA_HAEIN

Accession

Primary (citable) accession number: P43902

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 70 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)