Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

T-protein

Gene

tyrA

Organism
Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

Chorismate = prephenate.
Prephenate + NAD+ = 4-hydroxyphenylpyruvate + CO2 + NADH.

Pathway: L-tyrosine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes (4-hydroxyphenyl)pyruvate from prephenate (NAD(+) route).
Proteins known to be involved in this subpathway in this organism are:
  1. T-protein (tyrA)
This subpathway is part of the pathway L-tyrosine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (4-hydroxyphenyl)pyruvate from prephenate (NAD(+) route), the pathway L-tyrosine biosynthesis and in Amino-acid biosynthesis.

Pathway: prephenate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes prephenate from chorismate.
Proteins known to be involved in this subpathway in this organism are:
  1. P-protein (pheA), T-protein (tyrA), Monofunctional chorismate mutase (aroQ)
This subpathway is part of the pathway prephenate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes prephenate from chorismate, the pathway prephenate biosynthesis and in Metabolic intermediate biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Tyrosine biosynthesis

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00120; UER00203.
UPA00122; UER00961.

Names & Taxonomyi

Protein namesi
Recommended name:
T-protein
Including the following 2 domains:
Chorismate mutase (EC:5.4.99.5)
Short name:
CM
Prephenate dehydrogenase (EC:1.3.1.12)
Short name:
PDH
Gene namesi
Name:tyrA
OrganismiEnterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans)
Taxonomic identifieri549 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePantoea

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 373373T-proteinPRO_0000119196Add
BLAST

Proteomic databases

PRIDEiQ02287.

Structurei

3D structure databases

ProteinModelPortaliQ02287.
SMRiQ02287. Positions 90-368.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9090Chorismate mutasePROSITE-ProRule annotationAdd
BLAST
Domaini99 – 361263Prephenate/arogenate dehydrogenasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 chorismate mutase domain.PROSITE-ProRule annotation
Contains 1 prephenate/arogenate dehydrogenase domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di1.20.59.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR008244. Chor_mut/prephenate_DH_T.
IPR002701. Chorismate_mutase.
IPR020822. Chorismate_mutase_type_II.
IPR011277. CM_T.
IPR016040. NAD(P)-bd_dom.
IPR003099. Prephen_DH.
[Graphical view]
PfamiPF01817. CM_2. 1 hit.
PF02153. PDH. 1 hit.
[Graphical view]
PIRSFiPIRSF001499. Chor_mut_pdh_Tpr. 1 hit.
SMARTiSM00830. CM_2. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF48600. SSF48600. 1 hit.
TIGRFAMsiTIGR01799. CM_T. 1 hit.
PROSITEiPS51168. CHORISMATE_MUT_2. 1 hit.
PS51176. PDH_ADH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q02287-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVAELTALRD QIDSVDKALL DLLAKRLELV AEVGEVKSRY GLPIYVPERE
60 70 80 90 100
ASMLASRRKE AEALGVPPDL IEDVLRRVMR ESYTSENDKG FKTLCPELRP
110 120 130 140 150
VVIVGGKGQM GRLFEKMLGL SGYTVKTLDK EDWPQAETLL SDAGMVIISV
160 170 180 190 200
PIHLTEQVIA QLPPLPEDCI LVDLASVKNR PLQAMLAAHN GPVLGLHPMF
210 220 230 240 250
GPDSGSLAKQ VVVWCDGRQP EAYQWFLEQI QVWGARLHRI SAVEHDQNMA
260 270 280 290 300
FIQALRHFAT FAYGLHLAEE NVNLDQLLAL SSPIYRLELA MVGRLFAQDP
310 320 330 340 350
QLYADIIMSS ESNLALIKRY YQRFGEAIAL LEQGDKQAFI ASFNRVEQWF
360 370
GDHAKRFLVE SRSLLRSAND SRP
Length:373
Mass (Da):41,847
Last modified:April 1, 1993 - v1
Checksum:iC6E3C3B877A0628C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60420 Genomic DNA. Translation: CAA42950.1.
M74135 Genomic DNA. Translation: AAA24868.1.
PIRiS29934.
RefSeqiWP_010248465.1. NZ_JFOK01000009.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60420 Genomic DNA. Translation: CAA42950.1.
M74135 Genomic DNA. Translation: AAA24868.1.
PIRiS29934.
RefSeqiWP_010248465.1. NZ_JFOK01000009.1.

3D structure databases

ProteinModelPortaliQ02287.
SMRiQ02287. Positions 90-368.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ02287.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00120; UER00203.
UPA00122; UER00961.

Family and domain databases

Gene3Di1.20.59.10. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR008244. Chor_mut/prephenate_DH_T.
IPR002701. Chorismate_mutase.
IPR020822. Chorismate_mutase_type_II.
IPR011277. CM_T.
IPR016040. NAD(P)-bd_dom.
IPR003099. Prephen_DH.
[Graphical view]
PfamiPF01817. CM_2. 1 hit.
PF02153. PDH. 1 hit.
[Graphical view]
PIRSFiPIRSF001499. Chor_mut_pdh_Tpr. 1 hit.
SMARTiSM00830. CM_2. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF48600. SSF48600. 1 hit.
TIGRFAMsiTIGR01799. CM_T. 1 hit.
PROSITEiPS51168. CHORISMATE_MUT_2. 1 hit.
PS51176. PDH_ADH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "A monofunctional prephenate dehydrogenase created by cleavage of the 5' 109 bp of the tyrA gene from Erwinia herbicola."
    Xia T., Zhao G., Fischer R.S., Jensen R.A.
    J. Gen. Microbiol. 138:1309-1316(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiTYRA_ENTAG
AccessioniPrimary (citable) accession number: Q02287
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: May 27, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.