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Protein

Putative tagatose-6-phosphate ketose/aldose isomerase

Gene

agaS

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

May be a tagatose-6-phosphate ketose/aldose isomerase.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

BioCyciEcoCyc:G7634-MONOMER.
ECOL316407:JW3105-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative tagatose-6-phosphate ketose/aldose isomerase (EC:5.3.1.-)
Gene namesi
Name:agaS
Synonyms:yraB
Ordered Locus Names:b3136, JW3105
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12767. agaS.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 384384Putative tagatose-6-phosphate ketose/aldose isomerasePRO_0000136590Add
BLAST

Proteomic databases

PaxDbiP42907.
PRIDEiP42907.

Interactioni

Protein-protein interaction databases

BioGridi4261158. 779 interactions.
IntActiP42907. 5 interactions.
STRINGi511145.b3136.

Structurei

Secondary structure

1
384
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 217Combined sources
Helixi23 – 4927Combined sources
Beta strandi55 – 595Combined sources
Helixi63 – 7917Combined sources
Beta strandi81 – 855Combined sources
Helixi88 – 936Combined sources
Helixi95 – 984Combined sources
Beta strandi105 – 11410Combined sources
Helixi117 – 12913Combined sources
Beta strandi131 – 14010Combined sources
Helixi145 – 1517Combined sources
Helixi163 – 1653Combined sources
Beta strandi169 – 1713Combined sources
Helixi174 – 18714Combined sources
Turni189 – 1913Combined sources
Turni194 – 1974Combined sources
Helixi198 – 21013Combined sources
Turni211 – 2133Combined sources
Beta strandi225 – 2328Combined sources
Helixi235 – 24915Combined sources
Turni250 – 2523Combined sources
Beta strandi253 – 2597Combined sources
Helixi261 – 2644Combined sources
Turni265 – 2673Combined sources
Helixi268 – 2714Combined sources
Beta strandi276 – 2816Combined sources
Helixi288 – 30215Combined sources
Beta strandi305 – 31410Combined sources
Helixi317 – 3204Combined sources
Beta strandi322 – 3265Combined sources
Helixi335 – 35622Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3C3JX-ray1.80A/B/C/D/E/F1-384[»]
ProteinModelPortaliP42907.
SMRiP42907. Positions 4-384.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42907.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 197153SIS 1PROSITE-ProRule annotationAdd
BLAST
Domaini215 – 364150SIS 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the SIS family. AgaS subfamily.Curated
Contains 2 SIS domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105E70. Bacteria.
COG2222. LUCA.
HOGENOMiHOG000272306.
InParanoidiP42907.
KOiK02082.
OMAiYHLIITC.
OrthoDBiEOG6QCDB4.
PhylomeDBiP42907.

Family and domain databases

InterProiIPR001347. SIS.
IPR014180. Sugar_isomerase_AgaS.
[Graphical view]
PfamiPF01380. SIS. 2 hits.
[Graphical view]
TIGRFAMsiTIGR02815. agaS_fam. 1 hit.
PROSITEiPS51464. SIS. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42907-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPENYTPAAA ATGTWTEEEI RHQPRAWIRS LTNIDALRSA LNNFLEPLLR
60 70 80 90 100
KENLRIILTG AGTSAFIGDI IAPWLASHTG KNFSAVPTTD LVTNPMDYLN
110 120 130 140 150
PAHPLLLISF GRSGNSPESV AAVELANQFV PECYHLPITC NEAGALYQNA
160 170 180 190 200
INSDNAFALL MPAETHDRGF AMTSSITTMM ASCLAVFAPE TINSQTFRDV
210 220 230 240 250
ADRCQAILTS LGDFSEGVFG YAPWKRIVYL GSGGLQGAAR ESALKVLELT
260 270 280 290 300
AGKLAAFYDS PTGFRHGPKS LVDDETLVVV FVSSHPYTRQ YDLDLLAELR
310 320 330 340 350
RDNQAMRVIA IAAESSDIVA AGPHIILPPS RHFIDVEQAF CFLMYAQTFA
360 370 380
LMQSLHMGNT PDTPSASGTV NRVVQGVIIH PWQA
Length:384
Mass (Da):41,783
Last modified:November 1, 1995 - v1
Checksum:i463F9458476DC46B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18997 Genomic DNA. Translation: AAA57939.1.
U00096 Genomic DNA. Translation: AAC76170.1.
AP009048 Genomic DNA. Translation: BAE77182.1.
PIRiD65103.
RefSeqiNP_417605.1. NC_000913.3.
WP_001114869.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76170; AAC76170; b3136.
BAE77182; BAE77182; BAE77182.
GeneIDi947645.
KEGGiecj:JW3105.
eco:b3136.
PATRICi32121690. VBIEscCol129921_3231.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18997 Genomic DNA. Translation: AAA57939.1.
U00096 Genomic DNA. Translation: AAC76170.1.
AP009048 Genomic DNA. Translation: BAE77182.1.
PIRiD65103.
RefSeqiNP_417605.1. NC_000913.3.
WP_001114869.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3C3JX-ray1.80A/B/C/D/E/F1-384[»]
ProteinModelPortaliP42907.
SMRiP42907. Positions 4-384.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261158. 779 interactions.
IntActiP42907. 5 interactions.
STRINGi511145.b3136.

Proteomic databases

PaxDbiP42907.
PRIDEiP42907.

Protocols and materials databases

DNASUi947645.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76170; AAC76170; b3136.
BAE77182; BAE77182; BAE77182.
GeneIDi947645.
KEGGiecj:JW3105.
eco:b3136.
PATRICi32121690. VBIEscCol129921_3231.

Organism-specific databases

EchoBASEiEB2620.
EcoGeneiEG12767. agaS.

Phylogenomic databases

eggNOGiENOG4105E70. Bacteria.
COG2222. LUCA.
HOGENOMiHOG000272306.
InParanoidiP42907.
KOiK02082.
OMAiYHLIITC.
OrthoDBiEOG6QCDB4.
PhylomeDBiP42907.

Enzyme and pathway databases

BioCyciEcoCyc:G7634-MONOMER.
ECOL316407:JW3105-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP42907.
PROiP42907.

Family and domain databases

InterProiIPR001347. SIS.
IPR014180. Sugar_isomerase_AgaS.
[Graphical view]
PfamiPF01380. SIS. 2 hits.
[Graphical view]
TIGRFAMsiTIGR02815. agaS_fam. 1 hit.
PROSITEiPS51464. SIS. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. "Novel phosphotransferase genes revealed by bacterial genome sequencing: a gene cluster encoding a putative N-acetylgalactosamine metabolic pathway in Escherichia coli."
    Reizer J., Ramseier T.M., Reizer A., Charbit A., Saier M.H. Jr.
    Microbiology 142:231-250(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISCUSSION OF SEQUENCE.
  4. "The crystal structure of the tagatose-6-phosphate ketose/aldose isomerase from Escherichia coli."
    Midwest center for structural genomics (MCSG)
    Submitted (FEB-2008) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

Entry informationi

Entry nameiAGAS_ECOLI
AccessioniPrimary (citable) accession number: P42907
Secondary accession number(s): Q2M974
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 8, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

In contrast to E.coli strains C and EC3132, K-12 strains cannot grow on N-acetylgalactosamine and D-galactosamine, because they carry a deletion and thus lack active PTS systems specific for these compounds. Therefore, AgaS in K-12 strains is not involved in the degradation of these compounds.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.