ECMDB: Phosphatase yqaB (P77475)

Identification

Name:

Phosphatase yqaB

Synonyms:

Not Available

Gene Name:

yqaB

Enzyme Class:

Not Available

Biological Properties

General Function:

Involved in catalytic activity

Specific Function:

Catalyzes the dephosphorylation of the artificial chromogenic substrate p-nitrophenyl phosphate (pNPP) and of the natural substrates fructose 1-phosphate and 6-phosphogluconate

Cellular Location:

Cytoplasmic

SMPDB Pathways:

Not Available

KEGG Pathways:

Not Available

KEGG Reactions:

1.0

↔

1.0

1.0Glucose 1-phosphate ↔ 1.0Glucose 6-phosphate
ReactionCard

EcoCyc Reactions:

1.0

→

1.0D-fructose

1.0

1.0Fructose 1-phosphate + 1.0Water → 1.0D-fructose + 1.0Phosphate
ReactionCard

Metabolites:

ECMDB ID	Name	View
ECMDB01076	Fructose 1-phosphate	MetaboCard
ECMDB01586	Glucose 1-phosphate	MetaboCard
ECMDB01401	Glucose 6-phosphate	MetaboCard
ECMDB01429	Phosphate	MetaboCard
ECMDB00494	Water	MetaboCard

GO Classification:

Function
catalytic activity
hydrolase activity
Process
metabolic process

Gene Properties

Blattner:

b2690

Gene Orientation

Counterclockwise

Centisome Percentage:

60.67

Left Sequence End

2814959

Right Sequence End

2815525

Gene Sequence:

>567 bp
ATGAATATCACTGCTACTGTTCTTCTTGCGTTTGGTATGTCGATGGATGCATTTGCTGCA
TCAATCGGTAAAGGTGCCACCCTCCATAAACCGAAATTTTCTGAAGCATTGCGAACCGGC
CTTATTTTTGGTGCCGTCGAAACCCTGACGCCGCTGATCGGCTGGGGAATGGGCATGTTA
GCCAGCCGGTTTGTCCTTGAATGGAACCACTGGATTGCGTTTGTGCTGCTGATATTCCTC
GGCGGGCGAATGATTATTGAGGGTTTTCGTGGCGCAGATGATGAAGATGAAGAGCCGCGC
CGTCGACACGGTTTCTGGCTACTGGTAACCACCGCGATTGCCACCAGCCTGGATGCCATG
GCTGTGGGTGTTGGTCTTGCTTTCCTGCAGGTCAACATTATCGCGACCGCATTGGCCATT
GGTTGTGCAACCTTGATTATGTCAACATTAGGGATGATGGTTGGTCGCTTTATCGGCTCA
ATTATTGGGAAAAAAGCGGAAATTCTCGGCGGGCTGGTGCTGATCGGCATCGGCGTCCAG
ATCCTCTGGACGCACTTCCACGGTTAA

Protein Properties

Pfam Domain Function:

Hydrolase (PF00702 )

Protein Residues:

188

Protein Molecular Weight:

20780

Protein Theoretical pI:

Signaling Regions:

None

Transmembrane Regions:

None

Protein Sequence:

>Phosphatase yqaB
MYERYAGLIFDMDGTILDTEPTHRKAWREVLGHYGLQYDIQAMIALNGSPTWRIAQAIIE
LNQADLDPHALAREKTEAVRSMLLDSVEPLPLVDVVKSWHGRRPMAVGTGSESAIAEALL
AHLGLRHYFDAVVAADHVKHHKPAPDTFLLCAQRMGVQPTQCVVFEDADFGIQAARAAGM
DAVDVRLL

References

External Links:

Resource	Link
Uniprot ID:	P77475
Uniprot Name:	YQAB_ECOLI
GenBank Gene ID:	AP009048
Genebank Protein ID:	85675134
Ecogene ID:	EG13530
Ecocyc:	EG13530
ColiBase:	b2690
Kegg Gene:	b2690
EchoBASE ID:	EB3301
CCDB:	YQAB_ECOLI
BacMap:	16130602

General Reference:

Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
Kuznetsova, E., Proudfoot, M., Sanders, S. A., Reinking, J., Savchenko, A., Arrowsmith, C. H., Edwards, A. M., Yakunin, A. F. (2005). "Enzyme genomics: Application of general enzymatic screens to discover new enzymes." FEMS Microbiol Rev 29:263-279. Pubmed: 15808744
Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837