BBa_K1988011

BBa_K1988011 Version 1

Component

Source:
http://parts.igem.org/Part:BBa_K1988011
Generated By: https://synbiohub.org/public/igem/igem2sbol/1
Created by: Bowman Clark
Date created: 2016-10-13 11:00:00
Date modified: 2016-10-14 06:12:31

his-tagged PPGK ATPi homologue w/ Anderson Promoter J23106



Types
DnaRegion

Roles
CDS

Coding

Sequences BBa_K1988011_sequence (Version 1)

Description

PPGK



Overview


Name:Polyphosphate Dependent Glucokinase




Function:


PPGK catalyzes the first step in glycolysis, and therefore the presence of this enzyme suggests the importance of polyphosphate to metabolism in M. phosphovorus. [1]. Still, polyphosphate is not the only source of phosphorus in glycolysis, as evidenced by an ATP-only phosphofructokinase, which catalyzes the phosphorylation of D-fructose 6-phosphate [2].



In Microlunatus phosphovorus: M. phosphovorus is the first organism reported to have two homologs of PPGK. Microlunatus phosphovorus is unique because, whereas other Actinobacteria species have PPGKs that utilize both ATP and polyphosphate as a phosphorus donor, M. phosphovorus has a PPGK that has been found to only use polyphosphate as a phosphorus donor. The second PPGK homolog has yet to be characterized, so whether or not that PPGK utilizes both ATP and polyphosphate or just polyphosphate is unknown. [1]



Location: Cytoplasm


While the exact location of PPGK in the cytoplasm of Microlunatus phosphovorus is unknown, PPGK is located in the volutin granules of the Actinobacteria Corynebacterium glutamicum[3].The PPGKs in M. phosphovorus could possibly be located in the volutin granules as well.



Cofactors and Modifications: There are currently no known cofactors or modifications of the PPGK homolog and ATP independent PPGK in M. phosphovorus.



Images: The three-dimensional structure of all proteins were predicted using the I-TASSER software [4]. All images shown are the models with the highest confidence, which is quantitatively measured with a C-score that typically falls within the range [-5,2], in which 2 represents the highest level of confidence, and -5 represents the lowest level of confidence.




PPGK ATP Independent (ATPI)


Locus tag: MLP_05430



Image




C-score: 0.91



Gene length: 801 base pairs



Protein size: 28.1 kDa



Amino acid sequence: MTDTPPVAAP GRSVLGIDIG GSGIKGAPVD LATGLFAAER LRIDTPAKST PANVAKVVAE IVDHFKAEVG DGPIGITIPA VVTHGQTRSA ANIDHSWIDA EAEQIFEDVL QRDIYLMNDA DAAGIAEVHY GAAKGHPGLV IVTTLGTGIG SAMIHRGVLI PNSELGHLEI DGLDAETNAA SSAKERNDWS YSEWAPKLQR YYERLEALFW PDLIVVGGGV SKKAHKFLPK LKLKSQIIPA QLLNTAGIVG AAWLAADRLV HPDPMG [5]



In Microlunatus phosphovorus: PPGK ATPI can only use polyphosphate, and not ATP, as a phosphate donor. [1]



pH Range Optimal pH: 5.5



Temperature Range Optimal temperature: 30??C [2]



PPGK homolog


Locus tag: MLP_26610



Image




C-score: 1.25



Gene length: 762 base pairs



Protein size:

Amino acid sequence: MNETANIALG IDIGGTGIKG ALVDLETGAL VSDRFRLDTP RPALPAAVAD TVVAVAAHFD FAGPVGVAFP GVVLDGVVHT AANLHPDWIG ASLAELVGSR LSGPSVFLND ADAAGLAEAR FGAAKGVSGV VLLVTLGTGI GTAMISDGQL VPNSEFGHLE LDGLDAETYA AASARKRNNH TWEEWAGHAE HYLKYLEGLV WPKLFVLGGG ITKNPELWLH YLKPRTPIVL ATNINNAGII GAAAAAAQTQ QAG [6]



In Microlunatus phosphovorus: This PPGK homolog has yet to be characterized, so it is unknown whether or not this PPGK homolog can utilize ATP as a phosphate donor. [1]



pH Range The PPGK homolog in M. phosphovorus has yet to be characterized, and so there is no data for the pH range in which it functions.



Temperature Range The PPGK homolog in M. phosphovorus has yet to be characterized, and so there is no data for the temperature range in which it functions.





References



[1] A. Kawakoshi, H. Nakazawa, J. Fukada, M. Sasagawa, Y. Katano, S. Nakamura, A. Hosoyama, H. Sasaki, N. Ichikawa, S. Hanada, Y. Kamagata, K. Nakamura, S. Yamazaki and N. Fujita, "Deciphering the Genome of Polyphosphate Accumulating Actinobacterium Microlunatus phosphovorus", DNA Research, vol. 19, no. 5, pp. 383-394, 2012.

[2] S. Tanaka, S. Lee, K. Hamaoka, J. Kato, N. Takiguchi, K. Nakamura, H. Ohtake and A. Kuroda, "Strictly Polyphosphate-Dependent Glucokinase in a Polyphosphate-Accumulating Bacterium, Microlunatus phosphovorus", Journal of Bacteriology, vol. 185, no. 18, pp. 5654-5656, 2003.

[3] S. Pallerla, S. Knebel, T. Polen, P. Klauth, J. Hollender, V. Wendisch and S. Schoberth, "Formation of volutin granules in Corynebacterium glutamicum", FEMS Microbiology Letters, vol. 243, no. 1, pp. 133-140, 2005.

[4] Yang, R. Yan, A. Roy, D. Xu, J. Poisson and Y. Zhang, "The I-TASSER Suite: protein structure and function prediction", Nature Methods, vol. 12, no. 1, pp. 7-8, 2014.

[5] "ppgK - Polyphosphate-dependent glucokinase - Microlunatus phosphovorus - ppgK gene & protein", Uniprot, 2016. [Online]. Available: http://www.uniprot.org/uniprot/Q76LT2. [Accessed: 22- Jul- 2016].

[6] "ppgK - Polyphosphate-dependent glucokinase - Microlunatus phosphovorus (strain ATCC 700054 / DSM 10555 / JCM 9379 / NBRC 101784 / NCIMB 13414 / VKM Ac-1990 / NM-1) - ppgK gene & protein", Uniprot, 2016. [Online]. Available: http://www.uniprot.org/uniprot/F5XI06. [Accessed: 22- Jul- 2016].



Notes

Codon optimized for E. coli K-12 using IDT Codon Optimizer

Source

Genetic sequence from 'Deciphering the Genome of Polyphosphate Accumulating Actinobacterium Microlunatus Phosphovorus' by Kawakoshi, et. al.

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