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B6db families:
Description Phosphorylase
Notes Very distinct family, the only one belonging to fold-type V.
Sequences are in general long (>700 aa), but some Archaea employ a shorter (monomeric) form of the enzyme.
PLP Fold Type V
PLP-dependent Domain
Domain alignment
Domain hmm
Fold type V

Number of sequences 50
Sequences in seed alignment
ArchaeaWP_015324508 (Methanomethylovorans hollandica); WP_011250357 (Thermococcus kodakarensis); AAL81659 (Pyrococcus furiosus); WP_069806710 (Vulcanisaeta thermophila); WP_014127284 (Thermoproteus tenax); WP_011844103 (Methanoculleus marisnigri); AAK42667 (Sulfolobus solfataricus);
BacteriaPHSG_CHLPN (Chlamydia pneumoniae); PHSG_HAEIN (Haemophilus influenzae); PHSG_BACSU (Bacillus subtilis); BAB11741 (Thermus aquaticus); PHSG_SYNY3 (Synechocystis sp. (strain PCC 6803)); PHSG_CHLTR (Chlamydia trachomatis); PHSM_STRPN (Streptococcus pneumoniae); PHSG_ECOLI (Escherichia coli); PHSG_AQUAE (Aquifex aeolicus); BAA19592 (Geobacillus stearothermophilus); PHSG_CHLMU (Chlamydia muridarum); ABN51595 (Ruminiclostridium thermocellum ATCC 27405); CCH24475 (Corynebacterium glutamicum); AAM52219 (Corynebacterium callunae); PHSM_ECOLI (Escherichia coli);
FungiCAD28434 (Aspergillus fumigatus); ABN66962 (Pichia stipitis); XP_363893 (Magnaporthe grisea); PHSG_YEAST (Saccharomyces cerevisiae);
MetazoaPHS2_HUMAN (Homo sapiens); PHS1_RAT (Rattus norvegicus); PHS2_RABIT (Oryctolagus cuniculus); PHS2_BOVIN (Bos taurus); PHS2_MOUSE (Mus musculus); PHSG_DROME (Drosophila melanogaster); PHS3_HUMAN (Homo sapiens); PHS1_HUMAN (Homo sapiens); PHS2_SHEEP (Ovis aries); PHS1_MOUSE (Mus musculus); PHS2_RAT (Rattus norvegicus); PHS3_RAT (Rattus norvegicus);
Other_EukaryaPHS2_DICDI (Dictyostelium discoideum); XP_001024430 (Tetrahymena thermophila); PHS1_DICDI (Dictyostelium discoideum); XP_001449904 (Paramecium tetraurelia);
ViridiplantaePHSH_WHEAT (Triticum aestivum); PHS2_SOLTU (Solanum tuberosum); PHSH_VICFA (Vicia faba); PHSH_ARATH (Arabidopsis thaliana); PHSH_SOLTU (Solanum tuberosum); PHS1_SOLTU (Solanum tuberosum); PHSL_VICFA (Vicia faba); PHSL_IPOBA (Ipomoea batatas);

DISPLAY: Fasta format, alignment, hmm, hmm_local

Reference sequence PHSG_YEAST
Domain interval 164-900
Catalytic site 751 K
 Clermont L, Macha A, Müller LM, Derya SM, von Zaluskowski P, Eck A, Eikmanns BJ, Seibold GM (2015) The α-glucan phosphorylase MalP of Corynebacterium glutamicum is subject to transcriptional regulation and competitive inhibition by ADP-glucose J Bacteriol 197 1394-407.

 Ye, X.; Rollin, J.; Zhang, Y. (2010) Thermophilic alpha-glucan phosphorylase from Clostridium thermocellum: cloning, characterization and enhanced thermostability J Mol Catal B: Enzymatic 65 110-116.

 Mueller M, Takemasa R, Schwarz A, Atomi H, Nidetzky B. (2009) "Short-chain" alpha-1,4-glucan phosphorylase having a truncated N-terminal domain: functional expression and characterization of the enzyme from Sulfolobus solfataricus Biochim Biophys Acta 1794 1709-14.

 Nahálka J (2008) Physiological aggregation of maltodextrin phosphorylase from Pyrococcus furiosus and its application in a process of batch starch degradation to alpha-D-glucose-1-phosphate J Ind Microbiol Biotechnol 35 219-23.

 Schwarz A, Pierfederici FM, Nidetzky B. (2005) Catalytic mechanism of alpha-retaining glucosyl transfer by Corynebacterium callunae starch phosphorylase: the role of histidine-334 examined through kinetic characterization of site-directed mutants. Biochem J 210 437-45.

 Bhuiyan, S.H.; Rus'd, A.A.; Kitaoka, M.; Hayashi, K. (2003) Characterization of a hyperthermostable glycogen phosphorylase from Aquifex aeolicus expressed in Escherichia coli J Mol Catal B: Enzymatic 22 173-80.

 Takaha, T.; Yanase, M.; Takata, H.; Okada, S. (2001) Structure and properties of Thermus aquaticus alpha-glucan phosphorylase expressed in Escherichia coli J. Appl. Glycosci. 48 71-78.

 O'Reilly, M.; Watson, K. A.; Johnson, L. N. (1999) The crystal structure of the Escherichia coli maltodextrin phosphorylase-acarbose complex Biochemistry 38 5337-45.

 Takata, H.; Takaha, T.; Okada, S.; Takagi, M.; Imanaka, T.; (1998) Purification and characterization of alpha-glucan phosphorylase from Bacillus stearothermophilus J. Ferment Bioeng 85 156-161.

 Rath, V. L.; Hwang, P. K.; Fletterick, R. J. (1992) Purification and crystallization of glycogen phosphorylase from Saccharomyces cerevisiae J Mol Biol 225 1027-34.

 Mori, H.; Tanizawa, K.; Fukui, T. (1991) Potato tuber type H phosphorylase isozyme. Molecular cloning, nucleotide sequence, and expression of a full-length cDNA in Escherichia coli J Biol Chem 266 18446-53.

 Sprang SR, Withers SG, Goldsmith EJ, Fletterick RJ, Madsen NB. (1991) Structural basis for the activation of glycogen phosphorylase b by adenosine monophosphate Science 254 1367-1371.

 Titani K, Koide A, Hermann J, Ericsson LH, Kumar S, Wade RD, Walsh KA, Neurath H, Fischer EH. (1977) Complete amino acid sequence of rabbit muscle glycogen phosphorylase. Proc Natl Acad Sci U S A 74 4762-6.

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last changed 2018/05/25 09:33

B6db families