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pagL

Gene
pagL
Protein
Phospho-alpha-glucosidase PagL
Organism
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Length
445 amino acids
Function
Phospho-alpha-glucosidase that catalyzes the hydrolysis of p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate, but is not able to cleave 'natural' phospho-alpha-glucosides produced via the phosphoenolpyruvate-dependent sugar phosphotransferase system (PEP-PTS).
Similarity
Belongs to the glycosyl hydrolase 4 family.
Mass
51.156 kDa
Sequence
MKKYSICIVGGGSRYTPDMLAMLCNQKERFPLRKIVLYDNESERQETVGNYAKILFKEYYPELEEVIWTTDEKEAFEDIDFALMQIRAGRLKMREKDEKISLKHGCLGQETCGAGGFAYGLRSVPAVIDLIKSIRTYSPKCWILNYSNPAAIVAEATKRVFPNDYRIINICDMPIAIMDIYAAVLGLKRRDLEPKYFGLNHFGWFTHILDKKTGENYLPKLREILKTPVDVQTEPLFQEKSWKSTFEFMSQMINDYDEYLPNTYLQYYLYPAKMRNKENPEYTRANEVMDGNEKETYERMHKIISLGKIHGTKYELTSDVGCHAEYIVDLATAIANNTNEIFLIITENKGTINNVSKDMMVEVPCRVGSNGVEPLVVGSIPAFYKGLMENQYAYEKLSVDACLEGSYQKALQALVLNRTVVNTDVAKELLKDLIEANKGYWNELH

Gene
pagL
Protein
6-phospho-alpha-glucosidase
Organism
Leptotrichia buccalis (strain ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b)
Length
440 amino acids
Function
In vitro, readily hydrolyzes p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate (pNPalphaG6P), a chromogenic analog of the phosphorylated isomers of sucrose. In vivo, is probably involved in the degradation of the 6-phosphate derivatives of the sucrose isomers trehalulose, turanose, maltulose and palatinose, catalyzing their hydrolysis into glucose 6-phosphate (G6P) and fructose, which allows the bacterium to use these sugars as energy sources for growth. Is not able to hydrolyze the C2 or C4 chromogenic stereomers (i.e. pNPalpha-mannopyranoside-6P and pNPalpha-galactopyranoside-6P, respectively).
Similarity
Belongs to the glycosyl hydrolase 4 family.
Mass
49.678 kDa
Sequence
MKKFSIVVAGGGSTFTPGIVLMLLENLDKFPIRQIKFYDNDAQRQEVIAKACDIIIKEKAPDINFVYTTDPETAFTDIDFVMAHIRVGKYAMREKDEKIPLRHGVLGQETCGPGGISYGMRSIGGVIELVDYMEKYSPNAWMLNYSNPAAIVAEATRRLRPNSKILNICDMPIGIEIRMAEMLGLKSRKDMVIRYFGLNHFGWWTDIRDKKGNDLMPALREKVAKIGYNVEIEGENTEASWNDTFTKARDVFAIDPTTMPNTYLKYYFFPDYVVEHSNPNHTRANEVMEGREKFVFGECRAIAEKGTAKDSKLHVDDHASYIVDLARAIAYDTKERMLLIVENDGAISNFDPTAMVEVPCIVGSNGPEKIVQGKIPQFQKGLMEQQVSVEKLTVEAWMEGSYQKLWQAITLSRTVPSASVAKAILDDLIEANKDFWPVLK

Gene
pagL
Protein
Lipid A deacylase PagL
Organism
Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
Length
178 amino acids
Function
Has lipid A 3-O-deacylase activity. Hydrolyzes the ester bond at the 3 position of lipid A, a bioactive component of lipopolysaccharide (LPS), thereby releasing the primary fatty acyl moiety.
Similarity
Belongs to the PagL family.
Mass
19.824 kDa
Sequence
MQFLKKNKPLFGIVTLALACATAQAQPTQGGVSLHYGIGDHYQRVTLNYETPTLWSHQFGGNWGRLDLTPELGASYWWADGSRSPGHVWQASAIPMFRWWTGERFYIEAGIGATVFSSTSFADKRIGSAFQFGDHIGLGFLLTPSNRIGLRYSHFSNAGIKEPNPGLDIVQLTYTYQF

Gene
pagL
Protein
Lipid A deacylase PagL
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Length
173 amino acids
Function
Has lipid A 3-O-deacylase activity. Hydrolyzes the ester bond at the 3 position of lipid A, a bioactive component of lipopolysaccharide (LPS), thereby releasing the primary fatty acyl moiety. Lacks fatty acyl chain-length specificity as removes both 3-OH C10 and 3-OH C14 fatty acids from lipid A.
Similarity
Belongs to the PagL family.
Mass
18.394 kDa
Sequence
MKKLLPLAVLAALSSVHVASAQAADVSAAVGATGQSGMTYRLGLSWDWDKSWWQTSTGRLTGYWDAGYTYWEGGDEGAGKHSLSFAPVFVYEFAGDSIKPFIEAGIGVAAFSGTRVGDQNLGSSLNFEDRIGAGLKFANGQSVGVRAIHYSNAGLKQPNDGIESYSLFYKIPI