CAZyme Information: MGYG000002357_03231

Basic Information

• Species: Bacillus licheniformis
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; Bacillus licheniformis
• CAZyme ID: MGYG000002357_03231
• CAZy Family: GT35
• CAZyme Description: Glycogen phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
294	MGYG000002357_1|CGC40	33538.18	6.1013

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002357	4208157	Isolate	South Korea	Asia

• Gene Location: Start: 3110689; End: 3111573 Strand: -

Full Sequence      

MFSSKESFKQCFLKRVERLCGKSFRDSSTLDQYQTLGIMVREHISANWIGTNERSRSNQN
KQTYYLSIEFLLGRLLGQNLLNLGVREVVQEGLSELGICLEDIEEAEMDAGLGNGGLGRL
AACFLDSLASLDLPGHGMGIRYKHGFFEQKIVDGHQVELPEQWLKHGYVWEIRNADQAVC
VRFGGRVKMAQEGGRLRFWQEDAEVMTAVPYDIPIIGYETETVNTLRLWNAEPCSLHHEP
NILKYKRETEAVSECLYPDDTHDEGKILRLKQQYFLVSASLQSIVKRYKSPVTP

Enzyme Prediction     

EC	2.4.1.1

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04300	GT35_Glycogen_Phosphorylase	2.31e-118	9	290	1	290	glycogen phosphorylase and similar proteins. This is a family of oligosaccharide phosphorylases. It includes yeast and mammalian glycogen phosphorylases, plant starch/glucan phosphorylase, as well as the maltodextrin phosphorylases of bacteria. The members of this family catalyze the breakdown of oligosaccharides into glucose-1-phosphate units. They are important allosteric enzymes in carbohydrate metabolism. The allosteric control mechanisms of yeast and mammalian members of this family are different from that of bacterial members. The members of this family belong to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
TIGR02093	P_ylase	1.65e-116	12	290	1	287	glycogen/starch/alpha-glucan phosphorylases. This family consists of phosphorylases. Members use phosphate to break alpha 1,4 linkages between pairs of glucose residues at the end of long glucose polymers, releasing alpha-D-glucose 1-phosphate. The nomenclature convention is to preface the name according to the natural substrate, as in glycogen phosphorylase, starch phosphorylase, maltodextrin phosphorylase, etc. Name differences among these substrates reflect differences in patterns of branching with alpha 1,6 linkages. Members include allosterically regulated and unregulated forms. A related family, TIGR02094, contains examples known to act well on particularly small alpha 1,4 glucans, as may be found after import from exogenous sources. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
pfam00343	Phosphorylase	2.29e-98	93	289	1	205	Carbohydrate phosphorylase. The members of this family catalyze the formation of glucose 1-phosphate from one of the following polyglucoses; glycogen, starch, glucan or maltodextrin.
COG0058	GlgP	4.83e-74	4	289	5	257	Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14986	PRK14986	9.19e-65	40	288	49	301	glycogen phosphorylase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ARC74881.1	1.42e-215	1	294	1	294
ARW44029.1	1.42e-215	1	294	1	294
BCE09882.1	7.23e-210	1	289	1	289
QII50341.1	2.20e-205	1	289	1	289
AOP16454.1	7.18e-204	1	290	1	290

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5IKO_A	2.69e-68	31	290	54	317	Crystalstructure of human brain glycogen phosphorylase [Homo sapiens],5IKP_A Crystal structure of human brain glycogen phosphorylase bound to AMP [Homo sapiens]
3CEH_A	3.31e-68	9	290	6	291	Humanliver glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE5688 [Homo sapiens],3CEH_B Human liver glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE5688 [Homo sapiens],3CEJ_A Human glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE2865 [Homo sapiens],3CEJ_B Human glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE2865 [Homo sapiens],3CEM_A Human glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE9423 [Homo sapiens],3CEM_B Human glycogen phosphorylase (tense state) in complex with the allosteric inhibitor AVE9423 [Homo sapiens]
1XOI_A	5.17e-68	9	290	28	313	HumanLiver Glycogen Phosphorylase A complexed with Chloroindoloyl glycine amide [Homo sapiens],1XOI_B Human Liver Glycogen Phosphorylase A complexed with Chloroindoloyl glycine amide [Homo sapiens]
1FC0_A	5.17e-68	9	290	28	313	HUMANLIVER GLYCOGEN PHOSPHORYLASE COMPLEXED WITH N-ACETYL-BETA-D-GLUCOPYRANOSYLAMINE [Homo sapiens],1FC0_B HUMAN LIVER GLYCOGEN PHOSPHORYLASE COMPLEXED WITH N-ACETYL-BETA-D-GLUCOPYRANOSYLAMINE [Homo sapiens],2ATI_A Glycogen Phosphorylase Inhibitors [Homo sapiens],2ATI_B Glycogen Phosphorylase Inhibitors [Homo sapiens]
1FA9_A	5.17e-68	9	290	28	313	HUMANLIVER GLYCOGEN PHOSPHORYLASE A COMPLEXED WITH AMP [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P39123	4.84e-151	1	289	1	289	Glycogen phosphorylase OS=Bacillus subtilis (strain 168) OX=224308 GN=glgP PE=2 SV=1
Q3B7M9	2.76e-71	31	290	51	314	Glycogen phosphorylase, brain form OS=Bos taurus OX=9913 GN=PYGB PE=2 SV=3
Q5MIB6	2.76e-71	31	290	51	314	Glycogen phosphorylase, brain form OS=Ovis aries OX=9940 GN=PYGB PE=2 SV=3
Q9PKE6	9.76e-70	6	288	11	302	Glycogen phosphorylase OS=Chlamydia muridarum (strain MoPn / Nigg) OX=243161 GN=glgP PE=3 SV=1
O84250	3.72e-68	6	288	11	302	Glycogen phosphorylase OS=Chlamydia trachomatis (strain D/UW-3/Cx) OX=272561 GN=glgP PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000028	0.000016	0.000001	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002357_03231.