CAZyme Information: MGYG000002522_01345

Basic Information

• Species: Lachnoanaerobaculum umeaense
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnoanaerobaculum; Lachnoanaerobaculum umeaense
• CAZyme ID: MGYG000002522_01345
• CAZy Family: GT35
• CAZyme Description: Maltodextrin phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
752	MGYG000002522_1|CGC11	86545	5.0645

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002522	2810441	Isolate	Sweden	Europe

• Gene Location: Start: 1479924; End: 1482182 Strand: -

Full Sequence      

MSLEEMLKNKLGREIEVASDAEIYTALLNITKEKMEGMEHNAGNRKLYYISAEFLIGKLL
SNNMINLGIFDEVRDILAKNGHDITAVEEVEPEPSLGNGGLGRLAACFLDSIATLGLNGD
GVGLNYHDGLFLQKFIDKKQYEEKNPWITDNSWLTRTDVSFEVPFKDFTLRSTMYDIDIP
GYQQSKCNKLHLFDIDSVDESIIRDGINFDKHDIGKNLTLFLYPDDSDEAGHLLRIYQQY
FMVSNAAQLIIREAEGRGVDLYRLHEHVCVQINDTHPTMVIPELIRILTQQKGFNMDTAI
DVVRKTCAYTNHTILAEALEKWPISYLEKVVPQLLPIIYELDARIKREFSDERVYIIDNQ
SRVHMAHIDIHFGYAVNGVAALHTEILKNSELKPFYDIYPEKFNNKTNGITFRRWLVHCN
HELSEYLNELIGTDYMEDAANLSKLLDYKDDEKVLKKLREIKKDAKLELKKYLKHTQNID
IDENSVFDIQIKRLHEYKRQQMNALYAIYKYKEIKKGHLPKRPITMIFGAKAAPAYTIAK
DIIHLILCLQQLVENDSAVSPYLKIVMVENYNVTKAEKLIPACDISEQISLASKEASGTG
NMKFMLNGAVTLGTEDGANVEIHELVGDDNIYIFGKKSEDVIKLYETSSYRSADIYDNDP
EVEELVDFIISKELIRIGDPMNLCRLYKEIVNKDWFMALLDVKDYIKTKEQMLNDYEDEM
TWSKKALVNMAKAGFFSSDRTIAEYNNDIWHL

Enzyme Prediction     

EC	2.4.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT35	77	752	1.6e-224	0.9955489614243324

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK14986	PRK14986	0.0	45	752	70	810	glycogen phosphorylase; Provisional
COG0058	GlgP	0.0	2	752	12	748	Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985	PRK14985	0.0	40	750	54	794	maltodextrin phosphorylase; Provisional
TIGR02093	P_ylase	0.0	7	752	5	794	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]
cd04300	GT35_Glycogen_Phosphorylase	0.0	2	752	3	795	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AYA99648.1	0.0	1	752	1	752
QUI96245.1	0.0	1	752	1	752
QHB23533.1	0.0	3	752	5	753
QEI31025.1	0.0	3	752	5	753
QRT29815.1	0.0	3	752	5	753

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4L22_A	0.0	7	751	12	756	Crystalstructure of putative glycogen phosphorylase from Streptococcus mutans [Streptococcus mutans UA159]
2FFR_A	2.42e-170	11	750	28	814	Crystallographicstudies on N-azido-beta-D-glucopyranosylamine, an inhibitor of glycogen phosphorylase: comparison with N-acetyl-beta-D-glucopyranosylamine [Oryctolagus cuniculus]
1Z8D_A	2.81e-170	11	750	40	826	ChainA, Glycogen phosphorylase, muscle form [Homo sapiens]
2C4M_A	8.10e-170	12	752	22	788	Starchphosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control. [Corynebacterium callunae],2C4M_B Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control. [Corynebacterium callunae],2C4M_C Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control. [Corynebacterium callunae],2C4M_D Starch phosphorylase: structural studies explain oxyanion-dependent kinetic stability and regulatory control. [Corynebacterium callunae]
2GJ4_A	1.31e-169	11	750	28	814	Structureof rabbit muscle glycogen phosphorylase in complex with ligand [Oryctolagus cuniculus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P29849	0.0	1	752	2	751	Maltodextrin phosphorylase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=malP PE=3 SV=2
P11217	1.96e-170	11	750	40	826	Glycogen phosphorylase, muscle form OS=Homo sapiens OX=9606 GN=PYGM PE=1 SV=6
Q9XTL9	2.07e-170	11	750	40	826	Glycogen phosphorylase OS=Drosophila melanogaster OX=7227 GN=GlyP PE=2 SV=2
Q9WUB3	2.76e-170	11	750	40	826	Glycogen phosphorylase, muscle form OS=Mus musculus OX=10090 GN=Pygm PE=1 SV=3
O18751	1.09e-169	11	750	40	826	Glycogen phosphorylase, muscle form OS=Ovis aries OX=9940 GN=PYGM PE=2 SV=3

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
0.999655	0.000346	0.000029	0.000002	0.000001	0.000013

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002522_01345.