CAZyme Information: MGYG000000039_01848

Basic Information

• Species: Faecalibacterium prausnitzii_H
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Faecalibacterium; Faecalibacterium prausnitzii_H
• CAZyme ID: MGYG000000039_01848
• CAZy Family: GT35
• CAZyme Description: Maltodextrin phosphorylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
753	MGYG000000039_10|CGC3	84431.16	5.1594

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000039	2848022	Isolate	United Kingdom	Europe

• Gene Location: Start: 82800; End: 85061 Strand: +

Full Sequence      

MNFTETLQNLTGKPLADCTNQELYLALLEVVRQKSANRIQPVTGRKLYYISAEFLIGKLL
SNNLINLGLYDEARNALAAAGKSLSDIEELEPEPSLGNGGLGRLAACFLDSLATLNLPGD
GVGLRYHFGLFHQSFENGMQNEKPDPWLTAHSWAEKTDITYPVELAGKEYTARLYKLAVT
GYEGRTNTLNLFDLDTIDESIVHDGIAFDKTAIDKNLTLFLYPDDSDEAGRRLRVYQQYL
MVSAGAQLILAECAARGCNYHDLADYAAIQINDTHPSMVIPELIRLLGEKGIEFEEAVEI
VTKTCAYTNHTILAEALEKWPRAYLDAVVPQLMPIIEKLDKLARTRTKDESLAIIDKDDR
VHMAHMDIHFTHSTNGVAALHTEILKNSELHGFYELYPEKFNNKTNGITFRRWLLECDPC
LTAELEQRIGSGFRKDAAELEKLLAFADDETVLNELTAVKKANKEALADWLLRTQNVKVN
TEAMFDIQSKRLHEYKRQQLNLLYLIHQYYEIKAGHLPAVPLVSIFGAKAAPAYTIAKDI
IHALLTLSKVIAADPEVSRWLQVVFVENYNVTAAEKLIPACDLSEQISLASKEASGTGNM
KFMLNGALTLGTMDGANVEISQQVGEENIYIFGQTSDQVIHRYAVGDYVAAQWYEGDPNL
RRAIDFLTGPEMLAAGHAENLTRLHDELIHKDWFQTLPDFNAYVVRKGQALSDYACDPMG
WRKKCLVNIAKAGMFSSDRTIAEYNRDIWHLGK

Enzyme Prediction     

EC	2.4.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT35	76	751	6.1e-222	0.9970326409495549

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK14986	PRK14986	0.0	45	751	70	810	glycogen phosphorylase; Provisional
COG0058	GlgP	0.0	2	753	12	750	Glucan phosphorylase [Carbohydrate transport and metabolism].
PRK14985	PRK14985	0.0	21	749	36	794	maltodextrin phosphorylase; Provisional
TIGR02093	P_ylase	0.0	3	751	1	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	751	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
CCG34911.1	0.0	1	753	1	753
AXB27758.1	0.0	1	753	1	753
CBL01526.1	0.0	1	753	1	753
ATL89620.1	0.0	1	753	1	753
QIA42218.1	0.0	1	753	1	753

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4L22_A	1.11e-310	3	750	8	756	Crystalstructure of putative glycogen phosphorylase from Streptococcus mutans [Streptococcus mutans UA159]
2C4M_A	2.82e-186	12	751	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]
5IKO_A	9.67e-176	19	749	51	829	Crystalstructure of human brain glycogen phosphorylase [Homo sapiens],5IKP_A Crystal structure of human brain glycogen phosphorylase bound to AMP [Homo sapiens]
5OX0_A	7.77e-174	2	749	31	826	GlycogenPhosphorylase in complex with CK898 [Oryctolagus cuniculus]
2GJ4_A	1.25e-173	2	749	19	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	751	2	751	Maltodextrin phosphorylase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=malP PE=3 SV=2
Q3B7M9	1.12e-179	19	749	48	826	Glycogen phosphorylase, brain form OS=Bos taurus OX=9913 GN=PYGB PE=2 SV=3
Q5MIB6	1.96e-177	19	749	48	826	Glycogen phosphorylase, brain form OS=Ovis aries OX=9940 GN=PYGB PE=2 SV=3
P53534	9.48e-177	19	749	48	826	Glycogen phosphorylase, brain form (Fragment) OS=Rattus norvegicus OX=10116 GN=Pygb PE=1 SV=3
Q8CI94	2.19e-176	19	749	48	826	Glycogen phosphorylase, brain form OS=Mus musculus OX=10090 GN=Pygb PE=1 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
1.000048	0.000011	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000039_01848.