CAZyme Information: MGYG000002964_01925

Basic Information

• Species: Oscillibacter ruminantium
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; Oscillibacter; Oscillibacter ruminantium
• CAZyme ID: MGYG000002964_01925
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
652		74070.81	7.3609

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002964	2326356	MAG	United States	North America

• Gene Location: Start: 2484; End: 4442 Strand: -

Full Sequence      

MLFRSAVKNMARAEAPLGGEGESWVGFWPDLPQYTSYKYAVTGTDGKVRYKADPYGFHTE
TRPATASKLIDISGFSWTDEKFREKKGNRPVYTSPLNIYEVHLGSWRRPKDGGFYNYRAI
AKDLAAYVKDMGFNAVELLPITEHPLDDSWGYQCTGYFAPTSRYGTPADFMWFVDYMHKN
GVTVILDWVPAHFCKDEQGLYEFDGTCCYEYADPKKREHAGWGTRIFDYGRPEVVSFLLS
SARFWLEMYHIDGLRVDAVASMLYLDYDRPAGQWTPNKDGGRENLEAVEFLRSLNRMAFS
VDPSVLMVAEESTAWPLVTRPPESGGLGFNLKWNMGWMNDMCHYLKLDPYFRQFNHKDIT
FSMMYAFSENYVLPLSHDEVVHMKGSLVGKMPGDYENQLRSLRGFYAYLLAHPGKKLLFM
GPEIGQWHEWDAGGQLDWYLLDTEINRQTQMFFRAANRFYQKTPPLWEVDFQWQGFEWLV
PDDNHNNTVVFLRRDTKGRDLLCAVNFSPNAYADYRVGVPDHRRYVEGFNTDAMEFGGGG
YGNPEPVAVEAIPSHGREYSVALRIPPFGGVFLRGEGTAAAKKTTGKTTKRPTGKKTRPV
PQTVELSAEKAVKVPGKKPEKTAPQKAGGSTAEQERNPGKAAAKCAAARLEK

Enzyme Prediction     

EC	2.4.1.18

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	127	426	4.7e-150	0.9933554817275747

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11322	AmyAc_Glg_BE	0.0	62	462	2	402	Alpha amylase catalytic domain found in the Glycogen branching enzyme (also called 1,4-alpha-glucan branching enzyme). The glycogen branching enzyme catalyzes the third step of glycogen biosynthesis by the cleavage of an alpha-(1,4)-glucosidic linkage and the formation a new alpha-(1,6)-branch by subsequent transfer of cleaved oligosaccharide. They are part of a group called branching enzymes which catalyze the formation of alpha-1,6 branch points in either glycogen or starch. This group includes proteins from bacteria, eukaryotes, and archaea. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
TIGR01515	branching_enzym	0.0	24	574	67	618	alpha-1,4-glucan:alpha-1,4-glucan 6-glycosyltransferase. This model describes the glycogen branching enzymes which are responsible for the transfer of chains of approx. 7 alpha(1--4)-linked glucosyl residues to other similar chains (in new alpha(1--6) linkages) in the biosynthesis of glycogen. This enzyme is a member of the broader amylase family of starch hydrolases which fold as (beta/alpha)8 barrels, the so-called TIM-barrel structure. All of the sequences comprising the seed of this model have been experimentally characterized. This model encompasses both bacterial and eukaryotic species. No archaea have this enzyme, although Aquifex aolicus does. Two species, Bacillus thuringiensis and Clostridium perfringens have two sequences each which are annotated as amylases. These annotations are aparrently in error. GP|18143720 from C. perfringens, for instance, contains the note "674 aa, similar to gp:A14658_1 amylase (1,4-alpha-glucan branching enzyme (EC 2.4.1.18) ) from Bacillus thuringiensis (648 aa); 51.1% identity in 632 aa overlap." A branching enzyme from Porphyromonas gingivales, OMNI|PG1793, appears to be more closely related to the eukaryotic species (across a deep phylogenetic split) and may represent an instance of lateral transfer from this species' host. A sequence from Arabidopsis thaliana, GP|9294564, scores just above trusted, but appears either to contain corrupt sequence or, more likely, to be a pseudogene as some of the conserved catalytic residues common to the alpha amylase family are not conserved here. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
PRK14705	PRK14705	0.0	17	573	671	1220	glycogen branching enzyme; Provisional
PRK12313	PRK12313	0.0	24	574	76	626	1,4-alpha-glucan branching protein GlgB.
PRK14706	PRK14706	0.0	24	567	76	613	glycogen branching enzyme; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAL00803.1	0.0	16	649	71	681
QCI58888.1	0.0	15	578	61	624
QUO39422.1	0.0	15	578	61	624
BCK84469.1	0.0	17	577	63	621
QNL44653.1	0.0	16	585	55	620

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5GQW_A	1.41e-200	24	587	198	785	Crystalstructure of branching enzyme W610N mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142],5GQX_A Crystal structure of branching enzyme W610N mutant from Cyanothece sp. ATCC 51142 in complex with maltoheptaose [Crocosphaera subtropica ATCC 51142]
5GR5_A	1.41e-200	24	587	198	785	Crystalstructure of branching enzyme W610A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142]
5GR1_A	1.41e-200	24	587	198	785	Crystalstructure of branching enzyme Y500A/D501A mutant from Cyanothece sp. ATCC 51142 in complex with maltoheptaose [Crocosphaera subtropica ATCC 51142],5GR6_A Crystal structure of branching enzyme Y500A/D501A double mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142]
5GQZ_A	1.99e-200	24	587	198	785	Crystalstructure of branching enzyme Y500A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142]
5GR0_A	1.99e-200	24	587	198	785	Crystalstructure of branching enzyme D501A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B8CVY1	3.98e-212	24	574	76	626	1,4-alpha-glucan branching enzyme GlgB OS=Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562) OX=373903 GN=glgB PE=3 SV=1
Q8DLB8	6.70e-208	24	574	175	749	1,4-alpha-glucan branching enzyme GlgB OS=Thermosynechococcus vestitus (strain IAM M-273 / NIES-2133 / BP-1) OX=197221 GN=glgB PE=3 SV=1
Q1AZ86	3.81e-204	16	574	159	718	1,4-alpha-glucan branching enzyme GlgB OS=Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1) OX=266117 GN=glgB PE=3 SV=1
P30538	3.92e-204	24	574	76	617	1,4-alpha-glucan branching enzyme GlgB OS=Geobacillus stearothermophilus OX=1422 GN=glgB PE=1 SV=1
O66936	1.33e-202	35	577	89	630	1,4-alpha-glucan branching enzyme GlgB OS=Aquifex aeolicus (strain VF5) OX=224324 GN=glgB 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
1.000057	0.000002	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002964_01925.