CAZyme Information: MGYG000000313_01069

Basic Information

• Species: Collinsella vaginalis
• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella; Collinsella vaginalis
• CAZyme ID: MGYG000000313_01069
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
538		60104.84	6.2583

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000313	1450348	MAG	Sweden	Europe

• Gene Location: Start: 92; End: 1708 Strand: +

Full Sequence      

MPLNIYEVHLGSWRRHGDEPQGEPLPDGTYPGPGDPFPAQRGTPLSYEELSRELVVYVVE
MGYTHIEIMPLNEHPFDGSWGYQATGYFAATSRYGTPQQLMTLIDACHAAGVGVIMDWVP
GHFCADAQGLSSFNGHMLYEREIHPNWGTHKVDFGRGEVVSFFTSNALFWTDVFHVDGIR
VDGVSSMLYLNFGVDDAGAKKFNHLGTEEDLDASAFLRGVNTAMGAAHPDVLMIAEESTA
WPLVTYPHADGGLGFHLKWDMGWMNDTLHYMQTDFPWRPGNHGLLTFSIMYAFNENFVLP
LSHDEVVNGKCSLIQRMPGDQWRQFAGLRSLFLYQMTHPGAKLSFMGNEIGQYIEWRYYE
SIQWFLADEFPLHEGQRTFMRELNRLYAAEPALWERAYEQGGFEWVDPDDAERSIISFIR
HGARAEDDLLVIINLTPAYYERFPVGVPAAGSWKEIFNSDAGRFGGSGKVNPRALRSRAG
EVNGRENSISPSLPPLAGVIFKRTSPRGASAKAAKGAAKAKPAAKKQKKAAAPKKRKS

Enzyme Prediction     

EC	2.4.1.18

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	57	352	3.3e-131	0.9933554817275747

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11322	AmyAc_Glg_BE	0.0	2	387	35	400	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.
PRK05402	PRK05402	0.0	2	503	241	723	1,4-alpha-glucan branching protein GlgB.
COG0296	GlgB	0.0	2	503	144	628	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
TIGR01515	branching_enzym	0.0	2	502	138	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]
PRK12313	PRK12313	0.0	2	502	147	626	1,4-alpha-glucan branching protein GlgB.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QWT17135.1	2.65e-294	2	477	156	631
ATP53564.1	2.95e-277	2	506	171	677
AZH69616.1	1.89e-275	2	506	171	677
QIA34706.1	3.08e-275	2	506	170	676
QOY61640.1	4.87e-273	2	522	198	718

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5GQZ_A	3.18e-160	2	502	270	772	Crystalstructure of branching enzyme Y500A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142]
5GQU_A	2.52e-159	2	502	270	772	Crystalstructure of branching enzyme from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142],5GQV_A Crystal structure of branching enzyme from Cyanothece sp. ATCC 51142 in complex with maltohexaose [Crocosphaera subtropica ATCC 51142],5GQY_A Crystal structure of branching enzyme from Cyanothece sp. ATCC 51142 in complex with maltoheptaose [Crocosphaera subtropica ATCC 51142]
5GR1_A	5.04e-159	2	502	270	772	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]
5GR2_A	7.11e-159	2	502	270	772	Crystalstructure of branching enzyme L541A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142],5GR4_A Crystal structure of branching enzyme L541A mutant from Cyanothece sp. ATCC 51142 in complex with maltoheptaose [Crocosphaera subtropica ATCC 51142]
5GQW_A	1.00e-158	2	502	270	772	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B8CVY1	9.96e-180	2	502	147	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
Q24VW3	1.06e-179	1	502	152	628	1,4-alpha-glucan branching enzyme GlgB OS=Desulfitobacterium hafniense (strain Y51) OX=138119 GN=glgB PE=3 SV=1
Q5NXV7	3.02e-172	2	501	147	624	1,4-alpha-glucan branching enzyme GlgB OS=Aromatoleum aromaticum (strain EbN1) OX=76114 GN=glgB PE=3 SV=1
Q8CZE8	1.84e-168	2	502	145	626	1,4-alpha-glucan branching enzyme GlgB OS=Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831) OX=221109 GN=glgB PE=3 SV=1
A1U0K1	3.93e-166	2	502	147	628	1,4-alpha-glucan branching enzyme GlgB OS=Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) OX=351348 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
1.000035	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000313_01069.