CAZyme Information: MGYG000002287_00099

Basic Information

• Species: Agathobaculum sp003481705
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Butyricicoccaceae; Agathobaculum; Agathobaculum sp003481705
• CAZyme ID: MGYG000002287_00099
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
753		86011.69	7.0928

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002287	2881212	Isolate	China	Asia

• Gene Location: Start: 109218; End: 111479 Strand: -

Full Sequence      

MRKKSASPAVEKRSELFYSGRDCRAYDYMGAHPFVQDGEQGYLFRVYAPEAANVSVMGEF
NGWNREADYMTRDEQGIWEKFIPNIAEYTAYKYSVWAKSGDVFDKSDPYGFHFETRPGNA
TKAYDIGGYEWGDDSWLQWRKNHLPYSSPVNIYECHLGSWKMHEDGNFYSYRQMADGLVP
YVKEMGYTHIEFMPLTEYPFDGSWGYQVIGYFAATSRYGTPKDLMYLIDKAHQAGLGVIM
DWVPAHFPKDGCGLVEFDGSHLYEYADPLKMEHKEWGTRVFDYGKVSTRNLLFSSAMFWI
EKFHMDGLRVDAVASMLYLDYNRQNEWRPNIHGGRENLEAVDFLRLLNEYILTDHPDVMM
IAEESTAWPMVTKPGYDGGLGFNFKWNMGWMNDMLCYCSADPFFRKDMHDKITFSFMYAF
SENYILPLSHDEVVHGKCSLIGKMPPPYENQFGGLRALYGYMAAHPGKKMLFMGGEFAQF
SEWAYQRGLDWMLLDYPAHRQMQAYVKALNHFYLETPQLWEQDTDWHGFEWISHEDNRNN
IIAFRRIAKDGSDIVVVVNFSPEEQSEYRIGVPIMGTYEEIFTSDKSEFGGSGITNGKVK
TDSKPLHGQEQSINIKIPRFGVLFFKGKPKAKRRTRAEIEAAKKLAEQEKQEKKPARRTA
AKTKAVTKKTKAEVAVKAKAEVAVKAKADVAVKGETSVVKTGTKAVARTGPKEVTVKGEK
AVAVKGEKAVAIKGEKAVAVKSETAVTTIKEDK

Enzyme Prediction     

EC	2.4.1.18

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	180	479	5e-149	0.9966777408637874

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK14706	PRK14706	0.0	29	626	27	620	glycogen branching enzyme; Provisional
cd11322	AmyAc_Glg_BE	0.0	116	515	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	16	626	4	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]
PRK05402	PRK05402	0.0	16	630	107	726	1,4-alpha-glucan branching protein GlgB.
PRK14705	PRK14705	0.0	16	626	610	1221	glycogen branching enzyme; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAB1243441.1	1.43e-281	1	638	1	641
BCI60003.1	5.58e-279	16	626	15	629
QEY35933.1	1.39e-275	16	635	14	636
QNK41917.1	3.74e-274	1	637	1	637
ATL90043.1	3.74e-274	16	643	19	646

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5GQW_A	1.88e-220	16	629	136	775	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	2.66e-220	16	629	136	775	Crystalstructure of branching enzyme W610A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142]
5GQU_A	3.77e-220	16	629	136	775	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]
5GR2_A	1.07e-219	16	629	136	775	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]
6KLF_A	1.75e-219	16	629	112	751	ChainA, 1,4-alpha-glucan branching enzyme GlgB [Crocosphaera subtropica ATCC 51142]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8DLB8	1.02e-239	16	626	113	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
Q2JT08	8.66e-237	16	629	124	755	1,4-alpha-glucan branching enzyme GlgB OS=Synechococcus sp. (strain JA-3-3Ab) OX=321327 GN=glgB PE=3 SV=1
B8CVY1	1.33e-236	16	626	13	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
Q2JK68	1.11e-235	16	629	124	755	1,4-alpha-glucan branching enzyme GlgB OS=Synechococcus sp. (strain JA-2-3B'a(2-13)) OX=321332 GN=glgB PE=3 SV=1
Q5N4W5	9.09e-235	16	618	122	750	1,4-alpha-glucan branching enzyme GlgB OS=Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) OX=269084 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
1.000043	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002287_00099.