CAZyme Information: MGYG000001627_00108

Basic Information

• Species: Gemmiger sp900539695
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Gemmiger; Gemmiger sp900539695
• CAZyme ID: MGYG000001627_00108
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
591	MGYG000001627_1|CGC3	67311.45	5.0382

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001627	2528284	MAG	China	Asia

• Gene Location: Start: 114430; End: 116205 Strand: +

Full Sequence      

MNMQDFYTGHAFDAYEFFGAHTYFGGTHFAVWAPSAQHIAVETEVGTYDMHRTQSAVWEC
DVPGANAGMVYQYWVRGANGQTVAHCDPYGTAMTLRPDGRSIIADRPTGFTDDKWMAGRT
KCFDKPLNIYEVHAGSWRQKEDGSWYTYAELAELLPAYCKENGFTHIELMPLAEHPFDGS
WGYQITGFYAPTSRYGTPQQLAEFVNACHKEGIGVILDFVPVHFAIDSYGLKEFDGTPLY
EYPAAAVGQSEWGSCNFMHSRGEIRCFIQSCADYWLQVFHADGLRMDAVSRLIYWQGDPN
RGVNGSTLEFLKGMNQGLQQRHPTALLIAEDSTNYPKVTAPVEYGGLGFDYKWDLGWMND
TLDYFKKTSEERKENLGKLTFSMMYAWNEHYILPFSHDENVHGKATIVQKMYGDYAGKFP
QARALYLYMAIHPGKKLDFMGNEFAQLREFDESREQDWMVLDYPNHNDFRRFRQALNRAY
CAEDAFWRREYDPAAFQWLDCSHPELDACAILRQGSEAAVLAAFNFGDTELEDYTLTLPV
AGKLTLLLDTDWETFGGSTAAPKRSCARKTDGELKLTLPPFSGRLYRLEQA

Enzyme Prediction     

No EC number prediction in MGYG000001627_00108.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	158	446	1.8e-121	0.9933554817275747

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK05402	PRK05402	0.0	6	591	108	726	1,4-alpha-glucan branching protein GlgB.
TIGR01515	branching_enzym	0.0	6	582	5	613	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	6	591	15	630	1,4-alpha-glucan branching protein GlgB.
cd11322	AmyAc_Glg_BE	0.0	95	480	1	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.
COG0296	GlgB	0.0	6	588	14	628	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRT49649.1	6.20e-260	4	585	3	591
CBL24631.1	1.80e-237	1	589	1	594
AQP39749.1	7.11e-234	1	588	1	597
CBL37724.1	4.07e-233	1	588	1	597
QBF75938.1	6.63e-233	1	590	1	595

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4LPC_A	1.12e-138	15	582	6	603	CrystalStructure of E.Coli Branching Enzyme in complex with maltoheptaose [Escherichia coli],4LPC_B Crystal Structure of E.Coli Branching Enzyme in complex with maltoheptaose [Escherichia coli],4LPC_C Crystal Structure of E.Coli Branching Enzyme in complex with maltoheptaose [Escherichia coli],4LPC_D Crystal Structure of E.Coli Branching Enzyme in complex with maltoheptaose [Escherichia coli],4LQ1_A Crystal Structure of E.Coli Branching Enzyme in complex with maltohexaose [Escherichia coli],4LQ1_B Crystal Structure of E.Coli Branching Enzyme in complex with maltohexaose [Escherichia coli],4LQ1_C Crystal Structure of E.Coli Branching Enzyme in complex with maltohexaose [Escherichia coli],4LQ1_D Crystal Structure of E.Coli Branching Enzyme in complex with maltohexaose [Escherichia coli],5E6Y_A Crystal structure of E.Coli branching enzyme in complex with alpha cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Y_B Crystal structure of E.Coli branching enzyme in complex with alpha cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Y_C Crystal structure of E.Coli branching enzyme in complex with alpha cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Y_D Crystal structure of E.Coli branching enzyme in complex with alpha cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Z_A Crystal structure of Ecoli Branching Enzyme with beta cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Z_B Crystal structure of Ecoli Branching Enzyme with beta cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Z_C Crystal structure of Ecoli Branching Enzyme with beta cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Z_D Crystal structure of Ecoli Branching Enzyme with beta cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E70_A Crystal structure of Ecoli Branching Enzyme with gamma cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E70_B Crystal structure of Ecoli Branching Enzyme with gamma cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E70_C Crystal structure of Ecoli Branching Enzyme with gamma cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E70_D Crystal structure of Ecoli Branching Enzyme with gamma cyclodextrin [Escherichia coli O139:H28 str. E24377A]
1M7X_A	1.30e-138	15	582	11	608	TheX-ray Crystallographic Structure of Branching Enzyme [Escherichia coli],1M7X_B The X-ray Crystallographic Structure of Branching Enzyme [Escherichia coli],1M7X_C The X-ray Crystallographic Structure of Branching Enzyme [Escherichia coli],1M7X_D The X-ray Crystallographic Structure of Branching Enzyme [Escherichia coli]
6JOY_A	5.82e-138	8	589	14	619	TheX-ray Crystallographic Structure of Branching Enzyme from Rhodothermus obamensis STB05 [Rhodothermus marinus]
5GQW_A	9.83e-137	15	589	146	774	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	9.83e-137	15	589	146	774	Crystalstructure of branching enzyme W610A 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
Q8RF62	6.51e-166	6	564	13	579	1,4-alpha-glucan branching enzyme GlgB OS=Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355) OX=190304 GN=glgB PE=3 SV=1
Q65FS4	3.65e-158	6	587	14	617	1,4-alpha-glucan branching enzyme GlgB OS=Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) OX=279010 GN=glgB PE=3 SV=1
Q3SH78	7.24e-158	26	581	148	731	1,4-alpha-glucan branching enzyme GlgB OS=Thiobacillus denitrificans (strain ATCC 25259) OX=292415 GN=glgB PE=3 SV=1
P30537	3.47e-157	6	587	14	617	1,4-alpha-glucan branching enzyme GlgB OS=Bacillus caldolyticus OX=1394 GN=glgB PE=1 SV=1
Q632H1	3.19e-156	1	587	1	609	1,4-alpha-glucan branching enzyme GlgB OS=Bacillus cereus (strain ZK / E33L) OX=288681 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
1.000048	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001627_00108.