CAZyme Information: MGYG000002034_00933

Basic Information

• Species: CAG-170 sp900553545
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; CAG-170; CAG-170 sp900553545
• CAZyme ID: MGYG000002034_00933
• CAZy Family: CBM48
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
627	MGYG000002034_29|CGC1	72864.36	6.5037

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002034	1981843	MAG	China	Asia

• Gene Location: Start: 13648; End: 15531 Strand: +

Full Sequence      

MNKQLAAFLRQFESTGSPEADRYLGCHAVDEGFVFRVWAPRAQAVSVTGDFNFWNEEDLP
MHRLGSSGVWEAVSKFAKRGSAYKYCVTGANGSKVYKADPYANRAMPLPETSSVVDPPEK
FRWTDAAYRRNKLKQTSLQRPVNIYEVHAGSWKRHDDGSYLSYEELAAELIPYVKDMGYT
HIEFMPLMEYPYDPSWGYQVTGYYAPTHRYGSPEQLRMLVNACHAANIGVILDWVPAHFP
KDSYGLYEFDGTCCYELSDPAMREHPDWGTRIYDYAKPEVRSFLISNVCYWLREFHIDGI
RVDAVASMLYLDYNRPNYKPNRLGGRENLEAIAFLRQLNEEAFQADPTVMMIAEESTAFP
MITRPGYDGGLGFLYKWNMGWMNDMLKYMSLDPLYRKGSHNALTFAMTYAYSENFILPLS
HDEVVHGKCSLVNKMPGNYDDKFNNLRVFYAYQMAHPGKKLNFMGNEFAQFIEWNFTQGL
DWLLLDYDHHRQMREYVRMLNQFYLKHPAMWENDSDWNGFQWMSCDDRDCSVVAFRRISR
SGREVIAVFNFCPVLREDYPLPLPKAGWYEPVMNSDSSTWGGYGFEPVTVHAQRGKEGGH
WGQFRIPPMSAVYYLHRRTNPQRETEK

Enzyme Prediction     

EC	2.4.1.18

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	172	470	4.9e-151	0.9966777408637874
CBM48	24	105	1.3e-19	0.8947368421052632

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK14705	PRK14705	0.0	31	614	638	1220	glycogen branching enzyme; Provisional
PRK05402	PRK05402	0.0	22	619	118	726	1,4-alpha-glucan branching protein GlgB.
PRK14706	PRK14706	0.0	9	627	12	632	glycogen branching enzyme; Provisional
TIGR01515	branching_enzym	0.0	24	613	17	616	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	1	622	6	633	1,4-alpha-glucan branching protein GlgB.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBL01646.1	3.57e-254	12	614	20	631
AXB29737.1	7.35e-253	12	614	20	631
CBK98932.1	2.61e-248	12	627	20	649
AXA81819.1	1.00e-247	12	627	20	649
QNK41917.1	4.79e-247	1	584	10	595

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JOY_A	3.61e-199	9	584	9	583	TheX-ray Crystallographic Structure of Branching Enzyme from Rhodothermus obamensis STB05 [Rhodothermus marinus]
4LPC_A	4.77e-192	9	615	3	608	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	5.64e-192	9	615	8	613	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]
3K1D_A	4.48e-188	29	584	134	686	Crystalstructure of glycogen branching enzyme synonym: 1,4-alpha-D-glucan:1,4-alpha-D-GLUCAN 6-glucosyl-transferase from mycobacterium tuberculosis H37RV [Mycobacterium tuberculosis H37Rv]
5GQW_A	8.38e-184	24	601	149	746	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
Q30Z14	7.68e-218	22	612	32	633	1,4-alpha-glucan branching enzyme GlgB OS=Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20) OX=207559 GN=glgB PE=3 SV=1
A1VC54	1.86e-211	22	614	29	632	1,4-alpha-glucan branching enzyme GlgB OS=Desulfovibrio vulgaris subsp. vulgaris (strain DP4) OX=391774 GN=glgB PE=3 SV=1
Q729V5	7.49e-211	22	614	29	632	1,4-alpha-glucan branching enzyme GlgB OS=Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough) OX=882 GN=glgB PE=3 SV=1
B8CVY1	1.52e-210	23	614	25	625	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
Q2YB47	8.21e-208	19	616	129	736	1,4-alpha-glucan branching enzyme GlgB OS=Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71) OX=323848 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
1.000040	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002034_00933.