CAZyme Information: MGYG000003184_00875

Basic Information

• Species: Mixta calida
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Mixta; Mixta calida
• CAZyme ID: MGYG000003184_00875
• CAZy Family: CBM48
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
728	MGYG000003184_4|CGC2	84202.66	6.2096

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003184	4133670	MAG	United States	North America

• Gene Location: Start: 126155; End: 128341 Strand: +

Full Sequence      

MSELPDRQAINAIIEGHYADPFSLLGMHQTSNGLEVRTLLPDASEVWVIETSTGRKCAQL
KCLDSRGFFHGVIPRRKNPFRYQLAVTWHGEQNLIDDAYRFGPLLQELDSWLLAEGTHLR
PYETLGAHAEVIDGISGTRFMVWAPNARRVSVVGDFNYWDGRRHPMRLRREIGVWELFVP
AARPGQLYKYEIIDNKGHLRLKSDPFAFESQMRPDSASVICGLPEKVAMREERKAANAFD
APISIYEVHLGSWRRHTDNNFWLSYKELEEQLIPYVKEMGFTHIELMPINEHPFDGSWGY
QPVGMYAPTRRFGTRDEFRHFVAAAHAAGLNVLLDWVPGHFPSDDFGLAQFDGTALYEHE
DPREGFHQDWNTLIYNYGRREVSNYLAGNALYWLERFGIDGLRVDAVASMIYRDYSRPEG
EWVPNHFGGRENLEAIDFLRYTNRMLGHTAPGTVTIAEESTDFPGVSRPPEGGGLGFWFK
WNLGWMHDTLDYMKLDPIYRRHHHNLMTFGMVYNHTENFVLPLSHDEVVHGKRSILDRMP
GDAWQKFANLRAYYGWMWAFPGKKLLFMGGEFAQGREWNHDASLDWHLLEGEDNWHNGVQ
RLVRDLNLTYRHHTPMHQCDFDAHGFEWLVVDDYDNSVFIFVRRDREGNEMIVASNFTPV
PRYNYCFGITQPGGWREVINTDSTHYHGSNIGNSGTVWSEPVPSHNREHSLSLTLPPLAT
IWLMREAE

Enzyme Prediction     

EC	2.4.1.18

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	274	574	6.3e-158	0.9966777408637874
CBM48	124	211	2.5e-21	0.9210526315789473

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK05402	PRK05402	0.0	5	728	1	726	1,4-alpha-glucan branching protein GlgB.
PRK14705	PRK14705	0.0	6	723	504	1220	glycogen branching enzyme; Provisional
PRK12313	PRK12313	0.0	102	723	4	625	1,4-alpha-glucan branching protein GlgB.
cd11322	AmyAc_Glg_BE	0.0	212	612	1	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.
COG0296	GlgB	0.0	100	725	1	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
AIX75592.1	0.0	1	728	1	728
QNU43734.1	0.0	1	728	1	728
AUY23751.1	0.0	1	728	1	728
AUX91928.1	0.0	1	728	1	728
QHM73452.1	0.0	1	728	1	728

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4LPC_A	0.0	117	728	1	612	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	0.0	112	728	1	617	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]
5GQW_A	5.77e-250	10	723	30	771	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	1.64e-249	10	723	30	771	Crystalstructure of branching enzyme W610A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142]
5GR1_A	1.64e-249	10	723	30	771	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q32AV3	0.0	1	728	1	728	1,4-alpha-glucan branching enzyme GlgB OS=Shigella dysenteriae serotype 1 (strain Sd197) OX=300267 GN=glgB PE=3 SV=1
Q5PM06	0.0	1	728	1	728	1,4-alpha-glucan branching enzyme GlgB OS=Salmonella paratyphi A (strain ATCC 9150 / SARB42) OX=295319 GN=glgB PE=3 SV=1
Q57IT8	0.0	1	728	1	728	1,4-alpha-glucan branching enzyme GlgB OS=Salmonella choleraesuis (strain SC-B67) OX=321314 GN=glgB PE=3 SV=1
Q3YW93	0.0	1	728	1	728	1,4-alpha-glucan branching enzyme GlgB OS=Shigella sonnei (strain Ss046) OX=300269 GN=glgB PE=3 SV=1
Q6CZK0	0.0	8	727	6	725	1,4-alpha-glucan branching enzyme GlgB OS=Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) OX=218491 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
1.000068	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003184_00875.