CAZyme Information: MGYG000000664_00634

Basic Information

• Species: UBA733 sp900550795
• Lineage: Bacteria; Firmicutes; Bacilli; RFN20; CAG-826; UBA733; UBA733 sp900550795
• CAZyme ID: MGYG000000664_00634
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
652		76122.87	6.9227

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000664	1822500	MAG	Kazakhstan	Asia

• Gene Location: Start: 44217; End: 46175 Strand: -

Full Sequence      

MAYGLLYDYLMGQCINAYEYFGAHFVTKTIKRKKVNGVMFRLYAPMAEDVSVIGEWNGWD
VRVNKMDKVDPCGVFETFIPDLREYQSYKYHFKNAKGVYVDKADPFAFYSEFRPQTCSRL
YGIEGFPWDDNEYMSKRNRNFDEAMSIYEIHLGSWKGKIDGRYPSYEEVADYLIPYLQEN
GYTHVEIMPITQYPFDGSWGYQATGFYSVDSRYGNPKQLMSFVNRLHKAGFGVILDFAPV
HFATDSYALREFDGTCLYEYSDPNHTISPWGSAQFDLGKDPVRSFLMSAMNYFLEYFHFD
GLRIDAVSNIVYWDGDKSKGENTGATEFIRRLNGKLHYAHHSIMTIAEDSTDFTKVTHPI
EYGGLGFDYKWDLGWMNDTLKYYGLDPIYKKYHHNDLNFSMAYFFSENFLLPLSHDEVVH
GKGTIINKMWGDYETKFALLRNLYAYQFAHPGKKLNFMGNELASFDEWNENKSLPWNLLS
FPKHDSIKRLCRDLNLIYKYHIAMHKEEYNPAHFRWTMVDNSSQSVYAFERDFGDEVMLF
VFNMTPNYYDSYDVGTYQEGEFEEIFNSDKDVYGGYNNYNGDKKHTYPGGPEDRPYHINI
KLASFGACFFLLSKKDNSPIISKLKVAKKAKSTSKKTKTIKKTKKTSTKRSK

Enzyme Prediction     

EC	2.4.1.18

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	175	463	1.4e-123	0.9933554817275747

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11322	AmyAc_Glg_BE	0.0	113	499	2	401	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	18	607	23	623	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
PRK05402	PRK05402	0.0	6	615	105	726	1,4-alpha-glucan branching protein GlgB.
PRK12313	PRK12313	0.0	12	610	18	625	1,4-alpha-glucan branching protein GlgB.
TIGR01515	branching_enzym	0.0	18	606	14	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]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QOS39154.1	3.72e-255	8	609	8	602
QMW75175.1	7.26e-222	5	610	6	614
QPS14491.1	7.26e-222	5	610	6	614
QQV06374.1	7.26e-222	5	610	6	614
BBH27653.1	1.07e-220	9	616	10	620

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5GQW_A	3.00e-158	6	602	134	763	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]
1M7X_A	5.20e-158	12	602	5	604	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]
4LPC_A	8.87e-158	15	602	3	599	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]
5GR2_A	1.68e-157	6	602	134	763	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]
5GR1_A	4.71e-157	6	602	134	763	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
P30537	3.28e-180	6	606	11	612	1,4-alpha-glucan branching enzyme GlgB OS=Bacillus caldolyticus OX=1394 GN=glgB PE=1 SV=1
P30538	7.76e-180	6	617	11	623	1,4-alpha-glucan branching enzyme GlgB OS=Geobacillus stearothermophilus OX=1422 GN=glgB PE=1 SV=1
Q632H1	1.65e-178	17	606	14	604	1,4-alpha-glucan branching enzyme GlgB OS=Bacillus cereus (strain ZK / E33L) OX=288681 GN=glgB PE=3 SV=1
A7GUA1	3.03e-178	13	606	18	612	1,4-alpha-glucan branching enzyme GlgB OS=Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98) OX=315749 GN=glgB PE=3 SV=1
B9J2G8	8.57e-178	17	606	22	612	1,4-alpha-glucan branching enzyme GlgB OS=Bacillus cereus (strain Q1) OX=361100 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
1.000070	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000664_00634.