CAZyme Information: MGYG000001265_02874

Basic Information

• Species: Methylobacterium sp002778835
• Lineage: Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Beijerinckiaceae; Methylobacterium; Methylobacterium sp002778835
• CAZyme ID: MGYG000001265_02874
• CAZy Family: GH13
• CAZyme Description: 1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
345		38704.29	6.546

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001265	4213059	MAG	Italy	Europe

• Gene Location: Start: 54; End: 1091 Strand: +

Full Sequence      

MATFLAANARFWLEHYHLDGLRVDAVASMLYLDYSRRAGEWIPNQYGGNENLDAINFLRK
TNEATYSHAPGTITVAEESTSWPGVSHPTYTGGLGFGFKWNMGWMHDTLQFISKEPIHRR
YHHHDLTFGLLYAFSENFILPLSHDEVVHGKGSMLGKMPGDRWQKFANLRAYYGFMWGHP
GKKLLFMGGEFGQEREWNHNHSLDWHHLDDPLHRGVKDVIRDLNRLYTSTPALYARDTEG
AGFEWLVADDQDNSVIAWARKGTEPGQIAIVVSNFTPVPREGYRVGVPAAGWYREAFNSD
AEAYGGSNVGNHGGLGTDPTPSHGQAQSLSLTLPPLGTMIFVLQG

Enzyme Prediction     

EC	2.4.1.18

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	3	193	2.2e-100	0.6312292358803987

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK05402	PRK05402	0.0	4	345	384	725	1,4-alpha-glucan branching protein GlgB.
PRK12313	PRK12313	0.0	4	341	289	625	1,4-alpha-glucan branching protein GlgB.
TIGR01515	branching_enzym	1.38e-180	4	342	280	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]
PRK12568	PRK12568	6.00e-167	1	339	385	724	glycogen branching enzyme; Provisional
COG0296	GlgB	9.89e-162	4	341	283	626	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AWN38639.1	8.48e-243	1	344	414	757
AWN39286.1	2.19e-235	1	345	422	766
AYO81980.1	5.89e-234	1	344	417	760
APT30529.1	3.27e-233	1	345	416	760
AWV18004.1	4.63e-233	1	345	416	760

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JOY_A	1.63e-151	3	340	284	615	TheX-ray Crystallographic Structure of Branching Enzyme from Rhodothermus obamensis STB05 [Rhodothermus marinus]
4LPC_A	2.18e-144	1	345	266	611	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	2.53e-144	1	345	271	616	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	7.47e-133	3	343	433	773	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	1.17e-131	3	343	433	773	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
Q11EX1	5.33e-169	1	342	394	735	1,4-alpha-glucan branching enzyme GlgB OS=Chelativorans sp. (strain BNC1) OX=266779 GN=glgB PE=3 SV=1
Q2RR72	7.33e-167	3	345	393	734	1,4-alpha-glucan branching enzyme GlgB OS=Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1) OX=269796 GN=glgB PE=3 SV=1
Q2W2Q6	2.08e-166	1	341	396	736	1,4-alpha-glucan branching enzyme GlgB OS=Magnetospirillum magneticum (strain AMB-1 / ATCC 700264) OX=342108 GN=glgB PE=3 SV=1
Q1AZ86	3.43e-166	3	339	380	715	1,4-alpha-glucan branching enzyme GlgB OS=Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1) OX=266117 GN=glgB PE=3 SV=1
Q21M30	1.36e-164	3	345	388	729	1,4-alpha-glucan branching enzyme GlgB OS=Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024) OX=203122 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
1.000049	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001265_02874.