CAZyme Information: MGYG000001549_02463

Basic Information

• Species: Gracilibacillus phocaeensis
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales_D; Amphibacillaceae; Gracilibacillus; Gracilibacillus phocaeensis
• CAZyme ID: MGYG000001549_02463
• CAZy Family: CBM41
• CAZyme Description: Glycogen debranching enzyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1994	MGYG000001549_12|CGC5	225136.27	3.8573

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001549	4547476	Isolate	not provided	not provided

• Gene Location: Start: 175673; End: 181657 Strand: +

Full Sequence      

MKKQKRQYVMVRMMVIVMLFSLFAGIQPISDVQADEITEENVLRIHYDYGDDSVTDIGAW
LWGDVTTPSETTGEWPDGVWFEEDKTNDYGAYIDVEVMEEAEEVQLLINNRNGDELTEEI
TIEILSDQMQEVWLTNDGEVYYYEPMELEDNSIRIHYQTEGESYEPWGVWTWDDVLQPSD
EWPTDAHPFSDEQTGPYGAYVDIPLKDNPGSIGFLLVERIENGAQTNDFHFAELDKHRQI
FLKADSEEVYTNPYYVSDQVEEEIPEETEGKQDIKVSASVNRAFTYNDHAVLEVNINNQS
DLGIRQIYADTSALGGKERLEISPELNEVTLSASYHIEPGEKDIPVTVVDEAGGTYKTSV
TATVDAREIGEGTTDWDESIIYFMLTDRFYDGNSANNDPYDLGYQDYDNPRGTYQGGDFK
GVTEKLDYLAELGVNTIWITPIVENIGHDVNYNESQGSYFAYHGYWAKNFEELNPHLGTV
EEFHELIDAAAARNIDIMADVVLNHPGYGLKSVDALGENAPGGYPTSEDRLRFEDMLRES
SGSGDLTTELSGLPDFLTEEAAVREQMVEWQSNWVEKSTTPNGNSLASYRVDTVKHVDDT
TWQHFRNELTKKEPEFQLIGESWGAGQSNDHGYLQTGTMNSLLDFEFKGTANNFVNGNLE
SANQTLIERNQNMDNTSLLGQFLSSHDEDGFLYQLDGDEGKAMIAASLQITAKGQPVIYY
GEELGQSGANNWPEYDNRYDFAWDEVEGNEMLAHYQELVSFRNDHSDIMAKGERQQVAGS
DEEQFILVERSFQGKSAYVAFNTADTTKQVSLTVDNEETEIVDHYQDQTYEAERNEAGEF
EVFIDIPAMEDGGTVLLTANNGNIVDGEEGEEQPEGRDIPDNHLRVHFPEDGADFDGLGL
WLWEDVATPSESAGSWPDAALSFEEQNQTEYGRYIDVELAENPNEVGLLINHSNGDNLSG
DIFVQMLSPEMNEVWLNKDYEVFYYEPLEKENSLRVNFYQTAESYDPFGLWTWGDVAEPT
EDWPDGAHSFADDRQGMKGSYYDLPLTNEAEQIDFLLMNKETEWQSEELSFDQLEQHTQI
FVQKDDPMIYTNPYFVSQDGLVSAEVLSDQEIELKYTSVQGFTEAQLLEDITVLTSEEQE
VEMNSVTIIEDDNTVLLNGSFDLDQAPFTIQHNGREVIASIGWRLKDNMYGYEGDLGLEV
HDSSNATLKVWSPSADNVFVVLYDKDDAKQVIKDDLEMTRSEQGVWEVELNKETTGLDDM
IGYYYHFAIEREGETALTLDPYAKSMAAWNSNDAEANIGKAAIVDPSSLGPTLDYASIDG
FEKREDAIIYETHVRDFTSDPSIDDELEAQFGTFASFVEKLDYIEDLGVTHIQLLPVMSY
FHANEMNKDDRLLDWESTDTNYNWGYDPQSYFSLTGMYSENPEDPEKRIEEFKNLVDEIH
KRDMGVVLDVVYNHTAQLHILEDLEPNYYHFMDADGTPRESFGGGRLGTTHQMARRILVD
SITYWVDEYKVDGFRFDMMGDHDAESIQMAYDEAKELNPNVVMIGEGWVTYVGDENNPDV
QPADQSWMEDTTSVGSFSDDFRNELKSGFGSEGEPRFITGGARDINRIFENLTANPGNFT
ADDPGDVVPYIAAHDNLTLHDVIAQSIKKDPKDHAEEIHQRIRLGNLMVLTAQGTPFIHA
GQEYGRTKQFRHEDFKGEVTEPPYKSTYLTDKDGNPFEYPYFIHDSYDSTDAINQFDWQK
ATNTEAYPTETTTRDYTKGLIELRRSTDAFRHGTMEDVHDKVSLLDIPEIDNEDLVIAYR
SEDSAGKEEYFIFVNADDQTRSLTLSEDLTNGEIIVDQETAGMNVIEEPTGVTLSEHSIE
IEPLSAIVIRVAEQDDDSDNEDSTGGDDGSNGEDDSDGHDDSHGEEDGSGGNDDSDGDNG
TNGNDDPDGDDGSNENGGTESNSNKDTDANNDSKNGSLPDTATSTFNWIITGLLFVLLGF
VIVYFELRRKVEKE

Enzyme Prediction     

EC	3.2.1.41	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	1352	1687	9.5e-123	0.9964788732394366
GH13	417	729	3e-112	0.9931972789115646
CBM41	151	254	2.8e-24	0.9901960784313726
CBM41	882	987	3.7e-21	0.9803921568627451
CBM41	992	1094	3.5e-20	0.9901960784313726

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02102	pullulan_Gpos	0.0	879	1989	1	1110	pullulanase, extracellular, Gram-positive. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. In contrast, a glycogen debranching enzyme such GlgX, homologous to this family, can release glucose at alpha,1-6 linkages from glycogen first subjected to limit degradation by phosphorylase. Characterized members of this family include a surface-located pullulanase from Streptococcus pneumoniae () and an extracellular bifunctional amylase/pullulanase with C-terminal pullulanase activity (.
COG1523	PulA	2.60e-168	1146	1872	22	692	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
cd11341	AmyAc_Pullulanase_LD-like	2.44e-151	1325	1764	1	406	Alpha amylase catalytic domain found in Pullulanase (also called dextrinase; alpha-dextrin endo-1,6-alpha glucosidase), limit dextrinase, and related proteins. Pullulanase is an enzyme with action similar to that of isoamylase; it cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. Pullulanases are very similar to limit dextrinases, although they differ in their action on glycogen and the rate of hydrolysis of limit dextrins. 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.
TIGR02104	pulA_typeI	1.35e-130	1187	1845	3	605	pullulanase, type I. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. This family consists of pullulanases related to the subfamilies described in TIGR02102 and TIGR02103 but having a different domain architecture with shorter sequences. Members are called type I pullulanases.
TIGR02103	pullul_strch	2.85e-74	1187	1786	116	804	alpha-1,6-glucosidases, pullulanase-type. Members of this protein family include secreted (or membrane-anchored) pullulanases of Gram-negative bacteria and pullulanase-type starch debranching enzymes of plants. Both enzymes hydrolyze alpha-1,6 glycosidic linkages. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. This family is closely homologous to, but architecturally different from, the Gram-positive pullulanases of Gram-positive bacteria (TIGR02102). [Energy metabolism, Biosynthesis and degradation of polysaccharides]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGH37050.1	0.0	18	1882	1	1869
BAM47868.1	0.0	14	1873	15	1871
ADH98514.1	0.0	2	1875	4	1876
AOM81713.1	0.0	12	1875	12	1871
QFQ60721.1	0.0	13	1885	12	1887

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2YA1_A	0.0	881	1873	6	1013	Productcomplex of a multi-modular glycogen-degrading pneumococcal virulence factor SpuA [Streptococcus pneumoniae TIGR4]
2YA0_A	4.51e-280	1183	1873	2	706	CatalyticModule of the Multi-modular glycogen-degrading pneumococcal virulence factor SpuA [Streptococcus pneumoniae TIGR4]
2YA2_A	2.00e-279	1183	1873	3	707	CatalyticModule of the Multi-modular glycogen-degrading pneumococcal virulence factor SpuA in complex with an inhibitor. [Streptococcus pneumoniae TIGR4]
3FAW_A	9.62e-278	1071	1871	10	813	CrystalStructure of the Group B Streptococcus Pullulanase SAP [Streptococcus agalactiae COH1],3FAX_A The crystal structure of GBS pullulanase SAP in complex with maltotetraose [Streptococcus agalactiae COH1]
6JEQ_A	1.49e-70	1187	1778	31	572	Crystalstructure of Pullulanase from Paenibacillus barengoltzii complex with beta-cyclodextrin [Paenibacillus barengoltzii],6JFJ_A Crystal structure of Pullulanase from Paenibacillus barengoltzii complex with maltohexaose and alpha-cyclodextrin [Paenibacillus barengoltzii],6JFX_A Crystal structure of Pullulanase from Paenibacillus barengoltzii complex with maltopentaose [Paenibacillus barengoltzii],6JHF_A Crystal structure of apo Pullulanase from Paenibacillus barengoltzii [Paenibacillus barengoltzii],6JHG_A Crystal structure of apo Pullulanase from Paenibacillus barengoltzii in space group P212121 [Paenibacillus barengoltzii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A0A0H2ZL64	0.0	879	1873	118	1127	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
A0A0H2UNG0	0.0	879	1873	133	1142	Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
Q9F930	0.0	879	1873	140	1149	Pullulanase A OS=Streptococcus pneumoniae OX=1313 GN=spuA PE=1 SV=1
O33840	3.91e-69	991	1869	20	840	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	8.60e-69	1187	1803	97	647	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000449	0.996683	0.002285	0.000212	0.000188	0.000160

TMHMM  Annotations     

start	end
9	26
1965	1987