CAZyme Information: PV07_05958-t44_1-p1

Basic Information

• Species: Cladophialophora immunda
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Cladophialophora; Cladophialophora immunda
• CAZyme ID: PV07_05958-t44_1-p1
• CAZy Family: GH17
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
632	KN847042.1|CGC22	71433.98	5.1656

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CimmundaCBS83496	12879	N/A	49	12830

• Gene Location: location=KN847042.1:4466049-4467947(-)

Full Sequence      

MAAEINLQEVGAHPSFERPNRFSVQIGLYLPGIRHADGFQVVVRIIHRDDRFNQTVSPQD
FDLDWVDGSALDHWTKSIPITPVSGTHYGTEGVYLYRFQLWFTPGGGSRQLVTRWFTDPF
ARATDVGSLAAFTLSRSPTTFAWNDGSYKTPQLDDLVVYELQVEEFNDTFDGVAERLDYF
RSLGVNCLELMPVTSTKLDFDWGYGPLHYFAPNARFGGPDGLKRLVDACHKADIAVILDV
VYQHVDPSFPYKLVYQDVKDFPGTPQIDSPMIGGDGPFGPQIAFSKTFAQDYFACANRRW
LEEYHVDGFRYDEVTDLFVSPTDSGYAKLCYDTYQCSTRIDRFRREAGSYSRIIQCAEAL
SKAREVLRGTYTSCAWQDDLLNKSESMIRNNVADADFAHFLDPNFCQYPSTKTVEDANGK
SAEMPVAPFQYLETHDHSQLIVFAGTTGGGSYPSGDRSKFYKLQPFAVALYTLQGVPMLW
QGQEFADNYQLPKSGDERVGLRRDTHWEFFYDEVGSTLVRLYRRLGMLRRTYPALRSRDS
FFYFRQSLQGTQIVAYHRHAGPTSTAPEQFVMVLLNFADAAGSITLPFPKAGTWTEMIDA
DTRTLTVQVPVDGAEVSTDVPSHYGHVFVWAG

Enzyme Prediction     

No EC number prediction in PV07_05958-t44_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	168	486	5.1e-45	0.9840255591054313

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200488	AmyAc_4	9.25e-112	141	539	1	390	Alpha amylase catalytic domain found in an uncharacterized protein family. 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 (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.
223373	GlgB	2.85e-59	94	627	86	616	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
200464	AmyAc_GTHase	1.21e-53	138	531	20	435	Alpha amylase catalytic domain found in Glycosyltrehalose trehalohydrolase (also called Maltooligosyl trehalose Trehalohydrolase). Glycosyltrehalose trehalohydrolase (GTHase) was discovered as part of a coupled system for the production of trehalose from soluble starch. In the first half of the reaction, glycosyltrehalose synthase (GTSase), an intramolecular glycosyl transferase, converts the glycosidic bond between the last two glucose residues of amylose from an alpha-1,4 bond to an alpha-1,1 bond, making a non-reducing glycosyl trehaloside. In the second half of the reaction, GTHase cleaves the alpha-1,4 glycosidic bond adjacent to the trehalose moiety to release trehalose and malto-oligosaccharide. Like isoamylase and other glycosidases that recognize branched oligosaccharides, GTHase contains an N-terminal extension and does not have the conserved calcium ion present in other alpha amylase family enzymes. 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. Glycosyltrehalose Trehalohydrolase Maltooligosyltrehalose Trehalohydrolase
235445	PRK05402	5.77e-28	117	314	198	406	1,4-alpha-glucan branching protein GlgB.
200465	AmyAc_Glg_debranch	2.11e-27	141	312	1	204	Alpha amylase catalytic domain found in glycogen debranching enzymes. Debranching enzymes facilitate the breakdown of glycogen through glucosyltransferase and glucosidase activity. These activities are performed by a single enzyme in mammals, yeast, and some bacteria, but by two distinct enzymes in Escherichia coli and other bacteria. Debranching enzymes perform two activities: 4-alpha-D-glucanotransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33). 4-alpha-D-glucanotransferase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Amylo-alpha-1,6-glucosidase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. In Escherichia coli, GlgX is the debranching enzyme and malQ is the 4-alpha-glucanotransferase. TreX, an archaeal glycogen-debranching enzyme has dual activities like mammals and yeast, but is structurally similar to GlgX. TreX exists in two oligomeric states, a dimer and tetramer. Isoamylase (EC 3.2.1.68) is one of the starch-debranching enzymes that catalyzes the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen and their beta-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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAC91529.1|GH13	3.99e-215	4	632	31	653
UFP95017.1|GH13	2.09e-211	5	629	1	615
QEG41390.1|GH13	7.58e-197	5	628	2	617
UFH53132.1|GH13	1.72e-180	5	628	2	611
QOD05020.1|GH13	7.52e-178	5	628	3	624

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2BHU_A	2.04e-24	140	539	111	531	Crystal structure of Deinococcus radiodurans maltooligosyltrehalose trehalohydrolase [Deinococcus radiodurans]
1EH9_A	2.95e-24	154	487	100	421	Crystal Structure Of Sulfolobus Solfataricus Glycosyltrehalose Trehalohydrolase [Saccharolobus solfataricus],3VGB_A Crystal structure of glycosyltrehalose trehalohydrolase (GTHase) from Sulfolobus solfataricus KM1 [Saccharolobus solfataricus]
3VGG_A	2.95e-24	154	487	100	421	Crystal structure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltoheptaose [Saccharolobus solfataricus],3VGH_A Crystal structure of glycosyltrehalose trehalohydrolase (E283Q) complexed with maltotriosyltrehalose [Saccharolobus solfataricus]
1EHA_A	3.94e-24	154	314	100	254	CRYSTAL STRUCTURE OF GLYCOSYLTREHALOSE TREHALOHYDROLASE FROM SULFOLOBUS SOLFATARICUS [Saccharolobus solfataricus]
3VGE_A	9.31e-24	154	487	100	421	Crystal structure of glycosyltrehalose trehalohydrolase (D252S) [Saccharolobus solfataricus],3VGF_A Crystal structure of glycosyltrehalose trehalohydrolase (D252S) complexed with maltotriosyltrehalose [Saccharolobus solfataricus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q4V0E2|GLGB1_XANC8	2.98e-27	118	626	200	704	1,4-alpha-glucan branching enzyme GlgB 1 OS=Xanthomonas campestris pv. campestris (strain 8004) OX=314565 GN=glgB1 PE=3 SV=1
sp|Q8PE48|GLGB1_XANCP	2.98e-27	118	626	200	704	1,4-alpha-glucan branching enzyme GlgB 1 OS=Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) OX=190485 GN=glgB1 PE=3 SV=1
sp|Q8PR13|GLGB1_XANAC	1.64e-26	118	626	200	704	1,4-alpha-glucan branching enzyme GlgB 1 OS=Xanthomonas axonopodis pv. citri (strain 306) OX=190486 GN=glgB1 PE=3 SV=1
sp|Q2P949|GLGB2_XANOM	1.67e-26	118	626	207	711	1,4-alpha-glucan branching enzyme GlgB 2 OS=Xanthomonas oryzae pv. oryzae (strain MAFF 311018) OX=342109 GN=glgB2 PE=3 SV=1
sp|Q5H6H2|GLGB1_XANOR	3.93e-26	118	626	208	712	1,4-alpha-glucan branching enzyme GlgB 1 OS=Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85) OX=291331 GN=glgB1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000050	0.000002

TMHMM  Annotations     

There is no transmembrane helices in PV07_05958-t44_1-p1.