CAZyme Information: MGYG000001483_01274

Basic Information

• Species: Arachnia massiliensis
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Propionibacteriales; Propionibacteriaceae; Arachnia; Arachnia massiliensis
• CAZyme ID: MGYG000001483_01274
• CAZy Family: GH13
• CAZyme Description: Glycogen debranching enzyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2109		226621.09	4.028

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001483	3211248	Isolate	not provided	not provided

• Gene Location: Start: 73425; End: 79754 Strand: -

Full Sequence      

MSRLRSRLFSGIAITALLATSGVVTAISPPAPAAAATESVTLVGDFQTELGCTEDWQATC
NATALTDADGDGVWTGEFTVPAGSYEFKVAINGTWDESYGMGDGNYPLSLAADATLEFAF
DDRTNKVSLDVAGLPGGYAEADDALVRAPFRDPGSGNTFYFVMTDRFDNGDPTNDACIAT
GHVGADGVLPVDCTGTDRLVTGFDATDKGFFNGGDVQGLRDRLDYIDGLGATAIWLTPSF
VNRPVQGTGADASAGYHGYWITDFTQIDPHLGTNAELKAFIAEAHAKGIKVYFDIIANHT
ADVIHYAGLEGTNPPYVSKAASPYKDVDGNEFDPSDYADGAQAMPLMHPDTRSFPYDPEI
PAGMEEAKFPLWLNDPTLYHNRGFDPSWPQGEPAVYMDFGDLDDLMTENQKVVDGMTEIY
KAWADFGIDGFRIDTVKHVDFVFWQEFTEAVSNHADDEFFMFGEVYDADARLLSPYVRDT
DMNSVLDFAYQSSAENFAKGFTTRGLSGLFAADDFYTTADSSAASLPTFLGNHDMGRIGF
RLSGADNTLQRSELAHELMFLTRGQPVVYYGDEQGFVGDGDDKDARENMFVSQVPSYLDN
VQIDGTPYGAGPHFDTAYPLYQHISALAELRHSTPALESGAQIELHSEAGAGVYAFSRVD
RTEKIEHLVALNNTTTAQEVSLTTLTDDASYAPLYGATEAVSSGSDGGLTLTVPALSAVV
YKADGTVTDAGDAQAITVTSAAPVNGLTPITADVADGRWAETSFAYRPVGSSSYTALGTA
ETDQPRVFADFGDLAAGTLVEVRAVSTDADGSKVAHSATVVVGTDLGAAAPEAGEIDWST
AVTVPGSHNAAMGCAGDWDPGCEEALLTLDETSGLYTGTFSLPAGSYEYKVAIGGNWDVN
YGVGSVPNGDNAAYTLDEATDVTFFYNPVTHLFFNTAQSPIVTLPGSHQAAVGCSGDWQP
ECLATLMFPNGDGTYTWSTTSLPAGSYEVKVAHGMSWDENYGAGGAPGGGNYTFTTAAQT
QVVFTYDIDTHLLEITVEDPPLAGTGSLLGHWIDAETIAWPTDLAPGDRSARTWELWTDP
DGGLALVDGVVTSDGAVKVGDLTLDADGLTADQLENRGHLSGFLALKLDADRAAVEAALT
GDLAVVQRNADGLAEVFTGLQVPGVLDDLCADAARAVDLGVTFTGDTPSLTLWAPTAKNV
TLLLHGDATGAGEPTRVAMTRDDSGLWSVDGEASWKNRAYRFDVEVFVPSLDEVTHNVVT
DPYSVGLTRNSTHSVLVDLDDPAWAPEIWTANEAPVIEQFADRTIYELHIRDFSVSDETV
PEELRGTYEAFALEGTDGVEALTELADAGMNTVHLLPSFDIATIEEDRSEQVHPVIPDAG
PASEEQQAAVTAVADQDAFNWGYDPYHYSTPEGSYASDENQEGGKRTSAFREMVGGLHGM
GLQVVLDKVYNHTAQSGQAEKSVLDKVVPGYYHRLSLTGTVETSTCCENVATEHEMAEQL
MVDSVVTWARDYHVDGFRFDLMGHHSRANMEAVRAALDELTLEADGVDGANMYLYGEGWN
FGEVADNARFHQATQGQLGGTGIGAFNDRLRDAVHGGGPFDSNKSEMQGFGTGLYTDPNG
VTTRSADEQLRDLRHRQDLVRIGMAGNLAEYSFETSAGTVQKGSELDYNGARAGYATEPH
ESVNYVDAHDNETLFDLGMWKLPSDSTMDTRVRMNTVSLATVALGQAPSFWHAGTDLLRS
KSMDRDSYNSGDHFNTLDWSMQTNNFGVGLPPAEKNSEQWDAMRQYLENPANTPTPQDIA
TSRARALELLELRSTYPLLTLGSADAITEKVTFPNAGADQTAGLILMHIDDTVGADVDPE
VDSLLVAINASPEAIVEEVDGLAGAELELSPILTEGDDADPVLATTAWDAASGTLTVPAR
SAVVLVQPQEEVVDPTPEPTVEPTVDPTVDPTEDPTTPPVKKYVRTAPYTMPGLHRNLNG
RDWHTECEPYSQTERCRTDIWATIVVIEDGQFVRKDGWAFNNLTYLPFMTREAWGANPLA
NDGEWTASTDARKWMTECDTARTGRDGCRSYAFVTVYKATAKPEGGYAFSQSNQWVFNNI
VMFGGPELR

Enzyme Prediction     

EC	3.2.1.41	3.2.1.1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	1342	1737	6.4e-154	0.9944598337950139
GH13	222	574	4.1e-70	0.997229916897507

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PLN02877	PLN02877	0.0	1037	1929	81	970	alpha-amylase/limit dextrinase
TIGR02103	pullul_strch	0.0	1051	1929	8	898	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]
cd11341	AmyAc_Pullulanase_LD-like	3.10e-158	1302	1765	2	392	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.
cd11339	AmyAc_bac_CMD_like_2	6.82e-127	156	631	2	341	Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. 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	8.35e-114	1178	1874	11	581	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QTO38012.1	0.0	6	2103	7	2104
AQP51326.1	0.0	7	2103	5	2117
AQP48047.1	0.0	6	1937	4	1949
QTE27420.1	0.0	2	1936	6	1935
QNP55861.1	0.0	4	1981	10	1970

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2Y4S_A	2.61e-199	1051	1929	9	883	BarleyLimit Dextrinase In Complex With Beta-Cyclodextrin [Hordeum vulgare],2Y5E_A BARLEY LIMIT DEXTRINASE IN COMPLEX WITH ALPHA-CYCLODEXTRIN [Hordeum vulgare],4AIO_A Crystal structure of the starch debranching enzyme barley limit dextrinase [Hordeum vulgare],4CVW_A Structure of the barley limit dextrinase-limit dextrinase inhibitor complex [Hordeum vulgare],4CVW_B Structure of the barley limit dextrinase-limit dextrinase inhibitor complex [Hordeum vulgare]
4J3S_A	4.99e-199	1051	1929	30	904	Crystalstructure of barley limit dextrinase soaked with 300mM maltotetraose [Hordeum vulgare],4J3T_A Crystal structure of barley Limit dextrinase co-crystallized with 25mM maltotetraose [Hordeum vulgare],4J3U_A Crystal structure of barley limit dextrinase in complex with maltosyl-S-betacyclodextrin [Hordeum vulgare],4J3U_B Crystal structure of barley limit dextrinase in complex with maltosyl-S-betacyclodextrin [Hordeum vulgare],4J3V_A Crystal structure of barley limit dextrinase in complex with a branched thio-linked hexasaccharide [Hordeum vulgare]
4J3W_A	3.60e-198	1051	1929	30	904	Crystalstructure of barley limit dextrinase (E510A mutant) in complex with a branched maltohexasaccharide [Hordeum vulgare],4J3X_A Crystal structure of barley limit dextrinase (E510A mutant) in complex with a branched maltoheptasaccharide [Hordeum vulgare]
6J33_A	4.46e-183	1051	1931	150	1042	ChainA, pullulanase [Klebsiella pneumoniae],6J33_B Chain B, pullulanase [Klebsiella pneumoniae],6J34_A Chain A, Pullulanase [Klebsiella pneumoniae]
6J35_A	1.15e-181	1051	1931	150	1042	ChainA, Pullulanase [Klebsiella pneumoniae],6J35_B Chain B, Pullulanase [Klebsiella pneumoniae],6J4H_A Chain A, Pullulanase [Klebsiella pneumoniae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q8GTR4	8.07e-188	1051	1927	91	961	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
P07206	4.42e-179	1051	1931	187	1079	Pullulanase OS=Klebsiella pneumoniae OX=573 GN=pulA PE=1 SV=2
Q05884	3.75e-173	190	811	75	701	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P07811	1.71e-159	1051	1929	198	1087	Pullulanase OS=Klebsiella aerogenes OX=548 GN=pulA PE=1 SV=1
O33840	2.88e-53	1165	1762	215	728	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2

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
0.001793	0.992819	0.000355	0.004440	0.000306	0.000263

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001483_01274.