CAZyme Information: MGYG000000078_00999

Basic Information

• Species: Lachnospira rogosae_A
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnospira; Lachnospira rogosae_A
• CAZyme ID: MGYG000000078_00999
• CAZy Family: GH13
• CAZyme Description: Glycogen debranching enzyme

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1290		141869.44	4.5455

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000078	3032544	Isolate	United Kingdom	Europe

• Gene Location: Start: 103975; End: 107847 Strand: +

Full Sequence      

MKYLKKIIAVVLAAGMIISNAPVAGSAANQNSRASKRTYNWYDKCADDIDENYTYEGSDL
GIEATEDYTTFKIWAPSATYIKVNIYRKGVNDDDESSKVGSFTLEKMFANGNRDVWTGVW
TLTLIGDWRGFYYNYTISTTDITGAHDTKYQVADPYSIAVSADGKRSYIIDPDMVSPDGW
ENDKHIYVDTAKANNVYKVSIKDFSTDTSSGTTSNGKYSAFTEKGATVNNAGELSSGIDY
LKELGVTTVQLAPFSDYASDDEYVVANFNAPEPDYASDASNSEAIIKECKAMIQALHNAG
ISVVMEMPYTHTVTPTESVFEKVVPGYYYRHNTNGTYYTTTDYDNECATERAMYRKYVEN
SMKYWAEVYHIDGFSIDLVDCFDTKAYYSRLDKWLDEVKENVAKTDPRLVIWGDNYTKTD
RQNKTSIYDNIISSINGSTYGARNEKAIKMYKQQAAMKYATPGILYMDAGEEMCSSVEGT
TQQDKSVLEWQKCIDYTDVVSYYRGLMDIRKAFSPLADSQNISNNKEAYVLTNTTEGEWS
TMAVLNNDTADDKEIAIPASREAADWVIIANGESAGLVSLGEVSGSTVKVPAYTTMILVD
KESSLQVSVPEEKGRVIIDYLRTDGYGNSSFEIPLRESITLYGTVGTGFVVPQNLNISSY
YDLINAEYGKKGIFESGTIRLRYYYSAKYKPDRLVDGIINDGHYCEEVRFKVTDPAYTEV
RVDDKKLTPDSNGYYTVSYADKEQTIKLIDNNGCNVQLYIKVLENHIPNNNDCTKDSVCT
ICGKVFPAQASHKYSDSWSKDDTYHWKVCENDGCEVTSTKTEHSGTDDGDCTTPVICECG
QIVTAAKAEHTYGEWKSNGDGTHTRKCTIQGCTAEETKDCEGGEATCTKKAVCTYCNSEY
GALNPSNHSGSVEWVQTEGTHQKKYECCGAEYEAVESHKWENGHCSVCGYGCEHTGGEAT
CTEKAVCTICNLPYGKVDENNHTGTEECIKTTTTHEKKYTCCGKVTLAKENHKWKDGVCE
ICDYKCIHTGGEANYTSGAICENCGMEYTDKEPSKHTGNPEWVQTEDTHKKAYDCCGLEV
SAREEHIWEAGVCKICAYHCQHTGGEATCIQKAQCAICNEEYGTYNLGVHKGLKLVEAKA
ATKAEEGNIEYWHCEDCDRYYVEDNGYVEIQKADTVIAKIADNNNSNGAGSGDAGSNDTG
AGSGDVGSNDTGAGSGDAGSNGTGAGSGDVGSNDTGADSGSDGVNDTATEVKETPDTADN
NSIFVWLLMLSVGGMTVCMAISSKKRRTNG

Enzyme Prediction     

No EC number prediction in MGYG000000078_00999.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	238	452	7.5e-47	0.754325259515571

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
TIGR02104	pulA_typeI	1.83e-91	49	577	2	603	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.
cd11341	AmyAc_Pullulanase_LD-like	1.15e-63	196	510	5	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.
COG1523	PulA	3.10e-44	42	378	44	360	Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
PLN02877	PLN02877	3.45e-38	49	378	205	560	alpha-amylase/limit dextrinase
TIGR02102	pullulan_Gpos	4.32e-32	49	386	309	651	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 (.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ACR73263.1	0.0	1	1285	1	1387
QCT07748.1	6.48e-155	16	702	1	794
QCT05892.1	3.35e-107	4	803	1	906
APO32485.1	1.24e-99	23	620	4	688
QCT07019.1	3.07e-96	54	600	65	706

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7LSA_A	2.05e-159	1	686	1	793	ChainA, Pullulanase [Ruminococcus bromii]
7LST_A	8.60e-159	1	694	1	800	ChainA, Pullulanase [Ruminococcus bromii]
7LSU_A	2.29e-158	1	692	1	798	ChainA, Pullulanase [Ruminococcus bromii]
7LSR_A	3.02e-158	1	686	1	793	ChainA, Pullulanase [Ruminococcus bromii]
2WAN_A	1.42e-59	53	598	311	919	Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O33840	1.52e-46	48	598	214	840	Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0	8.78e-43	49	416	96	437	Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
Q8GTR4	1.63e-24	49	379	198	554	Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
A0A0H2ZL64	4.61e-24	50	416	427	794	Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
Q9F930	4.68e-24	50	416	449	816	Pullulanase A OS=Streptococcus pneumoniae OX=1313 GN=spuA 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
0.000273	0.999101	0.000198	0.000148	0.000138	0.000128

TMHMM  Annotations     

start	end
7	29
1262	1281