CAZyme Information: MGYG000003072_02879

Basic Information

• Species: Paenibacillus amylolyticus
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus amylolyticus
• CAZyme ID: MGYG000003072_02879
• CAZy Family: CBM66
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1733	MGYG000003072_11|CGC1	186859.25	4.4288

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003072	7042795	MAG	China	Asia

• Gene Location: Start: 13366; End: 18567 Strand: -

Full Sequence      

MIFMLSATLALSSGPLMLPSKAYADLSSIPATLLQDDFSDGNFTESPAWNVSSGNWEVFA
DPTDASNFTLFQSDTNEGIISTGDSMSDMTVSMRFYTGAGQGYPGILPRFQDKSNFYYFQ
MQVPNNKLVFSKRVNGSDTTLKTVDYAFAKDTWYTLKVVLSGTTIRGYIAENGSDRLVFD
LVDPTYGSGTVGIRNKWQSVHADDVTIAEQPPGNDIQLSIAEQTASSVSLQWSEIAGASA
YRLYRSSTPEGGYSLVTSTGTLEHMDEGLSGDTVYYYRLAYEYGGLTESLWTAPLEVRTT
ASAPQAPGELKAEALNATSVKLSWSAVDKSTGYRVVRAEASSEQYEQIYEGKGLTFTDNA
LEPGNSYSYRVTAYNVAGESAATVAEATTYSIDSPAEFVATAVTDTSISLGWNVLPGSDV
TYIVSRSTSATGTYQQVYSGNENTFNDSGLTMGTGYFYIIQATVDGVTSPASAPLGVATV
RTSITPGQLWPDLDGKPIDAHGAGFFYDEQTETYYWYGEYHKGGWPAVGVRVYSSKDLMN
WTDGGMALTTLQSMDDFDNDSLISKLYAGREDRVDIWADIRKGRIIERPKVIYNDKTQKY
VMWAHMDGDKDPYNDNANYGKARAGYAISDSPTGPFVYQKSYRMDRAPEGEKDFFPSDRG
MARDMTLFKDDDGTGYLIYSSEENLTLYISKLNEDYSDVTGWHKEGRTDDKGNPVRDSTY
QAEYGVDYVRVFPGGQREAPAMFKYQGKYYILTSGASGWAPNENKVTVADNIFGPWSTQT
NPFVRTLPSDPDPGKAFGTQTTSVIPVDPEKGKFIYVGDTWNGGNFSNDAAKYVFLPIEF
GIGSDIAIKWYNSWTPDLLNSMGKVDIADPLPEAVALGKVPSLPTTLNVREGGALVSTPA
VWTIDNRAMTAEDFAKPGPLTLQVTTPEYNNKKQAVHVNVIPENTLYFVNSGGYETADYS
LMGAYMKGTLANPGTADQMYAPAEGRNWGYVSADALASGSNGGDIFSTVRYLNGGNVSNS
PKGTDLTYTFDVPNGTYDVYAGFNDPWSNTSRRANLIINGTNTGAVSFTPASVRAHKDIS
VSDNKLELTVRNTASQDPMISWIMIVKPDAAPPANDSAGLNADALDSTSATLYWDAHLGA
ASYKLYRSDREQGEYKVVYNGNGREYTDSELNPGTEYYYKVEALDATGQSVRGVSSAYQV
HTVQQSATDVATSIAALEQPSAGAKKLKLPSVPQGFTVKITSSSAPSVIQTDGTIVPPSK
ETTVTLELEITRTSDDSKALTAPLTVKVLAFVPSPGGNPGSGGSPGGNSGGNPGDGSGSS
SNGGQSGSGNPSAENAVPQPKPEKDRSVLELQGQSDQKGVVQSNVDVSTIKDAFKLAPST
DAGQRLVELRLKPVSGATAYELSLPASVLIDQGESHVFNIVTELGMLELPATLLTKDIVG
DGIASIRLVRTELPKTVADQLGTQYGVQLELQVDGQPWPSESQLIVRLPFQSSQNAQQDR
IVAFAIGANGVATPLPQSYYDQKSGQLVFSVTSLTGNYAVVPVEQTFTDLAEVQWAKKAM
EALAVRGVIGTEASGDSTQLHPKQEMTRGQYMQWLMAALGLNASSGNAFSDVNETAPYYE
AVTAARSLGITSGTGDGRFLPESTITRQEMMTLTVRALAAAGLVDSETTVTDNLTRFRDA
SEIRSYARDSVALLVNLGIAHGYNGEVKPLAEATRAESATLLYAMMGKLVWNK

Enzyme Prediction     

No EC number prediction in MGYG000003072_02879.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	511	822	1.6e-96	0.975609756097561
CBM66	48	197	3e-17	0.9161290322580645

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd18825	GH43_CtGH43-like	9.72e-122	498	840	1	285	Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A. This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
cd08985	GH43_CtGH43-like	4.14e-94	498	840	1	273	Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A. This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
cd18822	GH43_CtGH43-like	4.71e-81	498	840	1	266	Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43). This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43), Streptomyces avermitilis MA-4680 = NBRC 14893 (Sa1,3Gal43A;SAV2109) (1,3Gal43A), and Ruminiclostridium thermocellum ATCC 27405 (Ct1,3Gal43A;CtGH43;Cthe_0661) (1,3Gal43A). It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
cd18821	GH43_Pc3Gal43A-like	1.50e-76	498	840	1	262	Glycosyl hydrolase family 43 protein such as Phanerochaete chrysosporium exo-beta-1,3-galactanase (Pc1, 3Gal43A, 1,3Gal43A). This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), Fusarium oxysporum 12S Fo/1 (3Gal), and Streptomyces sp. 19(2012) SGalase1 and SGalase2. It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
cd18826	GH43_CtGH43-like	1.19e-67	498	840	1	269	Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A. This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
APO45573.1	0.0	1	1733	8	1741
QLG41021.1	0.0	1	1733	8	1737
QZN73954.1	0.0	1	1732	8	1740
QOS78718.1	0.0	1	1733	8	1744
QKS54946.1	0.0	4	1733	11	1754

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6EUG_A	1.12e-69	484	857	29	374	TheGH43, Beta 1,3 Galactosidase, BT3683 with galactoimidazole [Bacteroides thetaiotaomicron],6EUH_A The GH43, Beta 1,3 Galactosidase, BT3683 with galactodeoxynojirimycin [Bacteroides thetaiotaomicron VPI-5482],6EUH_B The GH43, Beta 1,3 Galactosidase, BT3683 with galactodeoxynojirimycin [Bacteroides thetaiotaomicron VPI-5482],6EUH_C The GH43, Beta 1,3 Galactosidase, BT3683 with galactodeoxynojirimycin [Bacteroides thetaiotaomicron VPI-5482],6EUI_A The GH43, Beta 1,3 Galactosidase, BT3683 with galactose [Bacteroides thetaiotaomicron VPI-5482]
6EUF_A	8.24e-54	481	862	2	308	TheGH43, Beta 1,3 Galactosidase, BT0265 [Bacteroides thetaiotaomicron VPI-5482],6EUF_B The GH43, Beta 1,3 Galactosidase, BT0265 [Bacteroides thetaiotaomicron VPI-5482],6EUF_C The GH43, Beta 1,3 Galactosidase, BT0265 [Bacteroides thetaiotaomicron VPI-5482],6EUF_D The GH43, Beta 1,3 Galactosidase, BT0265 [Bacteroides thetaiotaomicron VPI-5482],6EUJ_A The GH43, Beta 1,3 Galactosidase, BT0265 [Bacteroides thetaiotaomicron VPI-5482],6EUJ_B The GH43, Beta 1,3 Galactosidase, BT0265 [Bacteroides thetaiotaomicron VPI-5482],6EUJ_C The GH43, Beta 1,3 Galactosidase, BT0265 [Bacteroides thetaiotaomicron VPI-5482],6EUJ_D The GH43, Beta 1,3 Galactosidase, BT0265 [Bacteroides thetaiotaomicron VPI-5482]
3VSF_A	2.95e-45	484	853	42	343	ChainA, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSF_B Chain B, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSF_C Chain C, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSF_D Chain D, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSF_E Chain E, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSF_F Chain F, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSZ_A Chain A, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSZ_B Chain B, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSZ_C Chain C, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSZ_D Chain D, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSZ_E Chain E, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VSZ_F Chain F, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT0_A Chain A, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT0_B Chain B, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT0_C Chain C, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT0_D Chain D, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT0_E Chain E, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT0_F Chain F, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT1_A Chain A, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT1_B Chain B, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT1_C Chain C, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT1_D Chain D, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT1_E Chain E, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT1_F Chain F, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT2_A Chain A, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT2_B Chain B, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT2_C Chain C, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT2_D Chain D, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT2_E Chain E, Ricin B lectin [Acetivibrio thermocellus ATCC 27405],3VT2_F Chain F, Ricin B lectin [Acetivibrio thermocellus ATCC 27405]
7BYS_A	2.51e-42	484	844	3	281	ChainA, Galactan 1,3-beta-galactosidase [Phanerodontia chrysosporium],7BYS_B Chain B, Galactan 1,3-beta-galactosidase [Phanerodontia chrysosporium],7BYT_A Chain A, Galactan 1,3-beta-galactosidase [Phanerodontia chrysosporium]
7BYV_A	3.46e-42	481	844	1	282	ChainA, Galactan 1,3-beta-galactosidase [Phanerodontia chrysosporium]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
C6CRV0	5.21e-39	1370	1723	1100	1456	Endo-1,4-beta-xylanase A OS=Paenibacillus sp. (strain JDR-2) OX=324057 GN=xynA1 PE=1 SV=1
P50899	1.31e-12	204	488	700	989	Exoglucanase B OS=Cellulomonas fimi (strain ATCC 484 / DSM 20113 / JCM 1341 / NBRC 15513 / NCIMB 8980 / NCTC 7547) OX=590998 GN=cbhB PE=1 SV=1
P19424	8.17e-12	1547	1729	41	217	Endoglucanase OS=Bacillus sp. (strain KSM-635) OX=1415 PE=1 SV=1
Q02388	4.57e-08	209	486	505	775	Collagen alpha-1(VII) chain OS=Homo sapiens OX=9606 GN=COL7A1 PE=1 SV=2
Q6NWW9	3.43e-07	252	462	911	1130	Fibronectin type III domain-containing protein 3B OS=Mus musculus OX=10090 GN=Fndc3b 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
0.001701	0.997187	0.000238	0.000339	0.000264	0.000247

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003072_02879.