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Conserved domains on  [gi|489502723|ref|WP_003407616|]
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MULTISPECIES: hypothetical protein [Mycobacterium]

Protein Classification

glycoside hydrolase family protein( domain architecture ID 52385)

glycoside hydrolase (GH) family protein may catalyze the hydrolysis of glycosidic bonds in complex sugars; may belong to glycosyl hydrolase families GH32, GH43, GH62, GH68, GH117, or GH130

Gene Ontology:  GO:0016798
PubMed:  8535779

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GH43_62_32_68_117_130 super family cl14647
Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl ...
 90-250 5.60e-10

Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl hydrolase families 32, 43, 62, 68, 117 and 130 (GH32, GH43, GH62, GH68, GH117, GH130) all possess 5-bladed beta-propeller domains and comprise clans F and J, as classified by the carbohydrate-active enzymes database (CAZY). Clan F consists of families GH43 and GH62. GH43 includes beta-xylosidases (EC 3.2.1.37), beta-xylanases (EC 3.2.1.8), alpha-L-arabinases (EC 3.2.1.99), and alpha-L-arabinofuranosidases (EC 3.2.1.55), using aryl-glycosides as substrates, while family GH62 contains alpha-L-arabinofuranosidases (EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose sidechains from xylans. These 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. Clan J consists of families GH32 and GH68. GH32 comprises sucrose-6-phosphate hydrolases, invertases (EC 3.2.1.26), inulinases (EC 3.2.1.7), levanases (EC 3.2.1.65), eukaryotic fructosyltransferases, and bacterial fructanotransferases while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), all of which use sucrose as their preferential donor substrate. Members of this clan are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) that catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. Structures of all families in the two clans manifest a funnel-shaped active site that comprises two subsites with a single route for access by ligands. Also included in this superfamily are GH117 enzymes that have exo-alpha-1,3-(3,6-anhydro)-l-galactosidase activity, removing terminal non-reducing alpha-1,3-linked 3,6-anhydro-l-galactose residues from their neoagarose substrate, and GH130 that are phosphorylases and hydrolases for beta-mannosides, involved in the bacterial utilization of mannans or N-linked glycans.


The actual alignment was detected with superfamily member cd08984:

Pssm-ID: 449341  Cd Length: 291  Bit Score: 58.80  E-value: 5.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723  90 SIVRAGDTR--LLYYTGWNLAVTVP-----WKNTIGVAISEAGApfeRWSTFPVVALDERDPFSLSY--PWVIQDGGTYR 160
Cdd:cd08984   14 VVIWNPATKewWMFYTQRRATVDGPgvawvHGTPIGIASSKDGA---TWTYRGTADGLGPEPGENTFwaPEVIVDGGTYH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723 161 MWygsnLGWGEGTDE---IPHVIRYAQSRDGVHWEKQDRVHIDTSGS-DnsaacrPCVVRDA-GVYRMWFCARGAKYRIY 235
Cdd:cd08984   91 MF----VTYIPGVPTdwgGPRRIVHYTSPDLWNWKFVGTLDLSSDRViD------ACVARLPdGTWRMWYKDEADGSTTY 160

                        170
                 ....*....|....*
gi 489502723 236 CATSEDGLTWRQLGK 250
Cdd:cd08984  161 AADSPDLYHWTVEGP 175
 
Name Accession Description Interval E-value
GH43-like cd08984
Glycosyl hydrolase family 43; This glycosyl hydrolase family 43 (GH43)-like subfamily includes ...
 90-250 5.60e-10

Glycosyl hydrolase family 43; This glycosyl hydrolase family 43 (GH43)-like subfamily includes uncharacterized enzymes similar to those with beta-1,4-xylosidase (xylan 1,4-beta-xylosidase; EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanase and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. These 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 of the enzymes in this family 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.


Pssm-ID: 350098  Cd Length: 291  Bit Score: 58.80  E-value: 5.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723  90 SIVRAGDTR--LLYYTGWNLAVTVP-----WKNTIGVAISEAGApfeRWSTFPVVALDERDPFSLSY--PWVIQDGGTYR 160
Cdd:cd08984   14 VVIWNPATKewWMFYTQRRATVDGPgvawvHGTPIGIASSKDGA---TWTYRGTADGLGPEPGENTFwaPEVIVDGGTYH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723 161 MWygsnLGWGEGTDE---IPHVIRYAQSRDGVHWEKQDRVHIDTSGS-DnsaacrPCVVRDA-GVYRMWFCARGAKYRIY 235
Cdd:cd08984   91 MF----VTYIPGVPTdwgGPRRIVHYTSPDLWNWKFVGTLDLSSDRViD------ACVARLPdGTWRMWYKDEADGSTTY 160

                        170
                 ....*....|....*
gi 489502723 236 CATSEDGLTWRQLGK 250
Cdd:cd08984  161 AADSPDLYHWTVEGP 175
XynB2 COG3507
Beta-xylosidase [Carbohydrate transport and metabolism];
114-288 3.95e-07

Beta-xylosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442730 [Multi-domain]  Cd Length: 351  Bit Score: 50.72  E-value: 3.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723 114 KNTIGVAISEAGAPFERWSTF--PVVALDERDPFslsypwVIQDGGTYRMwYGSNLGWGEGtdeiphvIRYAQSRDGVHW 191
Cdd:COG3507    2 KKLLLLLLLLLAAAAALGNTYtnPVLPGDYPDPS------IIRVGDTYYL-YGTSFEYFPG-------LPIFHSKDLVNW 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723 192 EKQDRVhIDTSGSDNSAACR----PCVVRDAGVYRMWFCARGAKYR---IYCATSED--GlTWrqlgKDEGIDVSPDSWD 262
Cdd:COG3507   68 ELVGHA-LDRLPQWADPYSGgiwaPDIRYHNGKYYLYYTAVDGGKNrsgIGVATADDpeG-PW----SDPGPLVCPGGNG 141

                        170       180
                 ....*....|....*....|....*..
gi 489502723 263 SDmieyPCVF-DHRGQRFMLYSGDGYG 288
Cdd:COG3507  142 ID----PSVFvDDDGKAYLVYGSGGGG 164
Glyco_hydro_130 pfam04041
beta-1,4-mannooligosaccharide phosphorylase; This is a family of glycosyl-hydrolases of the ...
 171-282 4.36e-04

beta-1,4-mannooligosaccharide phosphorylase; This is a family of glycosyl-hydrolases of the CAZy GH130 family. Several have been characterized as mannosylglucose phosphorylase. This enzyme is part of the mannan catalytic pathway and feeds into the glycolysis cycle. Specifically it catalyzes the reversible phosphorolysis of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine. This family was noted to belong to the Beta fructosidase superfamily in.


Pssm-ID: 397932 [Multi-domain]  Cd Length: 315  Bit Score: 41.32  E-value: 4.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723  171 EGTDEIPHVIRYAQSRDGVHWEKQDRVHIDTSGSDNSAACR-PCVVRDAGVYRMWFCARGAKY-RIYCATSEDGLTWRQL 248
Cdd:pfam04041  59 YVSDIASFRIGLEDSYDGIKKTLEPEPIFWPRDKQEFWGVEdPRVVKINSTYYMTYTGRDYKYwRIEVGTTKDFLTWARL 138

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 489502723  249 GKD-EGIDVSPDS-WDSDMIEYPcvFDHRGQRFMLY 282
Cdd:pfam04041 139 PVKiALFEKRYDSiKTSDGNAFP--VKIKGKYLMYH 172
 
Name Accession Description Interval E-value
GH43-like cd08984
Glycosyl hydrolase family 43; This glycosyl hydrolase family 43 (GH43)-like subfamily includes ...
 90-250 5.60e-10

Glycosyl hydrolase family 43; This glycosyl hydrolase family 43 (GH43)-like subfamily includes uncharacterized enzymes similar to those with beta-1,4-xylosidase (xylan 1,4-beta-xylosidase; EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanase and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. These 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 of the enzymes in this family 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.


Pssm-ID: 350098  Cd Length: 291  Bit Score: 58.80  E-value: 5.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723  90 SIVRAGDTR--LLYYTGWNLAVTVP-----WKNTIGVAISEAGApfeRWSTFPVVALDERDPFSLSY--PWVIQDGGTYR 160
Cdd:cd08984   14 VVIWNPATKewWMFYTQRRATVDGPgvawvHGTPIGIASSKDGA---TWTYRGTADGLGPEPGENTFwaPEVIVDGGTYH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723 161 MWygsnLGWGEGTDE---IPHVIRYAQSRDGVHWEKQDRVHIDTSGS-DnsaacrPCVVRDA-GVYRMWFCARGAKYRIY 235
Cdd:cd08984   91 MF----VTYIPGVPTdwgGPRRIVHYTSPDLWNWKFVGTLDLSSDRViD------ACVARLPdGTWRMWYKDEADGSTTY 160

                        170
                 ....*....|....*
gi 489502723 236 CATSEDGLTWRQLGK 250
Cdd:cd08984  161 AADSPDLYHWTVEGP 175
GH117 cd08992
Glycosyl hydrolase family 117 (GH117); This glycoside hydrolase 117 (GH117) family includes ...
 142-299 8.02e-09

Glycosyl hydrolase family 117 (GH117); This glycoside hydrolase 117 (GH117) family includes alpha-1,3-L-neoagarooligosaccharide hydrolase (EC 3.2.1.-); alpha-1,3-L-neoagarobiase/neoagarobiose hydrolase (NABH, EC 3.2.1.-). In the agarolytic pathway, in order to metabolize agar, NABH is an essential enzyme because it converts alpha-neoagarobiose (O-3,6-anhydro-alpha-l-galactopyranosyl-(1,3)-d-galactose) into fermentable monosaccharides (d-galactose and 3,6-anhydro-l-galactose). Thus, these enzymes have exo-alpha-1,3-(3,6-anhydro)-l-galactosidase activity, removing terminal non-reducing alpha-1,3-linked 3,6-anhydro-l-galactose residues from their neoagarose substrate. This family includes Zobellia galactanivorans enzymes, Zg4663 and Zg3615 (also known as ZgAhgA and ZgAhgB, respectively) that have been shown to have similar activity on unsubstituted agarose oligosaccharides while Zg3597 has been shown to be inactive, possibly due to differences in dimerization conformation, active-site structure and function. GH117 shares distant sequence similarity with families GH43 and GH32. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, 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.


Pssm-ID: 350106  Cd Length: 314  Bit Score: 55.72  E-value: 8.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723 142 RDPFSlsypwVIQDGGTYRMWY-----GSNLGWGEGTDEIPHV------IRYAQSRDGVHWEKQDR-VHIDTSGS-DNSA 208
Cdd:cd08992   23 RDPSS-----VIKVNGTYYVWYtksdeGPPVGFGKANDTLKVFpwdladIWYATSKDGWTWKEQGVaVGRGPKGAyDDRS 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723 209 ACRPCVVRDAGVYRMWFCARGAKY---RIYC------ATSEDGLtWRQL-------GKDEGIDVSPDSWDSDMIEYPCVF 272
Cdd:cd08992   98 VFTPEILVHKGKYYLYYQAVKSPYggiRDKNpigmavADSPDGP-WTKLdepilepGDEGEWEKAKGDFDSHKVHDPCLI 176

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 489502723 273 DHRGQRFMLYSGDGYGR--------TGFGLAVLEN 299
Cdd:cd08992  177 VYNGKFYLYYKGEPMGEgitgggreIKWGVAIADN 211
GH32-like cd18609
Glycosyl hydrolase family 32 family protein; The GH32 family contains glycosyl hydrolase ...
 73-245 2.32e-08

Glycosyl hydrolase family 32 family protein; The GH32 family contains glycosyl hydrolase family GH32 proteins that cleave sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). This family also contains other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, 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.


Pssm-ID: 350121  Cd Length: 303  Bit Score: 54.18  E-value: 2.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723  73 LRPGARGMFDDCGVSIGSIVRAGDTR-LLYYTG-WNLAVTVPwkNTIGVAISEAGAPFERWSTFPVVALDERDPFSLSY- 149
Cdd:cd18609   62 LGPGDPGAWDDLATWTGSVIRDPDGLwRMFYTGtSRAEDGLV--QRIGLATSDDLITWTKHPGNPLLAADPRWYETLGDs 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723 150 ---------PWVIQDGGTYrMWYG-----SNLG--WGEGtdeiphVIRYAQSRDGVHWEKQDRVHIdtsgsdnSAACR-- 211
Cdd:cd18609  140 gwhdeawrdPWVFRDPDGG-GWHMlitarANEGppDGRG------VIGHATSPDLEHWEVLPPLSA-------PGVFGhl 205

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 489502723 212 --PCVVRDAGVYRMWFCARGAKY-RIYCATSEDGLTW 245
Cdd:cd18609  206 evPQVFEIDGRWYLLFSCGADHLsRERRAAGGGGGTW 242
XynB2 COG3507
Beta-xylosidase [Carbohydrate transport and metabolism];
114-288 3.95e-07

Beta-xylosidase [Carbohydrate transport and metabolism];


Pssm-ID: 442730 [Multi-domain]  Cd Length: 351  Bit Score: 50.72  E-value: 3.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723 114 KNTIGVAISEAGAPFERWSTF--PVVALDERDPFslsypwVIQDGGTYRMwYGSNLGWGEGtdeiphvIRYAQSRDGVHW 191
Cdd:COG3507    2 KKLLLLLLLLLAAAAALGNTYtnPVLPGDYPDPS------IIRVGDTYYL-YGTSFEYFPG-------LPIFHSKDLVNW 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723 192 EKQDRVhIDTSGSDNSAACR----PCVVRDAGVYRMWFCARGAKYR---IYCATSED--GlTWrqlgKDEGIDVSPDSWD 262
Cdd:COG3507   68 ELVGHA-LDRLPQWADPYSGgiwaPDIRYHNGKYYLYYTAVDGGKNrsgIGVATADDpeG-PW----SDPGPLVCPGGNG 141

                        170       180
                 ....*....|....*....|....*..
gi 489502723 263 SDmieyPCVF-DHRGQRFMLYSGDGYG 288
Cdd:COG3507  142 ID----PSVFvDDDGKAYLVYGSGGGG 164
GH32_EcAec43-like cd08995
Glycosyl hydrolase family 32, such as the putative glycoside hydrolase Escherichia coli Aec43 ...
 152-290 7.75e-07

Glycosyl hydrolase family 32, such as the putative glycoside hydrolase Escherichia coli Aec43 (FosGH2); This glycosyl hydrolase family 32 (GH32) subgroup includes Escherichia coli strain BEN2908 putative glycoside hydrolase Aec43 (FosGH2). GH32 enzymes cleave sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). GH32 family also contains other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize.


Pssm-ID: 350109 [Multi-domain]  Cd Length: 281  Bit Score: 49.50  E-value: 7.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723 152 VIQDGGTYRMWY-GSNLGWGEGTDeiphVIRYAQSRDGVHWEKQ--DRVHIDTSGSDNSaACR-PCVVRD--AGVYRMWF 225
Cdd:cd08995   67 VIKDDGTYHAFYtGHNPDFGKPKQ----VIMHATSTDLKTWTKDpeFTFIADPEGYEKN-DFRdPFVFWNeeEGEYWMLV 141

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489502723 226 CAR---GAKYR---IYCATSEDGLTWrqlgKDEGIDVSPDSWdsDMIEYPCVFDHRGQRFMLYSGDGYGRT 290
Cdd:cd08995  142 AARkndGPGNRrgcIALYTSKDLKNW----TFEGPFYAPGSY--NMPECPDLFKMGDWWYLVFSEFSERRK 206
GH43_62_32_68_117_130-like cd08994
Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl ...
 70-202 8.44e-06

Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl hydrolase families 32, 43, 62, 68, 117 and 130 (GH32, GH43, GH62, GH68, GH117, GH130) all possess 5-bladed beta-propeller domains and comprise clans F and J, as classified by the carbohydrate-active enzymes database (CAZY). Clan F consists of families GH43 and GH62. GH43 includes beta-xylosidases (EC 3.2.1.37), beta-xylanases (EC 3.2.1.8), alpha-L-arabinases (EC 3.2.1.99), and alpha-L-arabinofuranosidases (EC 3.2.1.55), using aryl-glycosides as substrates, while family GH62 contains alpha-L-arabinofuranosidases (EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose sidechains from xylans. These 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. Clan J consists of families GH32 and GH68. GH32 comprises sucrose-6-phosphate hydrolases, invertases (EC 3.2.1.26), inulinases (EC 3.2.1.7), levanases (EC 3.2.1.65), eukaryotic fructosyltransferases, and bacterial fructanotransferases while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), all of which use sucrose as their preferential donor substrate. Members of this clan are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) that catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. Structures of all families in the two clans manifest a funnel-shaped active site that comprises two subsites with a single route for access by ligands. Also included in this superfamily are GH117 enzymes that have exo-alpha-1,3-(3,6-anhydro)-l-galactosidase activity, removing terminal non-reducing alpha-1,3-linked 3,6-anhydro-l-galactose residues from their neoagarose substrate, and GH130 that are phosphorylases and hydrolases for beta-mannosides, involved in the bacterial utilization of mannans or N-linked glycans.


Pssm-ID: 350108 [Multi-domain]  Cd Length: 294  Bit Score: 46.49  E-value: 8.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723  70 EPILRPGARGmFDDCGVSIGSIVRAGDTR-LLYYTGWNLAVtvPWKNTIGVAISEAGA-PFERWSTFPVVALDErdPFSL 147
Cdd:cd08994  135 KPILDPRPRS-WDDLITSNPAVLKRPDGSyLLYYKGGKKNP--GGNRKHGVAVSDSPEgPYTKLSDPPVYEPGV--NGQT 209

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489502723 148 SYPWVIQDGGTYRMWYGSNLGWGEGtdeIPHVIRYAQSRDGVHWEKQDRVHIDTS 202
Cdd:cd08994  210 EDPFIWYDKGQYHLIVKDMGGIFTG---EGGGGALLRSKDGINWKLAPGLAYSTE 261
GH32_FFase cd08996
Glycosyl hydrolase family 32, beta-fructosidases; Glycosyl hydrolase family GH32 cleaves ...
 152-283 8.84e-06

Glycosyl hydrolase family 32, beta-fructosidases; Glycosyl hydrolase family GH32 cleaves sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). This family also contains other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, 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.


Pssm-ID: 350110  Cd Length: 281  Bit Score: 46.48  E-value: 8.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723 152 VIQDGGTYRMWYGSNLGWGEGTDEIphVIRYAqSRDGVHWEKQDRVHIDTSGSD-NSAACR-PCVVRDAGVYRMWFCAR- 228
Cdd:cd08996   68 AVVDDGKPTLFYTGVRDLGDGRQTQ--CLATS-DDDLITWEKYPGNPVIPPPPGgGVTDFRdPFVWKEGGTWYMVVGGGl 144

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489502723 229 -GAKYRIYCATSEDGLTWRQLGKdeGIDVSPDSWDSDMIEYPCVFDHRGQRFMLYS 283
Cdd:cd08996  145 eDGGGAVLLYRSDDLRDWEYLGV--LLDAASDGDTGEMWECPDFFPLGGKWVLLFS 198
GH130 cd18607
Glycoside hydrolase family 130; Members of the glycosyl hydrolase family 130, as classified by ...
 113-267 1.04e-05

Glycoside hydrolase family 130; Members of the glycosyl hydrolase family 130, as classified by the carbohydrate-active enzymes database (CAZY), are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), beta-1,4-mannosyl-N-acetyl-glucosamine phosphorylase (EC 2.4.1.320), beta-1,2-mannobiose phosphorylase (EC 2.4.1.-), beta-1,2-oligomannan phosphorylase (EC 2.4.1.-) and beta-1,2-mannosidase (EC 3.2.1.-). They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor.


Pssm-ID: 350119 [Multi-domain]  Cd Length: 269  Bit Score: 46.15  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723 113 WKNTIGVAISEAGAPFERWSTfPVVALDERDPFSLSY---PWVIQDGGTYRMWYgsnlgwgegTDEIPHVIR--YAQSRD 187
Cdd:cd18607   30 RRSSIGYARSKDGIHFERLDE-PPLYPPPENPYEKGGcedPRITKIDDTYYMTY---------TAYDGFGPRlaLATTKD 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723 188 GVHWEKQDRVhidtsgSDNSAACRPCVV---RDAGVYRMWFcaRGAKYRIYCATSEDGLTWRQLGkdEGIDVSPDSWDSD 264
Cdd:cd18607  100 LKNWERHGLA------FPPAPENKNGVIfpeKINGKYAMLH--RPDGPDIWLATSDDLIHWGDHK--PLLKPRKGTWDSA 169


                 ...
gi 489502723 265 MIE 267
Cdd:cd18607  170 KVG 172
GH32_FFase cd08996
Glycosyl hydrolase family 32, beta-fructosidases; Glycosyl hydrolase family GH32 cleaves ...
 81-205 1.00e-04

Glycosyl hydrolase family 32, beta-fructosidases; Glycosyl hydrolase family GH32 cleaves sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). This family also contains other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, 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.


Pssm-ID: 350110  Cd Length: 281  Bit Score: 43.01  E-value: 1.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723  81 FDDCGVSIGSIVRAGDTRLLYYTGWNLavTVPWKNTIGVAISEAGApfERWSTFPVVALDERDPFSLSY----PWVIQDG 156
Cdd:cd08996   58 YDEDGCFSGSAVVDDGKPTLFYTGVRD--LGDGRQTQCLATSDDDL--ITWEKYPGNPVIPPPPGGGVTdfrdPFVWKEG 133

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489502723 157 GTYRMWYGSNLGWGEGTdeiphVIRYaQSRDGVHWEKQDRVHIDTSGSD 205
Cdd:cd08996  134 GTWYMVVGGGLEDGGGA-----VLLY-RSDDLRDWEYLGVLLDAASDGD 176
GH43_HoAraf43-like cd08991
Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 ...
 143-288 1.64e-04

Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (HoAraf43;Hore_20580); This glycosyl hydrolase family 43 (GH43) subgroup includes Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (EC 3.2.1.55) (HoAraf43;Hore_20580). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. This GH43_ HoAraf43-like subgroup includes enzymes that have been annotated as having xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities. 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.


Pssm-ID: 350105 [Multi-domain]  Cd Length: 283  Bit Score: 42.55  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723 143 DPFslsypwVIQDGGTYRMwYGSNLGWGEGtdeiphvIRYAQSRDGVHWEKQDRVHIDTSGSDNSAACRPCVVRDAGVYR 222
Cdd:cd08991    2 DPF------VLKHNGTYYL-YGTGGDDGRG-------FKVYVSDDLVNWEYPGGALEEPGLWGTKGFWAPEVFYYNGKFY 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489502723 223 MWFCARGA--KYRIYCATSEDgltwrQLG--KDEGIDVSPDSW---DSDMieypcVFDHRGQRFMLYSGDGYG 288
Cdd:cd08991   68 MYYSANGGdhGEHIAVAVSDS-----PLGpfRDKGKLLIPAGGfsiDAHV-----FIDDDGKWYLYYVRDDLG 130
GH130_BT3780-like cd18610
Glycosyl hydrolase family 130, such as beta-mammosidase BT3780 and BACOVA_03624; This ...
 117-267 2.43e-04

Glycosyl hydrolase family 130, such as beta-mammosidase BT3780 and BACOVA_03624; This subfamily contains glycosyl hydrolase family 130, as classified by the carbohydrate-active enzymes database (CAZY), and includes Bacteroides enzymes, BT3780 and BACOVA_03624. Members of this family possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. GH130 enzymes have also been shown to target beta-1,2- and beta-1,4-mannosidic linkages where these phosphorylases mediate bond cleavage by a single displacement reaction in which phosphate functions as the catalytic nucleophile. However, some lack the conserved basic residues that bind the phosphate nucleophile, as observed for the Bacteroides enzymes, BT3780 and BACOVA_03624, which are indeed beta-mannosidases that hydrolyze beta-1,2-mannosidic linkages through an inverting mechanism.


Pssm-ID: 350122 [Multi-domain]  Cd Length: 301  Bit Score: 41.80  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723 117 IGVAISEAGAPFERWSTfPVV--ALDERDPFSLSYPWVIQD-GGTYRMWYgsnLGWGEgtdeipHVIRY--AQSRDGVHW 191
Cdd:cd18610   46 IGLAVSDDGLHFTRLPE-PVLypEEDYEWPGGCEDPRIVEIeDGTYYMTY---TAYDG------KTARLclATSTDLVHW 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723 192 EKQ-------DRVHIDTSGSdNSAACRPCVVRDA---GVYRMWFcarGAKYrIYCATSEDGLTWRQLGKDEG----IDVS 257
Cdd:cd18610  116 TKHgpafpdaDGGKYRDLWS-KSGAIVPELKGAAkinGKYWMYW---GESN-IYLATSDDLIHWTPVEDDGSlrpvLSPR 190

                        170
                 ....*....|
gi 489502723 258 PDSWDSDMIE 267
Cdd:cd18610  191 PGKFDSDLVE 200
Glyco_hydro_130 pfam04041
beta-1,4-mannooligosaccharide phosphorylase; This is a family of glycosyl-hydrolases of the ...
 171-282 4.36e-04

beta-1,4-mannooligosaccharide phosphorylase; This is a family of glycosyl-hydrolases of the CAZy GH130 family. Several have been characterized as mannosylglucose phosphorylase. This enzyme is part of the mannan catalytic pathway and feeds into the glycolysis cycle. Specifically it catalyzes the reversible phosphorolysis of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine. This family was noted to belong to the Beta fructosidase superfamily in.


Pssm-ID: 397932 [Multi-domain]  Cd Length: 315  Bit Score: 41.32  E-value: 4.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723  171 EGTDEIPHVIRYAQSRDGVHWEKQDRVHIDTSGSDNSAACR-PCVVRDAGVYRMWFCARGAKY-RIYCATSEDGLTWRQL 248
Cdd:pfam04041  59 YVSDIASFRIGLEDSYDGIKKTLEPEPIFWPRDKQEFWGVEdPRVVKINSTYYMTYTGRDYKYwRIEVGTTKDFLTWARL 138

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 489502723  249 GKD-EGIDVSPDS-WDSDMIEYPcvFDHRGQRFMLY 282
Cdd:pfam04041 139 PVKiALFEKRYDSiKTSDGNAFP--VKIKGKYLMYH 172
Glyco_hydro_43 pfam04616
Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are ...
 135-288 5.48e-04

Glycosyl hydrolases family 43; The glycosyl hydrolase family 43 contains members that are arabinanases. Arabinanases hydrolyse the alpha-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The structure of arabinanase Arb43A from Cellvibrio japonicus reveals a five-bladed beta-propeller fold. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.


Pssm-ID: 398349 [Multi-domain]  Cd Length: 281  Bit Score: 40.77  E-value: 5.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723  135 PVVALDERDPfslsypWVIQDGGTYRMwYGSNLGWGEGtdeiphvIRYAQSRDGVHWEKQDRVHIDTSGSD---NSAACR 211
Cdd:pfam04616   4 PVLPGFYPDP------SILRVGDDYYL-TTSSFEWFPG-------IPIFHSKDLVNWKLVGPVLVRRSQLSgrgSNASWA 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489502723  212 PCVVRDAGVYRMWFCArgAKYRIYCATSEDGL-TWRQLGKdegidVSPDSWDSDmieyPCVF-DHRGQRFMLYSGDGYG 288
Cdd:pfam04616  70 PDISYHDGKYYLYYTA--VAHGIFVATADSPDgPWSDPGK-----LKSGGGGID----PSLFhDDDGKKYLVWGGWDPR 137
GH43_62_32_68_117_130-like cd08994
Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl ...
 69-246 8.51e-04

Glycosyl hydrolase families: GH43, GH62, GH32, GH68, GH117, CH130; Members of the glycosyl hydrolase families 32, 43, 62, 68, 117 and 130 (GH32, GH43, GH62, GH68, GH117, GH130) all possess 5-bladed beta-propeller domains and comprise clans F and J, as classified by the carbohydrate-active enzymes database (CAZY). Clan F consists of families GH43 and GH62. GH43 includes beta-xylosidases (EC 3.2.1.37), beta-xylanases (EC 3.2.1.8), alpha-L-arabinases (EC 3.2.1.99), and alpha-L-arabinofuranosidases (EC 3.2.1.55), using aryl-glycosides as substrates, while family GH62 contains alpha-L-arabinofuranosidases (EC 3.2.1.55) that specifically cleave either alpha-1,2 or alpha-1,3-L-arabinofuranose sidechains from xylans. These 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. Clan J consists of families GH32 and GH68. GH32 comprises sucrose-6-phosphate hydrolases, invertases (EC 3.2.1.26), inulinases (EC 3.2.1.7), levanases (EC 3.2.1.65), eukaryotic fructosyltransferases, and bacterial fructanotransferases while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), while GH68 consists of frucosyltransferases (FTFs) that include levansucrase (EC 2.4.1.10); beta-fructofuranosidase (EC 3.2.1.26); inulosucrase (EC 2.4.1.9), all of which use sucrose as their preferential donor substrate. Members of this clan are retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) that catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. Structures of all families in the two clans manifest a funnel-shaped active site that comprises two subsites with a single route for access by ligands. Also included in this superfamily are GH117 enzymes that have exo-alpha-1,3-(3,6-anhydro)-l-galactosidase activity, removing terminal non-reducing alpha-1,3-linked 3,6-anhydro-l-galactose residues from their neoagarose substrate, and GH130 that are phosphorylases and hydrolases for beta-mannosides, involved in the bacterial utilization of mannans or N-linked glycans.


Pssm-ID: 350108 [Multi-domain]  Cd Length: 294  Bit Score: 40.32  E-value: 8.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723  69 AEPILRPGARGMFDDCGVSIGSIVRAGDTRLLYYTG-------WNLAVTVPWKNTIGVAISE--AGaPFERwSTFPVVAL 139
Cdd:cd08994   63 VEVVLPGRGGGFWDGDTTHNPTIKKFDGKYYLYYIGntgpgpdPPLWWGHRNNQRIGVAVADspNG-PWKR-FDKPILDP 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723 140 DERDPFSLSY----PWVIQDGgTYRMWYGSNlGWGEGTDEIPHVIRyAQSRDGvHWEKQDRVhIDTSGSDNSAACRPCVV 215
Cdd:cd08994  141 RPRSWDDLITsnpaVLKRPDG-SYLLYYKGG-KKNPGGNRKHGVAV-SDSPEG-PYTKLSDP-PVYEPGVNGQTEDPFIW 215

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489502723 216 RDAGVYR-----MWFCARGAKYRIYCATSEDGLTWR 246
Cdd:cd08994  216 YDKGQYHlivkdMGGIFTGEGGGGALLRSKDGINWK 251
SacC COG1621
Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism];
152-291 1.11e-03

Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism];


Pssm-ID: 441228 [Multi-domain]  Cd Length: 459  Bit Score: 40.29  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723 152 VIQDGGTYRMWYGSNlGWGEGTDEIPHVIRyAQSRDGVHWEKQD-RVHIDTSGSDNSAACR-PCVVRDAGVYRMWFCAR- 228
Cdd:COG1621   83 AVVDDGNLVLFYTGN-VRDGDGGRRQYQCL-AYSTDGRTFTKYEgNPVIPNPPGGYTKDFRdPKVWWDDGKWYMVLGAQt 160

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489502723 229 ---GAKYRIYcaTSEDGLTWRQLGkdeGIDVSPDSWDsDMIEYPCVFDHRGQRFMLYSGDGYGRTG 291
Cdd:COG1621  161 gdgKGTVLLY--TSPDLKNWTYLG---EFGEGDGAFG-YMWECPDLFPLDGKWVLIFSPQGGGPEG 220
SacC COG1621
Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism];
70-192 1.29e-03

Sucrose-6-phosphate hydrolase SacC, GH32 family [Carbohydrate transport and metabolism];


Pssm-ID: 441228 [Multi-domain]  Cd Length: 459  Bit Score: 39.90  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723  70 EPI-LRPGARgmFDDCGVSIGSIVRAGDTRLLYYTGWNLAVTVPWKNTIGVAISEAGAPFERWSTFPVVAL-------DE 141
Cdd:COG1621   63 LPIaLAPDEE--YDSGGCFSGSAVVDDGNLVLFYTGNVRDGDGGRRQYQCLAYSTDGRTFTKYEGNPVIPNppggytkDF 140

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489502723 142 RDPFslsypwVIQDGGTYRMWYGSNLGwgegtDEIPHVIRYaQSRDGVHWE 192
Cdd:COG1621  141 RDPK------VWWDDGKWYMVLGAQTG-----DGKGTVLLY-TSPDLKNWT 179
GH32-like cd18609
Glycosyl hydrolase family 32 family protein; The GH32 family contains glycosyl hydrolase ...
 151-246 1.62e-03

Glycosyl hydrolase family 32 family protein; The GH32 family contains glycosyl hydrolase family GH32 proteins that cleave sucrose into fructose and glucose via beta-fructofuranosidase activity, producing invert sugar that is a mixture of dextrorotatory D-glucose and levorotatory D-fructose, thus named invertase (EC 3.2.1.26). This family also contains other fructofuranosidases such as inulinase (EC 3.2.1.7), exo-inulinase (EC 3.2.1.80), levanase (EC 3.2.1.65), and transfructosidases such sucrose:sucrose 1-fructosyltransferase (EC 2.4.1.99), fructan:fructan 1-fructosyltransferase (EC 2.4.1.100), sucrose:fructan 6-fructosyltransferase (EC 2.4.1.10), fructan:fructan 6G-fructosyltransferase (EC 2.4.1.243) and levan fructosyltransferases (EC 2.4.1.-). These retaining enzymes (i.e. they retain the configuration at anomeric carbon atom of the substrate) catalyze hydrolysis in two steps involving a covalent glycosyl enzyme intermediate: an aspartate located close to the N-terminus acts as the catalytic nucleophile and a glutamate acts as the general acid/base; a conserved aspartate residue in the Arg-Asp-Pro (RDP) motif stabilizes the transition state. These enzymes are predicted to display a 5-fold beta-propeller fold as found for GH43 and CH68. The breakdown of sucrose is widely used as a carbon or energy source by bacteria, fungi, and plants. Invertase is used commercially in the confectionery industry, since fructose has a sweeter taste than sucrose and a lower tendency to crystallize. A common structural feature of all these enzymes is a 5-bladed beta-propeller domain, similar to GH43, 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.


Pssm-ID: 350121  Cd Length: 303  Bit Score: 39.54  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723 151 WVIQDGGTYRMWYgSNLGWGEGTDEIPHV---IRYAQSRDGVHWEKQDRV--HIDTSGSDNSAACRPCVVRDA-GVYRM- 223
Cdd:cd18609   13 WLADDGGTYHLFY-LQAPRSLGDPELRHRnarIGHAVSTDLVHWERLGDAlgPGDPGAWDDLATWTGSVIRDPdGLWRMf 91

                         90       100
                 ....*....|....*....|....*..
gi 489502723 224 ----WFCARGAKYRIYCATSEDGLTWR 246
Cdd:cd18609   92 ytgtSRAEDGLVQRIGLATSDDLITWT 118
COG2152 COG2152
Predicted glycosyl hydrolase, GH43/DUF377 family [Carbohydrate transport and metabolism];
127-249 3.53e-03

Predicted glycosyl hydrolase, GH43/DUF377 family [Carbohydrate transport and metabolism];


Pssm-ID: 441755 [Multi-domain]  Cd Length: 304  Bit Score: 38.58  E-value: 3.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723 127 PFERWSTFPVVALDERDPFSLSY---PWVIQDGGTYRMWYGSnlgwgEGTDEIPHvIRYAQSRDGVHWEKQDRVHIDTSG 203
Cdd:COG2152    3 ILKRYPGNPILTPNDMPRWEVNAvfnPGAVRFNGKFLLLYRV-----EGRDGKSH-LGLARSDDGINFRRDDEPILFPET 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 489502723 204 SDNSAACR-PCVVRDAGVYRMWFCARG-AKYRIYCATSEDGLTWRQLG 249
Cdd:COG2152   77 DYEDTGVEdPRITKIDGRYYITYTAYSgAGARIGLARTKDFKTWERLG 124
GH43_Bt3655-like cd08983
Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 ...
 155-293 6.93e-03

Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron VPI-5482 arabinofuranosidase Bt3655; This glycosyl hydrolase family 43 (GH43)-like family includes the characterized arabinofuranosidases (EC 3.2.1.55): Bacteroides thetaiotaomicron VPI-5482 (Bt3655;BT_3655) and Penicillium chrysogenum 31B Abf43B, as well as Bifidobacterium adolescentis ATCC 15703 beta-xylosidase (EC 3.2.1.37) BAD_1527. It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43 includes enzymes with beta-xylosidase (EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanases (beta-xylanases) and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. 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.


Pssm-ID: 350097  Cd Length: 262  Bit Score: 37.21  E-value: 6.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489502723 155 DGGTYRMWYGSNLGWGEGTDeiPHVIRYAQSRDGVHWEK----QDRVH--IDTSgsdnsaacrpcVVRDAGVYRMWFCAR 228
Cdd:cd08983   91 ETGQYVVYWSSSLYGDGGGG--NHRIYYATTKDFKTFSEpkvlFDPGFnvIDTT-----------IVKDGGTYYRFYKDE 157

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489502723 229 GAKYRIYCATSEDGLTWRQLGKDEGIDVSPdswdsDMIEYPCVF-DHRGQRFMLYsGDGYGRTGFG 293
Cdd:cd08983  158 TTGKGIRLATSDSLTGPWTTVTTGGGAGTG-----GGVEGPTVFkLNDGGKWYLY-YDQYGGGGYG 217
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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