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Conserved domains on  [gi|1672826828|gb|QCV48443|]
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arabinogalactan endo-1,4-beta-galactosidase [Enterococcus faecium]

Protein Classification

arabinogalactan endo-beta-1,4-galactanase( domain architecture ID 10008085)

arabinogalactan endo-beta-1,4-galactanase that hydrolyzes the beta-1,4-galactan linkages of arabinogalactan type I, a pectic substance found in plants such as soybeans

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GanB COG3867
Arabinogalactan endo-1,4-beta-galactosidase [Carbohydrate transport and metabolism];
3-392 0e+00

Arabinogalactan endo-1,4-beta-galactosidase [Carbohydrate transport and metabolism];


:

Pssm-ID: 443076  Cd Length: 382  Bit Score: 519.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672826828   3 MGIWLRKAVLFAAVLGALGAVSKTVEASASEFIRGADISILSDMEKSGAKYYEDD-ISKDALEILKNNGVNYVRLRLWQD 81
Cdd:COG3867     1 MKKLTIARILLLLGLLLLACASNPAAKEAADFIKGADLSYLNEMEDCGGKFYDEDgVPKDPLQILKDHGVNLVRLRLWVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672826828  82 PYNSNgeSYGAGTNDLETTIDLAKRAKNLGLKVLLDFHYSDFWVDPGKQNLPKAWQGLTFEEMNTALYDYTKNVLSEMKQ 161
Cdd:COG3867    81 PYWAA--PYGGGYNDLADVLAMAKRAKAAGMKVLLDFHYSDFWADPGKQNKPKAWANLSFDQLKDAVYDYTYDVLTALKA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672826828 162 LDVYPDMVQIGNELNSGMLWPYGKSWgEGGGEFDRLAAFLKSGIQAVRDT-QPKTTPVMLHLADGGDTGAFTWWFDEITS 240
Cdd:COG3867   159 AGLLPDMVQVGNEINNGMLWPDGKTE-QGPGNWDRLAALLNAGIRAVRDVaASPDIKVMLHLAQGGNNGLFRWWFDNLTK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672826828 241 RGVSFDLIGVSYYPYWH-GSMNELQTNMNAISQRYGKEVIVVETAYGHTTANADTMPNAFGEAEAAAGGYEPTPTGQAEY 319
Cdd:COG3867   238 RGVDFDVIGLSYYPYWHtGSLDDLGANLNDLASRYGKDVMVVETAYPWTLENGDGAPNIFGTDDPYAGGYPATPQGQADF 317
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1672826828 320 LLDLADRIQAVPNNRGAGFFYWEPLWY-NGNVSWATQagmnylsvqstmGNEWDNQAMFDFAGNALPSLRAFKQ 392
Cdd:COG3867   318 LRDLIQAVKAVPNGGGLGVFYWEPAWIpVPGTGWAGE------------GSSWENQALFDFDGKALPALDAFKA 379
 
Name Accession Description Interval E-value
GanB COG3867
Arabinogalactan endo-1,4-beta-galactosidase [Carbohydrate transport and metabolism];
3-392 0e+00

Arabinogalactan endo-1,4-beta-galactosidase [Carbohydrate transport and metabolism];


Pssm-ID: 443076  Cd Length: 382  Bit Score: 519.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672826828   3 MGIWLRKAVLFAAVLGALGAVSKTVEASASEFIRGADISILSDMEKSGAKYYEDD-ISKDALEILKNNGVNYVRLRLWQD 81
Cdd:COG3867     1 MKKLTIARILLLLGLLLLACASNPAAKEAADFIKGADLSYLNEMEDCGGKFYDEDgVPKDPLQILKDHGVNLVRLRLWVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672826828  82 PYNSNgeSYGAGTNDLETTIDLAKRAKNLGLKVLLDFHYSDFWVDPGKQNLPKAWQGLTFEEMNTALYDYTKNVLSEMKQ 161
Cdd:COG3867    81 PYWAA--PYGGGYNDLADVLAMAKRAKAAGMKVLLDFHYSDFWADPGKQNKPKAWANLSFDQLKDAVYDYTYDVLTALKA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672826828 162 LDVYPDMVQIGNELNSGMLWPYGKSWgEGGGEFDRLAAFLKSGIQAVRDT-QPKTTPVMLHLADGGDTGAFTWWFDEITS 240
Cdd:COG3867   159 AGLLPDMVQVGNEINNGMLWPDGKTE-QGPGNWDRLAALLNAGIRAVRDVaASPDIKVMLHLAQGGNNGLFRWWFDNLTK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672826828 241 RGVSFDLIGVSYYPYWH-GSMNELQTNMNAISQRYGKEVIVVETAYGHTTANADTMPNAFGEAEAAAGGYEPTPTGQAEY 319
Cdd:COG3867   238 RGVDFDVIGLSYYPYWHtGSLDDLGANLNDLASRYGKDVMVVETAYPWTLENGDGAPNIFGTDDPYAGGYPATPQGQADF 317
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1672826828 320 LLDLADRIQAVPNNRGAGFFYWEPLWY-NGNVSWATQagmnylsvqstmGNEWDNQAMFDFAGNALPSLRAFKQ 392
Cdd:COG3867   318 LRDLIQAVKAVPNGGGLGVFYWEPAWIpVPGTGWAGE------------GSSWENQALFDFDGKALPALDAFKA 379
Glyco_hydro_53 pfam07745
Glycosyl hydrolase family 53; This domain belongs to family 53 of the glycosyl hydrolase ...
35-390 1.60e-135

Glycosyl hydrolase family 53; This domain belongs to family 53 of the glycosyl hydrolase classification. These enzymes are enzymes are endo-1,4- beta-galactanases (EC:3.2.1.89). The structure of this domain is known and has a TIM barrel fold.


Pssm-ID: 311610  Cd Length: 333  Bit Score: 396.39  E-value: 1.60e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672826828  35 IRGADISILSDMEKSGAKYYEDD-ISKDALEILKNNGVNYVRLRLWQDPYnsngesyGAGTNDLETTIDLAKRAKNLGLK 113
Cdd:pfam07745   1 IKGADISSLNELENAGVTFYNTNgKTQDLFQILKDHGVNSVRLRVWNDPY-------DGGNNDLDDVLKIAKRAKAAGMK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672826828 114 VLLDFHYSDFWVDPGKQNLPKAWQGLTFEEMNTALYDYTKNVLSEMKQLDVYPDMVQIGNELNSGMLWPYGKSwgeggGE 193
Cdd:pfam07745  74 VLLDFHYSDTWADPGKQTKPKAWASLDTDQLKKALYNYTYDVLNALKEAGIDPDMVQVGNEINSGFLWPDGKT-----PN 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672826828 194 FDRLAAFLKSGIQAVRDTQPkTTPVMLHLADGGDTGAFTWWFDEITSRGVSFDLIGVSYYPYWHGSMNELQTNMNAISQR 273
Cdd:pfam07745 149 WDNMAKLLNSGIKAVREVSP-NIKVAIHLANGENNGLYRWWFDNLTKAGVDFDVIGVSYYPFWSGTLENLTTNLKDMASR 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672826828 274 YGKEVIVVETAYGHTTANADTMPNAFGEAEAAAGGYEPTPTGQAEYLLDLADRIQAVPNNRGAGFFYWEPLWYNGNVSWA 353
Cdd:pfam07745 228 YGKDVMVVETAYPWTLDDGDGHGNLDPETSSLTSGYPATPQGQATMLRDVIELVNAVPGSRGLGVFYWEPAWIPVGDAGL 307
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1672826828 354 TQAgmnylsvqstmGNEWDNQAMFDFAGNALPSLRAF 390
Cdd:pfam07745 308 WGG-----------GSSWDNQALFDFNGRALPSLNVF 333
GH113_mannanase-like cd19608
Glycoside hydrolase family 113 beta-1,4-mannanase and similar proteins; Mannan endo-1,4-beta ...
54-285 3.67e-04

Glycoside hydrolase family 113 beta-1,4-mannanase and similar proteins; Mannan endo-1,4-beta mannosidase (E.C 3.2.1.78) randomly cleaves (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans and is also called beta-1,4-mannanase, endo-1,4-beta-mannanase, endo-beta-1,4-mannase, beta-mannanase B, beta-1, 4-mannan 4-mannanohydrolase, endo-beta-mannanase, beta-D-mannanase, 1,4-beta-D-mannan mannanohydrolase, and 4-beta-D-mannan mannanohydrolase. (1->4)-beta-linked mannans are polysaccharides with a linear polymer backbone of (1->4)-beta-linked mannose units (in plants and fungi) or alternating mannose and glucose/galactose units (glucomannan in plants and fungi, and galactomannan and galactoglucomannan in plants), such as in the hemicellulose fraction of hard- and softwoods. Complete degradation of mannan requires a series of enzymes, including beta-1,4-mannanase. According to the CAZy database beta-1,4-mannanases are grouped into various glycoside hydrolase (GH) families; GH family 113 beta-1,4-mannanases include mostly bacterial and archaeal sequences.


Pssm-ID: 381626  Cd Length: 310  Bit Score: 42.75  E-value: 3.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672826828  54 YEDDISKDALEILKNNGVNYVRL--RLWQDPYNSNGES-YGAGTNDLETTIDLAKRAKNLGLKVLLDFH-----YSDFWV 125
Cdd:cd19608    16 YGSPEAARSLDRLKALGANWVSLvpTWYQDTATSSTISpDPGSTPSDEDLIAAIRAAHARGLKVMLKPHldvqdPGSWRG 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672826828 126 DPGKQNLPKAWqgltFEEMNTALYDYTKnvLSEmkQLDVypDMVQIGNELNSgMLWPYGKSWgegggefDRLaaflksgI 205
Cdd:cd19608    96 DINPPDDWDAW----FASYRRFILHYAD--LAE--ENGV--ELFCIGTELVS-LTEDYEDRW-------RAL-------I 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672826828 206 QAVRDtqpkttpvmlhLADGGDTGAFTWWFDEITsrgVSF----DLIGVSYYP-----------YWHGSMNELQTNMNAI 270
Cdd:cd19608   151 AEVRS-----------VYSGKLTYAANWDSEYES---VPFwdalDYIGVDAYFpltdkptpsveELAAGWQPILDQLEAL 216
                         250
                  ....*....|....*
gi 1672826828 271 SQRYGKEVIVVETAY 285
Cdd:cd19608   217 ADKYGKPVLFTEIGY 231
 
Name Accession Description Interval E-value
GanB COG3867
Arabinogalactan endo-1,4-beta-galactosidase [Carbohydrate transport and metabolism];
3-392 0e+00

Arabinogalactan endo-1,4-beta-galactosidase [Carbohydrate transport and metabolism];


Pssm-ID: 443076  Cd Length: 382  Bit Score: 519.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672826828   3 MGIWLRKAVLFAAVLGALGAVSKTVEASASEFIRGADISILSDMEKSGAKYYEDD-ISKDALEILKNNGVNYVRLRLWQD 81
Cdd:COG3867     1 MKKLTIARILLLLGLLLLACASNPAAKEAADFIKGADLSYLNEMEDCGGKFYDEDgVPKDPLQILKDHGVNLVRLRLWVD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672826828  82 PYNSNgeSYGAGTNDLETTIDLAKRAKNLGLKVLLDFHYSDFWVDPGKQNLPKAWQGLTFEEMNTALYDYTKNVLSEMKQ 161
Cdd:COG3867    81 PYWAA--PYGGGYNDLADVLAMAKRAKAAGMKVLLDFHYSDFWADPGKQNKPKAWANLSFDQLKDAVYDYTYDVLTALKA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672826828 162 LDVYPDMVQIGNELNSGMLWPYGKSWgEGGGEFDRLAAFLKSGIQAVRDT-QPKTTPVMLHLADGGDTGAFTWWFDEITS 240
Cdd:COG3867   159 AGLLPDMVQVGNEINNGMLWPDGKTE-QGPGNWDRLAALLNAGIRAVRDVaASPDIKVMLHLAQGGNNGLFRWWFDNLTK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672826828 241 RGVSFDLIGVSYYPYWH-GSMNELQTNMNAISQRYGKEVIVVETAYGHTTANADTMPNAFGEAEAAAGGYEPTPTGQAEY 319
Cdd:COG3867   238 RGVDFDVIGLSYYPYWHtGSLDDLGANLNDLASRYGKDVMVVETAYPWTLENGDGAPNIFGTDDPYAGGYPATPQGQADF 317
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1672826828 320 LLDLADRIQAVPNNRGAGFFYWEPLWY-NGNVSWATQagmnylsvqstmGNEWDNQAMFDFAGNALPSLRAFKQ 392
Cdd:COG3867   318 LRDLIQAVKAVPNGGGLGVFYWEPAWIpVPGTGWAGE------------GSSWENQALFDFDGKALPALDAFKA 379
Glyco_hydro_53 pfam07745
Glycosyl hydrolase family 53; This domain belongs to family 53 of the glycosyl hydrolase ...
35-390 1.60e-135

Glycosyl hydrolase family 53; This domain belongs to family 53 of the glycosyl hydrolase classification. These enzymes are enzymes are endo-1,4- beta-galactanases (EC:3.2.1.89). The structure of this domain is known and has a TIM barrel fold.


Pssm-ID: 311610  Cd Length: 333  Bit Score: 396.39  E-value: 1.60e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672826828  35 IRGADISILSDMEKSGAKYYEDD-ISKDALEILKNNGVNYVRLRLWQDPYnsngesyGAGTNDLETTIDLAKRAKNLGLK 113
Cdd:pfam07745   1 IKGADISSLNELENAGVTFYNTNgKTQDLFQILKDHGVNSVRLRVWNDPY-------DGGNNDLDDVLKIAKRAKAAGMK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672826828 114 VLLDFHYSDFWVDPGKQNLPKAWQGLTFEEMNTALYDYTKNVLSEMKQLDVYPDMVQIGNELNSGMLWPYGKSwgeggGE 193
Cdd:pfam07745  74 VLLDFHYSDTWADPGKQTKPKAWASLDTDQLKKALYNYTYDVLNALKEAGIDPDMVQVGNEINSGFLWPDGKT-----PN 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672826828 194 FDRLAAFLKSGIQAVRDTQPkTTPVMLHLADGGDTGAFTWWFDEITSRGVSFDLIGVSYYPYWHGSMNELQTNMNAISQR 273
Cdd:pfam07745 149 WDNMAKLLNSGIKAVREVSP-NIKVAIHLANGENNGLYRWWFDNLTKAGVDFDVIGVSYYPFWSGTLENLTTNLKDMASR 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672826828 274 YGKEVIVVETAYGHTTANADTMPNAFGEAEAAAGGYEPTPTGQAEYLLDLADRIQAVPNNRGAGFFYWEPLWYNGNVSWA 353
Cdd:pfam07745 228 YGKDVMVVETAYPWTLDDGDGHGNLDPETSSLTSGYPATPQGQATMLRDVIELVNAVPGSRGLGVFYWEPAWIPVGDAGL 307
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1672826828 354 TQAgmnylsvqstmGNEWDNQAMFDFAGNALPSLRAF 390
Cdd:pfam07745 308 WGG-----------GSSWDNQALFDFNGRALPSLNVF 333
GH113_mannanase-like cd19608
Glycoside hydrolase family 113 beta-1,4-mannanase and similar proteins; Mannan endo-1,4-beta ...
54-285 3.67e-04

Glycoside hydrolase family 113 beta-1,4-mannanase and similar proteins; Mannan endo-1,4-beta mannosidase (E.C 3.2.1.78) randomly cleaves (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans and is also called beta-1,4-mannanase, endo-1,4-beta-mannanase, endo-beta-1,4-mannase, beta-mannanase B, beta-1, 4-mannan 4-mannanohydrolase, endo-beta-mannanase, beta-D-mannanase, 1,4-beta-D-mannan mannanohydrolase, and 4-beta-D-mannan mannanohydrolase. (1->4)-beta-linked mannans are polysaccharides with a linear polymer backbone of (1->4)-beta-linked mannose units (in plants and fungi) or alternating mannose and glucose/galactose units (glucomannan in plants and fungi, and galactomannan and galactoglucomannan in plants), such as in the hemicellulose fraction of hard- and softwoods. Complete degradation of mannan requires a series of enzymes, including beta-1,4-mannanase. According to the CAZy database beta-1,4-mannanases are grouped into various glycoside hydrolase (GH) families; GH family 113 beta-1,4-mannanases include mostly bacterial and archaeal sequences.


Pssm-ID: 381626  Cd Length: 310  Bit Score: 42.75  E-value: 3.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672826828  54 YEDDISKDALEILKNNGVNYVRL--RLWQDPYNSNGES-YGAGTNDLETTIDLAKRAKNLGLKVLLDFH-----YSDFWV 125
Cdd:cd19608    16 YGSPEAARSLDRLKALGANWVSLvpTWYQDTATSSTISpDPGSTPSDEDLIAAIRAAHARGLKVMLKPHldvqdPGSWRG 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672826828 126 DPGKQNLPKAWqgltFEEMNTALYDYTKnvLSEmkQLDVypDMVQIGNELNSgMLWPYGKSWgegggefDRLaaflksgI 205
Cdd:cd19608    96 DINPPDDWDAW----FASYRRFILHYAD--LAE--ENGV--ELFCIGTELVS-LTEDYEDRW-------RAL-------I 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1672826828 206 QAVRDtqpkttpvmlhLADGGDTGAFTWWFDEITsrgVSF----DLIGVSYYP-----------YWHGSMNELQTNMNAI 270
Cdd:cd19608   151 AEVRS-----------VYSGKLTYAANWDSEYES---VPFwdalDYIGVDAYFpltdkptpsveELAAGWQPILDQLEAL 216
                         250
                  ....*....|....*
gi 1672826828 271 SQRYGKEVIVVETAY 285
Cdd:cd19608   217 ADKYGKPVLFTEIGY 231
 
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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