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Conserved domains on  [gi|504695488|ref|WP_014882590|]
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MULTISPECIES: polysaccharide deacetylase family protein [Enterobacter]

Protein Classification

polysaccharide deacetylase family protein( domain architecture ID 10181050)

polysaccharide deacetylase family protein belonging to the carbohydrate esterase 4 (CE4) superfamily, may catalyze the N- or O-deacetylation of substrates such as acetylated chitin, peptidoglycan, and acetylated xylan; similar to Escherichia coli YadE

CATH:  3.20.20.370
CAZY:  CE4
EC:  3.-.-.-
Gene Ontology:  GO:0005975|GO:0046872|GO:0016787
PubMed:  12644381
SCOP:  3001025

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CE4_yadE_5s cd10966
Putative catalytic polysaccharide deacetylase domain of uncharacterized protein yadE and ...
 236-405 1.65e-67

Putative catalytic polysaccharide deacetylase domain of uncharacterized protein yadE and similar proteins; This family contains an uncharacterized protein yadE from Escherichia coli and its bacterial homologs. Although its molecular function remains unknown, yadE shows high sequence similarity with the catalytic NodB homology domain of outer membrane lipoprotein PgaB and the surface-attached protein intercellular adhesion protein IcaB. Both PgaB and IcaB are essential in bacterial biofilm formation.


:

Pssm-ID: 213024 [Multi-domain]  Cd Length: 164  Bit Score: 211.75  E-value: 1.65e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 236 PAKAVVITFDDGLKSVSRYAYPVLKEYGFNATAFIISSRIKGHPQkwDPKSLQFMSVQEIKGIQDVFDIQSHTHFLHRVD 315
Cdd:cd10966    1 PEKSVVITFDDGYKSNYEYAYPILKKYGFKATIFVIGSRIGEKPQ--DPKILQYLSIEELKEMRDVFEFQSHTYNMHRGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 316 GYKHPILLSRSYHVILFDFERSRRALSQfnprVLYLSYPFGGYDNKAIKAANDAGFHLAVTTVKGKVKPGDNPFLLKRLY 395
Cdd:cd10966   79 GTGGHGLLALSEEEILADLKKSEEILGS----SKAFAYPYGDYNDNAIEALKEAGVKLAFTTNEGKVTPGDDPYELPRVR 154

                        170
                 ....*....|
gi 504695488 396 ILRTDSLETM 405
Cdd:cd10966  155 ITGGTSLEDF 164
 
Name Accession Description Interval E-value
CE4_yadE_5s cd10966
Putative catalytic polysaccharide deacetylase domain of uncharacterized protein yadE and ...
 236-405 1.65e-67

Putative catalytic polysaccharide deacetylase domain of uncharacterized protein yadE and similar proteins; This family contains an uncharacterized protein yadE from Escherichia coli and its bacterial homologs. Although its molecular function remains unknown, yadE shows high sequence similarity with the catalytic NodB homology domain of outer membrane lipoprotein PgaB and the surface-attached protein intercellular adhesion protein IcaB. Both PgaB and IcaB are essential in bacterial biofilm formation.


Pssm-ID: 213024 [Multi-domain]  Cd Length: 164  Bit Score: 211.75  E-value: 1.65e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 236 PAKAVVITFDDGLKSVSRYAYPVLKEYGFNATAFIISSRIKGHPQkwDPKSLQFMSVQEIKGIQDVFDIQSHTHFLHRVD 315
Cdd:cd10966    1 PEKSVVITFDDGYKSNYEYAYPILKKYGFKATIFVIGSRIGEKPQ--DPKILQYLSIEELKEMRDVFEFQSHTYNMHRGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 316 GYKHPILLSRSYHVILFDFERSRRALSQfnprVLYLSYPFGGYDNKAIKAANDAGFHLAVTTVKGKVKPGDNPFLLKRLY 395
Cdd:cd10966   79 GTGGHGLLALSEEEILADLKKSEEILGS----SKAFAYPYGDYNDNAIEALKEAGVKLAFTTNEGKVTPGDDPYELPRVR 154

                        170
                 ....*....|
gi 504695488 396 ILRTDSLETM 405
Cdd:cd10966  155 ITGGTSLEDF 164
deacetyl_PgaB TIGR03938
poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB; Two well-characterized systems ...
 174-413 1.64e-28

poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB; Two well-characterized systems produce polysaccharide based on N-acetyl-D-glucosamine in straight chains with beta-1,6 linkages. These are encoded by the icaADBC operon in Staphylococcus species, where the system is designated polysaccharide intercellular adhesin (PIA), and the pgaABCD operon in Gram-negative bacteria such as E. coli. Both systems include a putative polysaccharide deacetylase. The PgaB protein, described here, contains an additional domain lacking from its Gram-positive counterpart IcaB (TIGR03933). Deacetylation by this protein appears necessary to allow export through the porin PgaA [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 274867  Cd Length: 619  Bit Score: 117.80  E-value: 1.64e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488  174 NGIPVLTYHHIlrdEENTRFRHTSTTTSVRAFSNQMTWLRDQGYATLTMYQLEGYVRNKMNLPAKAVVITFDDGLKSVSR 253
Cdd:TIGR03938   1 NTFVVLCYHDV---RDDSAADQDPYAVSTDALIEHFNWLRQNGYHPVSVDQILDARRGGKPLPEKAVLLTFDDGYRSFYT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488  254 YAYPVLKEYGFNATAFIISSRIK---GHPQKWDPKSL---QFMSVQEIKGIQD--VFDIQSHTHFLHR-----VDGYKHP 320
Cdd:TIGR03938  78 RVFPLLKAYNYPAVLALVGSWLDtpaNQKVDYGGEKLprdRFLTWEQIREMQAsgLVEIASHTYDLHHgilanPQGNELP 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488  321 ILLSRSYHV--------------ILFDFERSRRALSQF---NPRVLYlsYPFGGYDNKAIKAANDAGFHLAVTTVKGKVK 383
Cdd:TIGR03938 158 AATTRAYDPatgryetdaeyrqrIRDDLKKSSALIKKYtgkAPRVMV--WPYGAYNGTAIKIAKELGMPVALTLDDGPNT 235

                         250       260       270
                  ....*....|....*....|....*....|
gi 504695488  384 PGDNPFLLKRLYILRTDSLETMSRLISNQP 413
Cdd:TIGR03938 236 VDDPLNALRRILVDNNPSLEDLARELRNVQ 265
Polysacc_deac_1 pfam01522
Polysaccharide deacetylase; This domain is found in polysaccharide deacetylase. This family of ...
 232-374 7.82e-27

Polysaccharide deacetylase; This domain is found in polysaccharide deacetylase. This family of polysaccharide deacetylases includes NodB (nodulation protein B from Rhizobium) which is a chitooligosaccharide deacetylase. It also includes chitin deacetylase from yeast, and endoxylanases which hydrolyses glucosidic bonds in xylan.


Pssm-ID: 426305 [Multi-domain]  Cd Length: 124  Bit Score: 103.85  E-value: 7.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488  232 KMNLPAKAVVITFDDGLKSVSRYAYPVLKEYGFNATAFIISSRIKGHPqkwdpkslqfmsvQEIKGIQDV-FDIQSHThf 310
Cdd:pfam01522   1 KGPTPKKVVALTFDDGPSENTPAILDVLKKYGVKATFFVIGGNVERYP-------------DLVKRMVEAgHEIGNHT-- 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504695488  311 lhrvdgYKHPILLSRSYHVILFDFERSRRALSQ-FNPRVLYLSYPFGGYDNKAIKAANDAGFHLA 374
Cdd:pfam01522  66 ------WSHPNLTGLSPEEIRKEIERAQDALEKaTGKRPRLFRPPYGSYNDTVLEVAKKLGYTAV 124
CDA1 COG0726
Peptidoglycan/xylan/chitin deacetylase, PgdA/NodB/CDA1 family [Carbohydrate transport and ...
 219-377 1.31e-26

Peptidoglycan/xylan/chitin deacetylase, PgdA/NodB/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440490 [Multi-domain]  Cd Length: 195  Bit Score: 105.51  E-value: 1.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 219 TLTMYQLEGYVRNKmNLPAKAVVITFDDGLKSVSRYAYPVLKEYGFNATAFIISSRIKGHPQKwdpkslqfmsVQEIkgI 298
Cdd:COG0726    2 VLSLDELLPALRWG-PLPKKAVALTFDDGPREGTPRLLDLLKKYGVKATFFVVGSAVERHPEL----------VREI--A 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 299 QDVFDIQSHThflhrvdgYKHPILLSRSYHVILFDFERSRRALSQ-FNPRVLYLSYPFGGYDNKAIKAANDAGFHLAVTT 377
Cdd:COG0726   69 AAGHEIGNHT--------YTHPDLTKLSEEEERAEIARAKEALEElTGKRPRGFRPPYGRYSPETLDLLAELGYRYILWD 140
hmsF PRK14581
outer membrane N-deacetylase; Provisional
 174-413 1.49e-13

outer membrane N-deacetylase; Provisional


Pssm-ID: 184753 [Multi-domain]  Cd Length: 672  Bit Score: 72.32  E-value: 1.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 174 NGIPVLTYHHILRDEENTRFrhtsttTSVR--AFSNQMTWLRDQGYATLTMYQLEGYVRNKMNLPAKAVVITFDDGLKSV 251
Cdd:PRK14581  47 NTFVVIAYHDVEDDSADQRY------LSVRssALNEQFVWLRDNGYHVVSVDQILAARNGGPTLPDKAVLLTFDDGYSSF 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 252 SRYAYPVLKEYGFNATAFIISSRIKGHP-QKWDPKSL-----QFMSVQEIKGIQD--VFDIQSHTHFLH-----RVDGYK 318
Cdd:PRK14581 121 YRRVYPLLKAYKWSAVLAPVGTWIDTATdKKVDFGGLstdrdRFATWKQITEMSKsgLVEIGAHTYASHygviaNPQGNT 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 319 HPILLSRSYHVILFDFE-------RSRRALSQFNPRVLYLS--------YPFGGYDNKAIKAANDAGFHLAVTtvkgkVK 383
Cdd:PRK14581 201 EPAAANLQYDPKTKQYEtveafkqRMEKDVALITQRIVQATgkqprvwvWPYGAPNGTVLNILRQHGYQLAMT-----LD 275

                        250       260       270
                 ....*....|....*....|....*....|.
gi 504695488 384 PGdnpfllkrlyILRTDSLETMSR-LISNQP 413
Cdd:PRK14581 276 PG----------VANINDLMNIPRiLISNNP 296
 
Name Accession Description Interval E-value
CE4_yadE_5s cd10966
Putative catalytic polysaccharide deacetylase domain of uncharacterized protein yadE and ...
 236-405 1.65e-67

Putative catalytic polysaccharide deacetylase domain of uncharacterized protein yadE and similar proteins; This family contains an uncharacterized protein yadE from Escherichia coli and its bacterial homologs. Although its molecular function remains unknown, yadE shows high sequence similarity with the catalytic NodB homology domain of outer membrane lipoprotein PgaB and the surface-attached protein intercellular adhesion protein IcaB. Both PgaB and IcaB are essential in bacterial biofilm formation.


Pssm-ID: 213024 [Multi-domain]  Cd Length: 164  Bit Score: 211.75  E-value: 1.65e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 236 PAKAVVITFDDGLKSVSRYAYPVLKEYGFNATAFIISSRIKGHPQkwDPKSLQFMSVQEIKGIQDVFDIQSHTHFLHRVD 315
Cdd:cd10966    1 PEKSVVITFDDGYKSNYEYAYPILKKYGFKATIFVIGSRIGEKPQ--DPKILQYLSIEELKEMRDVFEFQSHTYNMHRGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 316 GYKHPILLSRSYHVILFDFERSRRALSQfnprVLYLSYPFGGYDNKAIKAANDAGFHLAVTTVKGKVKPGDNPFLLKRLY 395
Cdd:cd10966   79 GTGGHGLLALSEEEILADLKKSEEILGS----SKAFAYPYGDYNDNAIEALKEAGVKLAFTTNEGKVTPGDDPYELPRVR 154

                        170
                 ....*....|
gi 504695488 396 ILRTDSLETM 405
Cdd:cd10966  155 ITGGTSLEDF 164
CE4_NodB_like_5s_6s cd10918
Putative catalytic NodB homology domain of PgaB, IcaB, and similar proteins which consist of a ...
 239-396 3.94e-49

Putative catalytic NodB homology domain of PgaB, IcaB, and similar proteins which consist of a deformed (beta/alpha)8 barrel fold with 5- or 6-strands; This family belongs to the large and functionally diverse carbohydrate esterase 4 (CE4) superfamily, whose members show strong sequence similarity with some variability due to their distinct carbohydrate substrates. It includes bacterial poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB, hemin storage system HmsF protein in gram-negative species, intercellular adhesion proteins IcaB, and many uncharacterized prokaryotic polysaccharide deacetylases. It also includes a putative polysaccharide deacetylase YxkH encoded by the Bacillus subtilis yxkH gene, which is one of six polysaccharide deacetylase gene homologs present in the Bacillus subtilis genome. Sequence comparison shows all family members contain a conserved domain similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, which consists of a deformed (beta/alpha)8 barrel fold with 6 or 7 strands. However, in this family, most proteins have 5 strands and some have 6 strands. Moreover, long insertions are found in many family members, whose function remains unknown.


Pssm-ID: 213023 [Multi-domain]  Cd Length: 157  Bit Score: 163.92  E-value: 3.94e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 239 AVVITFDDGLKSVSRYAYPVLKEYGFNATAFIISSRIKGHPQKWD--PKSLQFMSVQEIKGIQD-VFDIQSHTHflhrvd 315
Cdd:cd10918    1 PVVLTFDDGYRDNYTYALPILKKYGLPATFFVITGYIGGGNPWWApaPPRPPYLTWDQLRELAAsGVEIGSHTH------ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 316 gyKHPILLSRSYHVILFDFERSRRALSQ-FNPRVLYLSYPFGGYDNKAIKAANDAGFHLAVTTVKGKVKPGDNPFLLKRL 394
Cdd:cd10918   75 --THPDLTTLSDEELRRELAESKERLEEeLGKPVRSFAYPYGRYNPRVIAALKEAGYKAAFTTDPGLNSPGDDPYALPRI 152


                 ..
gi 504695488 395 YI 396
Cdd:cd10918  153 NV 154
CE4_Ecf1_like_5s cd10969
Putative catalytic NodB homology domain of a hypothetical protein Ecf1 from Escherichia coli ...
 205-411 6.38e-43

Putative catalytic NodB homology domain of a hypothetical protein Ecf1 from Escherichia coli and similar proteins; This family contains a hypothetical protein Ecf1 from Escherichia coli and its prokaryotic homologs. Although their biochemical properties remain to be determined, members in this family contain a conserved domain with a 5-stranded beta/alpha barrel, which is similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, belonging to the larger carbohydrate esterase 4 (CE4) superfamily.


Pssm-ID: 213026 [Multi-domain]  Cd Length: 218  Bit Score: 149.74  E-value: 6.38e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 205 FSNQMTWLRDQGYATLTMYQLEGYVRNKMNLPAKAVVITFDDGLKSVSRYAYPVLKEYGFNATAFIISSRIKGHPQK--- 281
Cdd:cd10969    4 FEEQLKYLKKNGYRTLSLEELLAFLKGGKPLPKKSVLITFDDGYLDNYVYAYPILKKYGLKATIFVVTGFIDEASGVrpt 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 282 ----WDP-------------KSLQFMSVQEIKGIQD--VFDIQSHTHflhrvdgykhpillsrsYHV-ILFDFERSRRAL 341
Cdd:cd10969   84 lfdyWSGdmpeankifflkgRDEVFLSWEELREMEDsgVFDIQSHSH-----------------SHTrVEYELEESKRLL 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504695488 342 SQ-FNPRVLYLSYPFGGYDNKAIKAANDAGFHLAVTTVKGKVKPGDNPFLLKRLYILRTDSLETMSRLISN 411
Cdd:cd10969  147 EEnLGKKVDHFCWPWGHYSPESLRIAKELGFKFFFTTKKGVNVPGEDPDRIKRITVKKDGGFWLKKRLFLF 217
deacetyl_PgaB TIGR03938
poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB; Two well-characterized systems ...
 174-413 1.64e-28

poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB; Two well-characterized systems produce polysaccharide based on N-acetyl-D-glucosamine in straight chains with beta-1,6 linkages. These are encoded by the icaADBC operon in Staphylococcus species, where the system is designated polysaccharide intercellular adhesin (PIA), and the pgaABCD operon in Gram-negative bacteria such as E. coli. Both systems include a putative polysaccharide deacetylase. The PgaB protein, described here, contains an additional domain lacking from its Gram-positive counterpart IcaB (TIGR03933). Deacetylation by this protein appears necessary to allow export through the porin PgaA [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 274867  Cd Length: 619  Bit Score: 117.80  E-value: 1.64e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488  174 NGIPVLTYHHIlrdEENTRFRHTSTTTSVRAFSNQMTWLRDQGYATLTMYQLEGYVRNKMNLPAKAVVITFDDGLKSVSR 253
Cdd:TIGR03938   1 NTFVVLCYHDV---RDDSAADQDPYAVSTDALIEHFNWLRQNGYHPVSVDQILDARRGGKPLPEKAVLLTFDDGYRSFYT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488  254 YAYPVLKEYGFNATAFIISSRIK---GHPQKWDPKSL---QFMSVQEIKGIQD--VFDIQSHTHFLHR-----VDGYKHP 320
Cdd:TIGR03938  78 RVFPLLKAYNYPAVLALVGSWLDtpaNQKVDYGGEKLprdRFLTWEQIREMQAsgLVEIASHTYDLHHgilanPQGNELP 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488  321 ILLSRSYHV--------------ILFDFERSRRALSQF---NPRVLYlsYPFGGYDNKAIKAANDAGFHLAVTTVKGKVK 383
Cdd:TIGR03938 158 AATTRAYDPatgryetdaeyrqrIRDDLKKSSALIKKYtgkAPRVMV--WPYGAYNGTAIKIAKELGMPVALTLDDGPNT 235

                         250       260       270
                  ....*....|....*....|....*....|
gi 504695488  384 PGDNPFLLKRLYILRTDSLETMSRLISNQP 413
Cdd:TIGR03938 236 VDDPLNALRRILVDNNPSLEDLARELRNVQ 265
Polysacc_deac_1 pfam01522
Polysaccharide deacetylase; This domain is found in polysaccharide deacetylase. This family of ...
 232-374 7.82e-27

Polysaccharide deacetylase; This domain is found in polysaccharide deacetylase. This family of polysaccharide deacetylases includes NodB (nodulation protein B from Rhizobium) which is a chitooligosaccharide deacetylase. It also includes chitin deacetylase from yeast, and endoxylanases which hydrolyses glucosidic bonds in xylan.


Pssm-ID: 426305 [Multi-domain]  Cd Length: 124  Bit Score: 103.85  E-value: 7.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488  232 KMNLPAKAVVITFDDGLKSVSRYAYPVLKEYGFNATAFIISSRIKGHPqkwdpkslqfmsvQEIKGIQDV-FDIQSHThf 310
Cdd:pfam01522   1 KGPTPKKVVALTFDDGPSENTPAILDVLKKYGVKATFFVIGGNVERYP-------------DLVKRMVEAgHEIGNHT-- 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504695488  311 lhrvdgYKHPILLSRSYHVILFDFERSRRALSQ-FNPRVLYLSYPFGGYDNKAIKAANDAGFHLA 374
Cdd:pfam01522  66 ------WSHPNLTGLSPEEIRKEIERAQDALEKaTGKRPRLFRPPYGSYNDTVLEVAKKLGYTAV 124
CDA1 COG0726
Peptidoglycan/xylan/chitin deacetylase, PgdA/NodB/CDA1 family [Carbohydrate transport and ...
 219-377 1.31e-26

Peptidoglycan/xylan/chitin deacetylase, PgdA/NodB/CDA1 family [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440490 [Multi-domain]  Cd Length: 195  Bit Score: 105.51  E-value: 1.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 219 TLTMYQLEGYVRNKmNLPAKAVVITFDDGLKSVSRYAYPVLKEYGFNATAFIISSRIKGHPQKwdpkslqfmsVQEIkgI 298
Cdd:COG0726    2 VLSLDELLPALRWG-PLPKKAVALTFDDGPREGTPRLLDLLKKYGVKATFFVVGSAVERHPEL----------VREI--A 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 299 QDVFDIQSHThflhrvdgYKHPILLSRSYHVILFDFERSRRALSQ-FNPRVLYLSYPFGGYDNKAIKAANDAGFHLAVTT 377
Cdd:COG0726   69 AAGHEIGNHT--------YTHPDLTKLSEEEERAEIARAKEALEElTGKRPRGFRPPYGRYSPETLDLLAELGYRYILWD 140
CE4_IcaB_5s cd10965
Putative catalytic polysaccharide deacetylase domain of bacterial intercellular adhesion ...
 236-404 8.84e-22

Putative catalytic polysaccharide deacetylase domain of bacterial intercellular adhesion protein IcaB and similar proteins; The family is represented by the surface-attached protein intercellular adhesion protein IcaB (Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase, EC 3.5.1.-), encoded by Staphylococcus epidermidis icaB gene from the icaABC gene cluster that is involved in the synthesis of polysaccharide intercellular adhesin (PIA), which is located mainly on the cell surface. IcaB is a secreted, cell wall-associated protein that plays a crucial role in exopolysaccharide modification in bacterial biofilm formation. It catalyzes the N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine (PNAG, also referred to as PIA), a biofilm adhesin polysaccharide. IcaB shows high homology to the N-terminal NodB homology domain of Escherichia coli PgaB. At this point, they are classified in the same family.


Pssm-ID: 200587 [Multi-domain]  Cd Length: 172  Bit Score: 91.68  E-value: 8.84e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 236 PAKAVVITFDDGLKSVSRYAYPVLKEYGFNATAFIISSRIkghpqKWDPKSLQFMSVQEIKGIQD--VFDIQSHTHFLHR 313
Cdd:cd10965    1 PGKYVVITFDDVDQTVYDNAFPILKKLKIPFTQFVITGQV-----GSTNFGLNLATWSQIKEMVAsgLVTFGLHTNDLHY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 314 VDGYKHPILLSRSYHVILFDFERSRRALSQ---FNPRvlYLSYPFGGYDNKAIKAANDAGFHLAVTTVKGKVKPGDNPFL 390
Cdd:cd10965   76 LVKDKKKLFTPASYSRFAEDYAKSQKCLKEklgKKTR--YFAYPYGEGNKDTQKILKKQGIQYGFTLRDKVVTNDSDNYR 153

                        170
                 ....*....|....
gi 504695488 391 LKRLyILRTDSLET 404
Cdd:cd10965  154 IPRI-LVTNDSFWK 166
CE4_DAC_u1_6s cd10970
Putative catalytic NodB homology domain of uncharacterized prokaryotic polysaccharide ...
 239-409 1.92e-19

Putative catalytic NodB homology domain of uncharacterized prokaryotic polysaccharide deacetylases which consist of a 6-stranded beta/alpha barrel; This family contains uncharacterized prokaryotic polysaccharide deacetylases. Although their biological functions remain unknown, all members of the family contain a conserved domain with a 6-stranded beta/alpha barrel, which is similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, belonging to the larger carbohydrate esterase 4 (CE4) superfamily.


Pssm-ID: 213027 [Multi-domain]  Cd Length: 194  Bit Score: 85.83  E-value: 1.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 239 AVVITFDDGLKSVSRYAYPVLKEYGFNATAFIISSRIkGHPqkwdpkslQFMSVQEIKGIQDV-FDIQSHTHflhrvdgy 317
Cdd:cd10970    2 KVSLTFDDGYESQYTTAFPILQEYGIPATAAVIPDSI-GSS--------GRLTLDQLRELQDAgWEIASHTL-------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 318 KHPILLSRSYHVILFDFERSRRALSQ--FNPRVLYLSYPFGGYDNKAIKAANDAGFHLAVTTVKGKVKPGDNPFLLKRLY 395
Cdd:cd10970   65 THTDLTELSADEQRAELTESKRWLEDngFGDGADHFAYPYGRYDDEVLELVREYYDLGRSGGGGPNGRPPLDPYRLRRVT 144

                        170
                 ....*....|....
gi 504695488 396 ILRTDSLETMSRLI 409
Cdd:cd10970  145 GEADTTTEEVKTLL 158
CE4_PgaB_5s cd10964
N-terminal putative catalytic polysaccharide deacetylase domain of bacterial poly-beta-1, ...
 235-396 2.73e-19

N-terminal putative catalytic polysaccharide deacetylase domain of bacterial poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB, and similar proteins; This family is represented by an outer membrane lipoprotein, poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase (PgaB, EC 3.5.1.-), encoded by Escherichia coli pgaB gene from the pgaABCD (formerly ycdSRQP) operon, which affects biofilm development by promoting abiotic surface binding and intercellular adhesion. PgaB catalyzes the N-deacetylation of poly-beta-1,6-N-acetyl-D-glucosamine (PGA), a biofilm adhesin polysaccharide that stabilizes biofilms of E. coli and other bacteria. PgaB contains an N-terminal NodB homology domain with a 5-stranded beta/alpha barrel, and a C-terminal carbohydrate binding domain required for PGA N-deacetylation, which may be involved in binding to unmodified poly-beta-1,6-GlcNAc and assisting catalysis by the deacetylase domain. This family also includes several orthologs of PgaB, such as the hemin storage system HmsF protein, encoded by Yersinia pestis hmsF gene from the hmsHFRS operon, which is essential for Y. pestis biofilm formation. Like PgaB, HmsF is an outer membrane protein with an N-terminal NodB homology domain, which is likely involved in the modification of the exopolysaccharide (EPS) component of the biofilm. HmsF also has a conserved but uncharacterized C-terminal domain that is present in other HmsF-like proteins in Gram-negative bacteria. This alignment model corresponds to the N-terminal NodB homology domain.


Pssm-ID: 200586 [Multi-domain]  Cd Length: 193  Bit Score: 85.09  E-value: 2.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 235 LPAKAVVITFDDGLKSVSRYAYPVLKEYGFNATAFIISSRIKGHPQK---WDPKSL---QFMSVQEIKGIQD--VFDIQS 306
Cdd:cd10964    1 LPAKAVLLTFDDGYQSFYTRVYPLLKAYKYPAVLALVGSWLETPAGKkvdYGGEQLprdRFLSWEQIREMQAsgLVEIAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 307 HTHFLHR-----VDGYKHPILLSRSYHV--------------ILFDFERSRRALSQF---NPRVLYlsYPFGGYDNKAIK 364
Cdd:cd10964   81 HSHDLHHgipanPQGNLLPAATTRQYDPktgryetdaeyrqrIRNDLKKSSALIKKHtgrAPRVMV--WPYGAYNGTLIE 158

                        170       180       190
                 ....*....|....*....|....*....|...
gi 504695488 365 AANDAGFHLAVtTVKGKVKPGDNPFL-LKRLYI 396
Cdd:cd10964  159 EAAKLGMQLTF-TLEDGANNADQSLSsIPRILV 190
CE4_DAC_u4_5s cd10973
Putative catalytic NodB homology domain of uncharacterized bacterial polysaccharide ...
 238-393 2.36e-18

Putative catalytic NodB homology domain of uncharacterized bacterial polysaccharide deacetylases which consist of a 5-stranded beta/alpha barrel; This family contains many uncharacterized bacterial polysaccharide deacetylases. Although their biological functions remain unknown, all members of the family are predicted to contain a conserved domain with a 5-stranded beta/alpha barrel, which is similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, belonging to the larger carbohydrate esterase 4 (CE4) superfamily.


Pssm-ID: 213028 [Multi-domain]  Cd Length: 157  Bit Score: 81.55  E-value: 2.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 238 KAVVITFDDGLKSVSRYAYPVLKEYGFNATAFIISSRIKGHPQKwdpkslqFMSVQEIKGI-QDVFDIQSHThflhrvdg 316
Cdd:cd10973    1 KTVVITIDDGYKSVYTNAFPILKKYGYPFTLFVYTEAIGRGYPD-------YLSWDQIREMaKYGVEIANHS-------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 317 YKHPILLSRSYHVILF-------DFERSRRAL-SQFNPRVLYLSYPFGGYDNKAIKAANDAGFHLAVTTVKGKVKPGDNP 388
Cdd:cd10973   66 YSHPHLVRLGEKMQEQwlewirqDIEKSQQRFeKELGKKPKLFAYPYGEYNPAIIKLVKEAGFEAAFQQSGGVVSAGTDL 145


                 ....*
gi 504695488 389 FLLKR 393
Cdd:cd10973  146 TALPR 150
CE4_Mlr8448_like_5s cd10968
Putative catalytic NodB homology domain of Mesorhizobium loti Mlr8448 protein and its ...
 240-394 2.71e-16

Putative catalytic NodB homology domain of Mesorhizobium loti Mlr8448 protein and its bacterial homologs; This family contains Mesorhizobium loti Mlr8448 protein and its bacterial homologs. Although their biochemical properties are yet to be determined, members in this subfamily contain a conserved domain with a 5-stranded beta/alpha barrel, which is similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, belonging to the larger carbohydrate esterase 4 (CE4) superfamily.


Pssm-ID: 213025 [Multi-domain]  Cd Length: 161  Bit Score: 75.75  E-value: 2.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 240 VVITFDDGLKSVSRYAYPVLKEYGFNATAFIISSRIKGHPQKWdPKSLQFMSVQEIKGIQ--DVFDIQSHTHflhrvdgy 317
Cdd:cd10968    3 AVLTFDDGYRDNLEFALPVFERHGVPFTIYVTTGFPDGTGELW-WLTLECLDWDELRRLAadPLVTIGAHTI-------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 318 KHPIL--LSRSyhVILFDFERSRRAL-SQFNPRVLYLSYPFGG---YDNKAIKAANDAGFHLAVTTVKGKVKPG--DNPF 389
Cdd:cd10968   74 THPNLarLSDD--EARREIAASRARLeAELGREVRHFAYPYGDrtaAGPREADLAREAGFATAVTTRPGVLFAEhrENLH 151


                 ....*
gi 504695488 390 LLKRL 394
Cdd:cd10968  152 ALPRI 156
hmsF PRK14581
outer membrane N-deacetylase; Provisional
 174-413 1.49e-13

outer membrane N-deacetylase; Provisional


Pssm-ID: 184753 [Multi-domain]  Cd Length: 672  Bit Score: 72.32  E-value: 1.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 174 NGIPVLTYHHILRDEENTRFrhtsttTSVR--AFSNQMTWLRDQGYATLTMYQLEGYVRNKMNLPAKAVVITFDDGLKSV 251
Cdd:PRK14581  47 NTFVVIAYHDVEDDSADQRY------LSVRssALNEQFVWLRDNGYHVVSVDQILAARNGGPTLPDKAVLLTFDDGYSSF 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 252 SRYAYPVLKEYGFNATAFIISSRIKGHP-QKWDPKSL-----QFMSVQEIKGIQD--VFDIQSHTHFLH-----RVDGYK 318
Cdd:PRK14581 121 YRRVYPLLKAYKWSAVLAPVGTWIDTATdKKVDFGGLstdrdRFATWKQITEMSKsgLVEIGAHTYASHygviaNPQGNT 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 319 HPILLSRSYHVILFDFE-------RSRRALSQFNPRVLYLS--------YPFGGYDNKAIKAANDAGFHLAVTtvkgkVK 383
Cdd:PRK14581 201 EPAAANLQYDPKTKQYEtveafkqRMEKDVALITQRIVQATgkqprvwvWPYGAPNGTVLNILRQHGYQLAMT-----LD 275

                        250       260       270
                 ....*....|....*....|....*....|.
gi 504695488 384 PGdnpfllkrlyILRTDSLETMSR-LISNQP 413
Cdd:PRK14581 276 PG----------VANINDLMNIPRiLISNNP 296
pgaB PRK14582
poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB;
174-415 9.67e-12

poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase PgaB;


Pssm-ID: 184754 [Multi-domain]  Cd Length: 671  Bit Score: 66.71  E-value: 9.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 174 NGIPVLTYHHILRDEENTRFrhtsttTSVR--AFSNQMTWLRDQGYATLTMYQLEGYVRNKMNLPAKAVVITFDDGLKSV 251
Cdd:PRK14582  47 NGFVAIAYHDVEDEAADQRF------MSVRtsALREQFAWLRENGYQPVSVAQILEAHRGGKPLPEKAVLLTFDDGYSSF 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 252 SRYAYPVLKEYGFNATAFIISSRI---KGHPQKWD----PKSlQFMSVQEIKGIQD--VFDIQSHTHFLHR-----VDGY 317
Cdd:PRK14582 121 YTRVFPILQAFQWPAVWAPVGSWVdtpADQPVKFGgemvPRE-YFATWQQVREVARsrLVEIASHTWNSHYgiqanPQGS 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 318 KHPILLSRSYHVILFDFE-----RSR------------RALSQFNPRVLYlsYPFGGYDNKAIKAANDAGFHLAVTTVKG 380
Cdd:PRK14582 200 LLPAAVNRAYFTDHARYEtaaeyRERirldavkmteyiRTKAGKNPRVWV--WPYGEANGIALEELKKLGYDMAFTLESG 277

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 504695488 381 kvkPGDnpfllkrlyilrTDSLETMSR-LISNQPQG 415
Cdd:PRK14582 278 ---LAN------------ASQLDSIPRvLIANNPSL 298
CE4_DAC_u2_5s cd10971
Putative catalytic NodB homology domain of uncharacterized prokaryotic polysaccharide ...
 239-394 6.02e-09

Putative catalytic NodB homology domain of uncharacterized prokaryotic polysaccharide deacetylases which consist of a 5-stranded beta/alpha barrel; This family contains many uncharacterized prokaryotic polysaccharide deacetylases. Although their biological functions remain unknown, all members of this family are predicted to contain a conserved domain with a 5-stranded beta/alpha barrel, which is similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, belonging to the larger carbohydrate esterase 4 (CE4) superfamily.


Pssm-ID: 200593 [Multi-domain]  Cd Length: 198  Bit Score: 55.39  E-value: 6.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 239 AVVITFDDGLKSVSRYAYPVLKEYGF-------------------NATAFIIssRIKGHPQKWDP-KSLQFMSVQEIKGI 298
Cdd:cd10971    1 AILLTFDDGYKDHYTYVLPELEERGIqgsffvpakpveehkvldvNKIHFIL--FIKRLLQYELPeKLRTEILDKLFKKY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 299 QDVfdiqSHTHF-------------LHR------VDGYKHPILLSRSYHVILFDFERSRRALSQF--NPRVLYLSYPFGG 357
Cdd:cd10971   79 VDI----SEEAFakelymtkdqikqLERagmhigSHGYDHYWLGRLSPEEQEAEIKKSLKFLSEVggGHDRWTFCYPYGS 154

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 504695488 358 YDNKAIKAANDAGFHLAVTTVKGKVK-PGDNPFLLKRL 394
Cdd:cd10971  155 FNEETLEILKENGCRLGFTTEVAIADlDDLEPLELPRY 192
CE4_GLA_like_6s cd10967
Putative catalytic NodB homology domain of gellan lyase and similar proteins; This family is ...
 238-403 1.10e-08

Putative catalytic NodB homology domain of gellan lyase and similar proteins; This family is represented by the extracellular polysaccharide-degrading enzyme, gellan lyase (gellanase, EC 4.2.2.-), from Bacillus sp. The enzyme acts on gellan exolytically and releases a tetrasaccharide of glucuronyl-glucosyl-rhamnosyl-glucose with unsaturated glucuronic acid at the nonreducing terminus. The family also includes many uncharacterized prokaryotic polysaccharide deacetylases, which show high sequence similarity to Bacillus sp. gellan lyase. Although their biological functions remain unknown, all members of the family contain a conserved domain with a 6-stranded beta/alpha barrel, which is similar to the catalytic NodB homology domain of rhizobial NodB-like proteins, belonging to the larger carbohydrate esterase 4 (CE4) superfamily.


Pssm-ID: 200589 [Multi-domain]  Cd Length: 202  Bit Score: 54.69  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 238 KAVVITFDDGLKSVSRYAyPVLKEYGFNATAFIISSRIKGHPqkwdpkslqFMSVQEIKGIQDV-FDIQSHTHFlhrvdg 316
Cdd:cd10967    1 LAVSLTFDDGYAQDLRAA-PLLAKYGLKGTFFVNSGLLGRRG---------YLDLEELRELAAAgHEIGSHTVT------ 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 317 ykHPIL--LSRSYhvILFDFERSRRAL-SQFNPRVLYLSYPFGGYDNKAIKAAnDAGFHLAVTTVKGKVKPGDNPFLLKR 393
Cdd:cd10967   65 --HPDLtsLPPAE--LRREIAESRAALeEIGGFPVTSFAYPFGSTNPSIVPLL-ARGFIAARGVGGGGNPPNPSDPPADP 139

                        170
                 ....*....|
gi 504695488 394 LYILRTDSLE 403
Cdd:cd10967  140 ADCHNADSLA 149
CE4_NodB_like_6s_7s cd10917
Catalytic NodB homology domain of rhizobial NodB-like proteins; This family belongs to the ...
 238-378 7.09e-07

Catalytic NodB homology domain of rhizobial NodB-like proteins; This family belongs to the large and functionally diverse carbohydrate esterase 4 (CE4) superfamily, whose members show strong sequence similarity with some variability due to their distinct carbohydrate substrates. It includes many rhizobial NodB chitooligosaccharide N-deacetylase (EC 3.5.1.-)-like proteins, mainly from bacteria and eukaryotes, such as chitin deacetylases (EC 3.5.1.41), bacterial peptidoglycan N-acetylglucosamine deacetylases (EC 3.5.1.-), and acetylxylan esterases (EC 3.1.1.72), which catalyze the N- or O-deacetylation of substrates such as acetylated chitin, peptidoglycan, and acetylated xylan. All members of this family contain a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold with 6- or 7 strands. Their catalytic activity is dependent on the presence of a divalent cation, preferably cobalt or zinc, and they employ a conserved His-His-Asp zinc-binding triad closely associated with the conserved catalytic base (aspartic acid) and acid (histidine) to carry out acid/base catalysis. Several family members show diversity both in metal ion specificities and in the residues that coordinate the metal.


Pssm-ID: 213022 [Multi-domain]  Cd Length: 171  Bit Score: 48.77  E-value: 7.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 238 KAVVITFDDG--LKSVSRYAYpVLKEYGFNATAFIISSRIKGHPQKwdpkslqfmsVQEIkgIQDVFDIQSHThflhrvd 315
Cdd:cd10917    1 KVVALTFDDGpdPEYTPKILD-ILAEYGVKATFFVVGENVEKHPDL----------VRRI--VAEGHEIGNHT------- 60

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504695488 316 gYKHPILLSRSYHVILFDFERSRRALSQ-FNPRVLYLSYPFGGYDNKAIKAANDAGFHLAVTTV 378
Cdd:cd10917   61 -YSHPDLTKLSPEEIRAEIERTQDAIEEaTGVRPRLFRPPYGAYNPEVLAAAAELGLTVVLWSV 123
CE4_CtAXE_like cd10954
Catalytic NodB homology domain of Clostridium thermocellum acetylxylan esterase and its ...
 238-367 3.79e-04

Catalytic NodB homology domain of Clostridium thermocellum acetylxylan esterase and its bacterial homologs; This family is represented by Clostridium thermocellum acetylxylan esterase (CtAXE, EC 3.1.1.72), a member of the carbohydrate esterase 4 (CE4) superfamily. CtAXE deacetylates O-acetylated xylan, a key component of plant cell walls. It shows no detectable activity on generic esterase substrates including para-nitrophenyl acetate. It is specific for sugar-based substrates and will precipitate acetylxylan, as a consequence of deacetylation. CtAXE is a monomeric protein containing a catalytic NodB homology domain with the same overall topology and a deformed (beta/alpha)8 barrel fold as other CE4 esterases. However, due to differences in the topography of the substrate-binding groove, the chemistry of the active center, and metal ion coordination, CtAXE has different metal ion preference and lacks activity on N-acetyl substrates. It is significantly activated by Co2+. Moreover, CtAXE displays distinctly different ligand coordination to the metal ion, utilizing an aspartate, a histidine, and four water molecules, as opposed to the conserved His-His-Asp zinc-binding triad of other CE4 esterases.


Pssm-ID: 200578 [Multi-domain]  Cd Length: 180  Bit Score: 41.03  E-value: 3.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 238 KAVVITFDDGlkSVSRYAYPV---LKEYGFNATAFIISSRIKGHpqkwdPKSLQFMsvqeikgIQDVFDIQSHThflhrv 314
Cdd:cd10954    1 KMVALTFDDG--PNAKYTPRLldvLEKYNVRATFFLVGQNVNGN-----KEIVKRM-------VEMGCEIGNHS------ 60

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504695488 315 dgYKHPILLSRSYHVILFDFERSRRALSQ---FNPRvlYLSYPFGGYDNKAIKAAN 367
Cdd:cd10954   61 --YTHPDLTKLSPSEIKKEIEKTNEAIKKitgKRPK--LFRPPYGAVNDTVKKAID 112
CE4_BsYlxY_like cd10950
Putative catalytic NodB homology domain of uncharacterized protein YlxY from Bacillus subtilis ...
 257-378 2.23e-03

Putative catalytic NodB homology domain of uncharacterized protein YlxY from Bacillus subtilis and its bacterial homologs; The Bacillus subtilis genome contains six polysaccharide deacetylase gene homologs: pdaA, pdaB (previously known as ybaN), yheN, yjeA, yxkH and ylxY. This family is represented by Bacillus subtilis putative polysaccharide deacetylase BsYlxY, encoded by the ylxY gene, which is a member of the carbohydrate esterase 4 (CE4) superfamily. Although its biological function still remains unknown, BsYlxY shows high sequence homology to the catalytic domain of Bacillus subtilis pdaB gene encoding a putative polysaccharide deacetylase (BsPdaB), which is essential for the maintenance of spores after the late stage of sporulation and is highly conserved in spore-forming bacteria. However, disruption of the ylxY gene in B. subtilis did not cause any sporulation defect. Moreover, the Asp residue in the classical His-His-Asp zinc-binding motif of CE4 esterases is mutated to a Val residue in this family. Other catalytically relevant residues of CE4 esterases are also not conserved, which suggest that members of this family may be inactive.


Pssm-ID: 200574 [Multi-domain]  Cd Length: 188  Bit Score: 38.80  E-value: 2.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 257 PVLKEYGFNATAFIISSRIKGHPQKwdpkslqfmsVQEIKgiQDVFDIQSHthflhrvdGYKHPILLSRSYHVILFDFER 336
Cdd:cd10950   26 TILEKHDVKATFFLEGRWAKKNPDL----------VRKIA--KDGHEIGNH--------GYSHPDPSQLSYEQNREEIRK 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 504695488 337 SRRALSQF-NPRVLYLSYPFGGYDNKAIKAANDAGFHLAVTTV 378
Cdd:cd10950   86 TNEIIEEItGEKPKLFAPPYGEFNDAVVKAAAELGMRTILWTV 128
CE4_NodB_like_3 cd10959
Catalytic NodB homology domain of uncharacterized bacterial polysaccharide deacetylases; This ...
 238-358 2.61e-03

Catalytic NodB homology domain of uncharacterized bacterial polysaccharide deacetylases; This family includes many uncharacterized bacterial polysaccharide deacetylases. Although their biological function still remains unknown, members in this family show high sequence homology to the catalytic NodB homology domain of Streptococcus pneumoniae polysaccharide deacetylase PgdA (SpPgdA), which is an extracellular metal-dependent polysaccharide deacetylase with de-N-acetylase activity toward a hexamer of chitooligosaccharide N-acetylglucosamine, but not shorter chitooligosaccharides or a synthetic peptidoglycan tetrasaccharide. Like SpPgdA, this family is a member of the carbohydrate esterase 4 (CE4) superfamily.


Pssm-ID: 200582 [Multi-domain]  Cd Length: 187  Bit Score: 38.74  E-value: 2.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695488 238 KAVVITFDDGlksvsryayP----------VLKEYGFNATAFIISSRIKGHPqkwdpkslqfmsvQEIKGIQDvfdiQSH 307
Cdd:cd10959    1 KEVALTFDDG---------PdpeytpalldLLARHGAKATFFVVGERAERHP-------------DLIRRIVD----EGH 54

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504695488 308 THFLHrvdGYKHPILLSRSYHVILFDFERSRRALSQ-FNPRVLYLSYPFGGY 358
Cdd:cd10959   55 EIGNH---GYRHRHPWLRSPWKAIRDLRRAARIIEQlTGRPPRYYRPPWGHL 103
CE4_NodB_like_2 cd10958
Catalytic NodB homology domain of uncharacterized chitin deacetylases and hypothetical ...
 238-279 6.32e-03

Catalytic NodB homology domain of uncharacterized chitin deacetylases and hypothetical proteins; This family includes some uncharacterized chitin deacetylases and hypothetical proteins, mainly from eukaryotes. Although their biological function is unknown, members in this family show high sequence homology to the catalytic NodB homology domain of Colletotrichum lindemuthianum chitin deacetylase (endo-chitin de-N-acetylase, ClCDA, EC 3.5.1.41), which catalyzes the hydrolysis of N-acetamido groups of N-acetyl-D-glucosamine residues in chitin, converting it to chitosan in fungal cell walls. Like ClCDA, this family is a member the carbohydrate esterase 4 (CE4) superfamily.


Pssm-ID: 200581 [Multi-domain]  Cd Length: 190  Bit Score: 37.66  E-value: 6.32e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 504695488 238 KAVVITFDDGLKSVSRYAYPVLKEYGFNATAFIISSRIKGHP 279
Cdd:cd10958    1 KVVALTIDDAPSPSTEEILDLLEEHNVRATFFVIGSHAPRRE 42
 
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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