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Conserved domains on  [gi|1021073398|dbj|GAT67667|]
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dioxygenase [Planomonospora sphaerica]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PcaH COG3485
Protocatechuate 3,4-dioxygenase beta subunit [Secondary metabolites biosynthesis, transport ...
 59-209 7.40e-56

Protocatechuate 3,4-dioxygenase beta subunit [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 442708  Cd Length: 171  Bit Score: 177.32  E-value: 7.40e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021073398  59 TTVAQTEGPYFKPNSP--ERDDLTAGVSGTRLVVSGYVFDRACRPLSRVLMDFWQADNSGNYDNVR-------FTLRGHL 129
Cdd:COG3485     1 ETPSQTEGPFYVDGLPlpLGADLARDAPGEPIRVTGRVLDGDGRPVAGALVEIWQADADGRYSHQDdgpldpnFNGRGRF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021073398 130 FTGADGSYRLTTIVPGLYP-----GRTRHIHVKLQAPGQSRiLTTQLYFPGEPRNNTDTIFD--PSLLMNVRTAGGVREG 202
Cdd:COG3485    81 TTDADGRYRFRTIKPGPYPipnhpGRPAHIHFSVFAPGFER-LTTQLYFPGDPYNASDPVFGvrDTLIARFEPEDGALVY 159


                  ....*..
gi 1021073398 203 TFDFVLD 209
Cdd:COG3485   160 RFDIVLQ 166
ChiA1_BD cd12214
chitin-binding domain of Chi A1-like proteins; This group contains proteins related to the ...
 228-271 1.48e-22

chitin-binding domain of Chi A1-like proteins; This group contains proteins related to the chitin binding domain of chitinase A1 (ChiA1) of Bacillus circulans WL-12. Glycosidase ChiA1 hydrolyzes chitin and is comprised of several domains: the C-terminal chitin binding domain, an N-terminal and catalytic domain, and 2 fibronectin type III-like domains. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source. Bacillus circulans WL-12 ChiA1 facilitates invasion of fungal cell walls. The ChiAi chitin binding domain is required for the specific recognition of insoluble chitin. although topologically and structurally related, ChiA1 lacks the characteristic aromatic residues of Erwinia chrysanthemi endoglucanase Z (CBD(EGZ)).


:

Pssm-ID: 213177 [Multi-domain]  Cd Length: 45  Bit Score: 87.39  E-value: 1.48e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1021073398 228 WRAGTAYAAGDRVTYGGVTYRCLQAHTAQTGWEPPNVPSLWQRA 271
Cdd:cd12214     2 WAAGTTYKAGDIVTYNGKLYRCLQAHTSLAGWEPPAVPALWQPA 45
 
Name Accession Description Interval E-value
PcaH COG3485
Protocatechuate 3,4-dioxygenase beta subunit [Secondary metabolites biosynthesis, transport ...
 59-209 7.40e-56

Protocatechuate 3,4-dioxygenase beta subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442708  Cd Length: 171  Bit Score: 177.32  E-value: 7.40e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021073398  59 TTVAQTEGPYFKPNSP--ERDDLTAGVSGTRLVVSGYVFDRACRPLSRVLMDFWQADNSGNYDNVR-------FTLRGHL 129
Cdd:COG3485     1 ETPSQTEGPFYVDGLPlpLGADLARDAPGEPIRVTGRVLDGDGRPVAGALVEIWQADADGRYSHQDdgpldpnFNGRGRF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021073398 130 FTGADGSYRLTTIVPGLYP-----GRTRHIHVKLQAPGQSRiLTTQLYFPGEPRNNTDTIFD--PSLLMNVRTAGGVREG 202
Cdd:COG3485    81 TTDADGRYRFRTIKPGPYPipnhpGRPAHIHFSVFAPGFER-LTTQLYFPGDPYNASDPVFGvrDTLIARFEPEDGALVY 159


                  ....*..
gi 1021073398 203 TFDFVLD 209
Cdd:COG3485   160 RFDIVLQ 166
intradiol_dioxygenase cd00421
Intradiol dioxygenases catalyze the critical ring-cleavage step in the conversion of ...
 77-208 1.18e-41

Intradiol dioxygenases catalyze the critical ring-cleavage step in the conversion of catecholate derivatives to citric acid cycle intermediates. This family contains catechol 1,2-dioxygenases and protocatechuate 3,4-dioxygenases which are mononuclear non-heme iron enzymes that catalyze the oxygenation of catecholates to aliphatic acids via the cleavage of aromatic rings. The members are intradiol-cleaving enzymes which break the catechol C1-C2 bond and utilize Fe3+, as opposed to the extradiol-cleaving enzymes which break the C2-C3 or C1-C6 bond and utilize Fe2+ and Mn+. Catechol 1,2-dioxygenases are mostly homodimers with one catalytic ferric ion per monomer. Protocatechuate 3,4-dioxygenases form more diverse oligomers.


Pssm-ID: 238241  Cd Length: 146  Bit Score: 140.07  E-value: 1.18e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021073398  77 DDLTAGVSGTRLVVSGYVFDRACRPLSRVLMDFWQADNSGNYDNVR-------FTLRGHLFTGADGSYRLTTIVPGLYP- 148
Cdd:cd00421     1 ADLTEDAPGEPLTLTGTVLDGDGCPVPDALVEIWQADADGRYSGQDdsgldpeFFLRGRQITDADGRYRFRTIKPGPYPi 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021073398 149 GRTRHIHVKLQAPGQSRILTTQLYFPGEPRNNTDTIFDP------SLLMNVRTAGGVREGTFDFVL 208
Cdd:cd00421    81 GRPPHIHFKVFAPGYNRRLTTQLYFPGDPLNDSDPVFAPysenvrPTLIADFDGIEFLEYRFDIVL 146
Dioxygenase_C pfam00775
Dioxygenase;
65-209 1.52e-27

Dioxygenase;


Pssm-ID: 425863 [Multi-domain]  Cd Length: 181  Bit Score: 104.48  E-value: 1.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021073398  65 EGPYFKPNSPERDDLT----AGVSGTRLVVSGYVFDRACRPLSRVLMDFWQADNSGNYDNVR------FTLRGHLFTGAD 134
Cdd:pfam00775   2 EGPLYVEGAPSDEDLArmddGDPIGEPLILSGRVFDAAGKPLAGALVEIWHANDEGRYSHFDpteapePNFRGRILTDSQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021073398 135 GSYRLTTIVPGLYPGRTR------------------HIHVKLQAPGQSRiLTTQLYFPGEPRNNTDTIFD--PSLLMNVR 194
Cdd:pfam00775  82 GSYRFRTIQPAPYPIPNDgptgklldalgrhawrpaHIHFFISAPGHRR-LTTQLYFEGDPYLPDDIAYAvrQGLVANYD 160

                         170       180
                  ....*....|....*....|
gi 1021073398 195 -----TAGGVREGTFDFVLD 209
Cdd:pfam00775 161 eredgTPEKFLEYHFDFVLD 180
ChiA1_BD cd12214
chitin-binding domain of Chi A1-like proteins; This group contains proteins related to the ...
 228-271 1.48e-22

chitin-binding domain of Chi A1-like proteins; This group contains proteins related to the chitin binding domain of chitinase A1 (ChiA1) of Bacillus circulans WL-12. Glycosidase ChiA1 hydrolyzes chitin and is comprised of several domains: the C-terminal chitin binding domain, an N-terminal and catalytic domain, and 2 fibronectin type III-like domains. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source. Bacillus circulans WL-12 ChiA1 facilitates invasion of fungal cell walls. The ChiAi chitin binding domain is required for the specific recognition of insoluble chitin. although topologically and structurally related, ChiA1 lacks the characteristic aromatic residues of Erwinia chrysanthemi endoglucanase Z (CBD(EGZ)).


Pssm-ID: 213177 [Multi-domain]  Cd Length: 45  Bit Score: 87.39  E-value: 1.48e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1021073398 228 WRAGTAYAAGDRVTYGGVTYRCLQAHTAQTGWEPPNVPSLWQRA 271
Cdd:cd12214     2 WAAGTTYKAGDIVTYNGKLYRCLQAHTSLAGWEPPAVPALWQPA 45
protocat_beta TIGR02422
protocatechuate 3,4-dioxygenase, beta subunit; This model represents the beta chain of ...
 58-185 3.74e-22

protocatechuate 3,4-dioxygenase, beta subunit; This model represents the beta chain of protocatechuate 3,4-dioxygenase. The most closely related family outside this family is that of the alpha chain (TIGR02423), typically encoded in an adjacent locus. This enzyme acts in the degradation of aromatic compounds by way of p-hydroxybenzoate to succinate and acetyl-CoA. [Energy metabolism, Other]


Pssm-ID: 131475 [Multi-domain]  Cd Length: 220  Bit Score: 91.25  E-value: 3.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021073398  58 RTTVAQTEGPYFKPNS--PERDDLTAGVSGT----RLVVSGYVFDRACRPLSRVLMDFWQADNSGNYDNVR--------- 122
Cdd:TIGR02422  25 PQSLSELTGPVFGHDDlgPIDNDLTLAHGGEpigeRIIVHGRVLDEDGRPVPNTLVEVWQANAAGRYRHKNdqylapldp 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1021073398 123 -FTLRGHLFTGADGSYRLTTIVPGLYP-------GRTRHIHVKLQAPGQSRILTTQLYFPGEPRNNTDTIF 185
Cdd:TIGR02422 105 nFGGVGRTLTDSDGYYRFRTIKPGPYPwgnhhnaWRPAHIHFSLFGTSFAQRLITQMYFEGDPLIAYDPIV 175
ChtBD3 smart00495
Chitin-binding domain type 3;
228-268 5.66e-08

Chitin-binding domain type 3;


Pssm-ID: 197760 [Multi-domain]  Cd Length: 41  Bit Score: 48.03  E-value: 5.66e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1021073398  228 WRAGTAYAAGDRVTYGGVTYRClqahTAQTGWEPPN-VPSLW 268
Cdd:smart00495   4 WQAGTVYTAGDVVSYNGKVYKA----KWWTQGEEPGsSSGPW 41
 
Name Accession Description Interval E-value
PcaH COG3485
Protocatechuate 3,4-dioxygenase beta subunit [Secondary metabolites biosynthesis, transport ...
 59-209 7.40e-56

Protocatechuate 3,4-dioxygenase beta subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442708  Cd Length: 171  Bit Score: 177.32  E-value: 7.40e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021073398  59 TTVAQTEGPYFKPNSP--ERDDLTAGVSGTRLVVSGYVFDRACRPLSRVLMDFWQADNSGNYDNVR-------FTLRGHL 129
Cdd:COG3485     1 ETPSQTEGPFYVDGLPlpLGADLARDAPGEPIRVTGRVLDGDGRPVAGALVEIWQADADGRYSHQDdgpldpnFNGRGRF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021073398 130 FTGADGSYRLTTIVPGLYP-----GRTRHIHVKLQAPGQSRiLTTQLYFPGEPRNNTDTIFD--PSLLMNVRTAGGVREG 202
Cdd:COG3485    81 TTDADGRYRFRTIKPGPYPipnhpGRPAHIHFSVFAPGFER-LTTQLYFPGDPYNASDPVFGvrDTLIARFEPEDGALVY 159


                  ....*..
gi 1021073398 203 TFDFVLD 209
Cdd:COG3485   160 RFDIVLQ 166
intradiol_dioxygenase cd00421
Intradiol dioxygenases catalyze the critical ring-cleavage step in the conversion of ...
 77-208 1.18e-41

Intradiol dioxygenases catalyze the critical ring-cleavage step in the conversion of catecholate derivatives to citric acid cycle intermediates. This family contains catechol 1,2-dioxygenases and protocatechuate 3,4-dioxygenases which are mononuclear non-heme iron enzymes that catalyze the oxygenation of catecholates to aliphatic acids via the cleavage of aromatic rings. The members are intradiol-cleaving enzymes which break the catechol C1-C2 bond and utilize Fe3+, as opposed to the extradiol-cleaving enzymes which break the C2-C3 or C1-C6 bond and utilize Fe2+ and Mn+. Catechol 1,2-dioxygenases are mostly homodimers with one catalytic ferric ion per monomer. Protocatechuate 3,4-dioxygenases form more diverse oligomers.


Pssm-ID: 238241  Cd Length: 146  Bit Score: 140.07  E-value: 1.18e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021073398  77 DDLTAGVSGTRLVVSGYVFDRACRPLSRVLMDFWQADNSGNYDNVR-------FTLRGHLFTGADGSYRLTTIVPGLYP- 148
Cdd:cd00421     1 ADLTEDAPGEPLTLTGTVLDGDGCPVPDALVEIWQADADGRYSGQDdsgldpeFFLRGRQITDADGRYRFRTIKPGPYPi 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021073398 149 GRTRHIHVKLQAPGQSRILTTQLYFPGEPRNNTDTIFDP------SLLMNVRTAGGVREGTFDFVL 208
Cdd:cd00421    81 GRPPHIHFKVFAPGYNRRLTTQLYFPGDPLNDSDPVFAPysenvrPTLIADFDGIEFLEYRFDIVL 146
1,2-CCD cd03462
chlorocatechol 1,2-dioxygenases (1,2-CCDs) (type II enzymes) are homodimeric intradiol ...
 57-209 1.16e-28

chlorocatechol 1,2-dioxygenases (1,2-CCDs) (type II enzymes) are homodimeric intradiol dioxygenases that degrade chlorocatechols via the addition of molecular oxygen and the subsequent cleavage between two adjacent hydroxyl groups. This reaction is part of the modified ortho-cleavage pathway which is a central oxidative bacterial pathway that channels chlorocatechols, derived from the degradation of chlorinated benzoic acids, phenoxyacetic acids, phenols, benzenes, and other aromatics into the energy-generating tricarboxylic acid pathway.


Pssm-ID: 239545 [Multi-domain]  Cd Length: 247  Bit Score: 109.35  E-value: 1.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021073398  57 GRTTVAQTEGPYFKPNSPERDDLTAGV---SGTRLVVSGYVFDRACRPLSRVLMDFWQADNSGNY----DNV-RFTLRGH 128
Cdd:cd03462    66 RRGSTSAIEGPYFIENAPFVDGKLKTYdddDHKPLLFRGTVKDLAGAPVAGAVIDVWHSTPDGKYsgfhPNIpEDYYRGK 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021073398 129 LFTGADGSYRLTTIVP------------------GLYPGRTRHIHVKLQAPGQsRILTTQLYFPGEPRNNTDTI--FDPS 188
Cdd:cd03462   146 IRTDEDGRYEVRTTVPvpyqipndgptgalleamGGHSWRPAHVHFKVRADGY-ETLTTQLYFEGGEWVDDDCCngVKPE 224

                         170       180
                  ....*....|....*....|.
gi 1021073398 189 LLMNVRTAGGVREGTFDFVLD 209
Cdd:cd03462   225 LILPEVKEDGVRVMTYDFVLE 245
Catechol_intradiol_dioxygenases cd03458
Catechol intradiol dioxygenases can be divided into several subgroups according to their ...
 55-208 2.80e-28

Catechol intradiol dioxygenases can be divided into several subgroups according to their substrate specificity for catechol, chlorocatechols and hydroxyquinols. Almost all members of this family are homodimers containing one ferric ion (Fe3+) per monomer. They belong to the intradiol dioxygenase family, a family of mononuclear non-heme iron intradiol-cleaving enzymes that catalyze the oxygenation of catecholates to aliphatic acids via the cleavage of aromatic rings.


Pssm-ID: 239541 [Multi-domain]  Cd Length: 256  Bit Score: 108.41  E-value: 2.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021073398  55 TPGRTTVAQTEGPYFKPNSPERD---DLTAGVS-GTRLVVSGYVFDRACRPLSRVLMDFWQADNSGNYDN-----VRFTL 125
Cdd:cd03458    68 KDTGGTESTILGPFYVAGAPEVDngaTIDDDTAdGEPLFVHGTVTDTDGKPLAGATVDVWHADPDGFYSQqdpdqPEFNL 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021073398 126 RGHLFTGADGSYRLTTIVPGLYP----G--------------RTRHIHVKLQAPGQsRILTTQLYFPGEPRNNTDTIF-- 185
Cdd:cd03458   148 RGKFRTDEDGRYRFRTIRPVPYPippdGptgellealgrhpwRPAHIHFMVSAPGY-RTLTTQIYFEGDPYLDDDAVFav 226

                         170       180       190
                  ....*....|....*....|....*....|
gi 1021073398 186 DPSLLMNVRTA-------GGVREGTFDFVL 208
Cdd:cd03458   227 KDSLIVDFVPVedgtgvpGPFAELDFDFVL 256
Dioxygenase_C pfam00775
Dioxygenase;
65-209 1.52e-27

Dioxygenase;


Pssm-ID: 425863 [Multi-domain]  Cd Length: 181  Bit Score: 104.48  E-value: 1.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021073398  65 EGPYFKPNSPERDDLT----AGVSGTRLVVSGYVFDRACRPLSRVLMDFWQADNSGNYDNVR------FTLRGHLFTGAD 134
Cdd:pfam00775   2 EGPLYVEGAPSDEDLArmddGDPIGEPLILSGRVFDAAGKPLAGALVEIWHANDEGRYSHFDpteapePNFRGRILTDSQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021073398 135 GSYRLTTIVPGLYPGRTR------------------HIHVKLQAPGQSRiLTTQLYFPGEPRNNTDTIFD--PSLLMNVR 194
Cdd:pfam00775  82 GSYRFRTIQPAPYPIPNDgptgklldalgrhawrpaHIHFFISAPGHRR-LTTQLYFEGDPYLPDDIAYAvrQGLVANYD 160

                         170       180
                  ....*....|....*....|
gi 1021073398 195 -----TAGGVREGTFDFVLD 209
Cdd:pfam00775 161 eredgTPEKFLEYHFDFVLD 180
3,4-PCD cd03459
Protocatechuate 3,4-dioxygenase (3,4-PCD) catalyzes the oxidative ring cleavage of 3, ...
 85-208 8.39e-27

Protocatechuate 3,4-dioxygenase (3,4-PCD) catalyzes the oxidative ring cleavage of 3,4-dihydroxybenzoate to produce beta-carboxy-cis,cis-muconate. 3,4-PCDs are large aggregates of 12 protomers, each composed of an alpha- and beta-subunit and an Fe3+ ion bound in the beta-subunit at the alpha-beta-subunit interface. 3,4-PCD is a member of the aromatic dioxygenases which are non-heme iron intradiol-cleaving enzymes that break the C1-C2 bond and utilize Fe3+.


Pssm-ID: 239542 [Multi-domain]  Cd Length: 158  Bit Score: 101.96  E-value: 8.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021073398  85 GTRLVVSGYVFDRACRPLSRVLMDFWQADNSGNYDNVR----------FTLRGHLFTGADGSYRLTTIVPGLYPG----- 149
Cdd:cd03459    13 GERIILEGRVLDGDGRPVPDALVEIWQADAAGRYRHPRdshrapldpnFTGFGRVLTDADGRYRFRTIKPGAYPWrngaw 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021073398 150 RTRHIHVKLQAPGQSRILTTQLYFPGEPRNNTDTIF---DP---SLLMNVRTAG-GVREGTFDFVL 208
Cdd:cd03459    93 RAPHIHVSVFARGLLERLVTRLYFPGDPANAADPVLasvPEerrETLIARRDGSdGALAYRFDIVL 158
1,2-HQD cd03461
Hydroxyquinol 1,2-dioxygenase (1,2-HQD) catalyzes the ring cleavage of hydroxyquinol (1,2, ...
 66-208 5.74e-25

Hydroxyquinol 1,2-dioxygenase (1,2-HQD) catalyzes the ring cleavage of hydroxyquinol (1,2,4-trihydroxybenzene), a intermediate in the degradation of a large variety of aromatic compounds including some polychloro- and nitroaromatic pollutants, to form 3-hydroxy-cis,cis-muconates. 1,2-HQD blongs to the aromatic dioxygenase family, a family of mononuclear non-heme intradiol-cleaving enzymes.


Pssm-ID: 239544 [Multi-domain]  Cd Length: 277  Bit Score: 100.39  E-value: 5.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021073398  66 GPYFKPNSPERD---DLTAGVSGTRLVVSGYVFDRACRPLSRVLMDFWQADNSGNYDN-----VRFTLRGHLFTGADGSY 137
Cdd:cd03461    96 GPFYREDAPEYEngaSIVQGADGEPCFVHGRVTDTDGKPLPGATVDVWQADPNGLYDVqdpdqPEFNLRGKFRTDEDGRY 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021073398 138 RLTTIVPGLYP----G--------------RTRHIHVKLQAPGQsRILTTQLYFPGEPRNNTDTIF--DPSLLMN-VRTA 196
Cdd:cd03461   176 AFRTLRPTPYPiptdGpvgkllkamgrhpmRPAHIHFMVTAPGY-RTLVTQIFDSGDPYLDSDAVFgvKDSLVVDfVPVE 254

                         170       180
                  ....*....|....*....|..
gi 1021073398 197 GGVREG----------TFDFVL 208
Cdd:cd03461   255 DDDAPGrlvpgadlelEYDFVL 276
intradiol_dioxygenase_like cd03457
Intradiol dioxygenase supgroup. Intradiol dioxygenases catalyze the critical ring-cleavage ...
 62-174 2.12e-24

Intradiol dioxygenase supgroup. Intradiol dioxygenases catalyze the critical ring-cleavage step in the conversion of catecholate derivatives to citric acid cycle intermediates. They break the catechol C1-C2 bond and utilize Fe3+, as opposed to the extradiol-cleaving enzymes which break the C2-C3 or C1-C6 bond and utilize Fe2+ and Mn+. The family contains catechol 1,2-dioxygenases and protocatechuate 3,4-dioxygenases. The specific function of this subgroup is unknown.


Pssm-ID: 239540  Cd Length: 188  Bit Score: 96.57  E-value: 2.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021073398  62 AQTEGPYFKPNSPERDDLTAGVSGTRLVVSGYVFDRA-CRPLSRVLMDFWQADNSGNY-------------DNVRFtLRG 127
Cdd:cd03457     1 EVTEGPYYVDGELVRSDITEGQPGVPLTLDLQVVDVAtCCPPPNAAVDIWHCDATGVYsgysagggggedtDDETF-LRG 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1021073398 128 HLFTGADGSYRLTTIVPGLYPGRTRHIHVK------LQAPGQSRILTTQLYFP 174
Cdd:cd03457    80 VQPTDADGVVTFTTIFPGWYPGRATHIHFKvhpdatSATSGGNVAHTGQLFFD 132
ChiA1_BD cd12214
chitin-binding domain of Chi A1-like proteins; This group contains proteins related to the ...
 228-271 1.48e-22

chitin-binding domain of Chi A1-like proteins; This group contains proteins related to the chitin binding domain of chitinase A1 (ChiA1) of Bacillus circulans WL-12. Glycosidase ChiA1 hydrolyzes chitin and is comprised of several domains: the C-terminal chitin binding domain, an N-terminal and catalytic domain, and 2 fibronectin type III-like domains. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source. Bacillus circulans WL-12 ChiA1 facilitates invasion of fungal cell walls. The ChiAi chitin binding domain is required for the specific recognition of insoluble chitin. although topologically and structurally related, ChiA1 lacks the characteristic aromatic residues of Erwinia chrysanthemi endoglucanase Z (CBD(EGZ)).


Pssm-ID: 213177 [Multi-domain]  Cd Length: 45  Bit Score: 87.39  E-value: 1.48e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1021073398 228 WRAGTAYAAGDRVTYGGVTYRCLQAHTAQTGWEPPNVPSLWQRA 271
Cdd:cd12214     2 WAAGTTYKAGDIVTYNGKLYRCLQAHTSLAGWEPPAVPALWQPA 45
protocat_beta TIGR02422
protocatechuate 3,4-dioxygenase, beta subunit; This model represents the beta chain of ...
 58-185 3.74e-22

protocatechuate 3,4-dioxygenase, beta subunit; This model represents the beta chain of protocatechuate 3,4-dioxygenase. The most closely related family outside this family is that of the alpha chain (TIGR02423), typically encoded in an adjacent locus. This enzyme acts in the degradation of aromatic compounds by way of p-hydroxybenzoate to succinate and acetyl-CoA. [Energy metabolism, Other]


Pssm-ID: 131475 [Multi-domain]  Cd Length: 220  Bit Score: 91.25  E-value: 3.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021073398  58 RTTVAQTEGPYFKPNS--PERDDLTAGVSGT----RLVVSGYVFDRACRPLSRVLMDFWQADNSGNYDNVR--------- 122
Cdd:TIGR02422  25 PQSLSELTGPVFGHDDlgPIDNDLTLAHGGEpigeRIIVHGRVLDEDGRPVPNTLVEVWQANAAGRYRHKNdqylapldp 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1021073398 123 -FTLRGHLFTGADGSYRLTTIVPGLYP-------GRTRHIHVKLQAPGQSRILTTQLYFPGEPRNNTDTIF 185
Cdd:TIGR02422 105 nFGGVGRTLTDSDGYYRFRTIKPGPYPwgnhhnaWRPAHIHFSLFGTSFAQRLITQMYFEGDPLIAYDPIV 175
3,4-PCD_beta cd03464
Protocatechuate 3,4-dioxygenase (3,4-PCD) , beta subunit. 3,4-PCD catalyzes the oxidative ring ...
 85-185 2.19e-21

Protocatechuate 3,4-dioxygenase (3,4-PCD) , beta subunit. 3,4-PCD catalyzes the oxidative ring cleavage of 3,4-dihydroxybenzoate to produce beta-carboxy-cis,cis-muconate. 3,4-PCDs are large aggregates of 12 protomers, each composed of an alpha- and beta-subunit and an Fe3+ ion bound in the beta-subunit at the alpha-subunit-beta-subunit interface. 3,4-PCD is a member of the aromatic dioxygenases which are non-heme iron intradiol-cleaving enzymes that break the C1-C2 bond and utilize Fe3+.


Pssm-ID: 239547  Cd Length: 220  Bit Score: 89.30  E-value: 2.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021073398  85 GTRLVVSGYVFDRACRPLSRVLMDFWQADNSGNYDNVR----------FTLRGHLFTGADGSYRLTTIVPGLYP------ 148
Cdd:cd03464    63 GERIIVHGRVLDEDGRPVPNTLVEIWQANAAGRYRHKRdqhdapldpnFGGAGRTLTDDDGYYRFRTIKPGAYPwgnhpn 142

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1021073398 149 -GRTRHIHVKLQAPGQSRILTTQLYFPGEPRNNTDTIF 185
Cdd:cd03464   143 aWRPAHIHFSLFGPSFATRLVTQMYFPGDPLIPHDPIY 180
3,4-PCD_alpha cd03463
Protocatechuate 3,4-dioxygenase (3,4-PCD) , alpha subunit. 3,4-PCD catalyzes the oxidative ...
 60-182 6.10e-18

Protocatechuate 3,4-dioxygenase (3,4-PCD) , alpha subunit. 3,4-PCD catalyzes the oxidative ring cleavage of 3,4-dihydroxybenzoate to produce beta-carboxy-cis,cis-muconate. 3,4-PCDs are large aggregates of 12 protomers, each composed of an alpha- and beta-subunit and an Fe3+ ion bound in the beta-subunit at the alpha-subunit-beta-subunit interface. 3,4-PCD is a member of the aromatic dioxygenases which are non-heme iron intradiol-cleaving enzymes that break the C1-C2 bond and utilize Fe3+.


Pssm-ID: 239546  Cd Length: 185  Bit Score: 79.23  E-value: 6.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021073398  60 TVAQTEGPYFK----PNSPERDDLTA-GVSGTRLVVSGYVFDRACRPLSRVLMDFWQADNSGNY---------DNVRFTL 125
Cdd:cd03463     4 TPSQTVGPYVHiglpPTREGGNDLVPpDTAGERITLEGRVYDGDGAPVPDAMLEIWQADAAGRYahpadsrrrLDPGFRG 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1021073398 126 RGHLFTGADGSYRLTTIVPGLYPGRTR-----HIHVKLQAPGQSRILTTQLYFPGEPRNNTD 182
Cdd:cd03463    84 FGRVATDADGRFSFTTVKPGAVPGRDGagqapHINVWVFARGLLKHLFTRIYFPDEEANAAD 145
1,2-CTD cd03460
Catechol 1,2 dioxygenase (1,2-CTD) catalyzes an intradiol cleavage reaction of catechol to ...
 60-208 1.31e-15

Catechol 1,2 dioxygenase (1,2-CTD) catalyzes an intradiol cleavage reaction of catechol to form cis,cis-muconate. 1,2-CTDs is homodimers with one catalytic non-heme ferric ion per monomer. They belong to the aromatic dioxygenase family, a family of mononuclear non-heme iron intradiol-cleaving enzymes that catalyze the oxygenation of catecholates to aliphatic acids via the cleavage of aromatic rings.


Pssm-ID: 239543 [Multi-domain]  Cd Length: 282  Bit Score: 74.71  E-value: 1.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021073398  60 TVAQTEGPYFKPNSPERD-----DLTAGVSGTRLVVSGYVFDRACRPLSRVLMDFWQADNSGNYDNV-----RFTLRGHL 129
Cdd:cd03460    92 TPRTIEGPLYVAGAPESDgfarlDDGSDDDGETLVMHGTVTDTDGKPVPGAKVEVWHANSKGFYSHFdptqsPFNLRRSI 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021073398 130 FTGADGSYRLTTIVPGLY---PG---------------RTRHIHVKLQAPGQsRILTTQLYFPGEPRNNTDTIFD----- 186
Cdd:cd03460   172 ITDADGRYRFRSIMPSGYgvpPGgptqqllnalgrhgnRPAHIHFFVSAPGH-RKLTTQINIEGDPYIWDDFAFAtregl 250

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1021073398 187 -PSLLMNVRTAG---GVREGT-----FDFVL 208
Cdd:cd03460   251 iPEVVEVEDAAAlkqYGLDGPfaeiaFDFQL 281
ChtBD3 smart00495
Chitin-binding domain type 3;
228-268 5.66e-08

Chitin-binding domain type 3;


Pssm-ID: 197760 [Multi-domain]  Cd Length: 41  Bit Score: 48.03  E-value: 5.66e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1021073398  228 WRAGTAYAAGDRVTYGGVTYRClqahTAQTGWEPPN-VPSLW 268
Cdd:smart00495   4 WQAGTVYTAGDVVSYNGKVYKA----KWWTQGEEPGsSSGPW 41
ChtBD3 cd00036
Chitin/cellulose binding domains of chitinase and related enzymes; This group contains ...
 228-269 8.06e-06

Chitin/cellulose binding domains of chitinase and related enzymes; This group contains proteins related to the cellulose-binding domain of Erwinia chrysanthemi endoglucanase Z (EGZ) and Serratia marcescens chitinase B (ChiB). Gram negative plant parasite Erwinia chrysanthemi produces a variety of depolymerizing enzymes to metabolize pectin and cellulose on the host plant. Cellulase EGZ has a modular structure, with an N-terminal catalytic domain linked to a C-terminal cellulose-binding domain (CBD). CBD mediates the secretion activity of EGZ. Chitinases allow certain bacteria to utilize chitin as a energy source. Typically, non-plant chitinases are of the glycosidase family 18. Bacillus circulans Glycosidase ChiA1 hydrolyzes chitin and is comprised of several domains: the C-terminal chitin binding domain, an N-terminal catalytic domain, and 2 fibronectin type III-like domains. Bacillus circulans WL-12 ChiA1 facilitates invasion of fungal cell walls. The ChiA1 chitin binding domain is required for the specific recognition of insoluble chitin. although topologically and structurally related, ChiA1 lacks the characteristic aromatic residues of Erwinia chrysanthemi endoglucanase Z (CBD(EGZ)). Streptomyces griseus Chitinase C is a family 19 chitinase, and consists of a N-terminal chitin binding domain and a C-terminal chitin-catalytic domain that effects degradation. ChiC contains the characteristic chitin-binding aromatic residues. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source.


Pssm-ID: 213175  Cd Length: 40  Bit Score: 41.98  E-value: 8.06e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1021073398 228 WRAGTAYAAGDRVTYGGVTYRCLQAHtaqTGWEPPNVpSLWQ 269
Cdd:cd00036     2 WPNPTHYTAGQSVVYNGNLYTANWYT---AGSVPGSD-SSWT 39
ChiC_BD cd12215
Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of ...
 228-248 3.86e-04

Chitin-binding domain of chitinase C; Chitin-binding domain of chitinase C (ChiC) of Streptomyces griseus and related proteins. Chitinase C is a family 19 chitinase, and consists of a N-terminal chitin binding domain and a C-terminal chitin-catalytic domain that effects degradation. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source. ChiC contains the characteristic chitin-binding aromatic residues.


Pssm-ID: 213178 [Multi-domain]  Cd Length: 42  Bit Score: 37.17  E-value: 3.86e-04
                          10        20
                  ....*....|....*....|.
gi 1021073398 228 WRAGTAYAAGDRVTYGGVTYR 248
Cdd:cd12215     3 WDASTVYTGGDQVTYNGKVYE 23
 
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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