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Conserved domains on  [gi|110590285|pdb|2GHK|X]
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Chain X, cytosolic ascorbate peroxidase 1

Protein Classification

peroxidase( domain architecture ID 396)

peroxidase catalyzes removal of H(2)O(2), and is involved in the oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress

CATH:  1.10.420.10|1.10.520.10
EC:  1.11.1.-
Gene Ontology:  GO:0004601|GO:0006979|GO:0020037
PubMed:  11054546
SCOP:  4001128|3000844

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
plant_peroxidase_like super family cl00196
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
 14-260 1.84e-149

Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX), which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions. Several sub-families can be identified. Class I includes intracellular peroxidases present in fungi, plants, archaea and bacteria, called catalase-peroxidases, that can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. Catalase-peroxidases are typically comprised of two homologous domains that probably arose via a single gene duplication event. Class II includes ligninase and other extracellular fungal peroxidases, while class III is comprised of classic extracellular plant peroxidases, like horseradish peroxidase.


The actual alignment was detected with superfamily member PLN02879:

Pssm-ID: 444739 [Multi-domain]  Cd Length: 251  Bit Score: 417.54  E-value: 1.84e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X        14 KSYPTVSADYQKAVEKAKKKLRGFIAEKRCAPLMLRLAWHSAGTFDKGTKTGGPFGTIKHPAELAHSANNGLDIAVRLLE 93
Cdd:PLN02879   4 KSYPEVKEEYKKAVQRCKRKLRGLIAEKHCAPIVLRLAWHSAGTFDVKTKTGGPFGTIRHPQELAHDANNGLDIAVRLLD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X        94 PLKAEFPILSYADFYQLAGVVAVEVTGGPEVPFHPGREDKPEPPPEGRLPDATKGSDHLRDVFGKaMGLTDQDIVALSGG 173
Cdd:PLN02879  84 PIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPPEGRLPQATKGVDHLRDVFGR-MGLNDKDIVALSGG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X       174 HTIGAAHKERSGFEGPWTSNPLIFDNSYFTELLSGEKEGLLQLPSDKALLSDPVFRPLVDKYAADEDAFFADYAEAHQKL 253
Cdd:PLN02879 163 HTLGRCHKERSGFEGAWTPNPLIFDNSYFKEILSGEKEGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHLKL 242


                 ....*..
2GHK_X       254 SELGFAD 260
Cdd:PLN02879 243 SELGFAD 249
 
Name Accession Description Interval E-value
PLN02879 PLN02879
L-ascorbate peroxidase
 14-260 1.84e-149

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 417.54  E-value: 1.84e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X        14 KSYPTVSADYQKAVEKAKKKLRGFIAEKRCAPLMLRLAWHSAGTFDKGTKTGGPFGTIKHPAELAHSANNGLDIAVRLLE 93
Cdd:PLN02879   4 KSYPEVKEEYKKAVQRCKRKLRGLIAEKHCAPIVLRLAWHSAGTFDVKTKTGGPFGTIRHPQELAHDANNGLDIAVRLLD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X        94 PLKAEFPILSYADFYQLAGVVAVEVTGGPEVPFHPGREDKPEPPPEGRLPDATKGSDHLRDVFGKaMGLTDQDIVALSGG 173
Cdd:PLN02879  84 PIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPPEGRLPQATKGVDHLRDVFGR-MGLNDKDIVALSGG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X       174 HTIGAAHKERSGFEGPWTSNPLIFDNSYFTELLSGEKEGLLQLPSDKALLSDPVFRPLVDKYAADEDAFFADYAEAHQKL 253
Cdd:PLN02879 163 HTLGRCHKERSGFEGAWTPNPLIFDNSYFKEILSGEKEGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHLKL 242


                 ....*..
2GHK_X       254 SELGFAD 260
Cdd:PLN02879 243 SELGFAD 249
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
 16-261 2.32e-149

Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Along with related catalase-peroxidases, ascorbate peroxidases belong to class I of the plant superfamily. Ascorbate peroxidases are found in the chloroplasts and/or cytosol of algae and plants, where they have been shown to control the concentration of lethal hydrogen peroxide molecules. The yeast cytochrome c peroxidase is a divergent member of the family; it forms a complex with cytochrome c to catalyze the reduction of hydrogen peroxide to water.


Pssm-ID: 173825 [Multi-domain]  Cd Length: 253  Bit Score: 416.99  E-value: 2.32e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X       16 YPTVSADY-QKAVEKAKKKLRGFIAEKRCAPLMLRLAWHSAGTFDKGTKTGGPFGTIKHPAELAHSANNGLDIAVRLLEP 94
Cdd:cd00691   1 APVVSAAYaAKDLEAARNDIAKLIDDKNCAPILVRLAWHDSGTYDKETKTGGSNGTIRFDPELNHGANAGLDIARKLLEP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X       95 LKAEFPILSYADFYQLAGVVAVEVTGGPEVPFHPGREDKPEP---PPEGRLPDATKGSDHLRDVFGKaMGLTDQDIVALS 171
Cdd:cd00691  81 IKKKYPDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPeecPPEGRLPDASKGADHLRDVFYR-MGFNDQEIVALS 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X      172 GGHTIGAAHKERSGFEGPWTSNPLIFDNSYFTELLSGEK----EGLLQLPSDKALLSDPVFRPLVDKYAADEDAFFADYA 247
Cdd:cd00691 160 GAHTLGRCHKERSGYDGPWTKNPLKFDNSYFKELLEEDWklptPGLLMLPTDKALLEDPKFRPYVELYAKDQDAFFKDYA 239

                       250
                ....*....|....
2GHK_X      248 EAHQKLSELGFADA 261
Cdd:cd00691 240 EAHKKLSELGVPFP 253
peroxidase pfam00141
Peroxidase;
37-238 2.66e-54

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 173.52  E-value: 2.66e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X         37 FIAEKRCAPLMLRLAWHSAGTfdkgtktGGPFGTI---KHPAELAHSANNGLDIAVRLLEPLKAEFP-----ILSYADFY 108
Cdd:pfam00141   9 FKADPTMGPSLLRLHFHDCFV-------GGCDGSVlldGFKPEKDAPPNLGLRKGFEVIDDIKAKLEaacpgVVSCADIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X        109 QLAGVVAVEVTGGPEVPFHPGREDKPEPPPE---GRLPDATKGSDHLRDVFgKAMGLTDQDIVALSGGHTIGAAHKersg 185
Cdd:pfam00141  82 ALAARDAVELAGGPSWPVPLGRRDGTVSSAVeanSNLPAPTDSLDQLRDRF-ARKGLTAEDLVALSGAHTIGRAHK---- 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
2GHK_X        186 fegpwtsnplifdnsyftELLSGekEGLlqLPSDKALLSDPVFRPLVDKYAAD 238
Cdd:pfam00141 157 ------------------NLLDG--RGL--LTSDQALLSDPRTRALVERYAAD 187
cat_per_HPI TIGR00198
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ...
 22-254 5.76e-21

catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules of hydrogen peroxide to dioxygen and two molecules of water. As a peroxidase, it uses hydrogen peroxide to oxidize donor compounds and produce water. KatG from E. coli is a homotetramer with two non-covalently associated iron protoheme IX groups per tetramer, but the ortholog from Synechococcus sp. is a homodimer with one protoheme. Important sites (numbered according to E. coli KatG) include heme ligands His-106 and His-267 and active site Trp-318. Note that the translation PID:g296476 from accession X71420 from Rhodobacter capsulatus B10 contains extensive frameshift differences from the rest of the orthologous family. [Cellular processes, Detoxification]


Pssm-ID: 272957 [Multi-domain]  Cd Length: 716  Bit Score: 91.91  E-value: 5.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X         22 DYQKAVEK-----AKKKLRGFIAEKRC---------APLMLRLAWHSAGTFDKGTKTGGPF-GTIKHPAELAHSANNGLD 86
Cdd:TIGR00198  44 DYAEEFQQldlaaVKQDLKHLMTDSQSwwpadwghyGGLFIRMAWHAAGTYRIADGRGGAAtGNQRFAPLNSWPDNVNLD 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X         87 IAVRLLEPLKAEF-PILSYADFYQLAGVVAVEVTGGPEVPFHPGREDKPEPP---------------------------- 137
Cdd:TIGR00198 124 KARRLLWPIKKKYgNKLSWADLIILAGTVAYESMGLKVFGFAGGREDIWEPDkdiywgaekewltssredreslenplaa 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X        138 ---------PEG--RLPDATKGSDHLRDVFGKaMGLTDQDIVAL-SGGHTIGAAHKE----------------------- 182
Cdd:TIGR00198 204 temgliyvnPEGpdGHPDPLCTAQDIRTTFAR-MGMNDEETVALiAGGHTVGKCHGAgpaeligpdpegapieeqglgwh 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X        183 ------------RSGFEGPWTSNPLIFDNSYFTELLSGEKE------GLLQ------------------------LPSDK 220
Cdd:TIGR00198 283 nqygkgvgrdtmTSGLEVAWTTTPTQWDNGYFYMLFNYEWElkkspaGAWQweavdapeiipdvedpnkkhnpimLDADL 362

                         330       340       350
                  ....*....|....*....|....*....|....
2GHK_X        221 ALLSDPVFRPLVDKYAADEDAFFADYAEAHQKLS 254
Cdd:TIGR00198 363 ALRFDPEFRKISRRFLREPDYFAEAFAKAWFKLT 396
KatG COG0376
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
45-253 9.19e-17

Catalase (peroxidase I) [Inorganic ion transport and metabolism];


Pssm-ID: 440145 [Multi-domain]  Cd Length: 731  Bit Score: 79.39  E-value: 9.19e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X       45 PLMLRLAWHSAGTFDKGTKTGGpfgtikhpaelAHSAN-----------NG-LDIAVRLLEPLKAEF-PILSYADFYQLA 111
Cdd:COG0376  89 PLFIRMAWHSAGTYRIGDGRGG-----------AGGGQqrfaplnswpdNAnLDKARRLLWPIKQKYgNKISWADLMILA 157

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X      112 GVVAVEVTGGPEVPFHPGREDKPEPP--------------------------------------PEG--RLPDATKGSDH 151
Cdd:COG0376 158 GNVALESMGFKTFGFAGGREDVWEPEedvywgpetewlgderysgdrelenplaavqmgliyvnPEGpnGNPDPLAAARD 237

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X      152 LRDVFGKaMGLTDQDIVAL-SGGHTIGAAH------------------------KER-----------SGFEGPWTSNPL 195
Cdd:COG0376 238 IRETFGR-MAMNDEETVALiAGGHTFGKTHgagdaehvgpepeaapieeqglgwKNSfgsgkgedtitSGLEGAWTPTPT 316

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X      196 IFDNSYFTELL--------------------------------SGEKEGLLQLPSDKALLSDPVFRPLVDKYAADEDAfF 243
Cdd:COG0376 317 QWDNGYFDNLFgyeweltkspagahqwvpkdgaaadtvpdahdPSKRHAPMMLTTDLALRFDPAYEKISRRFLENPEE-F 395

                       330
                ....*....|.
2GHK_X      244 AD-YAEAHQKL 253
Cdd:COG0376 396 ADaFARAWFKL 406
 
Name Accession Description Interval E-value
PLN02879 PLN02879
L-ascorbate peroxidase
 14-260 1.84e-149

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 417.54  E-value: 1.84e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X        14 KSYPTVSADYQKAVEKAKKKLRGFIAEKRCAPLMLRLAWHSAGTFDKGTKTGGPFGTIKHPAELAHSANNGLDIAVRLLE 93
Cdd:PLN02879   4 KSYPEVKEEYKKAVQRCKRKLRGLIAEKHCAPIVLRLAWHSAGTFDVKTKTGGPFGTIRHPQELAHDANNGLDIAVRLLD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X        94 PLKAEFPILSYADFYQLAGVVAVEVTGGPEVPFHPGREDKPEPPPEGRLPDATKGSDHLRDVFGKaMGLTDQDIVALSGG 173
Cdd:PLN02879  84 PIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPPEGRLPQATKGVDHLRDVFGR-MGLNDKDIVALSGG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X       174 HTIGAAHKERSGFEGPWTSNPLIFDNSYFTELLSGEKEGLLQLPSDKALLSDPVFRPLVDKYAADEDAFFADYAEAHQKL 253
Cdd:PLN02879 163 HTLGRCHKERSGFEGAWTPNPLIFDNSYFKEILSGEKEGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHLKL 242


                 ....*..
2GHK_X       254 SELGFAD 260
Cdd:PLN02879 243 SELGFAD 249
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
 16-261 2.32e-149

Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Along with related catalase-peroxidases, ascorbate peroxidases belong to class I of the plant superfamily. Ascorbate peroxidases are found in the chloroplasts and/or cytosol of algae and plants, where they have been shown to control the concentration of lethal hydrogen peroxide molecules. The yeast cytochrome c peroxidase is a divergent member of the family; it forms a complex with cytochrome c to catalyze the reduction of hydrogen peroxide to water.


Pssm-ID: 173825 [Multi-domain]  Cd Length: 253  Bit Score: 416.99  E-value: 2.32e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X       16 YPTVSADY-QKAVEKAKKKLRGFIAEKRCAPLMLRLAWHSAGTFDKGTKTGGPFGTIKHPAELAHSANNGLDIAVRLLEP 94
Cdd:cd00691   1 APVVSAAYaAKDLEAARNDIAKLIDDKNCAPILVRLAWHDSGTYDKETKTGGSNGTIRFDPELNHGANAGLDIARKLLEP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X       95 LKAEFPILSYADFYQLAGVVAVEVTGGPEVPFHPGREDKPEP---PPEGRLPDATKGSDHLRDVFGKaMGLTDQDIVALS 171
Cdd:cd00691  81 IKKKYPDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPeecPPEGRLPDASKGADHLRDVFYR-MGFNDQEIVALS 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X      172 GGHTIGAAHKERSGFEGPWTSNPLIFDNSYFTELLSGEK----EGLLQLPSDKALLSDPVFRPLVDKYAADEDAFFADYA 247
Cdd:cd00691 160 GAHTLGRCHKERSGYDGPWTKNPLKFDNSYFKELLEEDWklptPGLLMLPTDKALLEDPKFRPYVELYAKDQDAFFKDYA 239

                       250
                ....*....|....
2GHK_X      248 EAHQKLSELGFADA 261
Cdd:cd00691 240 EAHKKLSELGVPFP 253
PLN02364 PLN02364
L-ascorbate peroxidase 1
 14-261 3.52e-147

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 411.40  E-value: 3.52e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X        14 KSYPTVSADYQKAVEKAKKKLRGFIAEKRCAPLMLRLAWHSAGTFDKGTKTGGPFGTIKHPAELAHSANNGLDIAVRLLE 93
Cdd:PLN02364   3 KNYPTVSEDYKKAVEKCRRKLRGLIAEKNCAPIMVRLAWHSAGTFDCQSRTGGPFGTMRFDAEQAHGANSGIHIALRLLD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X        94 PLKAEFPILSYADFYQLAGVVAVEVTGGPEVPFHPGREDKPEPPPEGRLPDATKGSDHLRDVFGKAMGLTDQDIVALSGG 173
Cdd:PLN02364  83 PIREQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPEGRLPDATKGCDHLRDVFAKQMGLSDKDIVALSGA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X       174 HTIGAAHKERSGFEGPWTSNPLIFDNSYFTELLSGEKEGLLQLPSDKALLSDPVFRPLVDKYAADEDAFFADYAEAHQKL 253
Cdd:PLN02364 163 HTLGRCHKDRSGFEGAWTSNPLIFDNSYFKELLSGEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHMKL 242


                 ....*...
2GHK_X       254 SELGFADA 261
Cdd:PLN02364 243 SELGFADA 250
PLN02608 PLN02608
L-ascorbate peroxidase
 17-258 1.83e-140

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 396.06  E-value: 1.83e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X        17 PTVSADYQKAVEKAKKKLRGFIAEKRCAPLMLRLAWHSAGTFDKGTKTGGPFGTIKHPAELAHSANNGLDIAVRLLEPLK 96
Cdd:PLN02608   4 PVVDAEYLKEIEKARRDLRALIASKNCAPIMLRLAWHDAGTYDAKTKTGGPNGSIRNEEEYSHGANNGLKIAIDLCEPVK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X        97 AEFPILSYADFYQLAGVVAVEVTGGPEVPFHPGREDKPEPPPEGRLPDATKGSDHLRDVFGKaMGLTDQDIVALSGGHTI 176
Cdd:PLN02608  84 AKHPKITYADLYQLAGVVAVEVTGGPTIDFVPGRKDSNACPEEGRLPDAKKGAKHLRDVFYR-MGLSDKDIVALSGGHTL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X       177 GAAHKERSGFEGPWTSNPLIFDNSYFTELLSGEKEGLLQLPSDKALLSDPVFRPLVDKYAADEDAFFADYAEAHQKLSEL 256
Cdd:PLN02608 163 GRAHPERSGFDGPWTKEPLKFDNSYFVELLKGESEGLLKLPTDKALLEDPEFRPYVELYAKDEDAFFRDYAESHKKLSEL 242


                 ..
2GHK_X       257 GF 258
Cdd:PLN02608 243 GF 244
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
 28-255 2.86e-65

Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX), which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions. Several sub-families can be identified. Class I includes intracellular peroxidases present in fungi, plants, archaea and bacteria, called catalase-peroxidases, that can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. Catalase-peroxidases are typically comprised of two homologous domains that probably arose via a single gene duplication event. Class II includes ligninase and other extracellular fungal peroxidases, while class III is comprised of classic extracellular plant peroxidases, like horseradish peroxidase.


Pssm-ID: 173823 [Multi-domain]  Cd Length: 255  Bit Score: 203.92  E-value: 2.86e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X       28 EKAKKKLRGFIAE-KRCAPLMLRLAWHSAGTFDKGT-KTGGPFGTIKHPAELAHSANNGLDIAVRLLEPLKAEFP---IL 102
Cdd:cd00314   1 DAIKAILEDLITQaGALAGSLLRLAFHDAGTYDIADgKGGGADGSIRFEPELDRPENGGLDKALRALEPIKSAYDggnPV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X      103 SYADFYQLAGVVAVEVT--GGPEVPFHPGREDKPEPP-----PEGRLPDATKGSDHLRDVFgKAMGLTDQDIVALS-GGH 174
Cdd:cd00314  81 SRADLIALAGAVAVESTfgGGPLIPFRFGRLDATEPDlgvpdPEGLLPNETSSATELRDKF-KRMGLSPSELVALSaGAH 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X      175 TI-GAAHKERSGFE--GPWTSNPLIFDNSYFTELLSGEKE------------GLLQLPSDKALLSDPVFRPLVDKYAADE 239
Cdd:cd00314 160 TLgGKNHGDLLNYEgsGLWTSTPFTFDNAYFKNLLDMNWEwrvgspdpdgvkGPGLLPSDYALLSDSETRALVERYASDQ 239

                       250
                ....*....|....*.
2GHK_X      240 DAFFADYAEAHQKLSE 255
Cdd:cd00314 240 EKFFEDFAKAWIKMVN 255
peroxidase pfam00141
Peroxidase;
37-238 2.66e-54

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 173.52  E-value: 2.66e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X         37 FIAEKRCAPLMLRLAWHSAGTfdkgtktGGPFGTI---KHPAELAHSANNGLDIAVRLLEPLKAEFP-----ILSYADFY 108
Cdd:pfam00141   9 FKADPTMGPSLLRLHFHDCFV-------GGCDGSVlldGFKPEKDAPPNLGLRKGFEVIDDIKAKLEaacpgVVSCADIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X        109 QLAGVVAVEVTGGPEVPFHPGREDKPEPPPE---GRLPDATKGSDHLRDVFgKAMGLTDQDIVALSGGHTIGAAHKersg 185
Cdd:pfam00141  82 ALAARDAVELAGGPSWPVPLGRRDGTVSSAVeanSNLPAPTDSLDQLRDRF-ARKGLTAEDLVALSGAHTIGRAHK---- 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
2GHK_X        186 fegpwtsnplifdnsyftELLSGekEGLlqLPSDKALLSDPVFRPLVDKYAAD 238
Cdd:pfam00141 157 ------------------NLLDG--RGL--LTSDQALLSDPRTRALVERYAAD 187
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
 69-257 3.68e-30

Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong to class III of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class III peroxidases are found in the extracellular space or in the vacuole in plants where they have been implicated in hydrogen peroxide detoxification, auxin catabolism and lignin biosynthesis, and stress response. Class III peroxidases contain four conserved disulphide bridges and two conserved calcium binding sites.


Pssm-ID: 173827 [Multi-domain]  Cd Length: 298  Bit Score: 114.15  E-value: 3.68e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X       69 GTIKHPAELAHSANNGL------DIAVRLLEplkAEFP-ILSYADFYQLAGVVAVEVTGGP--EVPFhpGRED--KPEPP 137
Cdd:cd00693  57 STANNTSEKDAPPNLSLrgfdviDDIKAALE---AACPgVVSCADILALAARDAVVLAGGPsyEVPL--GRRDgrVSSAN 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X      138 PEGRLPDATKGSDHLRDVFgKAMGLTDQDIVALSGGHTIGAAH----KER-SGFEG--------------------PWTS 192
Cdd:cd00693 132 DVGNLPSPFFSVSQLISLF-ASKGLTVTDLVALSGAHTIGRAHcssfSDRlYNFSGtgdpdptldpayaaqlrkkcPAGG 210

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2GHK_X      193 N-----------PLIFDNSYFTELLSGekEGLLQlpSDKALLSDPVFRPLVDKYAADEDAFFADYAEAHQKLSELG 257
Cdd:cd00693 211 DddtlvpldpgtPNTFDNSYYKNLLAG--RGLLT--SDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIG 282
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
 48-258 3.75e-24

Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related extracellular fungal peroxidases belong to class II of the plant heme-dependent peroxidase superfamily. All members of the superfamily share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Class II peroxidases are fungal glycoproteins that have been implicated in the oxidative breakdown of lignin, the main cell wall component of woody plants. They contain four conserved disulphide bridges and two conserved calcium binding sites.


Pssm-ID: 173826 [Multi-domain]  Cd Length: 328  Bit Score: 98.62  E-value: 3.75e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X       48 LRLAWHSAGTFDK----GTKTGG-------PFGTIkhpaELAHSANNGLDIAVRLLEPlKAEFPILSYADFYQLAGVVAV 116
Cdd:cd00692  42 LRLTFHDAIGFSPalaaGQFGGGgadgsivLFDDI----ETAFHANIGLDEIVEALRP-FHQKHNVSMADFIQFAGAVAV 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X      117 -EVTGGPEVPFHPGREDKPEPPPEGRLPDATKGSDHLRDVFGKAmGLTDQDIVALSGGHTIGAAHKERSGFEG-PWTSNP 194
Cdd:cd00692 117 sNCPGAPRLEFYAGRKDATQPAPDGLVPEPFDSVDKILARFADA-GFSPDELVALLAAHSVAAQDFVDPSIAGtPFDSTP 195

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X      195 LIFDNSYFTE-LLSGE---------------KEGLLQLPSDKALLSDPVFRPLVDKYAADEDAFFADYAEAHQKLSELGF 258
Cdd:cd00692 196 GVFDTQFFIEtLLKGTafpgsggnqgevespLPGEFRLQSDFLLARDPRTACEWQSFVNNQAKMNAAFAAAMLKLSLLGQ 275
catalase_peroxidase_1 cd00649
N-terminal catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ...
 45-253 3.03e-22

N-terminal catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Catalase-peroxidases can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. These enzymes are found in many archaeal and bacterial organisms, where they neutralize potentially lethal hydrogen peroxide molecules generated during photosynthesis or stationary phase. Along with related intracellular fungal and plant peroxidases, catalase-peroxidases belong to class I of the plant peroxidase superfamily. Unlike the eukaryotic enzymes, they are typically comprised of two homologous domains that probably arose via a single gene duplication event. The heme binding motif is present only in the N-terminal domain; the function of the C-terminal domain is not clear.


Pssm-ID: 173824 [Multi-domain]  Cd Length: 409  Bit Score: 94.68  E-value: 3.03e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X       45 PLMLRLAWHSAGTFDKGTKTGGPFGTIKHPAELAHSANNG-LDIAVRLLEPLKAEF-PILSYADFYQLAGVVAVEVTGGP 122
Cdd:cd00649  71 PLFIRMAWHSAGTYRIADGRGGAGTGQQRFAPLNSWPDNVnLDKARRLLWPIKQKYgNKISWADLMILAGNVALESMGFK 150

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X      123 EVPFHPGREDKPEPP--------------------------------------PEG--RLPDATKGSDHLRDVFGKaMGL 162
Cdd:cd00649 151 TFGFAGGREDVWEPDedvywgpekewladkrysgdrdlenplaavqmgliyvnPEGpdGNPDPLAAAKDIRETFAR-MAM 229

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X      163 TDQDIVAL-SGGHTIGAAH---------KE--------------------------RSGFEGPWTSNPLIFDNSYFTELL 206
Cdd:cd00649 230 NDEETVALiAGGHTFGKTHgagpashvgPEpeaapieqqglgwknsygtgkgkdtiTSGLEGAWTPTPTKWDNNYLKNLF 309

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
2GHK_X      207 S--------------------------------GEKEGLLQLPSDKALLSDPVFRPLVDKYAADEDAFFADYAEAHQKL 253
Cdd:cd00649 310 GyeweltkspagawqwvpknaagentvpdahdpSKKHAPMMLTTDLALRFDPEYEKISRRFLENPDEFADAFAKAWFKL 388
cat_per_HPI TIGR00198
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ...
 22-254 5.76e-21

catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules of hydrogen peroxide to dioxygen and two molecules of water. As a peroxidase, it uses hydrogen peroxide to oxidize donor compounds and produce water. KatG from E. coli is a homotetramer with two non-covalently associated iron protoheme IX groups per tetramer, but the ortholog from Synechococcus sp. is a homodimer with one protoheme. Important sites (numbered according to E. coli KatG) include heme ligands His-106 and His-267 and active site Trp-318. Note that the translation PID:g296476 from accession X71420 from Rhodobacter capsulatus B10 contains extensive frameshift differences from the rest of the orthologous family. [Cellular processes, Detoxification]


Pssm-ID: 272957 [Multi-domain]  Cd Length: 716  Bit Score: 91.91  E-value: 5.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X         22 DYQKAVEK-----AKKKLRGFIAEKRC---------APLMLRLAWHSAGTFDKGTKTGGPF-GTIKHPAELAHSANNGLD 86
Cdd:TIGR00198  44 DYAEEFQQldlaaVKQDLKHLMTDSQSwwpadwghyGGLFIRMAWHAAGTYRIADGRGGAAtGNQRFAPLNSWPDNVNLD 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X         87 IAVRLLEPLKAEF-PILSYADFYQLAGVVAVEVTGGPEVPFHPGREDKPEPP---------------------------- 137
Cdd:TIGR00198 124 KARRLLWPIKKKYgNKLSWADLIILAGTVAYESMGLKVFGFAGGREDIWEPDkdiywgaekewltssredreslenplaa 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X        138 ---------PEG--RLPDATKGSDHLRDVFGKaMGLTDQDIVAL-SGGHTIGAAHKE----------------------- 182
Cdd:TIGR00198 204 temgliyvnPEGpdGHPDPLCTAQDIRTTFAR-MGMNDEETVALiAGGHTVGKCHGAgpaeligpdpegapieeqglgwh 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X        183 ------------RSGFEGPWTSNPLIFDNSYFTELLSGEKE------GLLQ------------------------LPSDK 220
Cdd:TIGR00198 283 nqygkgvgrdtmTSGLEVAWTTTPTQWDNGYFYMLFNYEWElkkspaGAWQweavdapeiipdvedpnkkhnpimLDADL 362

                         330       340       350
                  ....*....|....*....|....*....|....
2GHK_X        221 ALLSDPVFRPLVDKYAADEDAFFADYAEAHQKLS 254
Cdd:TIGR00198 363 ALRFDPEFRKISRRFLREPDYFAEAFAKAWFKLT 396
PRK15061 PRK15061
catalase/peroxidase;
45-253 5.88e-17

catalase/peroxidase;


Pssm-ID: 237891 [Multi-domain]  Cd Length: 726  Bit Score: 80.18  E-value: 5.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X        45 PLMLRLAWHSAGTFDKGTKTGGpfgtikhpaelahsANNG---------------LDIAVRLLEPLKAEF-PILSYADFY 108
Cdd:PRK15061  83 PLFIRMAWHSAGTYRIGDGRGG--------------AGGGqqrfaplnswpdnvnLDKARRLLWPIKQKYgNKISWADLM 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X       109 QLAGVVAVEVTGGPEVPFHPGREDKPEP---------------------------P------------PEG--RLPDATK 147
Cdd:PRK15061 149 ILAGNVALESMGFKTFGFAGGREDVWEPeedvywgpekewlggderysgerdlenPlaavqmgliyvnPEGpnGNPDPLA 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X       148 GSDHLRDVFGKaMGLTDQDIVAL-SGGHTIGAAH-------------------------------KER----SGFEGPWT 191
Cdd:PRK15061 229 AARDIRETFAR-MAMNDEETVALiAGGHTFGKTHgagdashvgpepeaapieeqglgwknsygsgKGAdtitSGLEGAWT 307

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X       192 SNPLIFDNSYFTELLSGEKE------GLLQ--------------------------LPSDKALLSDPVFRPLVDKYAADE 239
Cdd:PRK15061 308 TTPTQWDNGYFENLFGYEWEltkspaGAWQwvpkdgaaedtvpdahdpskkhaptmLTTDLALRFDPEYEKISRRFLENP 387

                        330
                 ....*....|....*
2GHK_X       240 DAfFAD-YAEAHQKL 253
Cdd:PRK15061 388 EE-FADaFARAWFKL 401
KatG COG0376
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
45-253 9.19e-17

Catalase (peroxidase I) [Inorganic ion transport and metabolism];


Pssm-ID: 440145 [Multi-domain]  Cd Length: 731  Bit Score: 79.39  E-value: 9.19e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X       45 PLMLRLAWHSAGTFDKGTKTGGpfgtikhpaelAHSAN-----------NG-LDIAVRLLEPLKAEF-PILSYADFYQLA 111
Cdd:COG0376  89 PLFIRMAWHSAGTYRIGDGRGG-----------AGGGQqrfaplnswpdNAnLDKARRLLWPIKQKYgNKISWADLMILA 157

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X      112 GVVAVEVTGGPEVPFHPGREDKPEPP--------------------------------------PEG--RLPDATKGSDH 151
Cdd:COG0376 158 GNVALESMGFKTFGFAGGREDVWEPEedvywgpetewlgderysgdrelenplaavqmgliyvnPEGpnGNPDPLAAARD 237

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X      152 LRDVFGKaMGLTDQDIVAL-SGGHTIGAAH------------------------KER-----------SGFEGPWTSNPL 195
Cdd:COG0376 238 IRETFGR-MAMNDEETVALiAGGHTFGKTHgagdaehvgpepeaapieeqglgwKNSfgsgkgedtitSGLEGAWTPTPT 316

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X      196 IFDNSYFTELL--------------------------------SGEKEGLLQLPSDKALLSDPVFRPLVDKYAADEDAfF 243
Cdd:COG0376 317 QWDNGYFDNLFgyeweltkspagahqwvpkdgaaadtvpdahdPSKRHAPMMLTTDLALRFDPAYEKISRRFLENPEE-F 395

                       330
                ....*....|.
2GHK_X      244 AD-YAEAHQKL 253
Cdd:COG0376 396 ADaFARAWFKL 406
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
 48-253 1.57e-14

Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent peroxidases similar to plant peroxidases. Along with animal peroxidases, these enzymes belong to a group of peroxidases containing a heme prosthetic group (ferriprotoporphyrin IX) which catalyzes a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. The plant peroxidase-like superfamily is found in all three kingdoms of life and carries out a variety of biosynthetic and degradative functions.


Pssm-ID: 173829  Cd Length: 264  Bit Score: 71.34  E-value: 1.57e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X       48 LRLAWHSAGTFDKGTKTGGPFGTIKHPAELAHSANNGLDIAVRLLEPLKAefPILSYADFYQLAGVVAVEVTGGPEVPFH 127
Cdd:cd08201  46 LRTAFHDMATHNVDDGTGGLDASIQYELDRPENIGSGFNTTLNFFVNFYS--PRSSMADLIAMGVVTSVASCGGPVVPFR 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X      128 PGREDKPEPPPEGrLPDATKGSDHLRDVFGKaMGLTDQDIVALSG-GHTIGAAHKER-----------SGFEGPWTSNPl 195
Cdd:cd08201 124 AGRIDATEAGQAG-VPEPQTDLGTTTESFRR-QGFSTSEMIALVAcGHTLGGVHSEDfpeivppgsvpDTVLQFFDTTI- 200

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
2GHK_X      196 IFDNSYFTELLSGEKEGLLQLPSDKALLSD-PVFRplVDKYA-----ADEDAFFADYAEAHQKL 253
Cdd:cd08201 201 QFDNKVVTEYLSGTTNNPLVVGPNNTTNSDlRIFS--SDGNVtmnelASPDTFQKTCADILQRM 262
PLN03030 PLN03030
cationic peroxidase; Provisional
 37-257 5.49e-08

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 52.65  E-value: 5.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X        37 FIAEKRCAPLMLRLAWHSAgtFDKGTKTGGPF-GTIKHPAELAHSANNGLDIAVRLLEPLKAEFP-ILSYADFYQLAGVV 114
Cdd:PLN03030  49 FQSNPAIAPGLLRMHFHDC--FVRGCDASILIdGSNTEKTALPNLLLRGYDVIDDAKTQLEAACPgVVSCADILALAARD 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X       115 AVEVTGGPEVPFHPGREDkpepppeGR---------LPDATKGSDHLRDVFGkAMGLTDQDIVALSGGHTIGAAH----- 180
Cdd:PLN03030 127 SVVLTNGLTWPVPTGRRD-------GRvslasdasnLPGFTDSIDVQKQKFA-AKGLNTQDLVTLVGGHTIGTTAcqffr 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X       181 -----------------------------------KERSGFEgpwTSNPLIFDNSYFTELLSGekEGLLQlpSDKALLSD 225
Cdd:PLN03030 199 yrlynftttgngadpsidasfvpqlqalcpqngdgSRRIALD---TGSSNRFDASFFSNLKNG--RGILE--SDQKLWTD 271

                        250       260       270
                 ....*....|....*....|....*....|....*.
2GHK_X       226 PVFRPLVDKYAADED----AFFADYAEAHQKLSELG 257
Cdd:PLN03030 272 ASTRTFVQRFLGVRGlaglNFNVEFGRSMVKMSNIG 307
cat_per_HPI TIGR00198
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ...
 51-256 4.28e-07

catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules of hydrogen peroxide to dioxygen and two molecules of water. As a peroxidase, it uses hydrogen peroxide to oxidize donor compounds and produce water. KatG from E. coli is a homotetramer with two non-covalently associated iron protoheme IX groups per tetramer, but the ortholog from Synechococcus sp. is a homodimer with one protoheme. Important sites (numbered according to E. coli KatG) include heme ligands His-106 and His-267 and active site Trp-318. Note that the translation PID:g296476 from accession X71420 from Rhodobacter capsulatus B10 contains extensive frameshift differences from the rest of the orthologous family. [Cellular processes, Detoxification]


Pssm-ID: 272957 [Multi-domain]  Cd Length: 716  Bit Score: 50.70  E-value: 4.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X         51 AWHSAGTFDKGTKTGGPFGT-----------IKHPAELAHsanngldiAVRLLEPLKAEFPI--LSYADFYQLAGVVAVE 117
Cdd:TIGR00198 455 AWASASTFRSSDYRGGANGArirlepqknwpVNEPTRLAK--------VLAVLEKIQAEFAKgpVSLADLIVLGGGAAVE 526

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X        118 ---VTGGPE--VPFHPGREDKP------------EPPPEG----RLPDATKGSDHLRDVFGKAMGLTDQDIVALSGGHTI 176
Cdd:TIGR00198 527 kaaLDAGISvnVPFLPGRVDATqamtdaesftplEPIADGfrnyLKRDYAVTPEELLLDKAQLLTLTAPEMTVLIGGMRV 606

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X        177 GAAHKERSGFeGPWTSNPLIFDNSYFTELLS------------------GEKEGLLQLPSDKALL---SDPVFRPLVDKY 235
Cdd:TIGR00198 607 LGANHGGSKH-GVFTDRVGVLSNDFFVNLLDmayewraadnnrylfeggDRQTGEVKWTATRVDLvfgSNSILRAVAEVY 685

                         250       260
                  ....*....|....*....|...
2GHK_X        236 AADE--DAFFADYAEAHQKLSEL 256
Cdd:TIGR00198 686 AQDDarEKFVKDFVAAWTKVMNL 708
catalase_peroxidase_2 cd08200
C-terminal non-catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ...
 47-256 2.09e-05

C-terminal non-catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent peroxidases of the plant superfamily that share a heme prosthetic group and catalyze a multistep oxidative reaction involving hydrogen peroxide as the electron acceptor. Catalase-peroxidases can exhibit both catalase and broad-spectrum peroxidase activities depending on the steady-state concentration of hydrogen peroxide. These enzymes are found in many archaeal and bacterial organisms where they neutralize potentially lethal hydrogen peroxide molecules generated during photosynthesis or stationary phase. Along with related intracellular fungal and plant peroxidases, catalase-peroxidases belong to plant peroxidase superfamily. Unlike the eukaryotic enzymes, they are typically comprised of two homologous domains that probably arose via a single gene duplication event. The heme binding motif is present only in the N-terminal domain; the function of the C-terminal domain is not clear.


Pssm-ID: 173828  Cd Length: 297  Bit Score: 44.91  E-value: 2.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X       47 MLRLAWHSAGTFDKGTKTGGPFG-----------TIKHPAELAHsanngldiAVRLLEPLKAEFPI-------LSYADFY 108
Cdd:cd08200  33 LVSTAWASASTFRNSDKRGGANGarirlapqkdwEVNEPEELAK--------VLAVLEGIQKEFNEsqsggkkVSLADLI 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X      109 QLAGVVAVEVTGGP-----EVPFHPGREDKP------------EP---------------PPEGRLPDatkgsdhlrdvf 156
Cdd:cd08200 105 VLGGCAAVEKAAKDagvdiKVPFTPGRTDATqeqtdvesfevlEPkadgfrnylkkgyrvPPEEMLVD------------ 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X      157 gKA--MGLTDQDIVALSGG-HTIGAAHKERSgfEGPWTSNPLIFDNSYFTELL--------SGEKEGLLQL-------PS 218
Cdd:cd08200 173 -KAqlLTLTAPEMTVLVGGlRVLGANYGGSK--HGVFTDRPGVLTNDFFVNLLdmstewkpADEDDGLFEGrdrktgeVK 249

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
2GHK_X      219 DKALLSDPVF------RPLVDKYAAD--EDAFFADYAEAHQKLSEL 256
Cdd:cd08200 250 WTATRVDLVFgsnselRAVAEVYASDdaQEKFVKDFVAAWTKVMNL 295
PRK15061 PRK15061
catalase/peroxidase;
47-132 9.71e-05

catalase/peroxidase;


Pssm-ID: 237891 [Multi-domain]  Cd Length: 726  Bit Score: 43.20  E-value: 9.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GHK_X        47 MLRLAWHSAGTFDKGTKTGGPFG-----------TIKHPAELAHsanngldiAVRLLEPLKAEFPI-------LSYADFY 108
Cdd:PRK15061 458 LVSTAWASASTFRGSDKRGGANGarirlapqkdwEVNEPAQLAK--------VLAVLEGIQAEFNAaqsggkkVSLADLI 529

                         90       100       110
                 ....*....|....*....|....*....|...
2GHK_X       109 QLAGVVAVE---------VTggpeVPFHPGRED 132
Cdd:PRK15061 530 VLGGNAAVEqaakaaghdVT----VPFTPGRTD 558
 
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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