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Conserved domains on  [gi|1912456256|gb|QOE77468|]
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mitochondrial activity-enhanced ascorbate peroxidase mt-APEX2 [Vector pDP004]

Protein Classification

peroxidase( domain architecture ID 10091038)

peroxidase catalyzes an oxidative reaction involving hydrogen peroxide as the electron acceptor, such as plant ascorbate peroxidase and fungal cytochrome c peroxidase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
 39-284 4.49e-148

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: 415.45  E-value: 4.49e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256  39 YPTVSADY-QDAVEKAKKKLRGFIAEKRCAPLMLRLAFHSAGTFDKGTKTGGPFGTIKHPAELAHSANNGLDIAVRLLEP 117
Cdd:cd00691     1 APVVSAAYaAKDLEAARNDIAKLIDDKNCAPILVRLAWHDSGTYDKETKTGGSNGTIRFDPELNHGANAGLDIARKLLEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 118 LKAEFPILSYADFYQLAGVVAVEVTGGPKVPFHPGREDKPEP---PPEGRLPDPTKGSDHLRDVFGKaMGLTDQDIVALS 194
Cdd:cd00691    81 IKKKYPDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPeecPPEGRLPDASKGADHLRDVFYR-MGFNDQEIVALS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 195 GGHTIGAAHKERSGFEGPWTSNPLIFDNSYFTELLSGEK----EGLLQLPSDKALFSDPVFRPLVDKYAADEDAFFADYA 270
Cdd:cd00691   160 GAHTLGRCHKERSGYDGPWTKNPLKFDNSYFKELLEEDWklptPGLLMLPTDKALLEDPKFRPYVELYAKDQDAFFKDYA 239

                         250
                  ....*....|....
gi 1912456256 271 EAHQKLSELGFADA 284
Cdd:cd00691   240 EAHKKLSELGVPFP 253
 
Name Accession Description Interval E-value
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
 39-284 4.49e-148

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: 415.45  E-value: 4.49e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256  39 YPTVSADY-QDAVEKAKKKLRGFIAEKRCAPLMLRLAFHSAGTFDKGTKTGGPFGTIKHPAELAHSANNGLDIAVRLLEP 117
Cdd:cd00691     1 APVVSAAYaAKDLEAARNDIAKLIDDKNCAPILVRLAWHDSGTYDKETKTGGSNGTIRFDPELNHGANAGLDIARKLLEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 118 LKAEFPILSYADFYQLAGVVAVEVTGGPKVPFHPGREDKPEP---PPEGRLPDPTKGSDHLRDVFGKaMGLTDQDIVALS 194
Cdd:cd00691    81 IKKKYPDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPeecPPEGRLPDASKGADHLRDVFYR-MGFNDQEIVALS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 195 GGHTIGAAHKERSGFEGPWTSNPLIFDNSYFTELLSGEK----EGLLQLPSDKALFSDPVFRPLVDKYAADEDAFFADYA 270
Cdd:cd00691   160 GAHTLGRCHKERSGYDGPWTKNPLKFDNSYFKELLEEDWklptPGLLMLPTDKALLEDPKFRPYVELYAKDQDAFFKDYA 239

                         250
                  ....*....|....
gi 1912456256 271 EAHQKLSELGFADA 284
Cdd:cd00691   240 EAHKKLSELGVPFP 253
PLN02879 PLN02879
L-ascorbate peroxidase
 37-283 6.17e-145

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 407.52  E-value: 6.17e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256  37 KSYPTVSADYQDAVEKAKKKLRGFIAEKRCAPLMLRLAFHSAGTFDKGTKTGGPFGTIKHPAELAHSANNGLDIAVRLLE 116
Cdd:PLN02879    4 KSYPEVKEEYKKAVQRCKRKLRGLIAEKHCAPIVLRLAWHSAGTFDVKTKTGGPFGTIRHPQELAHDANNGLDIAVRLLD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 117 PLKAEFPILSYADFYQLAGVVAVEVTGGPKVPFHPGREDKPEPPPEGRLPDPTKGSDHLRDVFGKaMGLTDQDIVALSGG 196
Cdd:PLN02879   84 PIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPPEGRLPQATKGVDHLRDVFGR-MGLNDKDIVALSGG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 197 HTIGAAHKERSGFEGPWTSNPLIFDNSYFTELLSGEKEGLLQLPSDKALFSDPVFRPLVDKYAADEDAFFADYAEAHQKL 276
Cdd:PLN02879  163 HTLGRCHKERSGFEGAWTPNPLIFDNSYFKEILSGEKEGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHLKL 242


                  ....*..
gi 1912456256 277 SELGFAD 283
Cdd:PLN02879  243 SELGFAD 249
peroxidase pfam00141
Peroxidase;
60-261 4.77e-55

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 176.60  E-value: 4.77e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256  60 FIAEKRCAPLMLRLAFHSAGTfdkgtktGGPFGTI---KHPAELAHSANNGLDIAVRLLEPLKAEFP-----ILSYADFY 131
Cdd:pfam00141   9 FKADPTMGPSLLRLHFHDCFV-------GGCDGSVlldGFKPEKDAPPNLGLRKGFEVIDDIKAKLEaacpgVVSCADIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 132 QLAGVVAVEVTGGPKVPFHPGREDKPEPPPE---GRLPDPTKGSDHLRDVFgKAMGLTDQDIVALSGGHTIGAAHKersg 208
Cdd:pfam00141  82 ALAARDAVELAGGPSWPVPLGRRDGTVSSAVeanSNLPAPTDSLDQLRDRF-ARKGLTAEDLVALSGAHTIGRAHK---- 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1912456256 209 fegpwtsnplifdnsyftELLSGekEGLlqLPSDKALFSDPVFRPLVDKYAAD 261
Cdd:pfam00141 157 ------------------NLLDG--RGL--LTSDQALLSDPRTRALVERYAAD 187
cat_per_HPI TIGR00198
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ...
 67-277 3.23e-20

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: 90.76  E-value: 3.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256  67 APLMLRLAFHSAGTFDKGTKTGGPF-GTIKHPAELAHSANNGLDIAVRLLEPLKAEF-PILSYADFYQLAGVVAVEVTGG 144
Cdd:TIGR00198  80 GGLFIRMAWHAAGTYRIADGRGGAAtGNQRFAPLNSWPDNVNLDKARRLLWPIKKKYgNKLSWADLIILAGTVAYESMGL 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 145 PKVPFHPGREDKPEPP-------------------------------------PEG--RLPDPTKGSDHLRDVFGKaMGL 185
Cdd:TIGR00198 160 KVFGFAGGREDIWEPDkdiywgaekewltssredreslenplaatemgliyvnPEGpdGHPDPLCTAQDIRTTFAR-MGM 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 186 TDQDIVAL-SGGHTIGAAHKE-----------------------------------RSGFEGPWTSNPLIFDNSYFTELL 229
Cdd:TIGR00198 239 NDEETVALiAGGHTVGKCHGAgpaeligpdpegapieeqglgwhnqygkgvgrdtmTSGLEVAWTTTPTQWDNGYFYMLF 318

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1912456256 230 SGEKE------GLLQ------------------------LPSDKALFSDPVFRPLVDKYAADEDAFFADYAEAHQKLS 277
Cdd:TIGR00198 319 NYEWElkkspaGAWQweavdapeiipdvedpnkkhnpimLDADLALRFDPEFRKISRRFLREPDYFAEAFAKAWFKLT 396
KatG COG0376
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
68-276 6.05e-16

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


Pssm-ID: 440145 [Multi-domain]  Cd Length: 731  Bit Score: 77.85  E-value: 6.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256  68 PLMLRLAFHSAGTFDKGTKTGGpfgtikhpaelAHSAN-----------NG-LDIAVRLLEPLKAEF-PILSYADFYQLA 134
Cdd:COG0376    89 PLFIRMAWHSAGTYRIGDGRGG-----------AGGGQqrfaplnswpdNAnLDKARRLLWPIKQKYgNKISWADLMILA 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 135 GVVAVEVTGGPKVPFHPGREDKPEPP--------------------------------------PEG--RLPDPTKGSDH 174
Cdd:COG0376   158 GNVALESMGFKTFGFAGGREDVWEPEedvywgpetewlgderysgdrelenplaavqmgliyvnPEGpnGNPDPLAAARD 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 175 LRDVFGKaMGLTDQDIVAL-SGGHTIGAAH------------------------KER-----------SGFEGPWTSNPL 218
Cdd:COG0376   238 IRETFGR-MAMNDEETVALiAGGHTFGKTHgagdaehvgpepeaapieeqglgwKNSfgsgkgedtitSGLEGAWTPTPT 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 219 IFDNSYFTELL--------------------------------SGEKEGLLQLPSDKALFSDPVFRPLVDKYAADEDAfF 266
Cdd:COG0376   317 QWDNGYFDNLFgyeweltkspagahqwvpkdgaaadtvpdahdPSKRHAPMMLTTDLALRFDPAYEKISRRFLENPEE-F 395

                         330
                  ....*....|.
gi 1912456256 267 AD-YAEAHQKL 276
Cdd:COG0376   396 ADaFARAWFKL 406
 
Name Accession Description Interval E-value
ascorbate_peroxidase cd00691
Ascorbate peroxidases and cytochrome C peroxidases; Ascorbate peroxidases are a subgroup of ...
 39-284 4.49e-148

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: 415.45  E-value: 4.49e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256  39 YPTVSADY-QDAVEKAKKKLRGFIAEKRCAPLMLRLAFHSAGTFDKGTKTGGPFGTIKHPAELAHSANNGLDIAVRLLEP 117
Cdd:cd00691     1 APVVSAAYaAKDLEAARNDIAKLIDDKNCAPILVRLAWHDSGTYDKETKTGGSNGTIRFDPELNHGANAGLDIARKLLEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 118 LKAEFPILSYADFYQLAGVVAVEVTGGPKVPFHPGREDKPEP---PPEGRLPDPTKGSDHLRDVFGKaMGLTDQDIVALS 194
Cdd:cd00691    81 IKKKYPDISYADLWQLAGVVAIEEMGGPKIPFRPGRVDASDPeecPPEGRLPDASKGADHLRDVFYR-MGFNDQEIVALS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 195 GGHTIGAAHKERSGFEGPWTSNPLIFDNSYFTELLSGEK----EGLLQLPSDKALFSDPVFRPLVDKYAADEDAFFADYA 270
Cdd:cd00691   160 GAHTLGRCHKERSGYDGPWTKNPLKFDNSYFKELLEEDWklptPGLLMLPTDKALLEDPKFRPYVELYAKDQDAFFKDYA 239

                         250
                  ....*....|....
gi 1912456256 271 EAHQKLSELGFADA 284
Cdd:cd00691   240 EAHKKLSELGVPFP 253
PLN02879 PLN02879
L-ascorbate peroxidase
 37-283 6.17e-145

L-ascorbate peroxidase


Pssm-ID: 178467 [Multi-domain]  Cd Length: 251  Bit Score: 407.52  E-value: 6.17e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256  37 KSYPTVSADYQDAVEKAKKKLRGFIAEKRCAPLMLRLAFHSAGTFDKGTKTGGPFGTIKHPAELAHSANNGLDIAVRLLE 116
Cdd:PLN02879    4 KSYPEVKEEYKKAVQRCKRKLRGLIAEKHCAPIVLRLAWHSAGTFDVKTKTGGPFGTIRHPQELAHDANNGLDIAVRLLD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 117 PLKAEFPILSYADFYQLAGVVAVEVTGGPKVPFHPGREDKPEPPPEGRLPDPTKGSDHLRDVFGKaMGLTDQDIVALSGG 196
Cdd:PLN02879   84 PIKELFPILSYADFYQLAGVVAVEITGGPEIPFHPGRLDKVEPPPEGRLPQATKGVDHLRDVFGR-MGLNDKDIVALSGG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 197 HTIGAAHKERSGFEGPWTSNPLIFDNSYFTELLSGEKEGLLQLPSDKALFSDPVFRPLVDKYAADEDAFFADYAEAHQKL 276
Cdd:PLN02879  163 HTLGRCHKERSGFEGAWTPNPLIFDNSYFKEILSGEKEGLLQLPTDKALLDDPLFLPFVEKYAADEDAFFEDYTEAHLKL 242


                  ....*..
gi 1912456256 277 SELGFAD 283
Cdd:PLN02879  243 SELGFAD 249
PLN02364 PLN02364
L-ascorbate peroxidase 1
 37-284 1.37e-142

L-ascorbate peroxidase 1


Pssm-ID: 166005  Cd Length: 250  Bit Score: 401.38  E-value: 1.37e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256  37 KSYPTVSADYQDAVEKAKKKLRGFIAEKRCAPLMLRLAFHSAGTFDKGTKTGGPFGTIKHPAELAHSANNGLDIAVRLLE 116
Cdd:PLN02364    3 KNYPTVSEDYKKAVEKCRRKLRGLIAEKNCAPIMVRLAWHSAGTFDCQSRTGGPFGTMRFDAEQAHGANSGIHIALRLLD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 117 PLKAEFPILSYADFYQLAGVVAVEVTGGPKVPFHPGREDKPEPPPEGRLPDPTKGSDHLRDVFGKAMGLTDQDIVALSGG 196
Cdd:PLN02364   83 PIREQFPTISFADFHQLAGVVAVEVTGGPDIPFHPGREDKPQPPPEGRLPDATKGCDHLRDVFAKQMGLSDKDIVALSGA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 197 HTIGAAHKERSGFEGPWTSNPLIFDNSYFTELLSGEKEGLLQLPSDKALFSDPVFRPLVDKYAADEDAFFADYAEAHQKL 276
Cdd:PLN02364  163 HTLGRCHKDRSGFEGAWTSNPLIFDNSYFKELLSGEKEGLLQLVSDKALLDDPVFRPLVEKYAADEDAFFADYAEAHMKL 242


                  ....*...
gi 1912456256 277 SELGFADA 284
Cdd:PLN02364  243 SELGFADA 250
PLN02608 PLN02608
L-ascorbate peroxidase
 40-281 5.17e-136

L-ascorbate peroxidase


Pssm-ID: 178218 [Multi-domain]  Cd Length: 289  Bit Score: 386.04  E-value: 5.17e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256  40 PTVSADYQDAVEKAKKKLRGFIAEKRCAPLMLRLAFHSAGTFDKGTKTGGPFGTIKHPAELAHSANNGLDIAVRLLEPLK 119
Cdd:PLN02608    4 PVVDAEYLKEIEKARRDLRALIASKNCAPIMLRLAWHDAGTYDAKTKTGGPNGSIRNEEEYSHGANNGLKIAIDLCEPVK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 120 AEFPILSYADFYQLAGVVAVEVTGGPKVPFHPGREDKPEPPPEGRLPDPTKGSDHLRDVFGKaMGLTDQDIVALSGGHTI 199
Cdd:PLN02608   84 AKHPKITYADLYQLAGVVAVEVTGGPTIDFVPGRKDSNACPEEGRLPDAKKGAKHLRDVFYR-MGLSDKDIVALSGGHTL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 200 GAAHKERSGFEGPWTSNPLIFDNSYFTELLSGEKEGLLQLPSDKALFSDPVFRPLVDKYAADEDAFFADYAEAHQKLSEL 279
Cdd:PLN02608  163 GRAHPERSGFDGPWTKEPLKFDNSYFVELLKGESEGLLKLPTDKALLEDPEFRPYVELYAKDEDAFFRDYAESHKKLSEL 242


                  ..
gi 1912456256 280 GF 281
Cdd:PLN02608  243 GF 244
plant_peroxidase_like cd00314
Heme-dependent peroxidases similar to plant peroxidases; Along with animal peroxidases, these ...
 51-278 5.79e-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: 204.31  E-value: 5.79e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256  51 EKAKKKLRGFIAE-KRCAPLMLRLAFHSAGTFDKGT-KTGGPFGTIKHPAELAHSANNGLDIAVRLLEPLKAEFP---IL 125
Cdd:cd00314     1 DAIKAILEDLITQaGALAGSLLRLAFHDAGTYDIADgKGGGADGSIRFEPELDRPENGGLDKALRALEPIKSAYDggnPV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 126 SYADFYQLAGVVAVEVT--GGPKVPFHPGREDKPEPP-----PEGRLPDPTKGSDHLRDVFgKAMGLTDQDIVALS-GGH 197
Cdd:cd00314    81 SRADLIALAGAVAVESTfgGGPLIPFRFGRLDATEPDlgvpdPEGLLPNETSSATELRDKF-KRMGLSPSELVALSaGAH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 198 TI-GAAHKERSGFE--GPWTSNPLIFDNSYFTELLSGEKE------------GLLQLPSDKALFSDPVFRPLVDKYAADE 262
Cdd:cd00314   160 TLgGKNHGDLLNYEgsGLWTSTPFTFDNAYFKNLLDMNWEwrvgspdpdgvkGPGLLPSDYALLSDSETRALVERYASDQ 239

                         250
                  ....*....|....*.
gi 1912456256 263 DAFFADYAEAHQKLSE 278
Cdd:cd00314   240 EKFFEDFAKAWIKMVN 255
peroxidase pfam00141
Peroxidase;
60-261 4.77e-55

Peroxidase;


Pssm-ID: 425483 [Multi-domain]  Cd Length: 187  Bit Score: 176.60  E-value: 4.77e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256  60 FIAEKRCAPLMLRLAFHSAGTfdkgtktGGPFGTI---KHPAELAHSANNGLDIAVRLLEPLKAEFP-----ILSYADFY 131
Cdd:pfam00141   9 FKADPTMGPSLLRLHFHDCFV-------GGCDGSVlldGFKPEKDAPPNLGLRKGFEVIDDIKAKLEaacpgVVSCADIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 132 QLAGVVAVEVTGGPKVPFHPGREDKPEPPPE---GRLPDPTKGSDHLRDVFgKAMGLTDQDIVALSGGHTIGAAHKersg 208
Cdd:pfam00141  82 ALAARDAVELAGGPSWPVPLGRRDGTVSSAVeanSNLPAPTDSLDQLRDRF-ARKGLTAEDLVALSGAHTIGRAHK---- 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1912456256 209 fegpwtsnplifdnsyftELLSGekEGLlqLPSDKALFSDPVFRPLVDKYAAD 261
Cdd:pfam00141 157 ------------------NLLDG--RGL--LTSDQALLSDPRTRALVERYAAD 187
secretory_peroxidase cd00693
Horseradish peroxidase and related secretory plant peroxidases; Secretory peroxidases belong ...
 47-280 9.09e-33

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: 122.24  E-value: 9.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256  47 QDAVEKAkkklrgFIAEKRCAPLMLRLAFHSAgtFDKG-------TKTGGPfgtikhPAELAHSANNGL------DIAVR 113
Cdd:cd00693    19 RSVVRAA------VKADPRLAAALLRLHFHDC--FVRGcdasvllDSTANN------TSEKDAPPNLSLrgfdviDDIKA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 114 LLEplkAEFP-ILSYADFYQLAGVVAVEVTGGP--KVPFhpGRED--KPEPPPEGRLPDPTKGSDHLRDVFgKAMGLTDQ 188
Cdd:cd00693    85 ALE---AACPgVVSCADILALAARDAVVLAGGPsyEVPL--GRRDgrVSSANDVGNLPSPFFSVSQLISLF-ASKGLTVT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 189 DIVALSGGHTIGAAH----KER-SGFEG--------------------PWTSN-----------PLIFDNSYFTELLSGe 232
Cdd:cd00693   159 DLVALSGAHTIGRAHcssfSDRlYNFSGtgdpdptldpayaaqlrkkcPAGGDddtlvpldpgtPNTFDNSYYKNLLAG- 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1912456256 233 kEGLLQlpSDKALFSDPVFRPLVDKYAADEDAFFADYAEAHQKLSELG 280
Cdd:cd00693   238 -RGLLT--SDQALLSDPRTRAIVNRYAANQDAFFRDFAAAMVKMGNIG 282
ligninase cd00692
Ligninase and other manganese-dependent fungal peroxidases; Ligninases and related ...
 71-281 2.83e-26

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: 105.56  E-value: 2.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256  71 LRLAFHSAGTFDK----GTKTGG-------PFGTIkhpaELAHSANNGLDIAVRLLEPLKAEFPIlSYADFYQLAGVVAV 139
Cdd:cd00692    42 LRLTFHDAIGFSPalaaGQFGGGgadgsivLFDDI----ETAFHANIGLDEIVEALRPFHQKHNV-SMADFIQFAGAVAV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 140 -EVTGGPKVPFHPGREDKPEPPPEGRLPDPTKGSDHLRDVFGKAmGLTDQDIVALSGGHTIGAAHKERSGFEG-PWTSNP 217
Cdd:cd00692   117 sNCPGAPRLEFYAGRKDATQPAPDGLVPEPFDSVDKILARFADA-GFSPDELVALLAAHSVAAQDFVDPSIAGtPFDSTP 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 218 LIFDNSYFTE-LLSGE---------------KEGLLQLPSDKALFSDPVFRPLVDKYAADEDAFFADYAEAHQKLSELGF 281
Cdd:cd00692   196 GVFDTQFFIEtLLKGTafpgsggnqgevespLPGEFRLQSDFLLARDPRTACEWQSFVNNQAKMNAAFAAAMLKLSLLGQ 275
catalase_peroxidase_1 cd00649
N-terminal catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ...
 68-276 1.02e-21

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: 93.91  E-value: 1.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256  68 PLMLRLAFHSAGTFDKGTKTGGPFGTIKHPAELAHSANNG-LDIAVRLLEPLKAEF-PILSYADFYQLAGVVAVEVTGGP 145
Cdd:cd00649    71 PLFIRMAWHSAGTYRIADGRGGAGTGQQRFAPLNSWPDNVnLDKARRLLWPIKQKYgNKISWADLMILAGNVALESMGFK 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 146 KVPFHPGREDKPEPP--------------------------------------PEG--RLPDPTKGSDHLRDVFGKaMGL 185
Cdd:cd00649   151 TFGFAGGREDVWEPDedvywgpekewladkrysgdrdlenplaavqmgliyvnPEGpdGNPDPLAAAKDIRETFAR-MAM 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 186 TDQDIVAL-SGGHTIGAAH---------KE--------------------------RSGFEGPWTSNPLIFDNSYFTELL 229
Cdd:cd00649   230 NDEETVALiAGGHTFGKTHgagpashvgPEpeaapieqqglgwknsygtgkgkdtiTSGLEGAWTPTPTKWDNNYLKNLF 309

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1912456256 230 S--------------------------------GEKEGLLQLPSDKALFSDPVFRPLVDKYAADEDAFFADYAEAHQKL 276
Cdd:cd00649   310 GyeweltkspagawqwvpknaagentvpdahdpSKKHAPMMLTTDLALRFDPEYEKISRRFLENPDEFADAFAKAWFKL 388
cat_per_HPI TIGR00198
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ...
 67-277 3.23e-20

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: 90.76  E-value: 3.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256  67 APLMLRLAFHSAGTFDKGTKTGGPF-GTIKHPAELAHSANNGLDIAVRLLEPLKAEF-PILSYADFYQLAGVVAVEVTGG 144
Cdd:TIGR00198  80 GGLFIRMAWHAAGTYRIADGRGGAAtGNQRFAPLNSWPDNVNLDKARRLLWPIKKKYgNKLSWADLIILAGTVAYESMGL 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 145 PKVPFHPGREDKPEPP-------------------------------------PEG--RLPDPTKGSDHLRDVFGKaMGL 185
Cdd:TIGR00198 160 KVFGFAGGREDIWEPDkdiywgaekewltssredreslenplaatemgliyvnPEGpdGHPDPLCTAQDIRTTFAR-MGM 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 186 TDQDIVAL-SGGHTIGAAHKE-----------------------------------RSGFEGPWTSNPLIFDNSYFTELL 229
Cdd:TIGR00198 239 NDEETVALiAGGHTVGKCHGAgpaeligpdpegapieeqglgwhnqygkgvgrdtmTSGLEVAWTTTPTQWDNGYFYMLF 318

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1912456256 230 SGEKE------GLLQ------------------------LPSDKALFSDPVFRPLVDKYAADEDAFFADYAEAHQKLS 277
Cdd:TIGR00198 319 NYEWElkkspaGAWQweavdapeiipdvedpnkkhnpimLDADLALRFDPEFRKISRRFLREPDYFAEAFAKAWFKLT 396
plant_peroxidase_like_1 cd08201
Uncharacterized family of plant peroxidase-like proteins; This is a subgroup of heme-dependent ...
 71-247 4.48e-17

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: 79.05  E-value: 4.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256  71 LRLAFHSAGTFDKGTKTGGPFGTIKHPAELAHSANNGLDIAVRLLEPLKAefPILSYADFYQLAGVVAVEVTGGPKVPFH 150
Cdd:cd08201    46 LRTAFHDMATHNVDDGTGGLDASIQYELDRPENIGSGFNTTLNFFVNFYS--PRSSMADLIAMGVVTSVASCGGPVVPFR 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 151 PGREDKPEPPPEGrLPDPTKGSDHLRDVFGKaMGLTDQDIVALSG-GHTIGAAHKER-----------SGFEGPWTSNPl 218
Cdd:cd08201   124 AGRIDATEAGQAG-VPEPQTDLGTTTESFRR-QGFSTSEMIALVAcGHTLGGVHSEDfpeivppgsvpDTVLQFFDTTI- 200

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1912456256 219 IFDNSYFTELLSGEKEGLL------QLPSDKALFS 247
Cdd:cd08201   201 QFDNKVVTEYLSGTTNNPLvvgpnnTTNSDLRIFS 235
PRK15061 PRK15061
catalase/peroxidase;
68-276 2.17e-16

catalase/peroxidase;


Pssm-ID: 237891 [Multi-domain]  Cd Length: 726  Bit Score: 79.03  E-value: 2.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256  68 PLMLRLAFHSAGTFDKGTKTGGpfgtikhpaelahsANNG---------------LDIAVRLLEPLKAEF-PILSYADFY 131
Cdd:PRK15061   83 PLFIRMAWHSAGTYRIGDGRGG--------------AGGGqqrfaplnswpdnvnLDKARRLLWPIKQKYgNKISWADLM 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 132 QLAGVVAVEVTGGPKVPFHPGREDKPEP---------------------------P------------PEG--RLPDPTK 170
Cdd:PRK15061  149 ILAGNVALESMGFKTFGFAGGREDVWEPeedvywgpekewlggderysgerdlenPlaavqmgliyvnPEGpnGNPDPLA 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 171 GSDHLRDVFGKaMGLTDQDIVAL-SGGHTIGAAH-------------------------------KER----SGFEGPWT 214
Cdd:PRK15061  229 AARDIRETFAR-MAMNDEETVALiAGGHTFGKTHgagdashvgpepeaapieeqglgwknsygsgKGAdtitSGLEGAWT 307

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 215 SNPLIFDNSYFTELLSGEKE------GLLQ--------------------------LPSDKALFSDPVFRPLVDKYAADE 262
Cdd:PRK15061  308 TTPTQWDNGYFENLFGYEWEltkspaGAWQwvpkdgaaedtvpdahdpskkhaptmLTTDLALRFDPEYEKISRRFLENP 387

                         330
                  ....*....|....*
gi 1912456256 263 DAfFAD-YAEAHQKL 276
Cdd:PRK15061  388 EE-FADaFARAWFKL 401
KatG COG0376
Catalase (peroxidase I) [Inorganic ion transport and metabolism];
68-276 6.05e-16

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


Pssm-ID: 440145 [Multi-domain]  Cd Length: 731  Bit Score: 77.85  E-value: 6.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256  68 PLMLRLAFHSAGTFDKGTKTGGpfgtikhpaelAHSAN-----------NG-LDIAVRLLEPLKAEF-PILSYADFYQLA 134
Cdd:COG0376    89 PLFIRMAWHSAGTYRIGDGRGG-----------AGGGQqrfaplnswpdNAnLDKARRLLWPIKQKYgNKISWADLMILA 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 135 GVVAVEVTGGPKVPFHPGREDKPEPP--------------------------------------PEG--RLPDPTKGSDH 174
Cdd:COG0376   158 GNVALESMGFKTFGFAGGREDVWEPEedvywgpetewlgderysgdrelenplaavqmgliyvnPEGpnGNPDPLAAARD 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 175 LRDVFGKaMGLTDQDIVAL-SGGHTIGAAH------------------------KER-----------SGFEGPWTSNPL 218
Cdd:COG0376   238 IRETFGR-MAMNDEETVALiAGGHTFGKTHgagdaehvgpepeaapieeqglgwKNSfgsgkgedtitSGLEGAWTPTPT 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 219 IFDNSYFTELL--------------------------------SGEKEGLLQLPSDKALFSDPVFRPLVDKYAADEDAfF 266
Cdd:COG0376   317 QWDNGYFDNLFgyeweltkspagahqwvpkdgaaadtvpdahdPSKRHAPMMLTTDLALRFDPAYEKISRRFLENPEE-F 395

                         330
                  ....*....|.
gi 1912456256 267 AD-YAEAHQKL 276
Cdd:COG0376   396 ADaFARAWFKL 406
PLN03030 PLN03030
cationic peroxidase; Provisional
 60-280 5.25e-10

cationic peroxidase; Provisional


Pssm-ID: 215545 [Multi-domain]  Cd Length: 324  Bit Score: 59.20  E-value: 5.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256  60 FIAEKRCAPLMLRLAFHSAgtFDKGTKTGGPF-GTIKHPAELAHSANNGLDIAVRLLEPLKAEFP-ILSYADFYQLAGVV 137
Cdd:PLN03030   49 FQSNPAIAPGLLRMHFHDC--FVRGCDASILIdGSNTEKTALPNLLLRGYDVIDDAKTQLEAACPgVVSCADILALAARD 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 138 AVEVTGGPKVPFHPGREDkpepppeGR---------LPDPTKGSDHLRDVFGkAMGLTDQDIVALSGGHTIGAAH----- 203
Cdd:PLN03030  127 SVVLTNGLTWPVPTGRRD-------GRvslasdasnLPGFTDSIDVQKQKFA-AKGLNTQDLVTLVGGHTIGTTAcqffr 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 204 -----------------------------------KERSGFEgpwTSNPLIFDNSYFTELLSGekEGLLQlpSDKALFSD 248
Cdd:PLN03030  199 yrlynftttgngadpsidasfvpqlqalcpqngdgSRRIALD---TGSSNRFDASFFSNLKNG--RGILE--SDQKLWTD 271

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1912456256 249 PVFRPLVDKYAADED----AFFADYAEAHQKLSELG 280
Cdd:PLN03030  272 ASTRTFVQRFLGVRGlaglNFNVEFGRSMVKMSNIG 307
cat_per_HPI TIGR00198
catalase/peroxidase HPI; As catalase, this enzyme catalyzes the dismutation of two molecules ...
 74-229 1.52e-05

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: 46.46  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256  74 AFHSAGTFDKGTKTGGPFGT-----------IKHPAELAHsanngldiAVRLLEPLKAEFPI--LSYADFYQLAGVVAVE 140
Cdd:TIGR00198 455 AWASASTFRSSDYRGGANGArirlepqknwpVNEPTRLAK--------VLAVLEKIQAEFAKgpVSLADLIVLGGGAAVE 526

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 141 ---VTGG--PKVPFHPGREDKPEPPPEGRLPDPTKG-SDHLRDVFGK---------------AMGLTDQDIVALSGGHTI 199
Cdd:TIGR00198 527 kaaLDAGisVNVPFLPGRVDATQAMTDAESFTPLEPiADGFRNYLKRdyavtpeellldkaqLLTLTAPEMTVLIGGMRV 606

                         170       180       190
                  ....*....|....*....|....*....|
gi 1912456256 200 GAAHKERSGFeGPWTSNPLIFDNSYFTELL 229
Cdd:TIGR00198 607 LGANHGGSKH-GVFTDRVGVLSNDFFVNLL 635
catalase_peroxidase_2 cd08200
C-terminal non-catalytic domain of catalase-peroxidases; This is a subgroup of heme-dependent ...
 70-279 1.43e-04

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: 42.60  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256  70 MLRLAFHSAGTFDKGTKTGGPFG-----------TIKHPAELAHsanngldiAVRLLEPLKAEFPI-------LSYADFY 131
Cdd:cd08200    33 LVSTAWASASTFRNSDKRGGANGarirlapqkdwEVNEPEELAK--------VLAVLEGIQKEFNEsqsggkkVSLADLI 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 132 QLAGVVAVEVTGGP-----KVPFHPGREDKP------------EPPPEG-----RLPDPTKGSDHLRDvfgKA--MGLTD 187
Cdd:cd08200   105 VLGGCAAVEKAAKDagvdiKVPFTPGRTDATqeqtdvesfevlEPKADGfrnylKKGYRVPPEEMLVD---KAqlLTLTA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256 188 QDIVALSGG-HTIGAAHKERSgfEGPWTSNPLIFDNSYFTELL--------SGEKEGLLQL-------PSDKALFSDPVF 251
Cdd:cd08200   182 PEMTVLVGGlRVLGANYGGSK--HGVFTDRPGVLTNDFFVNLLdmstewkpADEDDGLFEGrdrktgeVKWTATRVDLVF 259

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1912456256 252 ------RPLVDKYAAD--EDAFFADYAEAHQKLSEL 279
Cdd:cd08200   260 gsnselRAVAEVYASDdaQEKFVKDFVAAWTKVMNL 295
PRK15061 PRK15061
catalase/peroxidase;
70-155 4.10e-03

catalase/peroxidase;


Pssm-ID: 237891 [Multi-domain]  Cd Length: 726  Bit Score: 38.58  E-value: 4.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1912456256  70 MLRLAFHSAGTFDKGTKTGGPFG-----------TIKHPAELAHsanngldiAVRLLEPLKAEFPI-------LSYADFY 131
Cdd:PRK15061  458 LVSTAWASASTFRGSDKRGGANGarirlapqkdwEVNEPAQLAK--------VLAVLEGIQAEFNAaqsggkkVSLADLI 529

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1912456256 132 QLAGVVAVE---------VTggpkVPFHPGRED 155
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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