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Conserved domains on  [gi|334184487|ref|NP_001189610|]
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heme oxygenase 2 [Arabidopsis thaliana]

Protein Classification

biliverdin-producing heme oxygenase( domain architecture ID 13040583)

biliverdin-producing heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin, which is subsequently converted to bilirubin by biliverdin reductase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HemeO cd19165
heme oxygenase in eukaryotes and some bacteria; This subfamily contains heme oxygenase (HO, EC ...
 127-297 5.39e-45

heme oxygenase in eukaryotes and some bacteria; This subfamily contains heme oxygenase (HO, EC 1.14.14.18) found in eukaryotes as well as some proteobacteria, including cyanobacteria. Heme oxygenase (HO) catalyzes the rate limiting step in the degradation of heme to biliverdin in a multi-step reaction. HO is essential for recycling of iron from heme which is used as a substrate and cofactor for its own degradation to biliverdin, iron, and carbon monoxide. In vertebrates, HO plays a role in heme homeostasis and oxidative stress response, and cellular signaling in mammals that include isoforms HO-1, HO-2 and HO-3. HO-1 is ubiquitously expressed after induction while HO-2 expression is constitutive, mostly limited to certain organs, such as the brain, testes, and the vascular system. HO-3 is non-functional in humans, suggesting that the Hmox3 gene is a pseudogene derived from HO-2 transcripts. In higher plants and cyanobacteria, heme oxygenase is required for the synthesis of light-harvesting pigments, which contain tetrapyrrols derived from biliverdin. Candida albicans expresses a heme oxygenase that is required for the utilization of heme as a nutritional iron source, whereas Saccharomyces cerevisiae responds to iron deprivation by increasing Hmx1p transcription, which is controlled by the major iron-dependent transcription factor, Aft1p, and promotes both the re-utilization of heme iron and the regulation of heme-dependent transcription during periods of iron scarcity. In pathogenic bacteria, HO is part of a pathway for iron acquisition from host heme. In Leptospira interrogans, a pathogenic spirochete that causes leptospirosis, HO is required for iron utilization when hemoglobin is the sole iron source, thus making HO an interesting target for novel antimicrobial agents. HO shares tertiary structure similarity to methane monooxygenase (EC 1.14.13.25), ribonucleotide reductase (EC 1.17.4.1) and thiaminase II (EC 3.5.99.2), but shares little sequence homology.


:

Pssm-ID: 350856  Cd Length: 205  Bit Score: 151.59  E-value: 5.39e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184487 127 KPSKEGFLKYLVDSKLVFDTIERIVDESENVSYA--YFRRTGLERCESIEKDLQWLREQDLVIPE-PSNVGVSYAKYLEE 203
Cdd:cd19165   30 PLDREAYARLLVQLYFVYEALEEALDRLADDPVLaaALYDPELERSEALEADLAFLLGPDWREPIpPSPATAAYVARIRE 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184487 204 QAGESAPLFLSHFYSIYFSHIAGGQVLVRQVSEK--LLEGKELEFNRWEG--DAQDLLKGVREKLNVLGehWSRDEKNKC 279
Cdd:cd19165  110 LAEEKPHLLLAHAYVRYLGDLSGGQIIRRKLAKAygLFGGEGLSFYDFDGigDGKDLKDEYRARLDALE--LTEEEKDAI 187

                        170
                 ....*....|....*...
gi 334184487 280 LKETAKAFKYMGQIVRLI 297
Cdd:cd19165  188 VEEAKLAFELNIALFEEL 205
 
Name Accession Description Interval E-value
HemeO cd19165
heme oxygenase in eukaryotes and some bacteria; This subfamily contains heme oxygenase (HO, EC ...
 127-297 5.39e-45

heme oxygenase in eukaryotes and some bacteria; This subfamily contains heme oxygenase (HO, EC 1.14.14.18) found in eukaryotes as well as some proteobacteria, including cyanobacteria. Heme oxygenase (HO) catalyzes the rate limiting step in the degradation of heme to biliverdin in a multi-step reaction. HO is essential for recycling of iron from heme which is used as a substrate and cofactor for its own degradation to biliverdin, iron, and carbon monoxide. In vertebrates, HO plays a role in heme homeostasis and oxidative stress response, and cellular signaling in mammals that include isoforms HO-1, HO-2 and HO-3. HO-1 is ubiquitously expressed after induction while HO-2 expression is constitutive, mostly limited to certain organs, such as the brain, testes, and the vascular system. HO-3 is non-functional in humans, suggesting that the Hmox3 gene is a pseudogene derived from HO-2 transcripts. In higher plants and cyanobacteria, heme oxygenase is required for the synthesis of light-harvesting pigments, which contain tetrapyrrols derived from biliverdin. Candida albicans expresses a heme oxygenase that is required for the utilization of heme as a nutritional iron source, whereas Saccharomyces cerevisiae responds to iron deprivation by increasing Hmx1p transcription, which is controlled by the major iron-dependent transcription factor, Aft1p, and promotes both the re-utilization of heme iron and the regulation of heme-dependent transcription during periods of iron scarcity. In pathogenic bacteria, HO is part of a pathway for iron acquisition from host heme. In Leptospira interrogans, a pathogenic spirochete that causes leptospirosis, HO is required for iron utilization when hemoglobin is the sole iron source, thus making HO an interesting target for novel antimicrobial agents. HO shares tertiary structure similarity to methane monooxygenase (EC 1.14.13.25), ribonucleotide reductase (EC 1.17.4.1) and thiaminase II (EC 3.5.99.2), but shares little sequence homology.


Pssm-ID: 350856  Cd Length: 205  Bit Score: 151.59  E-value: 5.39e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184487 127 KPSKEGFLKYLVDSKLVFDTIERIVDESENVSYA--YFRRTGLERCESIEKDLQWLREQDLVIPE-PSNVGVSYAKYLEE 203
Cdd:cd19165   30 PLDREAYARLLVQLYFVYEALEEALDRLADDPVLaaALYDPELERSEALEADLAFLLGPDWREPIpPSPATAAYVARIRE 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184487 204 QAGESAPLFLSHFYSIYFSHIAGGQVLVRQVSEK--LLEGKELEFNRWEG--DAQDLLKGVREKLNVLGehWSRDEKNKC 279
Cdd:cd19165  110 LAEEKPHLLLAHAYVRYLGDLSGGQIIRRKLAKAygLFGGEGLSFYDFDGigDGKDLKDEYRARLDALE--LTEEEKDAI 187

                        170
                 ....*....|....*...
gi 334184487 280 LKETAKAFKYMGQIVRLI 297
Cdd:cd19165  188 VEEAKLAFELNIALFEEL 205
Heme_oxygenase pfam01126
Heme oxygenase;
129-295 1.62e-07

Heme oxygenase;


Pssm-ID: 395895  Cd Length: 204  Bit Score: 50.82  E-value: 1.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184487  129 SKEGFLKYLVDSKLVFDTIER-IVDESENVSYAYFRRTGLERCESIEKDLQWLR-EQDLVIPEPSNVGVSYAKYLEEQAG 206
Cdd:pfam01126  33 DKDAYAKLLANLYFVYSALEEeLERNRDSPVAAPIYFPELNRKAALERDLAYLYgADWRADIQDSPATQEYVPRIREIGN 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184487  207 ESAPLFLSHFYSIYFSHIAGGQVLVR--QVSEKLLEGKELEFNRWEG--DAQDLLKGVREKLNVLgeHWSRDEKNKCLKE 282
Cdd:pfam01126 113 ESPELLVAHAYTRYLGDLSGGQLLKKiaQRALGLPPGEGTAFYEFEGisDRKVFKQEYREALNAL--ELDDEARARAVEE 190

                         170
                  ....*....|...
gi 334184487  283 TAKAFKYMGQIVR 295
Cdd:pfam01126 191 ANDAFALNIQVFR 203
COG5398 COG5398
Heme oxygenase [Coenzyme transport and metabolism];
167-289 6.34e-07

Heme oxygenase [Coenzyme transport and metabolism];


Pssm-ID: 444157  Cd Length: 211  Bit Score: 49.05  E-value: 6.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184487 167 LERCESIEKDLQWL-----REQdlviPEPSNVGVSYAKYLEEQAGESAPLFLSHFYSIYFSHIAGGQVLVRQVSE--KLL 239
Cdd:COG5398   72 LNRLPALEADLAFLygpdwRDQ----ITPLPATRAYVARIREVAAEWPELLVAHHYTRYLGDLSGGQIIKRILQRayGLP 147

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334184487 240 EGKELEFnrWEGDAQDLLKGV----REKLNVLGehWSRDEKNKCLKETAKAFKY 289
Cdd:COG5398  148 DGEGTAF--YEFDEIPDPKAFkdryRAALDALP--LDEAERERIVDEANLAFRL 197
 
Name Accession Description Interval E-value
HemeO cd19165
heme oxygenase in eukaryotes and some bacteria; This subfamily contains heme oxygenase (HO, EC ...
 127-297 5.39e-45

heme oxygenase in eukaryotes and some bacteria; This subfamily contains heme oxygenase (HO, EC 1.14.14.18) found in eukaryotes as well as some proteobacteria, including cyanobacteria. Heme oxygenase (HO) catalyzes the rate limiting step in the degradation of heme to biliverdin in a multi-step reaction. HO is essential for recycling of iron from heme which is used as a substrate and cofactor for its own degradation to biliverdin, iron, and carbon monoxide. In vertebrates, HO plays a role in heme homeostasis and oxidative stress response, and cellular signaling in mammals that include isoforms HO-1, HO-2 and HO-3. HO-1 is ubiquitously expressed after induction while HO-2 expression is constitutive, mostly limited to certain organs, such as the brain, testes, and the vascular system. HO-3 is non-functional in humans, suggesting that the Hmox3 gene is a pseudogene derived from HO-2 transcripts. In higher plants and cyanobacteria, heme oxygenase is required for the synthesis of light-harvesting pigments, which contain tetrapyrrols derived from biliverdin. Candida albicans expresses a heme oxygenase that is required for the utilization of heme as a nutritional iron source, whereas Saccharomyces cerevisiae responds to iron deprivation by increasing Hmx1p transcription, which is controlled by the major iron-dependent transcription factor, Aft1p, and promotes both the re-utilization of heme iron and the regulation of heme-dependent transcription during periods of iron scarcity. In pathogenic bacteria, HO is part of a pathway for iron acquisition from host heme. In Leptospira interrogans, a pathogenic spirochete that causes leptospirosis, HO is required for iron utilization when hemoglobin is the sole iron source, thus making HO an interesting target for novel antimicrobial agents. HO shares tertiary structure similarity to methane monooxygenase (EC 1.14.13.25), ribonucleotide reductase (EC 1.17.4.1) and thiaminase II (EC 3.5.99.2), but shares little sequence homology.


Pssm-ID: 350856  Cd Length: 205  Bit Score: 151.59  E-value: 5.39e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184487 127 KPSKEGFLKYLVDSKLVFDTIERIVDESENVSYA--YFRRTGLERCESIEKDLQWLREQDLVIPE-PSNVGVSYAKYLEE 203
Cdd:cd19165   30 PLDREAYARLLVQLYFVYEALEEALDRLADDPVLaaALYDPELERSEALEADLAFLLGPDWREPIpPSPATAAYVARIRE 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184487 204 QAGESAPLFLSHFYSIYFSHIAGGQVLVRQVSEK--LLEGKELEFNRWEG--DAQDLLKGVREKLNVLGehWSRDEKNKC 279
Cdd:cd19165  110 LAEEKPHLLLAHAYVRYLGDLSGGQIIRRKLAKAygLFGGEGLSFYDFDGigDGKDLKDEYRARLDALE--LTEEEKDAI 187

                        170
                 ....*....|....*...
gi 334184487 280 LKETAKAFKYMGQIVRLI 297
Cdd:cd19165  188 VEEAKLAFELNIALFEEL 205
Heme_oxygenase pfam01126
Heme oxygenase;
129-295 1.62e-07

Heme oxygenase;


Pssm-ID: 395895  Cd Length: 204  Bit Score: 50.82  E-value: 1.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184487  129 SKEGFLKYLVDSKLVFDTIER-IVDESENVSYAYFRRTGLERCESIEKDLQWLR-EQDLVIPEPSNVGVSYAKYLEEQAG 206
Cdd:pfam01126  33 DKDAYAKLLANLYFVYSALEEeLERNRDSPVAAPIYFPELNRKAALERDLAYLYgADWRADIQDSPATQEYVPRIREIGN 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184487  207 ESAPLFLSHFYSIYFSHIAGGQVLVR--QVSEKLLEGKELEFNRWEG--DAQDLLKGVREKLNVLgeHWSRDEKNKCLKE 282
Cdd:pfam01126 113 ESPELLVAHAYTRYLGDLSGGQLLKKiaQRALGLPPGEGTAFYEFEGisDRKVFKQEYREALNAL--ELDDEARARAVEE 190

                         170
                  ....*....|...
gi 334184487  283 TAKAFKYMGQIVR 295
Cdd:pfam01126 191 ANDAFALNIQVFR 203
COG5398 COG5398
Heme oxygenase [Coenzyme transport and metabolism];
167-289 6.34e-07

Heme oxygenase [Coenzyme transport and metabolism];


Pssm-ID: 444157  Cd Length: 211  Bit Score: 49.05  E-value: 6.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184487 167 LERCESIEKDLQWL-----REQdlviPEPSNVGVSYAKYLEEQAGESAPLFLSHFYSIYFSHIAGGQVLVRQVSE--KLL 239
Cdd:COG5398   72 LNRLPALEADLAFLygpdwRDQ----ITPLPATRAYVARIREVAAEWPELLVAHHYTRYLGDLSGGQIIKRILQRayGLP 147

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 334184487 240 EGKELEFnrWEGDAQDLLKGV----REKLNVLGehWSRDEKNKCLKETAKAFKY 289
Cdd:COG5398  148 DGEGTAF--YEFDEIPDPKAFkdryRAALDALP--LDEAERERIVDEANLAFRL 197
HemeO-like cd00232
heme oxygenase; Heme oxygenase (HO, EC 1.14.14.18) catalyzes the rate limiting step in the ...
 129-295 1.64e-05

heme oxygenase; Heme oxygenase (HO, EC 1.14.14.18) catalyzes the rate limiting step in the degradation of heme to biliverdin in a multi-step reaction. HO is essential for recycling iron from heme which is used as a substrate and cofactor for its own degradation to biliverdin, iron, and carbon monoxide. This family serves a variety of specific needs in different branches of life: in vertebrates, HO plays a role in heme homeostasis and oxidative stress response, and cellular signaling in mammals that include isoforms HO-1 and HO-2; in photosynthetic organisms including cyanobacteria, algae, and higher plants, biliverdin is used for photosynthetic pigment formation or light-sensing; and, in pathogenic bacteria, HO is part of a pathway for iron acquisition from host heme and heme products. HO shares tertiary structure similarity to methane monooxygenase (EC 1.14.13.25), ribonucleotide reductase (EC 1.17.4.1) and thiaminase II (EC 3.5.99.2), but shares little sequence homology.


Pssm-ID: 350855  Cd Length: 201  Bit Score: 44.92  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184487 129 SKEGFLKYLVDSKLVFDTIERIVDESE--NVSYAYFRRTGLERCESIEKDLQWLREQ--DLVIPEPSNVGvSYAKYLEEQ 204
Cdd:cd00232   30 SKDNYAKFLACQYYFFVALEAAYDEALlkGDFDKDPLLEGLARADAFKQDLADLGGPtwQADLGTKSQAK-DYEAHLAEL 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334184487 205 AGESAPLFLSHFYSIYFSHIAGGQVLVRqVSEKLLEGKELE----FNRWEGDAQDLLKGVREKLNVLGehWSRDEKNKCL 280
Cdd:cd00232  109 GRSSPALLLAHLYTQELSMLSGGQFLKK-WAQKLFQLPDDVgaahFAYPGESRNKLWSAFVKQLDELE--LTPELEDQAI 185

                        170
                 ....*....|....*
gi 334184487 281 KETAKAFKYMGQIVR 295
Cdd:cd00232  186 SEALAAFGHNNALLE 200
 
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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