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Conserved domains on  [gi|186503279|ref|NP_001118392|]
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Plant heme oxygenase (decyclizing) family protein [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 ...
 73-232 1.77e-39

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: 135.03  E-value: 1.77e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503279  73 GFVEEMRFVAMRLHTKDQAK------------------------------EDA------------EFKNTGLERAEKLST 110
Cdd:cd19165    1 PLSERLREATRKLHTAAERSifaklllagpldreayarllvqlyfvyealEEAldrladdpvlaaALYDPELERSEALEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503279 111 DLEWFKEQGYEIPE-PTAPGKTYSQYLKELAEKDPQAFICHFYNIYFAHSAGGRMIGRKVAER--ILDNKELEFYKWDG- 186
Cdd:cd19165   81 DLAFLLGPDWREPIpPSPATAAYVARIRELAEEKPHLLLAHAYVRYLGDLSGGQIIRRKLAKAygLFGGEGLSFYDFDGi 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 186503279 187 -ELSQLLQNVREKLNKVaeEWTREEKNHCLEETEKSFKYSGEILRLI 232
Cdd:cd19165  161 gDGKDLKDEYRARLDAL--ELTEEEKDAIVEEAKLAFELNIALFEEL 205
 
Name Accession Description Interval E-value
HemeO cd19165
heme oxygenase in eukaryotes and some bacteria; This subfamily contains heme oxygenase (HO, EC ...
 73-232 1.77e-39

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: 135.03  E-value: 1.77e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503279  73 GFVEEMRFVAMRLHTKDQAK------------------------------EDA------------EFKNTGLERAEKLST 110
Cdd:cd19165    1 PLSERLREATRKLHTAAERSifaklllagpldreayarllvqlyfvyealEEAldrladdpvlaaALYDPELERSEALEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503279 111 DLEWFKEQGYEIPE-PTAPGKTYSQYLKELAEKDPQAFICHFYNIYFAHSAGGRMIGRKVAER--ILDNKELEFYKWDG- 186
Cdd:cd19165   81 DLAFLLGPDWREPIpPSPATAAYVARIRELAEEKPHLLLAHAYVRYLGDLSGGQIIRRKLAKAygLFGGEGLSFYDFDGi 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 186503279 187 -ELSQLLQNVREKLNKVaeEWTREEKNHCLEETEKSFKYSGEILRLI 232
Cdd:cd19165  161 gDGKDLKDEYRARLDAL--ELTEEEKDAIVEEAKLAFELNIALFEEL 205
COG5398 COG5398
Heme oxygenase [Coenzyme transport and metabolism];
102-230 3.72e-10

Heme oxygenase [Coenzyme transport and metabolism];


Pssm-ID: 444157  Cd Length: 211  Bit Score: 57.53  E-value: 3.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503279 102 LERAEKLSTDLE-WFKEQGYEIPEPTAPGKTYSQYLKELAEKDPQAFICHFYNIYFAHSAGGRMIGRkVAERIL---DNK 177
Cdd:COG5398   72 LNRLPALEADLAfLYGPDWRDQITPLPATRAYVARIREVAAEWPELLVAHHYTRYLGDLSGGQIIKR-ILQRAYglpDGE 150

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 186503279 178 ELEFYKWD--GELSQLLQNVREKLNKVaeEWTREEKNHCLEETEKSFKYSGEILR 230
Cdd:COG5398  151 GTAFYEFDeiPDPKAFKDRYRAALDAL--PLDEAERERIVDEANLAFRLNTAVFA 203
pbsA CHL00168
heme oxygenase; Provisional
 100-185 1.07e-04

heme oxygenase; Provisional


Pssm-ID: 214383  Cd Length: 238  Bit Score: 42.08  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503279 100 TGLERAEKLSTDLEWFKEQGYE-IPEPTAPGKTYSQYLKELAEKDPQAFICHFYNIYFAHSAGGRMIgRKVAERIL---D 175
Cdd:CHL00168  72 QELNRKESLEKDLNYYYGDDWKsIIEPSPATKIYVDRIHKISAKKPELLIAHAYTRYLGDLSGGQIL-KKIAQRAMnlsD 150

                         90
                 ....*....|
gi 186503279 176 NKELEFYKWD 185
Cdd:CHL00168 151 SGGLAFYDFD 160
Heme_oxygenase pfam01126
Heme oxygenase;
102-230 2.00e-04

Heme oxygenase;


Pssm-ID: 395895  Cd Length: 204  Bit Score: 41.19  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503279  102 LERAEKLSTDLE-WFKEQGYEIPEPTAPGKTYSQYLKELAEKDPQAFICHFYNIYFAHSAGGRMIgRKVAERILD---NK 177
Cdd:pfam01126  72 LNRKAALERDLAyLYGADWRADIQDSPATQEYVPRIREIGNESPELLVAHAYTRYLGDLSGGQLL-KKIAQRALGlppGE 150

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 186503279  178 ELEFYKWDGELS--QLLQNVREKLNKVaeEWTREEKNHCLEETEKSFKYSGEILR 230
Cdd:pfam01126 151 GTAFYEFEGISDrkVFKQEYREALNAL--ELDDEARARAVEEANDAFALNIQVFR 203
 
Name Accession Description Interval E-value
HemeO cd19165
heme oxygenase in eukaryotes and some bacteria; This subfamily contains heme oxygenase (HO, EC ...
 73-232 1.77e-39

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: 135.03  E-value: 1.77e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503279  73 GFVEEMRFVAMRLHTKDQAK------------------------------EDA------------EFKNTGLERAEKLST 110
Cdd:cd19165    1 PLSERLREATRKLHTAAERSifaklllagpldreayarllvqlyfvyealEEAldrladdpvlaaALYDPELERSEALEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503279 111 DLEWFKEQGYEIPE-PTAPGKTYSQYLKELAEKDPQAFICHFYNIYFAHSAGGRMIGRKVAER--ILDNKELEFYKWDG- 186
Cdd:cd19165   81 DLAFLLGPDWREPIpPSPATAAYVARIRELAEEKPHLLLAHAYVRYLGDLSGGQIIRRKLAKAygLFGGEGLSFYDFDGi 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 186503279 187 -ELSQLLQNVREKLNKVaeEWTREEKNHCLEETEKSFKYSGEILRLI 232
Cdd:cd19165  161 gDGKDLKDEYRARLDAL--ELTEEEKDAIVEEAKLAFELNIALFEEL 205
COG5398 COG5398
Heme oxygenase [Coenzyme transport and metabolism];
102-230 3.72e-10

Heme oxygenase [Coenzyme transport and metabolism];


Pssm-ID: 444157  Cd Length: 211  Bit Score: 57.53  E-value: 3.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503279 102 LERAEKLSTDLE-WFKEQGYEIPEPTAPGKTYSQYLKELAEKDPQAFICHFYNIYFAHSAGGRMIGRkVAERIL---DNK 177
Cdd:COG5398   72 LNRLPALEADLAfLYGPDWRDQITPLPATRAYVARIREVAAEWPELLVAHHYTRYLGDLSGGQIIKR-ILQRAYglpDGE 150

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 186503279 178 ELEFYKWD--GELSQLLQNVREKLNKVaeEWTREEKNHCLEETEKSFKYSGEILR 230
Cdd:COG5398  151 GTAFYEFDeiPDPKAFKDRYRAALDAL--PLDEAERERIVDEANLAFRLNTAVFA 203
pbsA CHL00168
heme oxygenase; Provisional
 100-185 1.07e-04

heme oxygenase; Provisional


Pssm-ID: 214383  Cd Length: 238  Bit Score: 42.08  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503279 100 TGLERAEKLSTDLEWFKEQGYE-IPEPTAPGKTYSQYLKELAEKDPQAFICHFYNIYFAHSAGGRMIgRKVAERIL---D 175
Cdd:CHL00168  72 QELNRKESLEKDLNYYYGDDWKsIIEPSPATKIYVDRIHKISAKKPELLIAHAYTRYLGDLSGGQIL-KKIAQRAMnlsD 150

                         90
                 ....*....|
gi 186503279 176 NKELEFYKWD 185
Cdd:CHL00168 151 SGGLAFYDFD 160
Heme_oxygenase pfam01126
Heme oxygenase;
102-230 2.00e-04

Heme oxygenase;


Pssm-ID: 395895  Cd Length: 204  Bit Score: 41.19  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503279  102 LERAEKLSTDLE-WFKEQGYEIPEPTAPGKTYSQYLKELAEKDPQAFICHFYNIYFAHSAGGRMIgRKVAERILD---NK 177
Cdd:pfam01126  72 LNRKAALERDLAyLYGADWRADIQDSPATQEYVPRIREIGNESPELLVAHAYTRYLGDLSGGQLL-KKIAQRALGlppGE 150

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 186503279  178 ELEFYKWDGELS--QLLQNVREKLNKVaeEWTREEKNHCLEETEKSFKYSGEILR 230
Cdd:pfam01126 151 GTAFYEFEGISDrkVFKQEYREALNAL--ELDDEARARAVEEANDAFALNIQVFR 203
HemeO-like cd00232
heme oxygenase; Heme oxygenase (HO, EC 1.14.14.18) catalyzes the rate limiting step in the ...
 80-230 2.65e-04

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: 40.69  E-value: 2.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186503279  80 FVAMRLHTKDQAKEDAEFKNTGLE---RAEKLSTDLEWFKEQGYEIPEPTAPG-KTYSQYLKELAEKDPQAFICHFYNIY 155
Cdd:cd00232   45 FVALEAAYDEALLKGDFDKDPLLEglaRADAFKQDLADLGGPTWQADLGTKSQaKDYEAHLAELGRSSPALLLAHLYTQE 124

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186503279 156 FAHSAGGRMIgRKVAERILDNKE---LEFYKWDGE-LSQLLQNVREKLNKVaeEWTREEKNHCLEETEKSFKYSGEILR 230
Cdd:cd00232  125 LSMLSGGQFL-KKWAQKLFQLPDdvgAAHFAYPGEsRNKLWSAFVKQLDEL--ELTPELEDQAISEALAAFGHNNALLE 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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