NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2098610159|ref|XP_043664575|]
View 

heme oxygenase 1 isoform X2 [Vespula pensylvanica]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 8-215 1.28e-48

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: 158.91  E-value: 1.28e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098610159   8 TFCKKMRKATREIHAISDALVNAKLAF-GFLDDSVWADGLLVFYEIFRYLEGAMIRLKNTKIG--LLRLTELQRTEAFEQ 84
Cdd:cd19165     1 PLSERLREATRKLHTAAERSIFAKLLLaGPLDREAYARLLVQLYFVYEALEEALDRLADDPVLaaALYDPELERSEALEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098610159  85 DLEYYLGKGWMKNYSPRDSVIKYLMRLREIEDTEPALLMAYIYHLYMGLLSGGIILRRKrqLMQKISLFkeiTSSGNNIT 164
Cdd:cd19165    81 DLAFLLGPDWREPIPPSPATAAYVARIRELAEEKPHLLLAHAYVRYLGDLSGGQIIRRK--LAKAYGLF---GGEGLSFY 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2098610159 165 DF-GNHSIFELKHDLRETMNKIAetLDEDTKNKLIEESKIVYALNNEIIRSV 215
Cdd:cd19165   156 DFdGIGDGKDLKDEYRARLDALE--LTEEEKDAIVEEAKLAFELNIALFEEL 205
 
Name Accession Description Interval E-value
HemeO cd19165
heme oxygenase in eukaryotes and some bacteria; This subfamily contains heme oxygenase (HO, EC ...
 8-215 1.28e-48

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: 158.91  E-value: 1.28e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098610159   8 TFCKKMRKATREIHAISDALVNAKLAF-GFLDDSVWADGLLVFYEIFRYLEGAMIRLKNTKIG--LLRLTELQRTEAFEQ 84
Cdd:cd19165     1 PLSERLREATRKLHTAAERSIFAKLLLaGPLDREAYARLLVQLYFVYEALEEALDRLADDPVLaaALYDPELERSEALEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098610159  85 DLEYYLGKGWMKNYSPRDSVIKYLMRLREIEDTEPALLMAYIYHLYMGLLSGGIILRRKrqLMQKISLFkeiTSSGNNIT 164
Cdd:cd19165    81 DLAFLLGPDWREPIPPSPATAAYVARIRELAEEKPHLLLAHAYVRYLGDLSGGQIIRRK--LAKAYGLF---GGEGLSFY 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2098610159 165 DF-GNHSIFELKHDLRETMNKIAetLDEDTKNKLIEESKIVYALNNEIIRSV 215
Cdd:cd19165   156 DFdGIGDGKDLKDEYRARLDALE--LTEEEKDAIVEEAKLAFELNIALFEEL 205
Heme_oxygenase pfam01126
Heme oxygenase;
7-213 5.11e-30

Heme oxygenase;


Pssm-ID: 395895  Cd Length: 204  Bit Score: 110.91  E-value: 5.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098610159   7 DTFCKKMRKATREIHAISDALVNAKLAFGFLDDSVWADGLL-VFYEIFRYLEGAMIRLK-NTKIGLLRLTELQRTEAFEQ 84
Cdd:pfam01126   1 LNLAKRLREATKDVHVMAENLVFVKDFLKGVVDKDAYAKLLaNLYFVYSALEEELERNRdSPVAAPIYFPELNRKAALER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098610159  85 DLEYYLGKGWMKNYSPRDSVIKYLMRLREIEDTEPALLMAYIYHLYMGLLSGGIILRRK-RQLMQ-------KISLFKEI 156
Cdd:pfam01126  81 DLAYLYGADWRADIQDSPATQEYVPRIREIGNESPELLVAHAYTRYLGDLSGGQLLKKIaQRALGlppgegtAFYEFEGI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2098610159 157 TSSGNnitdfgnhsifeLKHDLRETMNKIaeTLDEDTKNKLIEESKIVYALNNEIIR 213
Cdd:pfam01126 161 SDRKV------------FKQEYREALNAL--ELDDEARARAVEEANDAFALNIQVFR 203
COG5398 COG5398
Heme oxygenase [Coenzyme transport and metabolism];
7-211 3.58e-26

Heme oxygenase [Coenzyme transport and metabolism];


Pssm-ID: 444157  Cd Length: 211  Bit Score: 101.06  E-value: 3.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098610159   7 DTFCKKMRKATREIH--AISDALVNAkLAFGFLDDSVWADGLLVFYEIFRYLEGAMIRLKNTKI-GLLRLTELQRTEAFE 83
Cdd:COG5398     1 SPLSTALREGTAKAHtaAENSGFMKA-LLKGRLDRDAYVALLAQLYFVYSALEEALERHRDHPVvGPFYFPELNRLPALE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098610159  84 QDLEYYLGKGWMKNYSPRDSVIKYLMRLREIEDTEPALLMAYIYHLYMGLLSGGIILRRkrqLMQKisLFKEITSSGNNI 163
Cdd:COG5398    80 ADLAFLYGPDWRDQITPLPATRAYVARIREVAAEWPELLVAHHYTRYLGDLSGGQIIKR---ILQR--AYGLPDGEGTAF 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2098610159 164 TDFGNH-SIFELKHDLRETMNKIAetLDEDTKNKLIEESKIVYALNNEI 211
Cdd:COG5398   155 YEFDEIpDPKAFKDRYRAALDALP--LDEAERERIVDEANLAFRLNTAV 201
pbsA CHL00168
heme oxygenase; Provisional
 50-226 3.61e-13

heme oxygenase; Provisional


Pssm-ID: 214383  Cd Length: 238  Bit Score: 66.73  E-value: 3.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098610159  50 YEIFRYLEGAMIRLK-NTKIGLLRLTELQRTEAFEQDLEYYLGKGWMKNYSPRDSVIKYLMRLREIEDTEPALLMAYIYH 128
Cdd:CHL00168   47 YFVYSAIEEEIEKNKeHPLIKPIYFQELNRKESLEKDLNYYYGDDWKSIIEPSPATKIYVDRIHKISAKKPELLIAHAYT 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098610159 129 LYMGLLSGGIILRRKRQlmqkislfKEITSSGNNITDFGNHSIFE----LKHDLRETMNKIAetLDEDTKNKLIEESKIV 204
Cdd:CHL00168  127 RYLGDLSGGQILKKIAQ--------RAMNLSDSGGLAFYDFDNIEddqeFKQIYKAALDNLP--LSDDQIQNIIAEANIA 196

                         170       180
                  ....*....|....*....|..
gi 2098610159 205 YALNNEIIRSVRGAGTVIFKKI 226
Cdd:CHL00168  197 FNLNMKMFQELNSSFIKIITML 218
 
Name Accession Description Interval E-value
HemeO cd19165
heme oxygenase in eukaryotes and some bacteria; This subfamily contains heme oxygenase (HO, EC ...
 8-215 1.28e-48

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: 158.91  E-value: 1.28e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098610159   8 TFCKKMRKATREIHAISDALVNAKLAF-GFLDDSVWADGLLVFYEIFRYLEGAMIRLKNTKIG--LLRLTELQRTEAFEQ 84
Cdd:cd19165     1 PLSERLREATRKLHTAAERSIFAKLLLaGPLDREAYARLLVQLYFVYEALEEALDRLADDPVLaaALYDPELERSEALEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098610159  85 DLEYYLGKGWMKNYSPRDSVIKYLMRLREIEDTEPALLMAYIYHLYMGLLSGGIILRRKrqLMQKISLFkeiTSSGNNIT 164
Cdd:cd19165    81 DLAFLLGPDWREPIPPSPATAAYVARIRELAEEKPHLLLAHAYVRYLGDLSGGQIIRRK--LAKAYGLF---GGEGLSFY 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2098610159 165 DF-GNHSIFELKHDLRETMNKIAetLDEDTKNKLIEESKIVYALNNEIIRSV 215
Cdd:cd19165   156 DFdGIGDGKDLKDEYRARLDALE--LTEEEKDAIVEEAKLAFELNIALFEEL 205
Heme_oxygenase pfam01126
Heme oxygenase;
7-213 5.11e-30

Heme oxygenase;


Pssm-ID: 395895  Cd Length: 204  Bit Score: 110.91  E-value: 5.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098610159   7 DTFCKKMRKATREIHAISDALVNAKLAFGFLDDSVWADGLL-VFYEIFRYLEGAMIRLK-NTKIGLLRLTELQRTEAFEQ 84
Cdd:pfam01126   1 LNLAKRLREATKDVHVMAENLVFVKDFLKGVVDKDAYAKLLaNLYFVYSALEEELERNRdSPVAAPIYFPELNRKAALER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098610159  85 DLEYYLGKGWMKNYSPRDSVIKYLMRLREIEDTEPALLMAYIYHLYMGLLSGGIILRRK-RQLMQ-------KISLFKEI 156
Cdd:pfam01126  81 DLAYLYGADWRADIQDSPATQEYVPRIREIGNESPELLVAHAYTRYLGDLSGGQLLKKIaQRALGlppgegtAFYEFEGI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2098610159 157 TSSGNnitdfgnhsifeLKHDLRETMNKIaeTLDEDTKNKLIEESKIVYALNNEIIR 213
Cdd:pfam01126 161 SDRKV------------FKQEYREALNAL--ELDDEARARAVEEANDAFALNIQVFR 203
COG5398 COG5398
Heme oxygenase [Coenzyme transport and metabolism];
7-211 3.58e-26

Heme oxygenase [Coenzyme transport and metabolism];


Pssm-ID: 444157  Cd Length: 211  Bit Score: 101.06  E-value: 3.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098610159   7 DTFCKKMRKATREIH--AISDALVNAkLAFGFLDDSVWADGLLVFYEIFRYLEGAMIRLKNTKI-GLLRLTELQRTEAFE 83
Cdd:COG5398     1 SPLSTALREGTAKAHtaAENSGFMKA-LLKGRLDRDAYVALLAQLYFVYSALEEALERHRDHPVvGPFYFPELNRLPALE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098610159  84 QDLEYYLGKGWMKNYSPRDSVIKYLMRLREIEDTEPALLMAYIYHLYMGLLSGGIILRRkrqLMQKisLFKEITSSGNNI 163
Cdd:COG5398    80 ADLAFLYGPDWRDQITPLPATRAYVARIREVAAEWPELLVAHHYTRYLGDLSGGQIIKR---ILQR--AYGLPDGEGTAF 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2098610159 164 TDFGNH-SIFELKHDLRETMNKIAetLDEDTKNKLIEESKIVYALNNEI 211
Cdd:COG5398   155 YEFDEIpDPKAFKDRYRAALDALP--LDEAERERIVDEANLAFRLNTAV 201
HemeO-like cd00232
heme oxygenase; Heme oxygenase (HO, EC 1.14.14.18) catalyzes the rate limiting step in the ...
 9-213 9.77e-26

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: 99.62  E-value: 9.77e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098610159   9 FCKKMRKATREIHAISDALVNAKLAFGFLDDSVWADGLLVFYEIFRYLEGAMIRLKNTKI--GLLRLTELQRTEAFEQDL 86
Cdd:cd00232     1 LSKRLKKATREVHNVSESLVNSRLPALFVSKDNYAKFLACQYYFFVALEAAYDEALLKGDfdKDPLLEGLARADAFKQDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098610159  87 EYYLGKGWMKNYSPRDSVIKYLMRLREIEDTEPALLMAYIYHLYMGLLSGGIILRRKRQlmqkiSLFKEITSSGNNITDF 166
Cdd:cd00232    81 ADLGGPTWQADLGTKSQAKDYEAHLAELGRSSPALLLAHLYTQELSMLSGGQFLKKWAQ-----KLFQLPDDVGAAHFAY 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2098610159 167 GNHSIFELKHDLRETMNKIAetLDEDTKNKLIEESKIVYALNNEIIR 213
Cdd:cd00232   156 PGESRNKLWSAFVKQLDELE--LTPELEDQAISEALAAFGHNNALLE 200
pbsA CHL00168
heme oxygenase; Provisional
 50-226 3.61e-13

heme oxygenase; Provisional


Pssm-ID: 214383  Cd Length: 238  Bit Score: 66.73  E-value: 3.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098610159  50 YEIFRYLEGAMIRLK-NTKIGLLRLTELQRTEAFEQDLEYYLGKGWMKNYSPRDSVIKYLMRLREIEDTEPALLMAYIYH 128
Cdd:CHL00168   47 YFVYSAIEEEIEKNKeHPLIKPIYFQELNRKESLEKDLNYYYGDDWKSIIEPSPATKIYVDRIHKISAKKPELLIAHAYT 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098610159 129 LYMGLLSGGIILRRKRQlmqkislfKEITSSGNNITDFGNHSIFE----LKHDLRETMNKIAetLDEDTKNKLIEESKIV 204
Cdd:CHL00168  127 RYLGDLSGGQILKKIAQ--------RAMNLSDSGGLAFYDFDNIEddqeFKQIYKAALDNLP--LSDDQIQNIIAEANIA 196

                         170       180
                  ....*....|....*....|..
gi 2098610159 205 YALNNEIIRSVRGAGTVIFKKI 226
Cdd:CHL00168  197 FNLNMKMFQELNSSFIKIITML 218
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH