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Conserved domains on  [gi|2175895653|ref|XP_045604684|]
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heme oxygenase 1-like [Procambarus clarkii]

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 ...
 8-215 1.10e-50

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: 164.30  E-value: 1.10e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175895653   8 PFTKQMRDVTREIHNISDTLINAKLGIAMSNDR-VWAEGLLIFYEVFQYLEGALERHSHS--LIGELDIPGIRRTEAFEK 84
Cdd:cd19165     1 PLSERLREATRKLHTAAERSIFAKLLLAGPLDReAYARLLVQLYFVYEALEEALDRLADDpvLAAALYDPELERSEALEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175895653  85 DLSYYLGADWKKDYTPRESVCQYLKHLEKLENENPYLLMAYIYHLYMGLLSGGQILRRKkvLLQKLRFSRKDTLEGMAVT 164
Cdd:cd19165    81 DLAFLLGPDWREPIPPSPATAAYVARIRELAEEKPHLLLAHAYVRYLGDLSGGQIIRRK--LAKAYGLFGGEGLSFYDFD 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2175895653 165 EITDGsvSKIKKQMTEAMNhiAGEIDEDIRQKLLEESKVVFILNNKIVHSI 215
Cdd:cd19165   159 GIGDG--KDLKDEYRARLD--ALELTEEEKDAIVEEAKLAFELNIALFEEL 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 1.10e-50

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: 164.30  E-value: 1.10e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175895653   8 PFTKQMRDVTREIHNISDTLINAKLGIAMSNDR-VWAEGLLIFYEVFQYLEGALERHSHS--LIGELDIPGIRRTEAFEK 84
Cdd:cd19165     1 PLSERLREATRKLHTAAERSIFAKLLLAGPLDReAYARLLVQLYFVYEALEEALDRLADDpvLAAALYDPELERSEALEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175895653  85 DLSYYLGADWKKDYTPRESVCQYLKHLEKLENENPYLLMAYIYHLYMGLLSGGQILRRKkvLLQKLRFSRKDTLEGMAVT 164
Cdd:cd19165    81 DLAFLLGPDWREPIPPSPATAAYVARIRELAEEKPHLLLAHAYVRYLGDLSGGQIIRRK--LAKAYGLFGGEGLSFYDFD 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2175895653 165 EITDGsvSKIKKQMTEAMNhiAGEIDEDIRQKLLEESKVVFILNNKIVHSI 215
Cdd:cd19165   159 GIGDG--KDLKDEYRARLD--ALELTEEEKDAIVEEAKLAFELNIALFEEL 205
Heme_oxygenase pfam01126
Heme oxygenase;
8-213 4.56e-34

Heme oxygenase;


Pssm-ID: 395895  Cd Length: 204  Bit Score: 121.70  E-value: 4.56e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175895653   8 PFTKQMRDVTREIHNISDTLINAKLGIAMSNDRVWAEGLL-IFYEVFQYLEGALERH-SHSLIGELDIPGIRRTEAFEKD 85
Cdd:pfam01126   2 NLAKRLREATKDVHVMAENLVFVKDFLKGVVDKDAYAKLLaNLYFVYSALEEELERNrDSPVAAPIYFPELNRKAALERD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175895653  86 LSYYLGADWKKDYTPRESVCQYLKHLEKLENENPYLLMAYIYHLYMGLLSGGQILrrKKVLLQKLRFSRKdtlEGMAVTE 165
Cdd:pfam01126  82 LAYLYGADWRADIQDSPATQEYVPRIREIGNESPELLVAHAYTRYLGDLSGGQLL--KKIAQRALGLPPG---EGTAFYE 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2175895653 166 ITDGSVSKIKKQM-TEAMNHIagEIDEDIRQKLLEESKVVFILNNKIVH 213
Cdd:pfam01126 157 FEGISDRKVFKQEyREALNAL--ELDDEARARAVEEANDAFALNIQVFR 203
COG5398 COG5398
Heme oxygenase [Coenzyme transport and metabolism];
49-218 2.55e-24

Heme oxygenase [Coenzyme transport and metabolism];


Pssm-ID: 444157  Cd Length: 211  Bit Score: 96.43  E-value: 2.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175895653  49 FYEVFQYLEGALERH-SHSLIGELDIPGIRRTEAFEKDLSYYLGADWKKDYTPRESVCQYLKHLEKLENENPYLLMAYIY 127
Cdd:COG5398    44 LYFVYSALEEALERHrDHPVVGPFYFPELNRLPALEADLAFLYGPDWRDQITPLPATRAYVARIREVAAEWPELLVAHHY 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175895653 128 HLYMGLLSGGQILRRkkvLLQK---------LRFSRKDTLEGMAVteitdgsvskIKKQMTEAMNHIagEIDEDIRQKLL 198
Cdd:COG5398   124 TRYLGDLSGGQIIKR---ILQRayglpdgegTAFYEFDEIPDPKA----------FKDRYRAALDAL--PLDEAERERIV 188

                         170       180
                  ....*....|....*....|
gi 2175895653 199 EESKVVFILNNKIVHSIEGA 218
Cdd:COG5398   189 DEANLAFRLNTAVFAELERD 208
pbsA CHL00168
heme oxygenase; Provisional
 50-228 1.82e-20

heme oxygenase; Provisional


Pssm-ID: 214383  Cd Length: 238  Bit Score: 86.76  E-value: 1.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175895653  50 YEVFQYLEGALERH-SHSLIGELDIPGIRRTEAFEKDLSYYLGADWKKDYTPRESVCQYLKHLEKLENENPYLLMAYIYH 128
Cdd:CHL00168   47 YFVYSAIEEEIEKNkEHPLIKPIYFQELNRKESLEKDLNYYYGDDWKSIIEPSPATKIYVDRIHKISAKKPELLIAHAYT 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175895653 129 LYMGLLSGGQILrrKKVLLQKLRFSRKDTLEGMAVTEITDgsVSKIKKQMTEAMNHIagEIDEDIRQKLLEESKVVFILN 208
Cdd:CHL00168  127 RYLGDLSGGQIL--KKIAQRAMNLSDSGGLAFYDFDNIED--DQEFKQIYKAALDNL--PLSDDQIQNIIAEANIAFNLN 200

                         170       180
                  ....*....|....*....|
gi 2175895653 209 NKIVHSIEGAGAIVTVKLIK 228
Cdd:CHL00168  201 MKMFQELNSSFIKIITMLIK 220
 
Name Accession Description Interval E-value
HemeO cd19165
heme oxygenase in eukaryotes and some bacteria; This subfamily contains heme oxygenase (HO, EC ...
 8-215 1.10e-50

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: 164.30  E-value: 1.10e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175895653   8 PFTKQMRDVTREIHNISDTLINAKLGIAMSNDR-VWAEGLLIFYEVFQYLEGALERHSHS--LIGELDIPGIRRTEAFEK 84
Cdd:cd19165     1 PLSERLREATRKLHTAAERSIFAKLLLAGPLDReAYARLLVQLYFVYEALEEALDRLADDpvLAAALYDPELERSEALEA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175895653  85 DLSYYLGADWKKDYTPRESVCQYLKHLEKLENENPYLLMAYIYHLYMGLLSGGQILRRKkvLLQKLRFSRKDTLEGMAVT 164
Cdd:cd19165    81 DLAFLLGPDWREPIPPSPATAAYVARIRELAEEKPHLLLAHAYVRYLGDLSGGQIIRRK--LAKAYGLFGGEGLSFYDFD 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2175895653 165 EITDGsvSKIKKQMTEAMNhiAGEIDEDIRQKLLEESKVVFILNNKIVHSI 215
Cdd:cd19165   159 GIGDG--KDLKDEYRARLD--ALELTEEEKDAIVEEAKLAFELNIALFEEL 205
Heme_oxygenase pfam01126
Heme oxygenase;
8-213 4.56e-34

Heme oxygenase;


Pssm-ID: 395895  Cd Length: 204  Bit Score: 121.70  E-value: 4.56e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175895653   8 PFTKQMRDVTREIHNISDTLINAKLGIAMSNDRVWAEGLL-IFYEVFQYLEGALERH-SHSLIGELDIPGIRRTEAFEKD 85
Cdd:pfam01126   2 NLAKRLREATKDVHVMAENLVFVKDFLKGVVDKDAYAKLLaNLYFVYSALEEELERNrDSPVAAPIYFPELNRKAALERD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175895653  86 LSYYLGADWKKDYTPRESVCQYLKHLEKLENENPYLLMAYIYHLYMGLLSGGQILrrKKVLLQKLRFSRKdtlEGMAVTE 165
Cdd:pfam01126  82 LAYLYGADWRADIQDSPATQEYVPRIREIGNESPELLVAHAYTRYLGDLSGGQLL--KKIAQRALGLPPG---EGTAFYE 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2175895653 166 ITDGSVSKIKKQM-TEAMNHIagEIDEDIRQKLLEESKVVFILNNKIVH 213
Cdd:pfam01126 157 FEGISDRKVFKQEyREALNAL--ELDDEARARAVEEANDAFALNIQVFR 203
HemeO-like cd00232
heme oxygenase; Heme oxygenase (HO, EC 1.14.14.18) catalyzes the rate limiting step in the ...
 9-212 4.78e-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: 100.78  E-value: 4.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175895653   9 FTKQMRDVTREIHNISDTLINAKLGIAMSNDRVWAEGLLIFYEVFQYLEGALERHSHS-LIGELDIPGIR-RTEAFEKDL 86
Cdd:cd00232     1 LSKRLKKATREVHNVSESLVNSRLPALFVSKDNYAKFLACQYYFFVALEAAYDEALLKgDFDKDPLLEGLaRADAFKQDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175895653  87 SYYLGADWKKDYTPRESVCQYLKHLEKLENENPYLLMAYIYHLYMGLLSGGQILRRKKvllQKLRFSRKDtlEGMAVTEI 166
Cdd:cd00232    81 ADLGGPTWQADLGTKSQAKDYEAHLAELGRSSPALLLAHLYTQELSMLSGGQFLKKWA---QKLFQLPDD--VGAAHFAY 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2175895653 167 TDGSVSKIKKQMTEAMNHIagEIDEDIRQKLLEESKVVFILNNKIV 212
Cdd:cd00232   156 PGESRNKLWSAFVKQLDEL--ELTPELEDQAISEALAAFGHNNALL 199
COG5398 COG5398
Heme oxygenase [Coenzyme transport and metabolism];
49-218 2.55e-24

Heme oxygenase [Coenzyme transport and metabolism];


Pssm-ID: 444157  Cd Length: 211  Bit Score: 96.43  E-value: 2.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175895653  49 FYEVFQYLEGALERH-SHSLIGELDIPGIRRTEAFEKDLSYYLGADWKKDYTPRESVCQYLKHLEKLENENPYLLMAYIY 127
Cdd:COG5398    44 LYFVYSALEEALERHrDHPVVGPFYFPELNRLPALEADLAFLYGPDWRDQITPLPATRAYVARIREVAAEWPELLVAHHY 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175895653 128 HLYMGLLSGGQILRRkkvLLQK---------LRFSRKDTLEGMAVteitdgsvskIKKQMTEAMNHIagEIDEDIRQKLL 198
Cdd:COG5398   124 TRYLGDLSGGQIIKR---ILQRayglpdgegTAFYEFDEIPDPKA----------FKDRYRAALDAL--PLDEAERERIV 188

                         170       180
                  ....*....|....*....|
gi 2175895653 199 EESKVVFILNNKIVHSIEGA 218
Cdd:COG5398   189 DEANLAFRLNTAVFAELERD 208
pbsA CHL00168
heme oxygenase; Provisional
 50-228 1.82e-20

heme oxygenase; Provisional


Pssm-ID: 214383  Cd Length: 238  Bit Score: 86.76  E-value: 1.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175895653  50 YEVFQYLEGALERH-SHSLIGELDIPGIRRTEAFEKDLSYYLGADWKKDYTPRESVCQYLKHLEKLENENPYLLMAYIYH 128
Cdd:CHL00168   47 YFVYSAIEEEIEKNkEHPLIKPIYFQELNRKESLEKDLNYYYGDDWKSIIEPSPATKIYVDRIHKISAKKPELLIAHAYT 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2175895653 129 LYMGLLSGGQILrrKKVLLQKLRFSRKDTLEGMAVTEITDgsVSKIKKQMTEAMNHIagEIDEDIRQKLLEESKVVFILN 208
Cdd:CHL00168  127 RYLGDLSGGQIL--KKIAQRAMNLSDSGGLAFYDFDNIED--DQEFKQIYKAALDNL--PLSDDQIQNIIAEANIAFNLN 200

                         170       180
                  ....*....|....*....|
gi 2175895653 209 NKIVHSIEGAGAIVTVKLIK 228
Cdd:CHL00168  201 MKMFQELNSSFIKIITMLIK 220
 
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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