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Conserved domains on  [gi|42742287|ref|NP_013306|]
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Hmx1p [Saccharomyces cerevisiae S288C]

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 ...
 17-254 6.31e-43

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: 146.58  E-value: 6.31e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742287  17 ALANRINFQTRDAHNKINTFMGIKMAIAMR-HGFIYRQGILAYYYVFDAIEQEIDRLLNDPVteeelqtstILKQFWLED 95
Cdd:cd19165   1 PLSERLREATRKLHTAAERSIFAKLLLAGPlDREAYARLLVQLYFVYEALEEALDRLADDPV---------LAAALYDPE 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742287  96 FRRSTQIYKDLKLLYSNTFKSTESLneflatfqkPPLLQQFINNIHENIHKEPCTILSYCHVLYLALFAGGKLIRSNLYR 175
Cdd:cd19165  72 LERSEALEADLAFLLGPDWREPIPP---------SPATAAYVARIRELAEEKPHLLLAHAYVRYLGDLSGGQIIRRKLAK 142

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42742287 176 RLGLFPNfeklsqkelvkKGTNFFTFSDLGPTEEtrLKWEYKKNYELAtrtELTEAQKLQIISVAEGIFDWNFNIVAEI 254
Cdd:cd19165 143 AYGLFGG-----------EGLSFYDFDGIGDGKD--LKDEYRARLDAL---ELTEEEKDAIVEEAKLAFELNIALFEEL 205
 
Name Accession Description Interval E-value
HemeO cd19165
heme oxygenase in eukaryotes and some bacteria; This subfamily contains heme oxygenase (HO, EC ...
 17-254 6.31e-43

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: 146.58  E-value: 6.31e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742287  17 ALANRINFQTRDAHNKINTFMGIKMAIAMR-HGFIYRQGILAYYYVFDAIEQEIDRLLNDPVteeelqtstILKQFWLED 95
Cdd:cd19165   1 PLSERLREATRKLHTAAERSIFAKLLLAGPlDREAYARLLVQLYFVYEALEEALDRLADDPV---------LAAALYDPE 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742287  96 FRRSTQIYKDLKLLYSNTFKSTESLneflatfqkPPLLQQFINNIHENIHKEPCTILSYCHVLYLALFAGGKLIRSNLYR 175
Cdd:cd19165  72 LERSEALEADLAFLLGPDWREPIPP---------SPATAAYVARIRELAEEKPHLLLAHAYVRYLGDLSGGQIIRRKLAK 142

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42742287 176 RLGLFPNfeklsqkelvkKGTNFFTFSDLGPTEEtrLKWEYKKNYELAtrtELTEAQKLQIISVAEGIFDWNFNIVAEI 254
Cdd:cd19165 143 AYGLFGG-----------EGLSFYDFDGIGDGKD--LKDEYRARLDAL---ELTEEEKDAIVEEAKLAFELNIALFEEL 205
Heme_oxygenase pfam01126
Heme oxygenase;
17-251 8.32e-09

Heme oxygenase;


Pssm-ID: 395895  Cd Length: 204  Bit Score: 54.67  E-value: 8.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742287    17 ALANRINFQTRDAHNKIN--TFMGIKMA-IAMRHGfiYRQGILAYYYVFDAIEQEIDRLLNDPVteeelqtstiLKQFWL 93
Cdd:pfam01126   2 NLAKRLREATKDVHVMAEnlVFVKDFLKgVVDKDA--YAKLLANLYFVYSALEEELERNRDSPV----------AAPIYF 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742287    94 EDFRRSTQIYKDLKLLYSNTFKsteslneflATFQKPPLLQQFINNIHENIHKEPCTILSYCHVLYLALFAGGKLIRSNL 173
Cdd:pfam01126  70 PELNRKAALERDLAYLYGADWR---------ADIQDSPATQEYVPRIREIGNESPELLVAHAYTRYLGDLSGGQLLKKIA 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42742287   174 YRRLGLFPNfeklsqkelvkKGTNFFTFSDLgpTEETRLKWEYKknyELATRTELTEAQKLQIISVAEGIFdwNFNIV 251
Cdd:pfam01126 141 QRALGLPPG-----------EGTAFYEFEGI--SDRKVFKQEYR---EALNALELDDEARARAVEEANDAF--ALNIQ 200
pbsA CHL00168
heme oxygenase; Provisional
 15-254 4.96e-05

heme oxygenase; Provisional


Pssm-ID: 214383  Cd Length: 238  Bit Score: 44.00  E-value: 4.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742287   15 VGALANRINFQTRDAHNKINTFMGIKMAIAmrhGFI----YRQGILAYYYVFDAIEQEIDRLLNDPVteeelqtstiLKQ 90
Cdd:CHL00168   2 VTNLATQLREGTTKSHSMAENVSFVKSFLG---GVIdkksYRKLVANLYFVYSAIEEEIEKNKEHPL----------IKP 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742287   91 FWLEDFRRSTQIYKDLKLLYSNTFKSteslneflatFQKP-PLLQQFINNIHENIHKEPCTILSYCHVLYLALFAGGKLI 169
Cdd:CHL00168  69 IYFQELNRKESLEKDLNYYYGDDWKS----------IIEPsPATKIYVDRIHKISAKKPELLIAHAYTRYLGDLSGGQIL 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742287  170 RSNLYRRLGLFPNfeklsqkelvkKGTNFFTFSDLGPTEetrlkwEYKKNYELATRT-ELTEAQKLQIISVAEGIFDWNF 248
Cdd:CHL00168 139 KKIAQRAMNLSDS-----------GGLAFYDFDNIEDDQ------EFKQIYKAALDNlPLSDDQIQNIIAEANIAFNLNM 201


                 ....*.
gi 42742287  249 NIVAEI 254
Cdd:CHL00168 202 KMFQEL 207
 
Name Accession Description Interval E-value
HemeO cd19165
heme oxygenase in eukaryotes and some bacteria; This subfamily contains heme oxygenase (HO, EC ...
 17-254 6.31e-43

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: 146.58  E-value: 6.31e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742287  17 ALANRINFQTRDAHNKINTFMGIKMAIAMR-HGFIYRQGILAYYYVFDAIEQEIDRLLNDPVteeelqtstILKQFWLED 95
Cdd:cd19165   1 PLSERLREATRKLHTAAERSIFAKLLLAGPlDREAYARLLVQLYFVYEALEEALDRLADDPV---------LAAALYDPE 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742287  96 FRRSTQIYKDLKLLYSNTFKSTESLneflatfqkPPLLQQFINNIHENIHKEPCTILSYCHVLYLALFAGGKLIRSNLYR 175
Cdd:cd19165  72 LERSEALEADLAFLLGPDWREPIPP---------SPATAAYVARIRELAEEKPHLLLAHAYVRYLGDLSGGQIIRRKLAK 142

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42742287 176 RLGLFPNfeklsqkelvkKGTNFFTFSDLGPTEEtrLKWEYKKNYELAtrtELTEAQKLQIISVAEGIFDWNFNIVAEI 254
Cdd:cd19165 143 AYGLFGG-----------EGLSFYDFDGIGDGKD--LKDEYRARLDAL---ELTEEEKDAIVEEAKLAFELNIALFEEL 205
Heme_oxygenase pfam01126
Heme oxygenase;
17-251 8.32e-09

Heme oxygenase;


Pssm-ID: 395895  Cd Length: 204  Bit Score: 54.67  E-value: 8.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742287    17 ALANRINFQTRDAHNKIN--TFMGIKMA-IAMRHGfiYRQGILAYYYVFDAIEQEIDRLLNDPVteeelqtstiLKQFWL 93
Cdd:pfam01126   2 NLAKRLREATKDVHVMAEnlVFVKDFLKgVVDKDA--YAKLLANLYFVYSALEEELERNRDSPV----------AAPIYF 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742287    94 EDFRRSTQIYKDLKLLYSNTFKsteslneflATFQKPPLLQQFINNIHENIHKEPCTILSYCHVLYLALFAGGKLIRSNL 173
Cdd:pfam01126  70 PELNRKAALERDLAYLYGADWR---------ADIQDSPATQEYVPRIREIGNESPELLVAHAYTRYLGDLSGGQLLKKIA 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42742287   174 YRRLGLFPNfeklsqkelvkKGTNFFTFSDLgpTEETRLKWEYKknyELATRTELTEAQKLQIISVAEGIFdwNFNIV 251
Cdd:pfam01126 141 QRALGLPPG-----------EGTAFYEFEGI--SDRKVFKQEYR---EALNALELDDEARARAVEEANDAF--ALNIQ 200
HemeO-like cd00232
heme oxygenase; Heme oxygenase (HO, EC 1.14.14.18) catalyzes the rate limiting step in the ...
 18-253 4.34e-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: 43.77  E-value: 4.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742287  18 LANRINFQTRDAHNKINT--FMGIKMAIAMRHGFIyrQGILAYYYVFDAIEQEIDRLLNDPVteeelqtstILKQFWLED 95
Cdd:cd00232   1 LSKRLKKATREVHNVSESlvNSRLPALFVSKDNYA--KFLACQYYFFVALEAAYDEALLKGD---------FDKDPLLEG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742287  96 FRRSTQIYKDLKLLYSNTFKsteslneflATFQKPPLLQQFINNIHENIHKEPCTILSYCHVLYLALFAGGKLIRSNLYR 175
Cdd:cd00232  70 LARADAFKQDLADLGGPTWQ---------ADLGTKSQAKDYEAHLAELGRSSPALLLAHLYTQELSMLSGGQFLKKWAQK 140

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42742287 176 RLGLFPNFeklsqkelvkkGTNFFTFSDLGpteETRLKWEYKKNYElatRTELTEAQKLQIISVAEGIFDWNFNIVAE 253
Cdd:cd00232 141 LFQLPDDV-----------GAAHFAYPGES---RNKLWSAFVKQLD---ELELTPELEDQAISEALAAFGHNNALLEE 201
pbsA CHL00168
heme oxygenase; Provisional
 15-254 4.96e-05

heme oxygenase; Provisional


Pssm-ID: 214383  Cd Length: 238  Bit Score: 44.00  E-value: 4.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742287   15 VGALANRINFQTRDAHNKINTFMGIKMAIAmrhGFI----YRQGILAYYYVFDAIEQEIDRLLNDPVteeelqtstiLKQ 90
Cdd:CHL00168   2 VTNLATQLREGTTKSHSMAENVSFVKSFLG---GVIdkksYRKLVANLYFVYSAIEEEIEKNKEHPL----------IKP 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742287   91 FWLEDFRRSTQIYKDLKLLYSNTFKSteslneflatFQKP-PLLQQFINNIHENIHKEPCTILSYCHVLYLALFAGGKLI 169
Cdd:CHL00168  69 IYFQELNRKESLEKDLNYYYGDDWKS----------IIEPsPATKIYVDRIHKISAKKPELLIAHAYTRYLGDLSGGQIL 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42742287  170 RSNLYRRLGLFPNfeklsqkelvkKGTNFFTFSDLGPTEetrlkwEYKKNYELATRT-ELTEAQKLQIISVAEGIFDWNF 248
Cdd:CHL00168 139 KKIAQRAMNLSDS-----------GGLAFYDFDNIEDDQ------EFKQIYKAALDNlPLSDDQIQNIIAEANIAFNLNM 201


                 ....*.
gi 42742287  249 NIVAEI 254
Cdd:CHL00168 202 KMFQEL 207
 
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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