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Conserved domains on  [gi|1080669252|gb|OFO42138|]
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heme oxygenase [Neisseria sp. HMSC075C10]

Protein Classification

biliverdin-producing heme oxygenase( domain architecture ID 10083246)

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-like cd00232
heme oxygenase; Heme oxygenase (HO, EC 1.14.14.18) catalyzes the rate limiting step in the ...
 9-188 1.38e-76

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: 228.67  E-value: 1.38e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080669252   9 FAKRLKEQTTVTHDSVDNLVMSVQP--FSSKENYIKFLKLQSVFHKAVDHIYKDAELNKAI---PELEYMARYDAVTQDL 83
Cdd:cd00232     1 LSKRLKKATREVHNVSESLVNSRLPalFVSKDNYAKFLACQYYFFVALEAAYDEALLKGDFdkdPLLEGLARADAFKQDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080669252  84 KDLGEEPYKFD--------------KELPHETGNKAIGWLYCAEGSNL-GAAFLFKHAQKLEY-TGEFGARHLAPHPNGR 147
Cdd:cd00232    81 ADLGGPTWQADlgtksqakdyeahlAELGRSSPALLLAHLYTQELSMLsGGQFLKKWAQKLFQlPDDVGAAHFAYPGESR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1080669252 148 GKHWRAFVEHLNALNLTPEAEAEAIQGACEAFEFYKVILRE 188
Cdd:cd00232   161 NKLWSAFVKQLDELELTPELEDQAISEALAAFGHNNALLEE 201
 
Name Accession Description Interval E-value
HemeO-like cd00232
heme oxygenase; Heme oxygenase (HO, EC 1.14.14.18) catalyzes the rate limiting step in the ...
 9-188 1.38e-76

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: 228.67  E-value: 1.38e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080669252   9 FAKRLKEQTTVTHDSVDNLVMSVQP--FSSKENYIKFLKLQSVFHKAVDHIYKDAELNKAI---PELEYMARYDAVTQDL 83
Cdd:cd00232     1 LSKRLKKATREVHNVSESLVNSRLPalFVSKDNYAKFLACQYYFFVALEAAYDEALLKGDFdkdPLLEGLARADAFKQDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080669252  84 KDLGEEPYKFD--------------KELPHETGNKAIGWLYCAEGSNL-GAAFLFKHAQKLEY-TGEFGARHLAPHPNGR 147
Cdd:cd00232    81 ADLGGPTWQADlgtksqakdyeahlAELGRSSPALLLAHLYTQELSMLsGGQFLKKWAQKLFQlPDDVGAAHFAYPGESR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1080669252 148 GKHWRAFVEHLNALNLTPEAEAEAIQGACEAFEFYKVILRE 188
Cdd:cd00232   161 NKLWSAFVKQLDELELTPELEDQAISEALAAFGHNNALLEE 201
HemO COG3230
Heme oxygenase [Inorganic ion transport and metabolism];
4-190 1.18e-65

Heme oxygenase [Inorganic ion transport and metabolism];


Pssm-ID: 442462  Cd Length: 192  Bit Score: 200.59  E-value: 1.18e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080669252   4 TQELTFAKRLKEQTTVTHDSVDNLVMSVQPFSSKENYIKFLKLQSVFHKAVDHIYKDAELNKAIPELEYMARYDAVTQDL 83
Cdd:COG3230     3 AAAPSLLARLRAATRALHERLDALVMLLDPFLTLEDYARFLRAQYGFHAPLEALLAAAALAALLPDLAERRRLALLEADL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080669252  84 KDLGEEPYKFDK--ELPHETGNKAIGWLYCAEGSNLGAAFLFKHA-QKLEYTGEFGARHLAPHPNGRGKHWRAFVEHLNA 160
Cdd:COG3230    83 ADLGLPPPAAAAaaLPALTSLAAALGALYVLEGSTLGGAVLLKRLrRALGLDPDFGARFLAGYGDGTGAMWRAFLAALDA 162

                         170       180       190
                  ....*....|....*....|....*....|
gi 1080669252 161 LNLTPEAEAEAIQGACEAFEFYKVILRETF 190
Cdd:COG3230   163 AALTEEEADAAIAGARAAFARFEAWLEAAF 192
Heme_oxygenase pfam01126
Heme oxygenase;
7-188 2.02e-46

Heme oxygenase;


Pssm-ID: 395895  Cd Length: 204  Bit Score: 151.74  E-value: 2.02e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080669252   7 LTFAKRLKEQTTVTHDSVDNLVMSVQPFS---SKENYIKFLKLQSVFHKAVD------------------HIYKDAELNK 65
Cdd:pfam01126   1 LNLAKRLREATKDVHVMAENLVFVKDFLKgvvDKDAYAKLLANLYFVYSALEeelernrdspvaapiyfpELNRKAALER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080669252  66 AIPELEYmARYDAVTQDLKDLGEEPYKFDKELPhETGNKAIGWLYCAEGSNLGAAFLFKH--AQKLEYTGEfGARHLAPH 143
Cdd:pfam01126  81 DLAYLYG-ADWRADIQDSPATQEYVPRIREIGN-ESPELLVAHAYTRYLGDLSGGQLLKKiaQRALGLPPG-EGTAFYEF 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1080669252 144 PN--GRGKHWRAFVEHLNALNLTPEAEAEAIQGACEAFEFYKVILRE 188
Cdd:pfam01126 158 EGisDRKVFKQEYREALNALELDDEARARAVEEANDAFALNIQVFRE 204
 
Name Accession Description Interval E-value
HemeO-like cd00232
heme oxygenase; Heme oxygenase (HO, EC 1.14.14.18) catalyzes the rate limiting step in the ...
 9-188 1.38e-76

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: 228.67  E-value: 1.38e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080669252   9 FAKRLKEQTTVTHDSVDNLVMSVQP--FSSKENYIKFLKLQSVFHKAVDHIYKDAELNKAI---PELEYMARYDAVTQDL 83
Cdd:cd00232     1 LSKRLKKATREVHNVSESLVNSRLPalFVSKDNYAKFLACQYYFFVALEAAYDEALLKGDFdkdPLLEGLARADAFKQDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080669252  84 KDLGEEPYKFD--------------KELPHETGNKAIGWLYCAEGSNL-GAAFLFKHAQKLEY-TGEFGARHLAPHPNGR 147
Cdd:cd00232    81 ADLGGPTWQADlgtksqakdyeahlAELGRSSPALLLAHLYTQELSMLsGGQFLKKWAQKLFQlPDDVGAAHFAYPGESR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1080669252 148 GKHWRAFVEHLNALNLTPEAEAEAIQGACEAFEFYKVILRE 188
Cdd:cd00232   161 NKLWSAFVKQLDELELTPELEDQAISEALAAFGHNNALLEE 201
HemO COG3230
Heme oxygenase [Inorganic ion transport and metabolism];
4-190 1.18e-65

Heme oxygenase [Inorganic ion transport and metabolism];


Pssm-ID: 442462  Cd Length: 192  Bit Score: 200.59  E-value: 1.18e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080669252   4 TQELTFAKRLKEQTTVTHDSVDNLVMSVQPFSSKENYIKFLKLQSVFHKAVDHIYKDAELNKAIPELEYMARYDAVTQDL 83
Cdd:COG3230     3 AAAPSLLARLRAATRALHERLDALVMLLDPFLTLEDYARFLRAQYGFHAPLEALLAAAALAALLPDLAERRRLALLEADL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080669252  84 KDLGEEPYKFDK--ELPHETGNKAIGWLYCAEGSNLGAAFLFKHA-QKLEYTGEFGARHLAPHPNGRGKHWRAFVEHLNA 160
Cdd:COG3230    83 ADLGLPPPAAAAaaLPALTSLAAALGALYVLEGSTLGGAVLLKRLrRALGLDPDFGARFLAGYGDGTGAMWRAFLAALDA 162

                         170       180       190
                  ....*....|....*....|....*....|
gi 1080669252 161 LNLTPEAEAEAIQGACEAFEFYKVILRETF 190
Cdd:COG3230   163 AALTEEEADAAIAGARAAFARFEAWLEAAF 192
HemeO-bac cd19166
heme oxygenase found in pathogenic bacteria; This subfamily contains bacterial heme oxygenase ...
 9-188 1.15e-51

heme oxygenase found in pathogenic bacteria; This subfamily contains bacterial heme oxygenase (HO, EC 1.14.14.18), where HO is part of a pathway for iron acquisition from host heme and heme products. Most of these proteins have yet to be characterized. 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. This family includes heme oxygenase (pa-HO) from Pseudomonas aeruginosa, an opportunistic pathogen that causes a variety of systemic infections, particularly in those afflicted with cystic fibrosis, as well as cancer and AIDS patients who are immunosuppressed. Pa-HO, expressed by the PigA gene, is critical for the acquisition of host iron since there is essentially no free iron in mammals, and is unusual since it hydroxylates heme predominantly at the delta-meso heme carbon, while all other well-studied HOs hydroxylate the alpha-meso carbon. Also included in this family is Neisseria meningitidis HO which is substantially different from the human HO, with the reaction product being ferric biliverdin IXalpha rather than reduced iron and free biliverdin IXalpha. 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: 350857 [Multi-domain]  Cd Length: 182  Bit Score: 164.73  E-value: 1.15e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080669252   9 FAKRLKEQTTVTHDSVDNLVMSVQPFSSKENYIKFLKLQSVFHKAVDHIYKDAELNKAIPELEYMARYDAVTQDLKDLGE 88
Cdd:cd19166     1 LRARLRAATRAAHERLEALLGLLDLFLTLADYARFLAAQYGFYAPLEAALAAALLAALLPDLAARRRLPLLAADLAALGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080669252  89 EPYKFDKELPHETGNK--AIGWLYCAEGSNLGAAFLFKHAQKLEYTGEFGARHLAPHPNGRGKHWRAFVEHLNALNLTPE 166
Cdd:cd19166    81 APPAPAAAPLPALPSLaaALGALYVLEGSTLGGRVIARRLAKLLGLADFGARFLAGYGEGTGARWRAFLAALEAAALTPA 160

                         170       180
                  ....*....|....*....|..
gi 1080669252 167 AEAEAIQGACEAFEFYKVILRE 188
Cdd:cd19166   161 DEDAAVAGARATFALFEAALAA 182
Heme_oxygenase pfam01126
Heme oxygenase;
7-188 2.02e-46

Heme oxygenase;


Pssm-ID: 395895  Cd Length: 204  Bit Score: 151.74  E-value: 2.02e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080669252   7 LTFAKRLKEQTTVTHDSVDNLVMSVQPFS---SKENYIKFLKLQSVFHKAVD------------------HIYKDAELNK 65
Cdd:pfam01126   1 LNLAKRLREATKDVHVMAENLVFVKDFLKgvvDKDAYAKLLANLYFVYSALEeelernrdspvaapiyfpELNRKAALER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080669252  66 AIPELEYmARYDAVTQDLKDLGEEPYKFDKELPhETGNKAIGWLYCAEGSNLGAAFLFKH--AQKLEYTGEfGARHLAPH 143
Cdd:pfam01126  81 DLAYLYG-ADWRADIQDSPATQEYVPRIREIGN-ESPELLVAHAYTRYLGDLSGGQLLKKiaQRALGLPPG-EGTAFYEF 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1080669252 144 PN--GRGKHWRAFVEHLNALNLTPEAEAEAIQGACEAFEFYKVILRE 188
Cdd:pfam01126 158 EGisDRKVFKQEYREALNALELDDEARARAVEEANDAFALNIQVFRE 204
 
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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