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Conserved domains on  [gi|3091146|gb|AAC15188|]
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iron-starvation protein PigA [Pseudomonas aeruginosa PAO1]

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 ...
 14-195 4.49e-57

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: 178.59  E-value: 4.49e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3091146   14 RSQRLNLLTNEPHQRLESLVKSKEP--FASRDNFARFVAAQYLFQHDLEPLYRNEALARLF---PGLASRARDDAARADL 88
Cdd:cd00232   1 LSKRLKKATREVHNVSESLVNSRLPalFVSKDNYAKFLACQYYFFVALEAAYDEALLKGDFdkdPLLEGLARADAFKQDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3091146   89 ADLGHPVPEGDQ------------SVREADLSLAEALGWLFVSEGSKL--GAAFLFKKAAALELDENFGARHLAEPEGGR 154
Cdd:cd00232  81 ADLGGPTWQADLgtksqakdyeahLAELGRSSPALLLAHLYTQELSMLsgGQFLKKWAQKLFQLPDDVGAAHFAYPGESR 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 3091146  155 AQGWKSFVAILDGIELNEEEERLAAKGASDAFNRFGDLLER 195
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 ...
 14-195 4.49e-57

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: 178.59  E-value: 4.49e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3091146   14 RSQRLNLLTNEPHQRLESLVKSKEP--FASRDNFARFVAAQYLFQHDLEPLYRNEALARLF---PGLASRARDDAARADL 88
Cdd:cd00232   1 LSKRLKKATREVHNVSESLVNSRLPalFVSKDNYAKFLACQYYFFVALEAAYDEALLKGDFdkdPLLEGLARADAFKQDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3091146   89 ADLGHPVPEGDQ------------SVREADLSLAEALGWLFVSEGSKL--GAAFLFKKAAALELDENFGARHLAEPEGGR 154
Cdd:cd00232  81 ADLGGPTWQADLgtksqakdyeahLAELGRSSPALLLAHLYTQELSMLsgGQFLKKWAQKLFQLPDDVGAAHFAYPGESR 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 3091146  155 AQGWKSFVAILDGIELNEEEERLAAKGASDAFNRFGDLLER 195
Cdd:cd00232 161 NKLWSAFVKQLDELELTPELEDQAISEALAAFGHNNALLEE 201
HemO COG3230
Heme oxygenase [Inorganic ion transport and metabolism];
7-197 3.51e-42

Heme oxygenase [Inorganic ion transport and metabolism];


Pssm-ID: 442462  Cd Length: 192  Bit Score: 140.50  E-value: 3.51e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3091146    7 ESTRQNLRSQRLNLLTNEPHQRLESLVKSKEPFASRDNFARFVAAQYLFQHDLEPLYRNEALARLFPGLASRARDDAARA 86
Cdd:COG3230   1 AAAAAPSLLARLRAATRALHERLDALVMLLDPFLTLEDYARFLRAQYGFHAPLEALLAAAALAALLPDLAERRRLALLEA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3091146   87 DLADLGHPVPEGDQSVREADLSLAEALGWLFVSEGSKLGAAF-LFKKAAALELDENFGARHLAEPEGGRAQGWKSFVAIL 165
Cdd:COG3230  81 DLADLGLPPPAAAAAALPALTSLAAALGALYVLEGSTLGGAVlLKRLRRALGLDPDFGARFLAGYGDGTGAMWRAFLAAL 160

                       170       180       190
                ....*....|....*....|....*....|..
gi 3091146  166 DGIELNEEEERLAAKGASDAFNRFGDLLERTF 197
Cdd:COG3230 161 DAAALTEEEADAAIAGARAAFARFEAWLEAAF 192
Heme_oxygenase pfam01126
Heme oxygenase;
15-195 4.33e-31

Heme oxygenase;


Pssm-ID: 395895  Cd Length: 204  Bit Score: 112.07  E-value: 4.33e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3091146     15 SQRLNLLTNEPHQRLESLVKSKEPFA---SRDNFARFVAAQYLFQHDLE------------------PLYRNEALARLFP 73
Cdd:pfam01126   4 AKRLREATKDVHVMAENLVFVKDFLKgvvDKDAYAKLLANLYFVYSALEeelernrdspvaapiyfpELNRKAALERDLA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3091146     74 GLASRARDDAARADLADlGHPVPEGDQSVREadlSLAEALGWLFVSEGSKL--GAAFLFKKAAALELDENfGARHLAEPE 151
Cdd:pfam01126  84 YLYGADWRADIQDSPAT-QEYVPRIREIGNE---SPELLVAHAYTRYLGDLsgGQLLKKIAQRALGLPPG-EGTAFYEFE 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 3091146    152 G--GRAQGWKSFVAILDGIELNEEEERLAAKGASDAFNRFGDLLER 195
Cdd:pfam01126 159 GisDRKVFKQEYREALNALELDDEARARAVEEANDAFALNIQVFRE 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 ...
 14-195 4.49e-57

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: 178.59  E-value: 4.49e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3091146   14 RSQRLNLLTNEPHQRLESLVKSKEP--FASRDNFARFVAAQYLFQHDLEPLYRNEALARLF---PGLASRARDDAARADL 88
Cdd:cd00232   1 LSKRLKKATREVHNVSESLVNSRLPalFVSKDNYAKFLACQYYFFVALEAAYDEALLKGDFdkdPLLEGLARADAFKQDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3091146   89 ADLGHPVPEGDQ------------SVREADLSLAEALGWLFVSEGSKL--GAAFLFKKAAALELDENFGARHLAEPEGGR 154
Cdd:cd00232  81 ADLGGPTWQADLgtksqakdyeahLAELGRSSPALLLAHLYTQELSMLsgGQFLKKWAQKLFQLPDDVGAAHFAYPGESR 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 3091146  155 AQGWKSFVAILDGIELNEEEERLAAKGASDAFNRFGDLLER 195
Cdd:cd00232 161 NKLWSAFVKQLDELELTPELEDQAISEALAAFGHNNALLEE 201
HemO COG3230
Heme oxygenase [Inorganic ion transport and metabolism];
7-197 3.51e-42

Heme oxygenase [Inorganic ion transport and metabolism];


Pssm-ID: 442462  Cd Length: 192  Bit Score: 140.50  E-value: 3.51e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3091146    7 ESTRQNLRSQRLNLLTNEPHQRLESLVKSKEPFASRDNFARFVAAQYLFQHDLEPLYRNEALARLFPGLASRARDDAARA 86
Cdd:COG3230   1 AAAAAPSLLARLRAATRALHERLDALVMLLDPFLTLEDYARFLRAQYGFHAPLEALLAAAALAALLPDLAERRRLALLEA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3091146   87 DLADLGHPVPEGDQSVREADLSLAEALGWLFVSEGSKLGAAF-LFKKAAALELDENFGARHLAEPEGGRAQGWKSFVAIL 165
Cdd:COG3230  81 DLADLGLPPPAAAAAALPALTSLAAALGALYVLEGSTLGGAVlLKRLRRALGLDPDFGARFLAGYGDGTGAMWRAFLAAL 160

                       170       180       190
                ....*....|....*....|....*....|..
gi 3091146  166 DGIELNEEEERLAAKGASDAFNRFGDLLERTF 197
Cdd:COG3230 161 DAAALTEEEADAAIAGARAAFARFEAWLEAAF 192
Heme_oxygenase pfam01126
Heme oxygenase;
15-195 4.33e-31

Heme oxygenase;


Pssm-ID: 395895  Cd Length: 204  Bit Score: 112.07  E-value: 4.33e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3091146     15 SQRLNLLTNEPHQRLESLVKSKEPFA---SRDNFARFVAAQYLFQHDLE------------------PLYRNEALARLFP 73
Cdd:pfam01126   4 AKRLREATKDVHVMAENLVFVKDFLKgvvDKDAYAKLLANLYFVYSALEeelernrdspvaapiyfpELNRKAALERDLA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3091146     74 GLASRARDDAARADLADlGHPVPEGDQSVREadlSLAEALGWLFVSEGSKL--GAAFLFKKAAALELDENfGARHLAEPE 151
Cdd:pfam01126  84 YLYGADWRADIQDSPAT-QEYVPRIREIGNE---SPELLVAHAYTRYLGDLsgGQLLKKIAQRALGLPPG-EGTAFYEFE 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 3091146    152 G--GRAQGWKSFVAILDGIELNEEEERLAAKGASDAFNRFGDLLER 195
Cdd:pfam01126 159 GisDRKVFKQEYREALNALELDDEARARAVEEANDAFALNIQVFRE 204
HemeO-bac cd19166
heme oxygenase found in pathogenic bacteria; This subfamily contains bacterial heme oxygenase ...
 14-195 2.15e-30

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: 109.65  E-value: 2.15e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3091146   14 RSQRLNLLTNEPHQRLESLVKSKEPFASRDNFARFVAAQYLFQHDLEPLYRNEALARLFPGLASRARDDAARADLADLGH 93
Cdd:cd19166   1 LRARLRAATRAAHERLEALLGLLDLFLTLADYARFLAAQYGFYAPLEAALAAALLAALLPDLAARRRLPLLAADLAALGL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3091146   94 PVPEGDQSVREADLSLAEALGWLFVSEGSKLGAAFLFKKAAALELDENFGARHLAEPEGGRAQGWKSFVAILDGIELNEE 173
Cdd:cd19166  81 APPAPAAAPLPALPSLAAALGALYVLEGSTLGGRVIARRLAKLLGLADFGARFLAGYGEGTGARWRAFLAALEAAALTPA 160

                       170       180
                ....*....|....*....|..
gi 3091146  174 EERLAAKGASDAFNRFGDLLER 195
Cdd:cd19166 161 DEDAAVAGARATFALFEAALAA 182
 
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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