1N3U,1J77,1SK7,4RAJ


Conserved Protein Domain Family
HemeO-like

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cd00232: HemeO-like 
Click on image for an interactive view with Cn3D
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.
Statistics
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PSSM-Id: 350855
Aligned: 4 rows
Threshold Bit Score: 178.589
Created: 4-Sep-2001
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 17 residues -Click on image for an interactive view with Cn3D
Feature 1:heme binding site [chemical binding site]
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1          #      #  ##                           #                                   
1N3U_A     13 LSEALKEATKEVHTQAENAefmrnfqkgqvtrdGFKLVMASLYHIYVALEEEIErnkespvfa----pvyfpeelhRKAA 88  human
1J77_A     11 FAKRLKADTTAVHDSVDNLvmsvqp---fvskeNYIKFLKLQSVFHKAVDHIYKdaelnkai-------peleymaRYDA 80  Neisseria meningit...
1SK7_A     14 RSQRLNLLTNEPHQRLESLvkskep---fasrdNFARFVAAQYLFQHDLEPLYRnealarlf-------pglasraRDDA 83  Pseudomonas aerugi...
4RAJ_A     20 LTKRLSKASRKIHNVSNSLvnarlia-lfsdkdLYAKALGCFYYVFVALEAALDealkkgdadvskfkdvlkgglyRAPG 98  Chlamydomonas rein...
Feature 1                                                   ### ##   #   #                    
1N3U_A     89 LEQDLAFWygprwqevipytpam-qryvkrlhevgrtepELLVAHAYTRYLGDLsGGQVLKKIAQKAldlpssgeGLAFF 167 human
1J77_A     81 VTQDLKDLgeepykfd---------------kelpyeagNKAIGWLYCAEGSNL-GAAFLFKHAQKLdyn--gehGARHL 142 Neisseria meningit...
1SK7_A     84 ARADLADLghpvpegdq-------------svreadlslAEALGWLFVSEGSKL-GAAFLFKKAAALeld--enfGARHL 147 Pseudomonas aerugi...
4RAJ_A     99 FKQDVQHYlgatwqaqlgtksqalkdyeahlaslgrsspALLLAHVYTQHLAMAsGGQIVKRWARKIfqlp-ddvGTAAF 177 Chlamydomonas rein...
Feature 1                #   #                         #  #   #  
1N3U_A    168 TFpniasaTKFKQLYRSRMNSlem--tpAVRQRVIEEAKTAFLLNIQLFEE 216 human
1J77_A    143 APhpd-grGKHWRAFVEHLNAlnl--tpEAEAEAIQGAREAFAFYKVVLRE 190 Neisseria meningitidis
1SK7_A    148 AEpeg-grAQGWKSFVAILDGiel--neEEERLAAKGASDAFNRFGDLLER 195 Pseudomonas aeruginosa PAO1
4RAJ_A    178 DYtge-snNTLRSAFKKQFDEwgaaqpqELQDQLLSEHLAAFGHNNAIIKA 227 Chlamydomonas reinhardtii

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