ChuX/HutX family heme-like substrate-binding protein [Klebsiella sp. CN_Kp107]
Protein Classification
hemin-degrading factor( domain architecture ID 11467279)
hemin-degrading factor is a cytoplasmic heme-binding protein which interacts and transports heme from the inner membrane heme transporter to the cytoplasm where it is degraded by heme oxygenase, releasing its iron
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| HemS | COG3720 | Putative heme degradation protein [Inorganic ion transport and metabolism]; |
6-336 | 0e+00 | ||||||
Putative heme degradation protein [Inorganic ion transport and metabolism]; : Pssm-ID: 442934 [Multi-domain] Cd Length: 338 Bit Score: 523.59 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||
| HemS | COG3720 | Putative heme degradation protein [Inorganic ion transport and metabolism]; |
6-336 | 0e+00 | ||||||
Putative heme degradation protein [Inorganic ion transport and metabolism]; Pssm-ID: 442934 [Multi-domain] Cd Length: 338 Bit Score: 523.59 E-value: 0e+00
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| HemS-like_C | cd16831 | C-terminal domain of heme degrading enzyme HemS, and similar proteins; This family contains ... |
182-336 | 8.55e-88 | ||||||
C-terminal domain of heme degrading enzyme HemS, and similar proteins; This family contains the C-terminal domain of heme degrading enzyme HemS, and similar proteins, including PhuS, ChuS, ShuS, and HmuS in proteobacteria. Despite low sequence identity between the N- and C-terminal halves, these segments represent a structural duplication, with each terminal half having similar fold to single domains of ChuX. HemS shares homology with both, heme degrading enzymes and heme trafficking enzymes. Heme is an iron source for pathogenic microorganisms to enable multiplication and survival within hosts they invade and therefore heme degrading enzyme activity is required for the release of iron from heme after its transportation into the cytoplasm. N- and C-terminal halves of ChuS are each a functional heme oxygenase (HO). The mode of heme coordination by ChuS has been shown to be distinct, whereby the heme is stabilized mostly by residues from the C-terminal domain, assisted by a distant arginine from the N-terminal domain. ChuS can use ascorbic acid or cytochrome P450 reductase-NADPH as electron sources for heme oxygenation. Shigella dysenteriae ShuS promotes utilization of heme as an iron source and protects against heme toxicity by physically sequestering DNA. Heme transporter protein PhuS in Pseudomonas aeruginosa is unique among this family since it contains three histidines in the heme-binding pocket, compared with only one in ChuX. Pssm-ID: 319360 Cd Length: 155 Bit Score: 260.49 E-value: 8.55e-88
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| HemS | pfam05171 | Haemin-degrading HemS.ChuX domain; The Yersinia enterocolitica O:8 periplasmic ... |
32-156 | 1.13e-50 | ||||||
Haemin-degrading HemS.ChuX domain; The Yersinia enterocolitica O:8 periplasmic binding-protein- dependent transport system consisted of four proteins: the periplasmic haemin-binding protein HemT, the haemin permease protein HemU, the ATP-binding hydrophilic protein HemV and the haemin-degrading protein HemS (this family). The structure for HemS has been solved and consists of a tandem repeat of this domain. Pssm-ID: 461567 Cd Length: 128 Bit Score: 164.63 E-value: 1.13e-50
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| Name | Accession | Description | Interval | E-value | ||||||
| HemS | COG3720 | Putative heme degradation protein [Inorganic ion transport and metabolism]; |
6-336 | 0e+00 | ||||||
Putative heme degradation protein [Inorganic ion transport and metabolism]; Pssm-ID: 442934 [Multi-domain] Cd Length: 338 Bit Score: 523.59 E-value: 0e+00
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| HemS-like_C | cd16831 | C-terminal domain of heme degrading enzyme HemS, and similar proteins; This family contains ... |
182-336 | 8.55e-88 | ||||||
C-terminal domain of heme degrading enzyme HemS, and similar proteins; This family contains the C-terminal domain of heme degrading enzyme HemS, and similar proteins, including PhuS, ChuS, ShuS, and HmuS in proteobacteria. Despite low sequence identity between the N- and C-terminal halves, these segments represent a structural duplication, with each terminal half having similar fold to single domains of ChuX. HemS shares homology with both, heme degrading enzymes and heme trafficking enzymes. Heme is an iron source for pathogenic microorganisms to enable multiplication and survival within hosts they invade and therefore heme degrading enzyme activity is required for the release of iron from heme after its transportation into the cytoplasm. N- and C-terminal halves of ChuS are each a functional heme oxygenase (HO). The mode of heme coordination by ChuS has been shown to be distinct, whereby the heme is stabilized mostly by residues from the C-terminal domain, assisted by a distant arginine from the N-terminal domain. ChuS can use ascorbic acid or cytochrome P450 reductase-NADPH as electron sources for heme oxygenation. Shigella dysenteriae ShuS promotes utilization of heme as an iron source and protects against heme toxicity by physically sequestering DNA. Heme transporter protein PhuS in Pseudomonas aeruginosa is unique among this family since it contains three histidines in the heme-binding pocket, compared with only one in ChuX. Pssm-ID: 319360 Cd Length: 155 Bit Score: 260.49 E-value: 8.55e-88
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| HemS-like_N | cd16830 | N-terminal domain of heme degrading enzyme HemS, and similar proteins; This family contains ... |
8-156 | 3.71e-69 | ||||||
N-terminal domain of heme degrading enzyme HemS, and similar proteins; This family contains the N-terminal domain of heme degrading enzyme HemS, and similar proteins, including PhuS, ChuS, ShuS, and HmuS in proteobacteria. Despite low sequence identity between the N- and C-terminal halves, these segments represent a structural duplication, with each terminal half having similar fold to single domains of ChuX. HemS shares homology with both heme degrading enzymes and heme trafficking enzymes. Heme is an iron source for pathogenic microorganisms to enable multiplication and survival within hosts they invade and therefore heme degrading enzyme activity is required for the release of iron from heme after its transportation into the cytoplasm. N- and C-terminal halves of ChuS are each a functional heme oxygenase (HO). The mode of heme coordination by ChuS has been shown to be distinct, whereby the heme is stabilized mostly by residues from the C-terminal domain, assisted by a distant arginine from the N-terminal domain. ChuS can use ascorbic acid or cytochrome P450 reductase-NADPH as electron sources for heme oxygenation. Shigella dysenteriae ShuS promotes utilization of heme as an iron source and protects against heme toxicity by physically sequestering DNA. Heme transporter protein PhuS in Pseudomonas aeruginosa is unique among this family since it contains three histidines in the heme-binding pocket, compared with only one in ChuX. Pssm-ID: 319359 Cd Length: 152 Bit Score: 213.09 E-value: 3.71e-69
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| HemS-like | cd16828 | N- and C-terminal domains of heme degrading enzyme HemS, and similar proteins; This family ... |
8-156 | 3.92e-51 | ||||||
N- and C-terminal domains of heme degrading enzyme HemS, and similar proteins; This family contains the N- and C-terminal domains of heme degrading enzyme HemS, and similar proteins, including PhuS, ChuS, ShuS, and HmuS in proteobacteria. Despite low sequence identity between the N- and C-terminal halves, these segments represent a structural duplication, with each terminal half having similar fold to single domains of ChuX. HemS shares homology with both heme degrading enzymes and heme trafficking enzymes. Heme is an iron source for pathogenic microorganisms to enable multiplication and survival within hosts they invade and therefore heme degrading enzyme activity is required for the release of iron from heme after its transportation into the cytoplasm. N- and C-terminal halves of ChuS are each a functional heme oxygenase (HO). The mode of heme coordination by ChuS has been shown to be distinct, whereby the heme is stabilized mostly by residues from the C-terminal domain, assisted by a distant arginine from the N-terminal domain. ChuS can use ascorbic acid or cytochrome P450 reductase-NADPH as electron sources for heme oxygenation. Shigella dysenteriae ShuS promotes utilization of heme as an iron source and protects against heme toxicity by physically sequestering DNA. PhuS in Pseudomonas aeruginosa has been reported as a heme chaperone and as a heme degrading enzyme, and is unique among this family since it contains three histidines in the heme-binding pocket, compared with only one in ChuX. Heme transporter protein PhuS in Pseudomonas aeruginosa is unique among this family since it contains three histidines in the heme-binding pocket, compared with only one in ChuX. Pssm-ID: 319357 Cd Length: 152 Bit Score: 166.96 E-value: 3.92e-51
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| HemS | pfam05171 | Haemin-degrading HemS.ChuX domain; The Yersinia enterocolitica O:8 periplasmic ... |
32-156 | 1.13e-50 | ||||||
Haemin-degrading HemS.ChuX domain; The Yersinia enterocolitica O:8 periplasmic binding-protein- dependent transport system consisted of four proteins: the periplasmic haemin-binding protein HemT, the haemin permease protein HemU, the ATP-binding hydrophilic protein HemV and the haemin-degrading protein HemS (this family). The structure for HemS has been solved and consists of a tandem repeat of this domain. Pssm-ID: 461567 Cd Length: 128 Bit Score: 164.63 E-value: 1.13e-50
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| HemS-like | cd16828 | N- and C-terminal domains of heme degrading enzyme HemS, and similar proteins; This family ... |
183-336 | 1.95e-50 | ||||||
N- and C-terminal domains of heme degrading enzyme HemS, and similar proteins; This family contains the N- and C-terminal domains of heme degrading enzyme HemS, and similar proteins, including PhuS, ChuS, ShuS, and HmuS in proteobacteria. Despite low sequence identity between the N- and C-terminal halves, these segments represent a structural duplication, with each terminal half having similar fold to single domains of ChuX. HemS shares homology with both heme degrading enzymes and heme trafficking enzymes. Heme is an iron source for pathogenic microorganisms to enable multiplication and survival within hosts they invade and therefore heme degrading enzyme activity is required for the release of iron from heme after its transportation into the cytoplasm. N- and C-terminal halves of ChuS are each a functional heme oxygenase (HO). The mode of heme coordination by ChuS has been shown to be distinct, whereby the heme is stabilized mostly by residues from the C-terminal domain, assisted by a distant arginine from the N-terminal domain. ChuS can use ascorbic acid or cytochrome P450 reductase-NADPH as electron sources for heme oxygenation. Shigella dysenteriae ShuS promotes utilization of heme as an iron source and protects against heme toxicity by physically sequestering DNA. PhuS in Pseudomonas aeruginosa has been reported as a heme chaperone and as a heme degrading enzyme, and is unique among this family since it contains three histidines in the heme-binding pocket, compared with only one in ChuX. Heme transporter protein PhuS in Pseudomonas aeruginosa is unique among this family since it contains three histidines in the heme-binding pocket, compared with only one in ChuX. Pssm-ID: 319357 Cd Length: 152 Bit Score: 165.04 E-value: 1.95e-50
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| HemS | pfam05171 | Haemin-degrading HemS.ChuX domain; The Yersinia enterocolitica O:8 periplasmic ... |
204-336 | 3.58e-48 | ||||||
Haemin-degrading HemS.ChuX domain; The Yersinia enterocolitica O:8 periplasmic binding-protein- dependent transport system consisted of four proteins: the periplasmic haemin-binding protein HemT, the haemin permease protein HemU, the ATP-binding hydrophilic protein HemV and the haemin-degrading protein HemS (this family). The structure for HemS has been solved and consists of a tandem repeat of this domain. Pssm-ID: 461567 Cd Length: 128 Bit Score: 158.46 E-value: 3.58e-48
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| ChuX-like | cd16827 | heme utilization protein ChuX and similar proteins; This family contains ChuX, a member of the ... |
196-336 | 3.55e-38 | ||||||
heme utilization protein ChuX and similar proteins; This family contains ChuX, a member of the conserved heme utilization operon from pathogenic E. coli, and similar proteins, which include ChuS, HutX, HuvX, HugX, and ShuX in proteobacteria, among others. It forms a dimer which displays a very similar fold and organization to the monomeric structure of other heme utilization proteins such as HemS, ChuS, HmuS, PhuS; these latter occurring as duplicated domains. They all bind heme via a key conserved histidine. The genes encoded within these heme utilization operons enable the effective uptake and utilization of heme as an iron source in pathogenic microorganisms to enable multiplication and survival within hosts they invade. Pssm-ID: 319356 Cd Length: 141 Bit Score: 132.90 E-value: 3.55e-38
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| ChuX-like | cd16827 | heme utilization protein ChuX and similar proteins; This family contains ChuX, a member of the ... |
24-155 | 8.19e-35 | ||||||
heme utilization protein ChuX and similar proteins; This family contains ChuX, a member of the conserved heme utilization operon from pathogenic E. coli, and similar proteins, which include ChuS, HutX, HuvX, HugX, and ShuX in proteobacteria, among others. It forms a dimer which displays a very similar fold and organization to the monomeric structure of other heme utilization proteins such as HemS, ChuS, HmuS, PhuS; these latter occurring as duplicated domains. They all bind heme via a key conserved histidine. The genes encoded within these heme utilization operons enable the effective uptake and utilization of heme as an iron source in pathogenic microorganisms to enable multiplication and survival within hosts they invade. Pssm-ID: 319356 Cd Length: 141 Bit Score: 124.05 E-value: 8.19e-35
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| ChuX_HutX | pfam06228 | Haem utilization ChuX/HutX; This family is found within haem utilization operons. It has a ... |
201-331 | 2.29e-31 | ||||||
Haem utilization ChuX/HutX; This family is found within haem utilization operons. It has a similar structure to that of pfam05171. pfam05171 usually occurs as a duplicated domain, but this domain occurs as a single domain and forms a dimer. The organization of the dimer is very similar to that of the duplicated pfam05171 domains. It binds haem via conserved histidines. Pssm-ID: 428836 Cd Length: 128 Bit Score: 114.57 E-value: 2.29e-31
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| ChuX_HutX | pfam06228 | Haem utilization ChuX/HutX; This family is found within haem utilization operons. It has a ... |
28-152 | 6.51e-30 | ||||||
Haem utilization ChuX/HutX; This family is found within haem utilization operons. It has a similar structure to that of pfam05171. pfam05171 usually occurs as a duplicated domain, but this domain occurs as a single domain and forms a dimer. The organization of the dimer is very similar to that of the duplicated pfam05171 domains. It binds haem via conserved histidines. Pssm-ID: 428836 Cd Length: 128 Bit Score: 110.72 E-value: 6.51e-30
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| ChuX_HutX-like | cd16829 | heme iron utilization protein ChuX and similar proteins; This family contains proteins similar ... |
26-139 | 2.33e-04 | ||||||
heme iron utilization protein ChuX and similar proteins; This family contains proteins similar to ChuX, a member of the conserved heme utilization operon from pathogenic E. coli, and includes ChuS, HutX, HuvX, HugX, and ShuX in proteobacteria, among others. It forms a dimer which displays a very similar fold and organization to the monomeric structure of other heme utilization proteins such as HemS, ChuS, HmuS, PhuS; these latter occurring as duplicated domains. They all bind heme via a key conserved histidine. The genes encoded within these heme utilization operons enable the effective uptake and utilization of heme as an iron source in pathogenic microorganisms to enable multiplication and survival within hosts they invade. ChuX, a member of the conserved heme utilization operon from pathogenic E. coli O157:H7, forms a dimer with a very similar fold to the monomer structure of two other heme utilization proteins, ChuS and HemS, despite low sequence homology. ChuX has been shown to bind heme in a 1:1 manner, inferring that the ChuX homodimer could coordinate two heme molecules in contrast to only one heme molecule bound in ChuS and HemS. Similarly, cytoplasmic heme-binding protein HutX in Vibrio cholera, an intracellular heme transport protein for the heme-degrading enzyme HutZ, forms a dimer, each domain binding heme that is transferred from HutX to HutZ via a specific protein-protein interaction. This family also includes AGR_C_4470p from Agrobacterium tumefaciens and found to be a dimer, with each subunit having strong structural homology and organization to the heme utilization protein ChuS from Escherichia coli and HemS from Yersinia enterocolitica. However, the heme binding site is not conserved in AGR_C_4470p, suggesting a possible different function. Pssm-ID: 319358 Cd Length: 143 Bit Score: 40.95 E-value: 2.33e-04
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| HugX | COG3721 | Putative heme iron utilization protein [Inorganic ion transport and metabolism]; |
26-139 | 6.97e-04 | ||||||
Putative heme iron utilization protein [Inorganic ion transport and metabolism]; Pssm-ID: 442935 Cd Length: 162 Bit Score: 39.82 E-value: 6.97e-04
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