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Conserved domains on  [gi|490355635|ref|WP_004235408|]
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MULTISPECIES: hemin-degrading factor [Morganella]

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HemS COG3720
Putative heme degradation protein [Inorganic ion transport and metabolism];
3-345 4.98e-178

Putative heme degradation protein [Inorganic ion transport and metabolism];


:

Pssm-ID: 442934 [Multi-domain]  Cd Length: 338  Bit Score: 497.01  E-value: 4.98e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635   3 SETLSRYLALKEQGHLIHARDIAAEMGISEAELAHCRAGYDACRLTRDIPAIFRMLGTAGELKGITRNDHAVHEHTGTYD 82
Cdd:COG3720    1 ATLYQRWRALRAENPKLRARDAAARLGISEAELLAARVGHGVTRLRPDWRALLPALEALGEVMALTRNESAVHEKVGVYE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635  83 NAEFGEHACLLLNPyGLDLRFFLSQWQTVFAFAENTPRGLRHSLQFFDRHGDAVHKIYTTADTDMGVWHHLTAQFAAYDN 162
Cdd:COG3720   81 NVSLGGHAGLVLGP-DIDLRLFLSHWAHGFAVEEETARGVRRSLQFFDAQGDAVHKVYLREESDVAAWEALVARFRAEDQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635 163 PQ---VVPEPAVIPACTSlTPEQQAEFTRHWQQMTDVHQFFVLLKIFNISRLQAFRCVDNTLAQRVDNSALSRLLTQCTE 239
Cdd:COG3720  160 SPlleVEPAPPPEAAKPD-AEIDVAALRQEWRAMTDTHQFFGLLKKHGLSRLQALRLAGDDLARRVDNDALRQLLEAAAA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635 240 EQNDIMIFVANRGCVQIFTGAIGRVEPYisprdgQHWINIFNPSFTLHLIESAVAESWITRKPTKDGIVTSLELFDKNGQ 319
Cdd:COG3720  239 DGLPIMVFVGNRGCIQIHTGPVEKVKPM------GPWLNVLDPGFNLHLREDHIAEAWVVRKPTKDGIVTSLELFDADGE 312
                        330       340
                 ....*....|....*....|....*.
gi 490355635 320 AIAQLFGQRTEGEPEQTIWRSQINAL 345
Cdd:COG3720  313 LIAQLFGQRKEGQPERAQWRELVEAL 338
 
Name Accession Description Interval E-value
HemS COG3720
Putative heme degradation protein [Inorganic ion transport and metabolism];
3-345 4.98e-178

Putative heme degradation protein [Inorganic ion transport and metabolism];


Pssm-ID: 442934 [Multi-domain]  Cd Length: 338  Bit Score: 497.01  E-value: 4.98e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635   3 SETLSRYLALKEQGHLIHARDIAAEMGISEAELAHCRAGYDACRLTRDIPAIFRMLGTAGELKGITRNDHAVHEHTGTYD 82
Cdd:COG3720    1 ATLYQRWRALRAENPKLRARDAAARLGISEAELLAARVGHGVTRLRPDWRALLPALEALGEVMALTRNESAVHEKVGVYE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635  83 NAEFGEHACLLLNPyGLDLRFFLSQWQTVFAFAENTPRGLRHSLQFFDRHGDAVHKIYTTADTDMGVWHHLTAQFAAYDN 162
Cdd:COG3720   81 NVSLGGHAGLVLGP-DIDLRLFLSHWAHGFAVEEETARGVRRSLQFFDAQGDAVHKVYLREESDVAAWEALVARFRAEDQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635 163 PQ---VVPEPAVIPACTSlTPEQQAEFTRHWQQMTDVHQFFVLLKIFNISRLQAFRCVDNTLAQRVDNSALSRLLTQCTE 239
Cdd:COG3720  160 SPlleVEPAPPPEAAKPD-AEIDVAALRQEWRAMTDTHQFFGLLKKHGLSRLQALRLAGDDLARRVDNDALRQLLEAAAA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635 240 EQNDIMIFVANRGCVQIFTGAIGRVEPYisprdgQHWINIFNPSFTLHLIESAVAESWITRKPTKDGIVTSLELFDKNGQ 319
Cdd:COG3720  239 DGLPIMVFVGNRGCIQIHTGPVEKVKPM------GPWLNVLDPGFNLHLREDHIAEAWVVRKPTKDGIVTSLELFDADGE 312
                        330       340
                 ....*....|....*....|....*.
gi 490355635 320 AIAQLFGQRTEGEPEQTIWRSQINAL 345
Cdd:COG3720  313 LIAQLFGQRKEGQPERAQWRELVEAL 338
HemS-like_C cd16831
C-terminal domain of heme degrading enzyme HemS, and similar proteins; This family contains ...
185-345 5.85e-79

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: 238.53  E-value: 5.85e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635 185 EFTRHWQQMTDVHQFFVLLKIFNISRLQAFRCVDNTLAQRVDNSALSRLLTQCTEEQNDIMIFVANRGCVQIFTGAIGRV 264
Cdd:cd16831    1 ALRADWRALTDVHDFFGLLRKFGVSRLQALRLAGEDFARQVDPDALEQLLEAAAEQGLPIMVFVGNRGCIQIHTGPVKKI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635 265 EPYisprdGQhWINIFNPSFTLHLIESAVAESWITRKPTKDGIVTSLELFDKNGQAIAQLFGQRTEGEPEQTIWRSQINA 344
Cdd:cd16831   81 KRM-----GP-WLNVLDPGFNLHLREDAIAEAWVVRKPTKDGIVTSLELFDADGELIAQFFGKRKPGQPELAAWRELVAS 154

                 .
gi 490355635 345 L 345
Cdd:cd16831  155 L 155
HemS pfam05171
Haemin-degrading HemS.ChuX domain; The Yersinia enterocolitica O:8 periplasmic ...
29-157 8.07e-43

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: 144.98  E-value: 8.07e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635   29 GISEAELAHCRAGYDACRLTRDIPAIFRMLGTAGELKGITRNDHAVHEHTGTYDNAEFGEHACLLLNPyGLDLRFFLSQW 108
Cdd:pfam05171   1 GVSEAQALAAAGGEFATRLDADLRALLEALAELGEVMAFTRNRGCVQEHTGPYENLKPMGPWGNVLDP-DFDLRLFLDHW 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 490355635  109 QTVFAFAENTPRGLRHSLQFFDRHGDAVHKIYTTADTDMGVWHHLTAQF 157
Cdd:pfam05171  80 ASAFAVRKPTADGVVTSLQFFDAAGDAVHKIFGTRKSELAAWRALVADL 128
 
Name Accession Description Interval E-value
HemS COG3720
Putative heme degradation protein [Inorganic ion transport and metabolism];
3-345 4.98e-178

Putative heme degradation protein [Inorganic ion transport and metabolism];


Pssm-ID: 442934 [Multi-domain]  Cd Length: 338  Bit Score: 497.01  E-value: 4.98e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635   3 SETLSRYLALKEQGHLIHARDIAAEMGISEAELAHCRAGYDACRLTRDIPAIFRMLGTAGELKGITRNDHAVHEHTGTYD 82
Cdd:COG3720    1 ATLYQRWRALRAENPKLRARDAAARLGISEAELLAARVGHGVTRLRPDWRALLPALEALGEVMALTRNESAVHEKVGVYE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635  83 NAEFGEHACLLLNPyGLDLRFFLSQWQTVFAFAENTPRGLRHSLQFFDRHGDAVHKIYTTADTDMGVWHHLTAQFAAYDN 162
Cdd:COG3720   81 NVSLGGHAGLVLGP-DIDLRLFLSHWAHGFAVEEETARGVRRSLQFFDAQGDAVHKVYLREESDVAAWEALVARFRAEDQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635 163 PQ---VVPEPAVIPACTSlTPEQQAEFTRHWQQMTDVHQFFVLLKIFNISRLQAFRCVDNTLAQRVDNSALSRLLTQCTE 239
Cdd:COG3720  160 SPlleVEPAPPPEAAKPD-AEIDVAALRQEWRAMTDTHQFFGLLKKHGLSRLQALRLAGDDLARRVDNDALRQLLEAAAA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635 240 EQNDIMIFVANRGCVQIFTGAIGRVEPYisprdgQHWINIFNPSFTLHLIESAVAESWITRKPTKDGIVTSLELFDKNGQ 319
Cdd:COG3720  239 DGLPIMVFVGNRGCIQIHTGPVEKVKPM------GPWLNVLDPGFNLHLREDHIAEAWVVRKPTKDGIVTSLELFDADGE 312
                        330       340
                 ....*....|....*....|....*.
gi 490355635 320 AIAQLFGQRTEGEPEQTIWRSQINAL 345
Cdd:COG3720  313 LIAQLFGQRKEGQPERAQWRELVEAL 338
HemS-like_C cd16831
C-terminal domain of heme degrading enzyme HemS, and similar proteins; This family contains ...
185-345 5.85e-79

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: 238.53  E-value: 5.85e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635 185 EFTRHWQQMTDVHQFFVLLKIFNISRLQAFRCVDNTLAQRVDNSALSRLLTQCTEEQNDIMIFVANRGCVQIFTGAIGRV 264
Cdd:cd16831    1 ALRADWRALTDVHDFFGLLRKFGVSRLQALRLAGEDFARQVDPDALEQLLEAAAEQGLPIMVFVGNRGCIQIHTGPVKKI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635 265 EPYisprdGQhWINIFNPSFTLHLIESAVAESWITRKPTKDGIVTSLELFDKNGQAIAQLFGQRTEGEPEQTIWRSQINA 344
Cdd:cd16831   81 KRM-----GP-WLNVLDPGFNLHLREDAIAEAWVVRKPTKDGIVTSLELFDADGELIAQFFGKRKPGQPELAAWRELVAS 154

                 .
gi 490355635 345 L 345
Cdd:cd16831  155 L 155
HemS-like_N cd16830
N-terminal domain of heme degrading enzyme HemS, and similar proteins; This family contains ...
5-157 4.36e-72

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: 220.79  E-value: 4.36e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635   5 TLSRYLALKEQGHLIHARDIAAEMGISEAELAHCRAGYDACRLTRDIPAIFRMLGTAGELKGITRNDHAVHEHTGTYDNA 84
Cdd:cd16830    1 LKQRWQALKAENPKLRARDAAARLGVSEAELLAARVGEGVTRLRPDWRALLKALESLGEVMALTRNESAVHEKKGVYENV 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490355635  85 EFGEHACLLLNPyGLDLRFFLSQWQTVFAFAENTPRGLRHSLQFFDRHGDAVHKIYTTADTDMGVWHHLTAQF 157
Cdd:cd16830   81 SLGGHMGLVLGP-DIDLRLFLSHWHHAFAVEEETRGGPRRSLQFFDAAGDAVHKIYLTEESDLAAWEALVARF 152
HemS-like cd16828
N- and C-terminal domains of heme degrading enzyme HemS, and similar proteins; This family ...
8-157 5.81e-43

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: 146.16  E-value: 5.81e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635   8 RYLALKEQGHLIHARDIAAEMGISEAELAHCRAGYDACRLTRDIPAIFRMLGTAGELKGITRNDHAVHEHTGTYDNAEFG 87
Cdd:cd16828    4 RWLALKDQHPGKYARDLAKLHNIREAELAFLRVGHDAWRLHNDLAEILEALEEVGEIMVFVRNEHCVHEQTGPVTNVHLN 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635  88 EHACLLLNPyGLDLRFFLSQWQTVFAFAENTPRGLRHSLQFFDRHGDAVHKIYTTADTDMGVWHHLTAQF 157
Cdd:cd16828   84 GHWGLILNP-RFDLRLFLNGWAEVFHIREPTARGEVTSIQFFDHQGDAILKVYGARNTDEAAWRELLARL 152
HemS pfam05171
Haemin-degrading HemS.ChuX domain; The Yersinia enterocolitica O:8 periplasmic ...
29-157 8.07e-43

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: 144.98  E-value: 8.07e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635   29 GISEAELAHCRAGYDACRLTRDIPAIFRMLGTAGELKGITRNDHAVHEHTGTYDNAEFGEHACLLLNPyGLDLRFFLSQW 108
Cdd:pfam05171   1 GVSEAQALAAAGGEFATRLDADLRALLEALAELGEVMAFTRNRGCVQEHTGPYENLKPMGPWGNVLDP-DFDLRLFLDHW 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 490355635  109 QTVFAFAENTPRGLRHSLQFFDRHGDAVHKIYTTADTDMGVWHHLTAQF 157
Cdd:pfam05171  80 ASAFAVRKPTADGVVTSLQFFDAAGDAVHKIFGTRKSELAAWRALVADL 128
HemS pfam05171
Haemin-degrading HemS.ChuX domain; The Yersinia enterocolitica O:8 periplasmic ...
207-345 2.73e-42

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: 143.44  E-value: 2.73e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635  207 NISRLQAFRCVDNTLAQRVDnSALSRLLTQcTEEQNDIMIFVANRGCVQIFTGAIGRVEPyisprdGQHWINIFNPSFTL 286
Cdd:pfam05171   1 GVSEAQALAAAGGEFATRLD-ADLRALLEA-LAELGEVMAFTRNRGCVQEHTGPYENLKP------MGPWGNVLDPDFDL 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 490355635  287 HLIESAVAESWITRKPTKDGIVTSLELFDKNGQAIAQLFGQRTegePEQTIWRSQINAL 345
Cdd:pfam05171  73 RLFLDHWASAFAVRKPTADGVVTSLQFFDAAGDAVHKIFGTRK---SELAAWRALVADL 128
HemS-like cd16828
N- and C-terminal domains of heme degrading enzyme HemS, and similar proteins; This family ...
188-345 1.71e-40

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: 139.62  E-value: 1.71e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635 188 RHWQQMTDVH---QFFVLLKIFNISRLQAFRCVDNTLAQRVDNsALSRLLtQCTEEQNDIMIFVANRGCVQIFTGAIGRV 264
Cdd:cd16828    3 TRWLALKDQHpgkYARDLAKLHNIREAELAFLRVGHDAWRLHN-DLAEIL-EALEEVGEIMVFVRNEHCVHEQTGPVTNV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635 265 EPyisprdGQHWINIFNPSFTLHLIESAVAESWITRKPTKDGIVTSLELFDKNGQAIAQLFGQRTEGEPEqtiWRSQINA 344
Cdd:cd16828   81 HL------NGHWGLILNPRFDLRLFLNGWAEVFHIREPTARGEVTSIQFFDHQGDAILKVYGARNTDEAA---WRELLAR 151

                 .
gi 490355635 345 L 345
Cdd:cd16828  152 L 152
ChuX_HutX pfam06228
Haem utilization ChuX/HutX; This family is found within haem utilization operons. It has a ...
25-153 5.63e-35

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: 124.59  E-value: 5.63e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635   25 AAEMGISEAELAHCRAGYDACRLT-RDIPAIFRMLGTAGELKGITRNDHAVHEHTGTYdnaefGEHACLLLNPYGLDLRF 103
Cdd:pfam06228   1 ARELGVSEAELVAALGEDMAVRLDgDDFDELLEALAAWGEVMAIVRNDGAVHEVKGPY-----PPYYNLLLGGGGLDLHL 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 490355635  104 FLSQWQTVFAFAENTPRGLRHSLQFFDRHGDAVHKIY---TTADTDMGVWHHL 153
Cdd:pfam06228  76 FLDHWAHIFAVSRPFDRGESHSLQFFDADGEAVFKVYlrdERSPEQVAAFRAL 128
ChuX-like cd16827
heme utilization protein ChuX and similar proteins; This family contains ChuX, a member of the ...
199-345 3.73e-26

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: 101.70  E-value: 3.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635 199 FFVLLKIFNISRLQAFRCVDNTLAQRVDNSALSRLLtQCTEEQNDIMIFVANRGCVQIFTGAIGRVepyiSPRDGqhWIN 278
Cdd:cd16827    1 AEDLAGQYNITEAEVVRALPTDQATKVPGDRFDEIL-EALEAWGEVTVIVRNRDAVLEFVGTFPKG----FHRHG--WFN 73
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490355635 279 IFNPS-FTLHLIESAVAESWITRKPTKDGIVTSLELFDKNGQAIAQLFGQRTEGEPEQTIWRSQINAL 345
Cdd:cd16827   74 IRGDRtLDGHILAESCASIFAIEKPFHGGETASIQFFDHDGDAAFKIFLGRDEDEQLLAEQVEAFATL 141
ChuX_HutX pfam06228
Haem utilization ChuX/HutX; This family is found within haem utilization operons. It has a ...
206-339 1.10e-24

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: 97.24  E-value: 1.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635  206 FNISRLQAFRCVDNTLAQRVDNSALSRLLTQCtEEQNDIMIFVANRGCVQIFTGAIGrvepyisprdgqHWINIFN--PS 283
Cdd:pfam06228   4 LGVSEAELVAALGEDMAVRLDGDDFDELLEAL-AAWGEVMAIVRNDGAVHEVKGPYP------------PYYNLLLggGG 70
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 490355635  284 FTLHLIESAVAESWITRKPTKDGIVTSLELFDKNGQAIAQLFGQRTEGEPEQTIWR 339
Cdd:pfam06228  71 LDLHLFLDHWAHIFAVSRPFDRGESHSLQFFDADGEAVFKVYLRDERSPEQVAAFR 126
ChuX-like cd16827
heme utilization protein ChuX and similar proteins; This family contains ChuX, a member of the ...
21-159 1.85e-21

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: 88.99  E-value: 1.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635  21 ARDIAAEMGISEAELAHCRAGYDACRLTRD-IPAIFRMLGTAGELKGITRNDHAVHEHTGTYDNAEFGEHACLLLNPYGL 99
Cdd:cd16827    1 AEDLAGQYNITEAEVVRALPTDQATKVPGDrFDEILEALEAWGEVTVIVRNRDAVLEFVGTFPKGFHRHGWFNIRGDRTL 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490355635 100 DLRFFLSQWQTVFAFAENTPRGLRHSLQFFDRHGDAVHKIYTTADTDMGVWHHLTAQFAA 159
Cdd:cd16827   81 DGHILAESCASIFAIEKPFHGGETASIQFFDHDGDAAFKIFLGRDEDEQLLAEQVEAFAT 140
 
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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