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Conserved domains on  [gi|15833638|ref|NP_312411|]
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heme utilization carrier protein [Escherichia coli O157:H7 str. Sakai]

Protein Classification

HugX family protein( domain architecture ID 10007914)

HugX family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HugX COG3721
Putative heme iron utilization protein [Inorganic ion transport and metabolism];
3-158 2.44e-90

Putative heme iron utilization protein [Inorganic ion transport and metabolism];


:

Pssm-ID: 442935  Cd Length: 162  Bit Score: 260.16  E-value: 2.44e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833638   3 HVSLQEFLKTEPDGTLEVVAEQYNTTLLEVVRNLPSS--TVVPGDKFDTVWDTVCEWGNVTTLVHTADVILEFSGELPSG 80
Cdd:COG3721   5 QQALRALLAENPDGVLEAIARELGVSELEVVAALPEEmaTLVPGERFDEILQELAGWGEVTTIVHTEDSIFEVKGPLPKG 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15833638  81 FHRHGYFNLRGKHGMSGHIKAENCTHIALIERKFMGMDTASILFFNKEGSAMLKIFLGRDDHRQLLSEQVSAFHTLAA 158
Cdd:COG3721  85 KHGHGYYNLHGKGGLHGHLKADNCAAIALVSRPFMGKESHSVQFFNAEGEAMFKIFLGRDEKRQLLPEQVERFRALKA 162
 
Name Accession Description Interval E-value
HugX COG3721
Putative heme iron utilization protein [Inorganic ion transport and metabolism];
3-158 2.44e-90

Putative heme iron utilization protein [Inorganic ion transport and metabolism];


Pssm-ID: 442935  Cd Length: 162  Bit Score: 260.16  E-value: 2.44e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833638   3 HVSLQEFLKTEPDGTLEVVAEQYNTTLLEVVRNLPSS--TVVPGDKFDTVWDTVCEWGNVTTLVHTADVILEFSGELPSG 80
Cdd:COG3721   5 QQALRALLAENPDGVLEAIARELGVSELEVVAALPEEmaTLVPGERFDEILQELAGWGEVTTIVHTEDSIFEVKGPLPKG 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15833638  81 FHRHGYFNLRGKHGMSGHIKAENCTHIALIERKFMGMDTASILFFNKEGSAMLKIFLGRDDHRQLLSEQVSAFHTLAA 158
Cdd:COG3721  85 KHGHGYYNLHGKGGLHGHLKADNCAAIALVSRPFMGKESHSVQFFNAEGEAMFKIFLGRDEKRQLLPEQVERFRALKA 162
HutX TIGR04108
putative heme utilization carrier protein HutX; Members of this protein family are HutX, found ...
 6-156 6.04e-90

putative heme utilization carrier protein HutX; Members of this protein family are HutX, found paired with HutW in some heme utilization loci although not shown directly to be necessary for heme utilization. This protein is homologous to the heme carrier protein HemS, while its partner HutW is homologous to (but does not complement) HemN, the radical SAM enzyme oxygen-independent coproporphyrinogen III oxidase involved in heme biosynthesis.


Pssm-ID: 274986  Cd Length: 154  Bit Score: 258.72  E-value: 6.04e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833638     6 LQEFLKTEPDGTLEVVAEQYNTTLLEVVRNLPSS--TVVPGDKFDTVWDTVCEWGNVTTLVHTADVILEFSGELPSGFHR 83
Cdd:TIGR04108   1 LRALLAENPDAVLEAIARELGVSELEVVRALPEEmvTLVPGDHFDEILQDLSGWGDVTTIVHTGDVIFEVKGPLPKGKVA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15833638    84 HGYFNLRG-KHGMSGHIKAENCTHIALIERKFMGMDTASILFFNKEGSAMLKIFLGRDDHRQLLSEQVSAFHTL 156
Cdd:TIGR04108  81 HGYYNLMGkKGGLHGHLKADNCAAIALVSRPFMGKETHSVQFFNAEGEAMFKVYLGRDEKRQLLPEQVERFRAL 154
ChuX_HutX-like cd16829
heme iron utilization protein ChuX and similar proteins; This family contains proteins similar ...
 17-157 5.95e-82

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: 238.17  E-value: 5.95e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833638  17 TLEVVAEQYNTTLLEVVRNLPSS--TVVPGDKFDTVWDTVCEWGNVTTLVHTADVILEFSGELPSGFHRHGYFNLRGKHG 94
Cdd:cd16829   1 VLEELAAELGVSELEVVRALPEEmaTFVPGEHFDEVWQELASWGEVTFIVHTPGSIFEFKGPLPKGKHGHGYYNLHGKSG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15833638  95 MSGHIKAENCTHIALIERKFMGMDTASILFFNKEGSAMLKIFLGRDDHRQLLSEQVSAFHTLA 157
Cdd:cd16829  81 LGGHLKADNCAAIAFVSRPFMGKESHSVQFFNADGEAMFKIYVGRDEKRQLLPEQVEAFEALK 143
ChuX_HutX pfam06228
Haem utilization ChuX/HutX; This family is found within haem utilization operons. It has a ...
 22-156 2.84e-37

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: 2.84e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833638    22 AEQYNTTLLEVVRNLPSSTVV--PGDKFDTVWDTVCEWGNVTTLVHTADVILEFSGELPsgfhrhGYFNL-RGKHGMSGH 98
Cdd:pfam06228   1 ARELGVSEAELVAALGEDMAVrlDGDDFDELLEALAAWGEVMAIVRNDGAVHEVKGPYP------PYYNLlLGGGGLDLH 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15833638    99 IKAENCTHIALIERKFMGMDTASILFFNKEGSAMLKIFLgRDDHRQllsEQVSAFHTL 156
Cdd:pfam06228  75 LFLDHWAHIFAVSRPFDRGESHSLQFFDADGEAVFKVYL-RDERSP---EQVAAFRAL 128
 
Name Accession Description Interval E-value
HugX COG3721
Putative heme iron utilization protein [Inorganic ion transport and metabolism];
3-158 2.44e-90

Putative heme iron utilization protein [Inorganic ion transport and metabolism];


Pssm-ID: 442935  Cd Length: 162  Bit Score: 260.16  E-value: 2.44e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833638   3 HVSLQEFLKTEPDGTLEVVAEQYNTTLLEVVRNLPSS--TVVPGDKFDTVWDTVCEWGNVTTLVHTADVILEFSGELPSG 80
Cdd:COG3721   5 QQALRALLAENPDGVLEAIARELGVSELEVVAALPEEmaTLVPGERFDEILQELAGWGEVTTIVHTEDSIFEVKGPLPKG 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15833638  81 FHRHGYFNLRGKHGMSGHIKAENCTHIALIERKFMGMDTASILFFNKEGSAMLKIFLGRDDHRQLLSEQVSAFHTLAA 158
Cdd:COG3721  85 KHGHGYYNLHGKGGLHGHLKADNCAAIALVSRPFMGKESHSVQFFNAEGEAMFKIFLGRDEKRQLLPEQVERFRALKA 162
HutX TIGR04108
putative heme utilization carrier protein HutX; Members of this protein family are HutX, found ...
 6-156 6.04e-90

putative heme utilization carrier protein HutX; Members of this protein family are HutX, found paired with HutW in some heme utilization loci although not shown directly to be necessary for heme utilization. This protein is homologous to the heme carrier protein HemS, while its partner HutW is homologous to (but does not complement) HemN, the radical SAM enzyme oxygen-independent coproporphyrinogen III oxidase involved in heme biosynthesis.


Pssm-ID: 274986  Cd Length: 154  Bit Score: 258.72  E-value: 6.04e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833638     6 LQEFLKTEPDGTLEVVAEQYNTTLLEVVRNLPSS--TVVPGDKFDTVWDTVCEWGNVTTLVHTADVILEFSGELPSGFHR 83
Cdd:TIGR04108   1 LRALLAENPDAVLEAIARELGVSELEVVRALPEEmvTLVPGDHFDEILQDLSGWGDVTTIVHTGDVIFEVKGPLPKGKVA 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15833638    84 HGYFNLRG-KHGMSGHIKAENCTHIALIERKFMGMDTASILFFNKEGSAMLKIFLGRDDHRQLLSEQVSAFHTL 156
Cdd:TIGR04108  81 HGYYNLMGkKGGLHGHLKADNCAAIALVSRPFMGKETHSVQFFNAEGEAMFKVYLGRDEKRQLLPEQVERFRAL 154
ChuX_HutX-like cd16829
heme iron utilization protein ChuX and similar proteins; This family contains proteins similar ...
 17-157 5.95e-82

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: 238.17  E-value: 5.95e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833638  17 TLEVVAEQYNTTLLEVVRNLPSS--TVVPGDKFDTVWDTVCEWGNVTTLVHTADVILEFSGELPSGFHRHGYFNLRGKHG 94
Cdd:cd16829   1 VLEELAAELGVSELEVVRALPEEmaTFVPGEHFDEVWQELASWGEVTFIVHTPGSIFEFKGPLPKGKHGHGYYNLHGKSG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15833638  95 MSGHIKAENCTHIALIERKFMGMDTASILFFNKEGSAMLKIFLGRDDHRQLLSEQVSAFHTLA 157
Cdd:cd16829  81 LGGHLKADNCAAIAFVSRPFMGKESHSVQFFNADGEAMFKIYVGRDEKRQLLPEQVEAFEALK 143
ChuX-like cd16827
heme utilization protein ChuX and similar proteins; This family contains ChuX, a member of the ...
 18-156 1.91e-66

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: 198.77  E-value: 1.91e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833638  18 LEVVAEQYNTTLLEVVRNLP--SSTVVPGDKFDTVWDTVCEWGNVTTLVHTADVILEFSGELPSGFHRHGYFNLRGKHGM 95
Cdd:cd16827   1 AEDLAGQYNITEAEVVRALPtdQATKVPGDRFDEILEALEAWGEVTVIVRNRDAVLEFVGTFPKGFHRHGWFNIRGDRTL 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15833638  96 SGHIKAENCTHIALIERKFMGMDTASILFFNKEGSAMLKIFLGRDDHRQLLSEQVSAFHTL 156
Cdd:cd16827  81 DGHILAESCASIFAIEKPFHGGETASIQFFDHDGDAAFKIFLGRDEDEQLLAEQVEAFATL 141
ChuX_HutX pfam06228
Haem utilization ChuX/HutX; This family is found within haem utilization operons. It has a ...
 22-156 2.84e-37

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: 2.84e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833638    22 AEQYNTTLLEVVRNLPSSTVV--PGDKFDTVWDTVCEWGNVTTLVHTADVILEFSGELPsgfhrhGYFNL-RGKHGMSGH 98
Cdd:pfam06228   1 ARELGVSEAELVAALGEDMAVrlDGDDFDELLEALAAWGEVMAIVRNDGAVHEVKGPYP------PYYNLlLGGGGLDLH 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15833638    99 IKAENCTHIALIERKFMGMDTASILFFNKEGSAMLKIFLgRDDHRQllsEQVSAFHTL 156
Cdd:pfam06228  75 LFLDHWAHIFAVSRPFDRGESHSLQFFDADGEAVFKVYL-RDERSP---EQVAAFRAL 128
 
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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