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Conserved domains on  [gi|527037697|ref|WP_020884350|]
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MULTISPECIES: heme-binding protein [Enterobacter]

Protein Classification

GlcG/HbpS family heme-binding protein( domain architecture ID 10007034)

heme-binding protein may degrade heme, sequester iron, and may protect from iron-mediated oxidative stress; similar to Salmonella enterica corrinoid adenosyltransferase PduO that converts cob(I)alamin to adenosylcobalamin (adenosylcob(III)alamin), the cofactor for propanediol dehydratase

CATH:  3.30.450.150
Gene Ontology:  GO:0020037
PubMed:  19244623|8606183
SCOP:  4003947

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GlcG COG3193
Heme-binding protein HbpS, GlcG/HbpS family [Signal transduction mechanisms];
25-158 5.68e-28

Heme-binding protein HbpS, GlcG/HbpS family [Signal transduction mechanisms];


:

Pssm-ID: 442426  Cd Length: 135  Bit Score: 100.61  E-value: 5.68e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037697  25 NQKNLSLAQANALATSAIQACVAKNYQVTVTVVDRAGVVKAVQRTDNAGPHTVKASEMKAYTALSAKNASGKVMEAAQSN 104
Cdd:COG3193    1 TKPSLTLEDARKIAAAALAKARELGVPVAIAVVDAGGNLLAFLRMDGAPLGSIDIAIGKAYTAAAFGRPTGELEERAQPG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527037697 105 AGAQNMRDI--PGFLLLAGGLPVKEGDEV--------IGAIGiggapgghlDEACAQAAIDGLK 158
Cdd:COG3193   81 PPLLGLNTSngPGLVPFGGGVPIKVDGEVigaigvsgGTSEQ---------DEAIAQAGLAALG 135
 
Name Accession Description Interval E-value
GlcG COG3193
Heme-binding protein HbpS, GlcG/HbpS family [Signal transduction mechanisms];
25-158 5.68e-28

Heme-binding protein HbpS, GlcG/HbpS family [Signal transduction mechanisms];


Pssm-ID: 442426  Cd Length: 135  Bit Score: 100.61  E-value: 5.68e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037697  25 NQKNLSLAQANALATSAIQACVAKNYQVTVTVVDRAGVVKAVQRTDNAGPHTVKASEMKAYTALSAKNASGKVMEAAQSN 104
Cdd:COG3193    1 TKPSLTLEDARKIAAAALAKARELGVPVAIAVVDAGGNLLAFLRMDGAPLGSIDIAIGKAYTAAAFGRPTGELEERAQPG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527037697 105 AGAQNMRDI--PGFLLLAGGLPVKEGDEV--------IGAIGiggapgghlDEACAQAAIDGLK 158
Cdd:COG3193   81 PPLLGLNTSngPGLVPFGGGVPIKVDGEVigaigvsgGTSEQ---------DEAIAQAGLAALG 135
HbpS-like pfam03928
Haem degrading protein HbpS-like; This entry includes haem degrading protein HbpS from ...
 29-131 6.96e-21

Haem degrading protein HbpS-like; This entry includes haem degrading protein HbpS from Streptomyces reticuli (swiss:Q9RIM2) and and GlcG from Escherichia coli. HbpS is up-regulated in response to haemin- and peroxide-based oxidative stress. It interacts with the SenS/SenR two-component signal transduction system. Iron binds to surface-exposed lysine residues of an octomeric assembly of the protein. The structure of GlcG is composed of an alpha-beta(2)-alpha(3)-beta(2)-alpha fold, similar to the Roadblock/LC7 domain.


Pssm-ID: 461095 [Multi-domain]  Cd Length: 116  Bit Score: 82.16  E-value: 6.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037697   29 LSLAQANALATSAIQACVAKNYQVTVTVVDRAGVVKAVQRTDNAGPHTVKASEMKAYTALSAKNASGKVMEAAQSnagaq 108
Cdd:pfam03928   1 LTLEDAWELGAAAVAKARELGVPVAIAVVDAGGHLLFFARMDGASLDSIDIARRKAYTAARFGRSTSALGERAGP----- 75

                          90       100
                  ....*....|....*....|...
gi 527037697  109 nmRDIPGFLLLAGGLPVKEGDEV 131
Cdd:pfam03928  76 --GDAPEYAPFGGGVPIRVDGVV 96
 
Name Accession Description Interval E-value
GlcG COG3193
Heme-binding protein HbpS, GlcG/HbpS family [Signal transduction mechanisms];
25-158 5.68e-28

Heme-binding protein HbpS, GlcG/HbpS family [Signal transduction mechanisms];


Pssm-ID: 442426  Cd Length: 135  Bit Score: 100.61  E-value: 5.68e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037697  25 NQKNLSLAQANALATSAIQACVAKNYQVTVTVVDRAGVVKAVQRTDNAGPHTVKASEMKAYTALSAKNASGKVMEAAQSN 104
Cdd:COG3193    1 TKPSLTLEDARKIAAAALAKARELGVPVAIAVVDAGGNLLAFLRMDGAPLGSIDIAIGKAYTAAAFGRPTGELEERAQPG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527037697 105 AGAQNMRDI--PGFLLLAGGLPVKEGDEV--------IGAIGiggapgghlDEACAQAAIDGLK 158
Cdd:COG3193   81 PPLLGLNTSngPGLVPFGGGVPIKVDGEVigaigvsgGTSEQ---------DEAIAQAGLAALG 135
HbpS-like pfam03928
Haem degrading protein HbpS-like; This entry includes haem degrading protein HbpS from ...
 29-131 6.96e-21

Haem degrading protein HbpS-like; This entry includes haem degrading protein HbpS from Streptomyces reticuli (swiss:Q9RIM2) and and GlcG from Escherichia coli. HbpS is up-regulated in response to haemin- and peroxide-based oxidative stress. It interacts with the SenS/SenR two-component signal transduction system. Iron binds to surface-exposed lysine residues of an octomeric assembly of the protein. The structure of GlcG is composed of an alpha-beta(2)-alpha(3)-beta(2)-alpha fold, similar to the Roadblock/LC7 domain.


Pssm-ID: 461095 [Multi-domain]  Cd Length: 116  Bit Score: 82.16  E-value: 6.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527037697   29 LSLAQANALATSAIQACVAKNYQVTVTVVDRAGVVKAVQRTDNAGPHTVKASEMKAYTALSAKNASGKVMEAAQSnagaq 108
Cdd:pfam03928   1 LTLEDAWELGAAAVAKARELGVPVAIAVVDAGGHLLFFARMDGASLDSIDIARRKAYTAARFGRSTSALGERAGP----- 75

                          90       100
                  ....*....|....*....|...
gi 527037697  109 nmRDIPGFLLLAGGLPVKEGDEV 131
Cdd:pfam03928  76 --GDAPEYAPFGGGVPIRVDGVV 96
 
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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