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Conserved domains on  [gi|2193613064|ref|WP_238460025|]
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1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase [Enterobacter mori]

Protein Classification

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase( domain architecture ID 10792056)

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase is an enzyme involved in the biosynthesis of histidine, specifically catalyzing the fourth step in the pathway, by converting a specific intermediate molecule through an isomerization reaction

CATH:  3.20.20.70
EC:  5.3.1.16
Gene Ontology:  GO:0003949|GO:0000162|GO:0000105
PubMed:  28416687|7687248|12634849
SCOP:  4003056

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK00748 PRK00748
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 1-238 9.26e-122

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated


:

Pssm-ID: 179108  Cd Length: 233  Bit Score: 345.51  E-value: 9.26e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064   1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLLKKLVAGVDVPVQVGG 80
Cdd:PRK00748    2 IIIPAIDLKDGKCVRLYQGDYDQATVYSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064  81 GVRTEDDVAALLDAGVARVVVGSTAVKDPDTVKGWFHRFGaDALVLALDVRideqgNKQVAVSGWQENSGVTLEELVDIY 160
Cdd:PRK00748   82 GIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFP-GKIVVGLDAR-----DGKVATDGWLETSGVTAEDLAKRF 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2193613064 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDIGDVAALRGTG-VQGVIVGRALLEGKFTVTEA 238
Cdd:PRK00748  156 EDAGVKAIIYTDISRDGTLSGPNVEATRELAAAVP-IPVIASGGVSSLDDIKALKGLGaVEGVIVGRALYEGKFDLAEA 233
 
Name Accession Description Interval E-value
PRK00748 PRK00748
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 1-238 9.26e-122

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated


Pssm-ID: 179108  Cd Length: 233  Bit Score: 345.51  E-value: 9.26e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064   1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLLKKLVAGVDVPVQVGG 80
Cdd:PRK00748    2 IIIPAIDLKDGKCVRLYQGDYDQATVYSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064  81 GVRTEDDVAALLDAGVARVVVGSTAVKDPDTVKGWFHRFGaDALVLALDVRideqgNKQVAVSGWQENSGVTLEELVDIY 160
Cdd:PRK00748   82 GIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFP-GKIVVGLDAR-----DGKVATDGWLETSGVTAEDLAKRF 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2193613064 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDIGDVAALRGTG-VQGVIVGRALLEGKFTVTEA 238
Cdd:PRK00748  156 EDAGVKAIIYTDISRDGTLSGPNVEATRELAAAVP-IPVIASGGVSSLDDIKALKGLGaVEGVIVGRALYEGKFDLAEA 233
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 1-243 5.57e-110

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino acid transport and metabolism]; Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439876  Cd Length: 236  Bit Score: 315.82  E-value: 5.57e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064   1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLLKKLVAGVDVPVQVGG 80
Cdd:COG0106     1 IIIPAIDLKDGKCVRLVQGDYDQETVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064  81 GVRTEDDVAALLDAGVARVVVGSTAVKDPDTVKGWFHRFGaDALVLALDVRideqgNKQVAVSGWQENSGVTLEELVDIY 160
Cdd:COG0106    81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFP-ERIVVGLDAR-----DGKVATDGWQETSGVDLEELAKRF 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDIGDVAALRGTGVQGVIVGRALLEGKFTVTEAIQ 240
Cdd:COG0106   155 EDAGVAAILYTDISRDGTLQGPNLELYRELAAATG-IPVIASGGVSSLDDLRALKELGVEGAIVGKALYEGKIDLEEALA 233


                  ...
gi 2193613064 241 CWQ 243
Cdd:COG0106   234 LAR 236
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 1-240 2.57e-108

HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene.


Pssm-ID: 240083  Cd Length: 234  Bit Score: 311.72  E-value: 2.57e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064   1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLLKKLVAGVDVPVQVGG 80
Cdd:cd04732     1 IIIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064  81 GVRTEDDVAALLDAGVARVVVGSTAVKDPDTVKGWFHRFGADALVLALDVRIDEqgnkqVAVSGWQENSGVTLEELVDIY 160
Cdd:cd04732    81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLDAKDGK-----VATKGWLETSEVSLEELAKRF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYpQVAFQSSGGIGDIGDVAALRGTGVQGVIVGRALLEGKFTVTEAIQ 240
Cdd:cd04732   156 EELGVKAIIYTDISRDGTLSGPNFELYKELAAAT-GIPVIASGGVSSLDDIKALKELGVAGVIVGKALYEGKITLEEALA 234
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 2-237 4.86e-100

phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family consists of HisA, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, the enzyme catalyzing the fourth step in histidine biosynthesis. It is closely related to the enzyme HisF for the sixth step. Examples of this enzyme in Actinobacteria have been found to be bifunctional, also possessing phosphoribosylanthranilate isomerase activity; the trusted cutoff here has now been raised to 275.0 to exclude the bifunctional group, now represented by model TIGR01919. HisA from Lactococcus lactis was reported to be inactive (MEDLINE:93322317). [Amino acid biosynthesis, Histidine family]


Pssm-ID: 272850 [Multi-domain]  Cd Length: 230  Bit Score: 290.64  E-value: 4.86e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064   2 IIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLLKKLVAGVDVPVQVGGG 81
Cdd:TIGR00007   1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064  82 VRTEDDVAALLDAGVARVVVGSTAVKDPDTVKGWFHRFGADALVLALDVRIDEqgnkqVAVSGWQENSGVTLEELVDIYL 161
Cdd:TIGR00007  81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSLDARGGE-----VAVKGWLEKSEVSLEELAKRLE 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2193613064 162 PVGLKHVLCTDISRDGTLAGSNVSLYEEVCARyPQVAFQSSGGIGDIGDVAALRGTGVQGVIVGRALLEGKFTVTE 237
Cdd:TIGR00007 156 ELGLEGIIYTDISRDGTLSGPNFELTKELVKA-VNVPVIASGGVSSIDDLIALKKLGVYGVIVGKALYEGKITLEE 230
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 1-234 2.58e-94

Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.


Pssm-ID: 425971  Cd Length: 228  Bit Score: 275.90  E-value: 2.58e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064   1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLLKKLVAGVDVPVQVGG 80
Cdd:pfam00977   1 RIIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064  81 GVRTEDDVAALLDAGVARVVVGSTAVKDPDTVKGWFHRFGADALVLALDVRideqgNKQVAVSGWQENSGVTLEELVDIY 160
Cdd:pfam00977  81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDAR-----RGKVAINGWREDTGIDAVEWAKEL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2193613064 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYpQVAFQSSGGIGDIGDVAALRGTGVQGVIVGRALLEGKFT 234
Cdd:pfam00977 156 EELGAGEILLTDIDRDGTLSGPDLELTRELAEAV-NIPVIASGGVGSLEDLKELFTEGVDGVIAGSALYEGEIT 228
 
Name Accession Description Interval E-value
PRK00748 PRK00748
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 1-238 9.26e-122

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Validated


Pssm-ID: 179108  Cd Length: 233  Bit Score: 345.51  E-value: 9.26e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064   1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLLKKLVAGVDVPVQVGG 80
Cdd:PRK00748    2 IIIPAIDLKDGKCVRLYQGDYDQATVYSDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064  81 GVRTEDDVAALLDAGVARVVVGSTAVKDPDTVKGWFHRFGaDALVLALDVRideqgNKQVAVSGWQENSGVTLEELVDIY 160
Cdd:PRK00748   82 GIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFP-GKIVVGLDAR-----DGKVATDGWLETSGVTAEDLAKRF 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2193613064 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDIGDVAALRGTG-VQGVIVGRALLEGKFTVTEA 238
Cdd:PRK00748  156 EDAGVKAIIYTDISRDGTLSGPNVEATRELAAAVP-IPVIASGGVSSLDDIKALKGLGaVEGVIVGRALYEGKFDLAEA 233
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 1-243 5.57e-110

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino acid transport and metabolism]; Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439876  Cd Length: 236  Bit Score: 315.82  E-value: 5.57e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064   1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLLKKLVAGVDVPVQVGG 80
Cdd:COG0106     1 IIIPAIDLKDGKCVRLVQGDYDQETVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064  81 GVRTEDDVAALLDAGVARVVVGSTAVKDPDTVKGWFHRFGaDALVLALDVRideqgNKQVAVSGWQENSGVTLEELVDIY 160
Cdd:COG0106    81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFP-ERIVVGLDAR-----DGKVATDGWQETSGVDLEELAKRF 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDIGDVAALRGTGVQGVIVGRALLEGKFTVTEAIQ 240
Cdd:COG0106   155 EDAGVAAILYTDISRDGTLQGPNLELYRELAAATG-IPVIASGGVSSLDDLRALKELGVEGAIVGKALYEGKIDLEEALA 233


                  ...
gi 2193613064 241 CWQ 243
Cdd:COG0106   234 LAR 236
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 1-240 2.57e-108

HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene.


Pssm-ID: 240083  Cd Length: 234  Bit Score: 311.72  E-value: 2.57e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064   1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLLKKLVAGVDVPVQVGG 80
Cdd:cd04732     1 IIIPAIDLKDGKCVRLYQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064  81 GVRTEDDVAALLDAGVARVVVGSTAVKDPDTVKGWFHRFGADALVLALDVRIDEqgnkqVAVSGWQENSGVTLEELVDIY 160
Cdd:cd04732    81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLDAKDGK-----VATKGWLETSEVSLEELAKRF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYpQVAFQSSGGIGDIGDVAALRGTGVQGVIVGRALLEGKFTVTEAIQ 240
Cdd:cd04732   156 EELGVKAIIYTDISRDGTLSGPNFELYKELAAAT-GIPVIASGGVSSLDDIKALKELGVAGVIVGKALYEGKITLEEALA 234
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 2-237 4.86e-100

phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family consists of HisA, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, the enzyme catalyzing the fourth step in histidine biosynthesis. It is closely related to the enzyme HisF for the sixth step. Examples of this enzyme in Actinobacteria have been found to be bifunctional, also possessing phosphoribosylanthranilate isomerase activity; the trusted cutoff here has now been raised to 275.0 to exclude the bifunctional group, now represented by model TIGR01919. HisA from Lactococcus lactis was reported to be inactive (MEDLINE:93322317). [Amino acid biosynthesis, Histidine family]


Pssm-ID: 272850 [Multi-domain]  Cd Length: 230  Bit Score: 290.64  E-value: 4.86e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064   2 IIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLLKKLVAGVDVPVQVGGG 81
Cdd:TIGR00007   1 IIPAIDIKDGKCVRLYQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064  82 VRTEDDVAALLDAGVARVVVGSTAVKDPDTVKGWFHRFGADALVLALDVRIDEqgnkqVAVSGWQENSGVTLEELVDIYL 161
Cdd:TIGR00007  81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSLDARGGE-----VAVKGWLEKSEVSLEELAKRLE 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2193613064 162 PVGLKHVLCTDISRDGTLAGSNVSLYEEVCARyPQVAFQSSGGIGDIGDVAALRGTGVQGVIVGRALLEGKFTVTE 237
Cdd:TIGR00007 156 ELGLEGIIYTDISRDGTLSGPNFELTKELVKA-VNVPVIASGGVSSIDDLIALKKLGVYGVIVGKALYEGKITLEE 230
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 1-234 2.58e-94

Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.


Pssm-ID: 425971  Cd Length: 228  Bit Score: 275.90  E-value: 2.58e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064   1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLLKKLVAGVDVPVQVGG 80
Cdd:pfam00977   1 RIIPAIDLKDGRVVRLVKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064  81 GVRTEDDVAALLDAGVARVVVGSTAVKDPDTVKGWFHRFGADALVLALDVRideqgNKQVAVSGWQENSGVTLEELVDIY 160
Cdd:pfam00977  81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDAR-----RGKVAINGWREDTGIDAVEWAKEL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2193613064 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYpQVAFQSSGGIGDIGDVAALRGTGVQGVIVGRALLEGKFT 234
Cdd:pfam00977 156 EELGAGEILLTDIDRDGTLSGPDLELTRELAEAV-NIPVIASGGVGSLEDLKELFTEGVDGVIAGSALYEGEIT 228
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 2-239 8.89e-56

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;


Pssm-ID: 184165  Cd Length: 241  Bit Score: 178.56  E-value: 8.89e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064   2 IIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLLKKLVAGVDVPVQVGGG 81
Cdd:PRK13585    5 VIPAVDMKGGKCVQLVQGEPGTETVSYGDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEKIIEAVGVPVQLGGG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064  82 VRTEDDVAALLDAGVARVVVGSTAVKDPDTVKGWFHRFGADALVLALDVRideqgNKQVAVSGWQENSGVTLEELVDIYL 161
Cdd:PRK13585   85 IRSAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEFGSERVMVSLDAK-----DGEVVIKGWTEKTGYTPVEAAKRFE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064 162 PVGLKHVLCTDISRDGTLAGSNVSLYEEVCARY--PQVAfqsSGGIGDIGDVAALRGTGVQGVIVGRALLEGKFTVTEAI 239
Cdd:PRK13585  160 ELGAGSILFTNVDVEGLLEGVNTEPVKELVDSVdiPVIA---SGGVTTLDDLRALKEAGAAGVVVGSALYKGKFTLEEAI 236
PRK14024 PRK14024
phosphoribosyl isomerase A; Provisional
 2-239 1.34e-41

phosphoribosyl isomerase A; Provisional


Pssm-ID: 237589  Cd Length: 241  Bit Score: 142.02  E-value: 1.34e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064   2 IIPALDLIDGTVVRLHQGDYGQQRDYGnDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQiPLLKKLVAGVDVPVQVGGG 81
Cdd:PRK14024    6 LLPAVDVVDGQAVRLVQGEAGSETSYG-SPLDAALAWQRDGAEWIHLVDLDAAFGRGSNR-ELLAEVVGKLDVKVELSGG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064  82 VRTEDDVAALLDAGVARVVVGSTAVKDPDTVKGWFHRFGaDALVLALDVRideqgNKQVAVSGWQENSG---VTLEELVD 158
Cdd:PRK14024   84 IRDDESLEAALATGCARVNIGTAALENPEWCARVIAEHG-DRVAVGLDVR-----GHTLAARGWTRDGGdlwEVLERLDS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064 159 iylpVGLKHVLCTDISRDGTLAGSNVSLYEEVCARY--PQVAfqsSGGIGDIGDVAALRG---TGVQGVIVGRALLEGKF 233
Cdd:PRK14024  158 ----AGCSRYVVTDVTKDGTLTGPNLELLREVCARTdaPVVA---SGGVSSLDDLRALAElvpLGVEGAIVGKALYAGAF 230


                  ....*.
gi 2193613064 234 TVTEAI 239
Cdd:PRK14024  231 TLPEAL 236
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 1-240 3.81e-32

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) and the cyclase subunit of imidazoleglycerol phosphate synthase (HisF). The ProFAR isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene. The Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.


Pssm-ID: 240074 [Multi-domain]  Cd Length: 233  Bit Score: 117.37  E-value: 3.81e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064   1 MIIPALDLIDGTVVRLHQGDYGQQRD------YGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAkRQIPLLKKLVAGVDV 74
Cdd:cd04723     1 RIIPVIDLKDGVVVHGVGGDRDNYRPitsnlcSTSDPLDVARAYKELGFRGLYIADLDAIMGRG-DNDEAIRELAAAWPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064  75 PVQVGGGVRTEDDVAALLDAGVARVVVGSTAVKDPDTVKGwFHRFGADALVLALDVRideqgNKQVAVSGWqensGVTLE 154
Cdd:cd04723    80 GLWVDGGIRSLENAQEWLKRGASRVIVGTETLPSDDDEDR-LAALGEQRLVLSLDFR-----GGQLLKPTD----FIGPE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064 155 ELVDiYLPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIGDIGDVAALRGTGVQGVIVGRALLEGKFT 234
Cdd:cd04723   150 ELLR-RLAKWPEELIVLDIDRVGSGQGPDLELLERLAARAD-IPVIAAGGVRSVEDLELLKKLGASGALVASALHDGGLT 227


                  ....*.
gi 2193613064 235 VTEAIQ 240
Cdd:cd04723   228 LEDVVR 233
PRK13587 PRK13587
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 4-227 5.31e-31

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; Provisional


Pssm-ID: 172156  Cd Length: 234  Bit Score: 114.54  E-value: 5.31e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064   4 PALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQDYAA-QGAEVLHLVDLTGAKDPAKRQIPLLKKLVAGVDVPVQVGGGV 82
Cdd:PRK13587    6 PAIDLIGSTSVRLTEGKYDSEEKMSRSAEESIAYYSQfECVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIEVGGGI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064  83 RTEDDVAALLDAGVARVVVGSTAVKDPDTVKGWFHRFgADALVLALDVRIDeqgnkQVAVSGWQENSGVTLEELVDIYLP 162
Cdd:PRK13587   86 RTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTF-PGRIYLSVDAYGE-----DIKVNGWEEDTELNLFSFVRQLSD 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2193613064 163 VGLKHVLCTDISRDGTLAGSNVSLYEEVcARYPQVAFQSSGGIGDIGDVAALRGTGVQGVIVGRA 227
Cdd:PRK13587  160 IPLGGIIYTDIAKDGKMSGPNFELTGQL-VKATTIPVIASGGIRHQQDIQRLASLNVHAAIIGKA 223
PRK04128 PRK04128
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 2-238 8.95e-31

1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;


Pssm-ID: 167709  Cd Length: 228  Bit Score: 113.71  E-value: 8.95e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064   2 IIPALDLIDGTVVRLHQGDYGQQRDYGnDPLP---RLQDYAaqgaEVLHLVDLTGAKDPAKRQIPLLKKLVAGVDVPVQV 78
Cdd:PRK04128    4 IYPAIDLMNGKAVRLYKGRKEEVKVYG-DPVEialRFSEYV----DKIHVVDLDGAFEGKPKNLDVVKNIIRETGLKVQV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064  79 GGGVRTEDDVAALLDAGVARVVVGSTAVkDPDTVKGWFHRFgaDALVLALDVRideqgNKQVAVSGWQENSGVTLEELVD 158
Cdd:PRK04128   79 GGGLRTYESIKDAYEIGVENVIIGTKAF-DLEFLEKVTSEF--EGITVSLDVK-----GGRIAVKGWLEESSIKVEDAYE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064 159 IyLPVGLKHVLCTDISRDGTLAGsnvslYEEVCARYPQVAFQSSGGIGDIGDVAALRGTGVQGVIVGRALLEGKFTVTEA 238
Cdd:PRK04128  151 M-LKNYVNRFIYTSIERDGTLTG-----IEEIERFWGDEEFIYAGGVSSAEDVKKLAEIGFSGVIIGKALYEGRISLEEL 224
PRK14114 PRK14114
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 1-235 2.86e-29

1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;


Pssm-ID: 172604  Cd Length: 241  Bit Score: 110.10  E-value: 2.86e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064   1 MIIPALDLIDGTVVRLHQGDYGQQRDYGNDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLLKKLVAGVDvPVQVGG 80
Cdd:PRK14114    2 LVVPAIDLFRGKVARMVKGKKENTIFYEKDPAELVEKLIEEGFTLIHVVDLSKAIENSVENLPVLEKLSEFAE-HIQIGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064  81 GVRTEDDVAALLDAGVARVVVGSTAVKDPDTVKgWFHRFGADAlVLALDVRideqgNKQVAVSGWQENSGVTLEELVDIY 160
Cdd:PRK14114   81 GIRSLDYAEKLRKLGYRRQIVSSKVLEDPSFLK-FLKEIDVEP-VFSLDTR-----GGKVAFKGWLAEEEIDPVSLLKRL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064 161 LPVGLKHVLCTDISRDGTLAGSNVSLYEEVcARYPQVAFQSSGGIGDIGDVAAL-----RGTG-VQGVIVGRALLEGKFT 234
Cdd:PRK14114  154 KEYGLEEIVHTEIEKDGTLQEHDFSLTRKI-AIEAEVKVFAAGGISSENSLKTAqrvhrETNGlLKGVIVGRAFLEGILT 232


                  .
gi 2193613064 235 V 235
Cdd:PRK14114  233 V 233
HisF cd04731
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ...
 2-240 8.53e-29

The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.


Pssm-ID: 240082  Cd Length: 243  Bit Score: 108.71  E-value: 8.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064   2 IIPALDLIDGTVVRLHQgdYGQQRDYGnDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLLKKLVAGVDVPVQVGGG 81
Cdd:cd04731     3 IIPCLDVKDGRVVKGVN--FKNLRDAG-DPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064  82 VRTEDDVAALLDAGVARVVVGSTAVKDPDTVKGWFHRFGADALVLALDVRIDEQGNKQVAVSGWQENSGVTLEELVDIYL 161
Cdd:cd04731    80 IRSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAKRRGDGGYEVYTHGGRKPTGLDAVEWAKEVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064 162 PVGLKHVLCTDISRDGTLAGSNVSLYEEVCAR--YPQVAfqsSGGIGDIGD-VAALRGTGVQGVIVGRALLEGKFTVTEA 238
Cdd:cd04731   160 ELGAGEILLTSMDRDGTKKGYDLELIRAVSSAvnIPVIA---SGGAGKPEHfVEAFEEGGADAALAASIFHFGEYTIAEL 236


                  ..
gi 2193613064 239 IQ 240
Cdd:cd04731   237 KE 238
hisF TIGR00735
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ...
 2-206 5.09e-26

imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273241  Cd Length: 254  Bit Score: 101.67  E-value: 5.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064   2 IIPALDLIDGTVVRLHQgdYGQQRDYGnDPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLLKKLVAGVDVPVQVGGG 81
Cdd:TIGR00735   6 IIPCLDVRDGRVVKGVQ--FLNLRDAG-DPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVGGG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064  82 VRTEDDVAALLDAGVARVVVGSTAVKDPDTVKGWFHRFGADALVLALDVR---IDEQGNKQVAVSGWQENSGVTLEELVD 158
Cdd:TIGR00735  83 IKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKrvyVNSYCWYEVYIYGGRESTGLDAVEWAK 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2193613064 159 IYLPVGLKHVLCTDISRDGTLAGSNVSLYEEVCARYPqVAFQSSGGIG 206
Cdd:TIGR00735 163 EVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVK-IPVIASGGAG 209
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 2-222 1.11e-24

Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; Imidazole glycerol phosphate synthase subunit HisF is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439877  Cd Length: 251  Bit Score: 98.17  E-value: 1.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064   2 IIPALDLIDGTVVRlhqgdyGQQ----RDYGnDPLPRLQDYAAQGAEVLHLVDLTGAKDpaKRQIPL--LKKLVAGVDVP 75
Cdd:COG0107     5 IIPCLDVKDGRVVK------GVNfvnlRDAG-DPVELAKRYNEQGADELVFLDITASSE--GRKTMLdvVRRVAEEVFIP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064  76 VQVGGGVRTEDDVAALLDAGVARVVVGSTAVKDPDTVKGWFHRFGADALVLALDVRIDEQGNKQVAVSGWQENSGVTLEE 155
Cdd:COG0107    76 LTVGGGIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRVPDGGWEVYTHGGRKPTGLDAVE 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2193613064 156 LVdiylpvglKHV--------LCTDISRDGTLAGSNVSLYEEVCA--RYPQVAfqsSGGIGDIGD-VAALRGTGVQGV 222
Cdd:COG0107   156 WA--------KEAeelgageiLLTSMDRDGTKDGYDLELTRAVSEavSIPVIA---SGGAGTLEHfVEVFTEGGADAA 222
PRK13586 PRK13586
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 2-232 8.29e-17

1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase;


Pssm-ID: 237439  Cd Length: 232  Bit Score: 76.70  E-value: 8.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064   2 IIPALDLIDGTVVRLHQGDYGQQRDYGNdPLPRLQDYAAQGAEVLHLVDLTGAKDPAKRQIPLLKKLVAGVDVpVQVGGG 81
Cdd:PRK13586    4 IIPSIDISLGKAVKRIRGVKGTGLILGN-PIEIASKLYNEGYTRIHVVDLDAAEGVGNNEMYIKEISKIGFDW-IQVGGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064  82 VRTEDDVAALLDAGVARVVVGSTAVKDPDTVKGWFHRFGADALVLAldvrIDEQGNKQVAVSGWQENSgVTLEELVDIYL 161
Cdd:PRK13586   82 IRDIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGSNRVLVS----IDYDNTKRVLIRGWKEKS-MEVIDGIKKVN 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2193613064 162 PVGLKHVLCTDISRDGTLAG--SNVSLYeevcARYPQVAFQSSGGIGDIGDVAALRGTGVQGVIVGRALLEGK 232
Cdd:PRK13586  157 ELELLGIIFTYISNEGTTKGidYNVKDY----ARLIRGLKEYAGGVSSDADLEYLKNVGFDYIIVGMAFYLGK 225
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
64-116 1.63e-05

putative N-acetylmannosamine-6-phosphate 2-epimerase;


Pssm-ID: 234907  Cd Length: 221  Bit Score: 44.37  E-value: 1.63e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2193613064  64 LLKKLVAGVDVPVQVGGGVRTEDDVAALLDAGVARVVVGsTAVKDPDTVKGWF 116
Cdd:PRK01130  164 LLKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVG-GAITRPEEITKWF 215
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 64-116 6.95e-05

N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.


Pssm-ID: 240080 [Multi-domain]  Cd Length: 219  Bit Score: 42.56  E-value: 6.95e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2193613064  64 LLKKLVAGVDVPVQVGGGVRTEDDVAALLDAGVARVVVGsTAVKDPDTVKGWF 116
Cdd:cd04729   168 LLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVG-SAITRPEHITGWF 219
PEP_mutase pfam13714
Phosphoenolpyruvate phosphomutase; This domain includes the enzyme Phosphoenolpyruvate ...
 34-103 1.86e-03

Phosphoenolpyruvate phosphomutase; This domain includes the enzyme Phosphoenolpyruvate phosphomutase (EC:5.4.2.9). This protein Swiss:O86937 has been characterized as catalysing the formation of a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr). This enzyme has a TIM barrel fold.


Pssm-ID: 433424  Cd Length: 241  Bit Score: 38.34  E-value: 1.86e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064  34 RLQDYAAQGAEVLHLvdlTGAKDPakrqiPLLKKLVAGVDVPVQVGGGVRTeDDVAALLDAGVARVVVGS 103
Cdd:pfam13714 163 RARAYAEAGADGIFV---PGLLDP-----ADIAALVAAVPGPVNVLAGPGT-LSVAELAALGVARISYGN 223
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 37-103 2.77e-03

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 37.95  E-value: 2.77e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064  37 DYAAQGAEVLHLVD---LTGAKDPAKRQIPLLKKLVAGVDVPVQVGGGVRTEDDVAALLDAGVARVVVGS 103
Cdd:cd04722   131 AAEEAGVDEVGLGNgggGGGGRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
PRK04302 PRK04302
triosephosphate isomerase; Provisional
 73-110 3.07e-03

triosephosphate isomerase; Provisional


Pssm-ID: 235274  Cd Length: 223  Bit Score: 37.92  E-value: 3.07e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2193613064  73 DVPVQVGGGVRTEDDVAALLDAGVARVVVGSTAVKDPD 110
Cdd:PRK04302  173 DVKVLCGAGISTGEDVKAALELGADGVLLASGVVKAKD 210
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 39-110 4.22e-03

3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate synthase (HPS). KGPDC catalyzes the formation of L-xylulose 5-phosphate and carbon dioxide from 3-keto-L-gulonate 6-phosphate as part of the anaerobic pathway for L-ascorbate utilization in some eubacteria. HPS catalyzes the formation of D-arabino-3-hexulose-6-phosphate from D-ribulose 5-phosphate and formaldehyde in microorganisms that can use formaldehyde as a carbon source. Both catalyze reactions that involve the Mg2+-assisted formation and stabilization of 1,2-enediolate reaction intermediates.


Pssm-ID: 240077 [Multi-domain]  Cd Length: 202  Bit Score: 37.17  E-value: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064  39 AAQGAEVLHLVDLTGAKDPAKRQ--------------------------IPLLKKLVAGVDVPVQVGGGVrTEDDVAALL 92
Cdd:cd04726    98 AAKKYGKEVQVDLIGVEDPEKRAkllklgvdivilhrgidaqaaggwwpEDDLKKVKKLLGVKVAVAGGI-TPDTLPEFK 176

                          90
                  ....*....|....*...
gi 2193613064  93 DAGVARVVVGSTAVKDPD 110
Cdd:cd04726   177 KAGADIVIVGRAITGAAD 194
OYE_like_4_FMN cd04735
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ...
 55-112 5.92e-03

Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Other members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 240086 [Multi-domain]  Cd Length: 353  Bit Score: 37.19  E-value: 5.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2193613064  55 KDPAKRQIPLLKKLVAGvDVPVQVGGGVRTEDDVAALLDAGVARVVVGSTAVKDPDTV 112
Cdd:cd04735   267 RDDNQTIMELVKERIAG-RLPLIAVGSINTPDDALEALETGADLVAIGRGLLVDPDWV 323
PcrB COG1646
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];
73-113 6.12e-03

Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];


Pssm-ID: 441252  Cd Length: 241  Bit Score: 37.06  E-value: 6.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2193613064  73 DVPVQVGGGVRTEDDVAALLDAGVARVVVGsTAV-KDPDTVK 113
Cdd:COG1646   196 DTPLIYGGGIRSPEKAREMAEAGADTIVVG-NAIeEDPDLAL 236
PLN02446 PLN02446
(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 77-155 7.59e-03

(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase


Pssm-ID: 215245  Cd Length: 262  Bit Score: 36.61  E-value: 7.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064  77 QVGGGVrTEDDVAALLDAGVARVVVGSTAVK----DPDTVKGWFHRFGADALVLALDVRiDEQGNKQVAVSGWQENSGVT 152
Cdd:PLN02446   87 QVGGGV-NSENAMSYLDAGASHVIVTSYVFRdgqiDLERLKDLVRLVGKQRLVLDLSCR-KKDGRYYVVTDRWQKFSDLA 164


                  ...
gi 2193613064 153 LEE 155
Cdd:PLN02446  165 VDE 167
OYE_like_FMN_family cd02803
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
 39-115 7.88e-03

Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 239201 [Multi-domain]  Cd Length: 327  Bit Score: 36.78  E-value: 7.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2193613064  39 AAQGAEVLHL---------VDLTGAKDPAKRQIPLLKKLVAGVDVPVQVGGGVRTEDDVAALLDAGVAR-VVVGSTAVKD 108
Cdd:cd02803   238 EEAGVDALHVsggsyesppPIIPPPYVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILAEGKADlVALGRALLAD 317


                  ....*..
gi 2193613064 109 PDTVKGW 115
Cdd:cd02803   318 PDLPNKA 324
 
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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