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Conserved domains on  [gi|488164351|ref|WP_002235559|]
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imidazole glycerol phosphate synthase subunit HisF [Neisseria meningitidis]

Protein Classification

imidazole glycerol phosphate synthase subunit HisF( domain architecture ID 10785016)

imidazole glycerol phosphate synthase cyclase subunit HisF catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring

EC:  4.3.2.10
Gene Symbol:  hisF
Gene Ontology:  GO:0000107|GO:0000105
PubMed:  12795596|12859215|9742729
SCOP:  4003056

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 3-255 5.89e-172

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: 473.74  E-value: 5.89e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   3 LAKRIIPCLDVKDGRVVKGVNFIGLRDAGDPVEAAKRYNGEGADELTFLDITASSDNRDTILHIIEEVAGQVFIPLTVGG 82
Cdd:COG0107    1 LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351  83 GVRTVADIRRLLNAGADKVSINTAAVTRPDLIDEAAGFFGSQAIVAAVDAKAVNPEntRWEIFTHGGRNPTGLDAVEWAI 162
Cdd:COG0107   81 GIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRVPDG--GWEVYTHGGRKPTGLDAVEWAK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351 163 EMQKRGAGEILLTGMDRDGTKQGFNLPLTRAVAEAVDIPVIASGGVGNVRHLIEGITEGKADAVLAAGVFHFGEIAIREA 242
Cdd:COG0107  159 EAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITIAEL 238

                        250
                 ....*....|...
gi 488164351 243 KRAMREAGIEVRL 255
Cdd:COG0107  239 KAYLAEAGIPVRL 251
 
Name Accession Description Interval E-value
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 3-255 5.89e-172

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: 473.74  E-value: 5.89e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   3 LAKRIIPCLDVKDGRVVKGVNFIGLRDAGDPVEAAKRYNGEGADELTFLDITASSDNRDTILHIIEEVAGQVFIPLTVGG 82
Cdd:COG0107    1 LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351  83 GVRTVADIRRLLNAGADKVSINTAAVTRPDLIDEAAGFFGSQAIVAAVDAKAVNPEntRWEIFTHGGRNPTGLDAVEWAI 162
Cdd:COG0107   81 GIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRVPDG--GWEVYTHGGRKPTGLDAVEWAK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351 163 EMQKRGAGEILLTGMDRDGTKQGFNLPLTRAVAEAVDIPVIASGGVGNVRHLIEGITEGKADAVLAAGVFHFGEIAIREA 242
Cdd:COG0107  159 EAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITIAEL 238

                        250
                 ....*....|...
gi 488164351 243 KRAMREAGIEVRL 255
Cdd:COG0107  239 KAYLAEAGIPVRL 251
HisF cd04731
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ...
 5-249 4.01e-144

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: 403.00  E-value: 4.01e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   5 KRIIPCLDVKDGRVVKGVNFIGLRDAGDPVEAAKRYNGEGADELTFLDITASSDNRDTILHIIEEVAGQVFIPLTVGGGV 84
Cdd:cd04731    1 KRIIPCLDVKDGRVVKGVNFKNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351  85 RTVADIRRLLNAGADKVSINTAAVTRPDLIDEAAGFFGSQAIVAAVDAKAVNpeNTRWEIFTHGGRNPTGLDAVEWAIEM 164
Cdd:cd04731   81 RSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAKRRG--DGGYEVYTHGGRKPTGLDAVEWAKEV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351 165 QKRGAGEILLTGMDRDGTKQGFNLPLTRAVAEAVDIPVIASGGVGNVRHLIEGITEGKADAVLAAGVFHFGEIAIREAKR 244
Cdd:cd04731  159 EELGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEAFEEGGADAALAASIFHFGEYTIAELKE 238


                 ....*
gi 488164351 245 AMREA 249
Cdd:cd04731  239 YLAER 243
hisF TIGR00735
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ...
 3-254 9.25e-134

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


Pssm-ID: 273241  Cd Length: 254  Bit Score: 377.48  E-value: 9.25e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351    3 LAKRIIPCLDVKDGRVVKGVNFIGLRDAGDPVEAAKRYNGEGADELTFLDITASSDNRDTILHIIEEVAGQVFIPLTVGG 82
Cdd:TIGR00735   2 LAKRIIPCLDVRDGRVVKGVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   83 GVRTVADIRRLLNAGADKVSINTAAVTRPDLIDEAAGFFGSQAIVAAVDAKAV-NPENTRWEIFTHGGRNPTGLDAVEWA 161
Cdd:TIGR00735  82 GIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRVyVNSYCWYEVYIYGGRESTGLDAVEWA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351  162 IEMQKRGAGEILLTGMDRDGTKQGFNLPLTRAVAEAVDIPVIASGGVGNVRHLIEGITEGKADAVLAAGVFHFGEIAIRE 241
Cdd:TIGR00735 162 KEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPEHFYEAFTKGKADAALAASVFHYREITIGE 241

                         250
                  ....*....|...
gi 488164351  242 AKRAMREAGIEVR 254
Cdd:TIGR00735 242 VKEYLAERGIPVR 254
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 6-237 3.05e-109

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: 314.42  E-value: 3.05e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351    6 RIIPCLDVKDGRVV---KGVNFIGLRDAGDPVEAAKRYNGEGADELTFLDITASSDNRDTILHIIEEVAGQVFIPLTVGG 82
Cdd:pfam00977   1 RIIPAIDLKDGRVVrlvKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   83 GVRTVADIRRLLNAGADKVSINTAAVTRPDLIDEAAGFFGSQAIVAAVDAKavnpentRWEIFTHGGRNPTGLDAVEWAI 162
Cdd:pfam00977  81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDAR-------RGKVAINGWREDTGIDAVEWAK 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488164351  163 EMQKRGAGEILLTGMDRDGTKQGFNLPLTRAVAEAVDIPVIASGGVGNVRHLIEGITEGKaDAVLAAGVFHFGEI 237
Cdd:pfam00977 154 ELEELGAGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTEGV-DGVIAGSALYEGEI 227
AglZ_HisF2_fam NF038364
AglZ/HisF2 family acetamidino modification protein;
3-233 7.92e-88

AglZ/HisF2 family acetamidino modification protein;


Pssm-ID: 439657  Cd Length: 248  Bit Score: 260.87  E-value: 7.92e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   3 LAKRIIPCLDVKDGRVVKGVNFIGLRDAGDPVEAAKRYNGEGADELTFLDITASSDNRDTILHIIEEVAGQVFIPLTVGG 82
Cdd:NF038364   1 LRPRIIPCLLLHNGGLVKTVKFKDPKYVGDPINAVRIFNEKEVDELIVLDIDATKEGREPDYELIEDLASECFMPLCYGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351  83 GVRTVADIRRLLNAGADKVSINTAAVTRPDLIDEAAGFFGSQAIVAAVDAKavNPENTRWEIFTHGGRNPTGLDAVEWAI 162
Cdd:NF038364  81 GIKTLEQARRIFSLGVEKVALNSAALENPELITEAAEEFGSQSVVVSIDVK--KNLFGGYEVYTHNGTKKTKLDPVEFAK 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488164351 163 EMQKRGAGEILLTGMDRDGTKQGFNLPLTRAVAEAVDIPVIASGGVGNVRHLIEGITEGKADAVlAAG---VFH 233
Cdd:NF038364 159 ELEALGAGEIVLNSIDRDGTMKGYDLELIKKVSSAVSIPVIALGGAGSLEDLKEAIKQAGASAV-AAGslfVFK 231
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 2-255 9.01e-57

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 189.54  E-value: 9.01e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   2 ALAKRIIPCLDVK-----DGRVVKGVNF--------IGLRDAGDPVEAAKRYNGEGADELTFLDITASSDN--RDT-ILH 65
Cdd:PLN02617 225 SLAKRVIACLDVRsndkgDLVVTKGDQYdvrehsegREVRNLGKPVELAGQYYKDGADEVAFLNITGFRDFplGDLpMLE 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351  66 IIEEVAGQVFIPLTVGGGVRTVAD-----------IRRLLNAGADKVSINTAAV------------TRPDLIDEAAGFFG 122
Cdd:PLN02617 305 VLRRASENVFVPLTVGGGIRDFTDangryysslevASEYFRSGADKISIGSDAVyaaeeyiasgvkTGKTSIEQISRVYG 384

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351 123 SQAIVAAVDAKAV---NPENTR------------------WEIFTHGGRNPTGLDAVEWAIEMQKRGAGEILLTGMDRDG 181
Cdd:PLN02617 385 NQAVVVSIDPRRVyvkDPSDVPfktvkvtnpgpngeeyawYQCTVKGGREGRPIGAYELAKAVEELGAGEILLNCIDCDG 464

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488164351 182 TKQGFNLPLTRAVAEAVDIPVIASGGVGNVRHLIEGITEGKADAVLAAGVFHFGEIAIREAKRAMREAGIEVRL 255
Cdd:PLN02617 465 QGKGFDIELVKLVSDAVTIPVIASSGAGTPEHFSDVFSKTNASAALAAGIFHRKEVPISSVKEHLLEEGIETRI 538
 
Name Accession Description Interval E-value
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 3-255 5.89e-172

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: 473.74  E-value: 5.89e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   3 LAKRIIPCLDVKDGRVVKGVNFIGLRDAGDPVEAAKRYNGEGADELTFLDITASSDNRDTILHIIEEVAGQVFIPLTVGG 82
Cdd:COG0107    1 LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351  83 GVRTVADIRRLLNAGADKVSINTAAVTRPDLIDEAAGFFGSQAIVAAVDAKAVNPEntRWEIFTHGGRNPTGLDAVEWAI 162
Cdd:COG0107   81 GIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRVPDG--GWEVYTHGGRKPTGLDAVEWAK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351 163 EMQKRGAGEILLTGMDRDGTKQGFNLPLTRAVAEAVDIPVIASGGVGNVRHLIEGITEGKADAVLAAGVFHFGEIAIREA 242
Cdd:COG0107  159 EAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITIAEL 238

                        250
                 ....*....|...
gi 488164351 243 KRAMREAGIEVRL 255
Cdd:COG0107  239 KAYLAEAGIPVRL 251
HisF cd04731
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ...
 5-249 4.01e-144

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: 403.00  E-value: 4.01e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   5 KRIIPCLDVKDGRVVKGVNFIGLRDAGDPVEAAKRYNGEGADELTFLDITASSDNRDTILHIIEEVAGQVFIPLTVGGGV 84
Cdd:cd04731    1 KRIIPCLDVKDGRVVKGVNFKNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351  85 RTVADIRRLLNAGADKVSINTAAVTRPDLIDEAAGFFGSQAIVAAVDAKAVNpeNTRWEIFTHGGRNPTGLDAVEWAIEM 164
Cdd:cd04731   81 RSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAKRRG--DGGYEVYTHGGRKPTGLDAVEWAKEV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351 165 QKRGAGEILLTGMDRDGTKQGFNLPLTRAVAEAVDIPVIASGGVGNVRHLIEGITEGKADAVLAAGVFHFGEIAIREAKR 244
Cdd:cd04731  159 EELGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEAFEEGGADAALAASIFHFGEYTIAELKE 238


                 ....*
gi 488164351 245 AMREA 249
Cdd:cd04731  239 YLAER 243
hisF TIGR00735
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ...
 3-254 9.25e-134

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


Pssm-ID: 273241  Cd Length: 254  Bit Score: 377.48  E-value: 9.25e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351    3 LAKRIIPCLDVKDGRVVKGVNFIGLRDAGDPVEAAKRYNGEGADELTFLDITASSDNRDTILHIIEEVAGQVFIPLTVGG 82
Cdd:TIGR00735   2 LAKRIIPCLDVRDGRVVKGVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   83 GVRTVADIRRLLNAGADKVSINTAAVTRPDLIDEAAGFFGSQAIVAAVDAKAV-NPENTRWEIFTHGGRNPTGLDAVEWA 161
Cdd:TIGR00735  82 GIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRVyVNSYCWYEVYIYGGRESTGLDAVEWA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351  162 IEMQKRGAGEILLTGMDRDGTKQGFNLPLTRAVAEAVDIPVIASGGVGNVRHLIEGITEGKADAVLAAGVFHFGEIAIRE 241
Cdd:TIGR00735 162 KEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPEHFYEAFTKGKADAALAASVFHYREITIGE 241

                         250
                  ....*....|...
gi 488164351  242 AKRAMREAGIEVR 254
Cdd:TIGR00735 242 VKEYLAERGIPVR 254
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 6-237 3.05e-109

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: 314.42  E-value: 3.05e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351    6 RIIPCLDVKDGRVV---KGVNFIGLRDAGDPVEAAKRYNGEGADELTFLDITASSDNRDTILHIIEEVAGQVFIPLTVGG 82
Cdd:pfam00977   1 RIIPAIDLKDGRVVrlvKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   83 GVRTVADIRRLLNAGADKVSINTAAVTRPDLIDEAAGFFGSQAIVAAVDAKavnpentRWEIFTHGGRNPTGLDAVEWAI 162
Cdd:pfam00977  81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDAR-------RGKVAINGWREDTGIDAVEWAK 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488164351  163 EMQKRGAGEILLTGMDRDGTKQGFNLPLTRAVAEAVDIPVIASGGVGNVRHLIEGITEGKaDAVLAAGVFHFGEI 237
Cdd:pfam00977 154 ELEELGAGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTEGV-DGVIAGSALYEGEI 227
WbuZ TIGR03572
glycosyl amidation-associated protein WbuZ; This clade of sequences is highly similar to the ...
 3-234 1.43e-102

glycosyl amidation-associated protein WbuZ; This clade of sequences is highly similar to the HisF protein, but generally represents the second HisF homolog in the genome where the other is an authentic HisF observed in the context of a complete histidine biosynthesis operon. The similarity between these WbuZ sequences and true HisFs is such that often the closest match by BLAST of a WbuZ is a HisF. Only by making a multiple sequence alignment is the homology relationship among the WbuZ sequences made apparent. WbuZ genes are invariably observed in the presence of a homolog of the HisH protein (designated WbuY) and a proposed N-acetyl sugar amidotransferase designated in WbuX in E. coli, IfnA in P. aeriginosa and PseA in C. jejuni. Similarly, this trio of genes is invariably found in the context of saccharide biosynthesis loci. It has been shown that the WbuYZ homologs are not essential components of the activity expressed by WbuX, leading to the proposal that these to proteins provide ammonium ions to the amidotransferase when these are in low concentration. WbuY (like HisH) is proposed to act as a glutaminase to release ammonium. In histidine biosynthesis this is also dispensible in the presence of exogenous ammonium ion. HisH and HisF form a complex such that the ammonium ion is passed directly to HisF where it is used in an amidation reaction causing a subsequent cleavage and cyclization. In the case of WbuYZ, the ammonium ion would be passed from WbuY to WbuZ. WbuZ, being non-essential and so similar to HisF that a sugar substrate is unlikely, would function instead as a amoonium channel to the WbuX protein which does the enzymatic work.


Pssm-ID: 132611 [Multi-domain]  Cd Length: 232  Bit Score: 297.64  E-value: 1.43e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351    3 LAKRIIPCLDVKDGRVVKGVNFIGLRDAGDPVEAAKRYNGEGADELTFLDITASSDNRDTILHIIEEVAGQVFIPLTVGG 82
Cdd:TIGR03572   2 LKKRIIPCLLLKDGRLVKTVQFKDPRYIGDPVNAARIYNAKGADELIVLDIDASKRGREPLFELISNLAEECFMPLTVGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   83 GVRTVADIRRLLNAGADKVSINTAAVTRPDLIDEAAGFFGSQAIVAAVDAKAvNPENTRWEIFTHGGRNPTGLDAVEWAI 162
Cdd:TIGR03572  82 GIRSLEDAKKLLSLGADKVSINTAALENPDLIEEAARRFGSQCVVVSIDVKK-ELDGSDYKVYSDNGRRATGRDPVEWAR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488164351  163 EMQKRGAGEILLTGMDRDGTKQGFNLPLTRAVAEAVDIPVIASGGVGNVRHLIEGITEGKADAVLAAGVFHF 234
Cdd:TIGR03572 161 EAEQLGAGEILLNSIDRDGTMKGYDLELIKTVSDAVSIPVIALGGAGSLDDLVEVALEAGASAVAAASLFHF 232
AglZ_HisF2_fam NF038364
AglZ/HisF2 family acetamidino modification protein;
3-233 7.92e-88

AglZ/HisF2 family acetamidino modification protein;


Pssm-ID: 439657  Cd Length: 248  Bit Score: 260.87  E-value: 7.92e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   3 LAKRIIPCLDVKDGRVVKGVNFIGLRDAGDPVEAAKRYNGEGADELTFLDITASSDNRDTILHIIEEVAGQVFIPLTVGG 82
Cdd:NF038364   1 LRPRIIPCLLLHNGGLVKTVKFKDPKYVGDPINAVRIFNEKEVDELIVLDIDATKEGREPDYELIEDLASECFMPLCYGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351  83 GVRTVADIRRLLNAGADKVSINTAAVTRPDLIDEAAGFFGSQAIVAAVDAKavNPENTRWEIFTHGGRNPTGLDAVEWAI 162
Cdd:NF038364  81 GIKTLEQARRIFSLGVEKVALNSAALENPELITEAAEEFGSQSVVVSIDVK--KNLFGGYEVYTHNGTKKTKLDPVEFAK 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488164351 163 EMQKRGAGEILLTGMDRDGTKQGFNLPLTRAVAEAVDIPVIASGGVGNVRHLIEGITEGKADAVlAAG---VFH 233
Cdd:NF038364 159 ELEALGAGEIVLNSIDRDGTMKGYDLELIKKVSSAVSIPVIALGGAGSLEDLKEAIKQAGASAV-AAGslfVFK 231
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 2-255 9.01e-57

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 189.54  E-value: 9.01e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   2 ALAKRIIPCLDVK-----DGRVVKGVNF--------IGLRDAGDPVEAAKRYNGEGADELTFLDITASSDN--RDT-ILH 65
Cdd:PLN02617 225 SLAKRVIACLDVRsndkgDLVVTKGDQYdvrehsegREVRNLGKPVELAGQYYKDGADEVAFLNITGFRDFplGDLpMLE 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351  66 IIEEVAGQVFIPLTVGGGVRTVAD-----------IRRLLNAGADKVSINTAAV------------TRPDLIDEAAGFFG 122
Cdd:PLN02617 305 VLRRASENVFVPLTVGGGIRDFTDangryysslevASEYFRSGADKISIGSDAVyaaeeyiasgvkTGKTSIEQISRVYG 384

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351 123 SQAIVAAVDAKAV---NPENTR------------------WEIFTHGGRNPTGLDAVEWAIEMQKRGAGEILLTGMDRDG 181
Cdd:PLN02617 385 NQAVVVSIDPRRVyvkDPSDVPfktvkvtnpgpngeeyawYQCTVKGGREGRPIGAYELAKAVEELGAGEILLNCIDCDG 464

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488164351 182 TKQGFNLPLTRAVAEAVDIPVIASGGVGNVRHLIEGITEGKADAVLAAGVFHFGEIAIREAKRAMREAGIEVRL 255
Cdd:PLN02617 465 QGKGFDIELVKLVSDAVTIPVIASSGAGTPEHFSDVFSKTNASAALAAGIFHRKEVPISSVKEHLLEEGIETRI 538
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 6-223 2.52e-51

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: 167.14  E-value: 2.52e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   6 RIIPCLDVKDGRVVKGVNfiGLRD-----AGDPVEAAKRYNGEGADELTFLDITASSDNRDTILHIIEEVAGQVFIPLTV 80
Cdd:COG0106    1 IIIPAIDLKDGKCVRLVQ--GDYDqetvySDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351  81 GGGVRTVADIRRLLNAGADKVSINTAAVTRPDLIDEAAGFFGSQaIVAAVDAKAvnpentrWEIFTHGGRNPTGLDAVEW 160
Cdd:COG0106   79 GGGIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPER-IVVGLDARD-------GKVATDGWQETSGVDLEEL 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351 161 AIEMQKRGAGEILLTGMDRDGTKQGFNLPLTRAVAEAVDIPVIASGGVGNVRHL-------IEGITEGKA 223
Cdd:COG0106  151 AKRFEDAGVAAILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLralkelgVEGAIVGKA 220
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 6-223 5.19e-50

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: 163.80  E-value: 5.19e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   6 RIIPCLDVKDGRVVKGVNfiGLRDA-----GDPVEAAKRYNGEGADELTFLDITASSDNRDTILHIIEEVAGQVFIPLTV 80
Cdd:cd04732    1 IIIPAIDLKDGKCVRLYQ--GDYDKktvysDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351  81 GGGVRTVADIRRLLNAGADKVSINTAAVTRPDLIDEAAGFFGSQAIVAAVDAKAVnpentrwEIFTHGGRNPTGLDAVEW 160
Cdd:cd04732   79 GGGIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLDAKDG-------KVATKGWLETSEVSLEEL 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351 161 AIEMQKRGAGEILLTGMDRDGTKQGFNLPLTRAVAEAVDIPVIASGGVGNVRHL-------IEGITEGKA 223
Cdd:cd04732  152 AKRFEELGVKAIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDDIkalkelgVAGVIVGKA 221
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 7-247 5.90e-45

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


Pssm-ID: 184165  Cd Length: 241  Bit Score: 151.21  E-value: 5.90e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   7 IIPCLDVKDGRVVKGVNfiGLRDA-----GDPVEAAKRYNGEGADELTFLDITASSDNRDTILHIIEEVAGQVFIPLTVG 81
Cdd:PRK13585   5 VIPAVDMKGGKCVQLVQ--GEPGTetvsyGDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEKIIEAVGVPVQLG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351  82 GGVRTVADIRRLLNAGADKVSINTAAVTRPDLIDEAAGFFGSQAIVAAVDAKAvnpentrWEIFTHGGRNPTGLDAVEWA 161
Cdd:PRK13585  83 GGIRSAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEFGSERVMVSLDAKD-------GEVVIKGWTEKTGYTPVEAA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351 162 IEMQKRGAGEILLTGMDRDGTKQGFNLPLTRAVAEAVDIPVIASGGVGNVRHLIEgITEGKADAVLAAGVFHFGEIAIRE 241
Cdd:PRK13585 156 KRFEELGAGSILFTNVDVEGLLEGVNTEPVKELVDSVDIPVIASGGVTTLDDLRA-LKEAGAAGVVVGSALYKGKFTLEE 234


                 ....*.
gi 488164351 242 AKRAMR 247
Cdd:PRK13585 235 AIEAVK 240
PRK00748 PRK00748
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 7-223 2.47e-43

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


Pssm-ID: 179108  Cd Length: 233  Bit Score: 146.75  E-value: 2.47e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   7 IIPCLDVKDGRVV---KGvnfiglrD-------AGDPVEAAKRYNGEGADELTFLDITASSDNRDTILHIIEEVAGQVFI 76
Cdd:PRK00748   3 IIPAIDLKDGKCVrlyQG-------DydqatvySDDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351  77 PLTVGGGVRTVADIRRLLNAGADKVSINTAAVTRPDLIDEAAGFFGSQaIVAAVDAKAvnpentrWEIFTHGGRNPTGLD 156
Cdd:PRK00748  76 PVQVGGGIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFPGK-IVVGLDARD-------GKVATDGWLETSGVT 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488164351 157 AVEWAIEMQKRGAGEILLTGMDRDGTKQGFNLPLTRAVAEAVDIPVIASGGVGNVRHL--------IEGITEGKA 223
Cdd:PRK00748 148 AEDLAKRFEDAGVKAIIYTDISRDGTLSGPNVEATRELAAAVPIPVIASGGVSSLDDIkalkglgaVEGVIVGRA 222
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 7-223 1.58e-40

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: 139.26  E-value: 1.58e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351    7 IIPCLDVKDGRVVKGVNfiGLRD-----AGDPVEAAKRYNGEGADELTFLDITASSDNRDTILHIIEEVAGQVFIPLTVG 81
Cdd:TIGR00007   1 IIPAIDIKDGKCVRLYQ--GDYDketvyGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   82 GGVRTVADIRRLLNAGADKVSINTAAVTRPDLIDEAAGFFGSQAIVAAVDAKAVnpentrwEIFTHGGRNPTGLDAVEWA 161
Cdd:TIGR00007  79 GGIRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSLDARGG-------EVAVKGWLEKSEVSLEELA 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488164351  162 IEMQKRGAGEILLTGMDRDGTKQGFNLPLTRAVAEAVDIPVIASGGVGNVRHLI-------EGITEGKA 223
Cdd:TIGR00007 152 KRLEELGLEGIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSIDDLIalkklgvYGVIVGKA 220
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 6-244 5.99e-33

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: 119.68  E-value: 5.99e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   6 RIIPCLDVKDGRVVKGVNfiGLRDA-----------GDPVEAAKRYNGEGADELTFLDITASSDNRDTiLHIIEEVAGQV 74
Cdd:cd04723    1 RIIPVIDLKDGVVVHGVG--GDRDNyrpitsnlcstSDPLDVARAYKELGFRGLYIADLDAIMGRGDN-DEAIRELAAAW 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351  75 FIPLTVGGGVRTVADIRRLLNAGADKVSINTAAVTRPDLIDEAAgFFGSQAIVAAVDAKAVNPENTRWEIfthggrnptg 154
Cdd:cd04723   78 PLGLWVDGGIRSLENAQEWLKRGASRVIVGTETLPSDDDEDRLA-ALGEQRLVLSLDFRGGQLLKPTDFI---------- 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351 155 lDAVEWAIEMQKRgAGEILLTGMDRDGTKQGFNLPLTRAVAEAVDIPVIASGGVGNVRHLiEGITEGKADAVLAAGVFHF 234
Cdd:cd04723  147 -GPEELLRRLAKW-PEELIVLDIDRVGSGQGPDLELLERLAARADIPVIAAGGVRSVEDL-ELLKKLGASGALVASALHD 223

                        250
                 ....*....|
gi 488164351 235 GEIAIREAKR 244
Cdd:cd04723  224 GGLTLEDVVR 233
PRK14024 PRK14024
phosphoribosyl isomerase A; Provisional
 7-232 1.10e-18

phosphoribosyl isomerase A; Provisional


Pssm-ID: 237589  Cd Length: 241  Bit Score: 82.31  E-value: 1.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   7 IIPCLDVKDGRVVKGVNfiGL----RDAGDPVEAAKRYNGEGADELTFLDITAS---SDNRDtilhIIEEVAGQVFIPLT 79
Cdd:PRK14024   6 LLPAVDVVDGQAVRLVQ--GEagseTSYGSPLDAALAWQRDGAEWIHLVDLDAAfgrGSNRE----LLAEVVGKLDVKVE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351  80 VGGGVRTVADIRRLLNAGADKVSINTAAVTRPDLIDEAAGFFGSQaIVAAVDAKAVNPENTRWEifTHGGrnptglDAVE 159
Cdd:PRK14024  80 LSGGIRDDESLEAALATGCARVNIGTAALENPEWCARVIAEHGDR-VAVGLDVRGHTLAARGWT--RDGG------DLWE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351 160 WAIEMQKRGAGEILLTGMDRDGTKQGFNLPLTRAVAEAVDIPVIASGGVGNVRHL----------IEGITEGKAdavLAA 229
Cdd:PRK14024 151 VLERLDSAGCSRYVVTDVTKDGTLTGPNLELLREVCARTDAPVVASGGVSSLDDLralaelvplgVEGAIVGKA---LYA 227


                 ...
gi 488164351 230 GVF 232
Cdd:PRK14024 228 GAF 230
PRK14114 PRK14114
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 7-247 4.29e-12

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


Pssm-ID: 172604  Cd Length: 241  Bit Score: 63.88  E-value: 4.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   7 IIPCLDV---KDGRVVKGVNFIGLRDAGDPVEAAKRYNGEGADELTFLDITASSDNRDTILHIIEEVAgQVFIPLTVGGG 83
Cdd:PRK14114   3 VVPAIDLfrgKVARMVKGKKENTIFYEKDPAELVEKLIEEGFTLIHVVDLSKAIENSVENLPVLEKLS-EFAEHIQIGGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351  84 VRTVADIRRLLNAGADKVSINTAAVTRPDLIDEaagffgsqaiVAAVDAKAVNPENTR-WEIFTHGGRNPTGLDAVEWAI 162
Cdd:PRK14114  82 IRSLDYAEKLRKLGYRRQIVSSKVLEDPSFLKF----------LKEIDVEPVFSLDTRgGKVAFKGWLAEEEIDPVSLLK 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351 163 EMQKRGAGEILLTGMDRDGTKQGFNLPLTRAVAEAVDIPVIASGGVGNVRHLIEGI-----TEGKADAVLAAGVFHFGEI 237
Cdd:PRK14114 152 RLKEYGLEEIVHTEIEKDGTLQEHDFSLTRKIAIEAEVKVFAAGGISSENSLKTAQrvhreTNGLLKGVIVGRAFLEGIL 231

                        250
                 ....*....|
gi 488164351 238 AIREAKRAMR 247
Cdd:PRK14114 232 TVEVMKRYAR 241
PRK04128 PRK04128
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 6-185 5.93e-12

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


Pssm-ID: 167709  Cd Length: 228  Bit Score: 63.25  E-value: 5.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   6 RIIPCLDVKDGRVVKGVNfiGLRDA----GDPVEAAKRYNgEGADELTFLD----ITASSDNRDTILHIIEEVAGQVfip 77
Cdd:PRK04128   3 RIYPAIDLMNGKAVRLYK--GRKEEvkvyGDPVEIALRFS-EYVDKIHVVDldgaFEGKPKNLDVVKNIIRETGLKV--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351  78 lTVGGGVRTVADIRRLLNAGADKVSINTAAVTRPDLIDEAAGFFGsqaIVAAVDAKavnpentRWEIFTHGGRNPTGLDA 157
Cdd:PRK04128  77 -QVGGGLRTYESIKDAYEIGVENVIIGTKAFDLEFLEKVTSEFEG---ITVSLDVK-------GGRIAVKGWLEESSIKV 145

                        170       180
                 ....*....|....*....|....*...
gi 488164351 158 VEwAIEMQKRGAGEILLTGMDRDGTKQG 185
Cdd:PRK04128 146 ED-AYEMLKNYVNRFIYTSIERDGTLTG 172
PRK13586 PRK13586
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 6-216 2.05e-11

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


Pssm-ID: 237439  Cd Length: 232  Bit Score: 62.06  E-value: 2.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   6 RIIPCLDVKDGRVVK---GVNFIGLRdAGDPVEAAKRYNGEGADELTFLDITASSDNRDTIlHIIEEVAGQVFIPLTVGG 82
Cdd:PRK13586   3 KIIPSIDISLGKAVKrirGVKGTGLI-LGNPIEIASKLYNEGYTRIHVVDLDAAEGVGNNE-MYIKEISKIGFDWIQVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351  83 GVRTVADIRRLLNAGADKVSINTAAVTRPDLIDEAAGFFGSQAIVAAVDAKavnpENTRWEIFTHGGRNPTGLDAVEWAI 162
Cdd:PRK13586  81 GIRDIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGSNRVLVSIDYD----NTKRVLIRGWKEKSMEVIDGIKKVN 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488164351 163 EMQKRGageILLTGMDRDGTKQGFNLPLTRaVAEAVDIPVIASGGVGNVRHLIE 216
Cdd:PRK13586 157 ELELLG---IIFTYISNEGTTKGIDYNVKD-YARLIRGLKEYAGGVSSDADLEY 206
PRK13587 PRK13587
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 28-213 5.03e-11

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


Pssm-ID: 172156  Cd Length: 234  Bit Score: 61.00  E-value: 5.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351  28 RDAGDPVEAAKRYNGegADELTFLDITASSDNRDTILHIIEEVAGQVFIPLTVGGGVRTVADIRRLLNAGADKVSINTAA 107
Cdd:PRK13587  31 RSAEESIAYYSQFEC--VNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIEVGGGIRTKSQIMDYFAAGINYCIVGTKG 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351 108 VTRPDLIDEAAGFFGSQaIVAAVDAkavnpenTRWEIFTHGGRNPTGLDAVEWAIEMQKRGAGEILLTGMDRDGTKQGFN 187
Cdd:PRK13587 109 IQDTDWLKEMAHTFPGR-IYLSVDA-------YGEDIKVNGWEEDTELNLFSFVRQLSDIPLGGIIYTDIAKDGKMSGPN 180

                        170       180
                 ....*....|....*....|....*.
gi 488164351 188 LPLTRAVAEAVDIPVIASGGvgnVRH 213
Cdd:PRK13587 181 FELTGQLVKATTIPVIASGG---IRH 203
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 5-106 1.40e-07

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: 50.66  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351    5 KRIIPCLDVKDGRV-VKGvnfiGLRDAG-DPVEAAKRYNGEGADELTFLDITassdnRDTILH-----IIEEVAGQVFIP 77
Cdd:TIGR00007 121 ERIVVSLDARGGEVaVKG----WLEKSEvSLEELAKRLEELGLEGIIYTDIS-----RDGTLSgpnfeLTKELVKAVNVP 191

                          90       100
                  ....*....|....*....|....*....
gi 488164351   78 LTVGGGVRTVADIRRLLNAGADKVSINTA 106
Cdd:TIGR00007 192 VIASGGVSSIDDLIALKKLGVYGVIVGKA 220
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 6-106 1.55e-06

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


Pssm-ID: 184165  Cd Length: 241  Bit Score: 47.98  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   6 RIIPCLDVKDGRVV-KGVNfiglRDAG-DPVEAAKRYNGEGADELTFLDITASSDNRDTILHIIEEVAGQVFIPLTVGGG 83
Cdd:PRK13585 126 RVMVSLDAKDGEVViKGWT----EKTGyTPVEAAKRFEELGAGSILFTNVDVEGLLEGVNTEPVKELVDSVDIPVIASGG 201

                         90       100
                 ....*....|....*....|...
gi 488164351  84 VRTVADIRRLLNAGADKVSINTA 106
Cdd:PRK13585 202 VTTLDDLRALKEAGAAGVVVGSA 224
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 5-106 3.61e-06

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: 46.70  E-value: 3.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   5 KRIIPCLDVKDGRVVkgvnFIGLRD--AGDPVEAAKRYNGEGADELTFLDI----TASSDNRDtilhIIEEVAGQVFIPL 78
Cdd:cd04732  122 ERIVVGLDAKDGKVA----TKGWLEtsEVSLEELAKRFEELGVKAIIYTDIsrdgTLSGPNFE----LYKELAAATGIPV 193

                         90       100
                 ....*....|....*....|....*...
gi 488164351  79 TVGGGVRTVADIRRLLNAGADKVSINTA 106
Cdd:cd04732  194 IASGGVSSLDDIKALKELGVAGVIVGKA 221
FadH COG1902
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ...
 156-254 1.62e-05

2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family [Energy production and conversion];


Pssm-ID: 441506 [Multi-domain]  Cd Length: 365  Bit Score: 45.16  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351 156 DAVEWAIEMQKRGA-------GEILLTGMDRDGTKQGFNLPLTRAVAEAVDIPVIASGGVGNVRHLIEGITEGKADAVLa 228
Cdd:COG1902  237 ESVELAKALEEAGVdylhvssGGYEPDAMIPTIVPEGYQLPFAARIRKAVGIPVIAVGGITTPEQAEAALASGDADLVA- 315

                         90       100
                 ....*....|....*....|....*....
gi 488164351 229 agvfhFGEIAIRE---AKRAMREAGIEVR 254
Cdd:COG1902  316 -----LGRPLLADpdlPNKAAAGRGDEIR 339
OYE_like_FMN_family cd02803
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
 156-226 1.13e-04

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: 42.56  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351 156 DAVEWAIEMQKRGAGEILLTG---------MDRDGTKQGFNLPLTRAVAEAVDIPVIASGGVGNVRHLIEGITEGKADAV 226
Cdd:cd02803  229 EAIEIAKALEEAGVDALHVSGgsyespppiIPPPYVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILAEGKADLV 308
PLN02446 PLN02446
(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 78-235 1.13e-03

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


Pssm-ID: 215245  Cd Length: 262  Bit Score: 39.30  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351  78 LTVGGGVrTVADIRRLLNAGADKVsINTAAVTRPDLIDEAAgffgSQAIVAAVDAKAV------NPENTRWEIFTHGGRN 151
Cdd:PLN02446  86 LQVGGGV-NSENAMSYLDAGASHV-IVTSYVFRDGQIDLER----LKDLVRLVGKQRLvldlscRKKDGRYYVVTDRWQK 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351 152 PTGLDAVEWAIEMQKRGAGEILLTGMDRDGTKQGFNLPLTRAVAEAVDIPVIASGGVGNVRHL--IEGITEGKADAVLAA 229
Cdd:PLN02446 160 FSDLAVDEETLEFLAAYCDEFLVHGVDVEGKRLGIDEELVALLGEHSPIPVTYAGGVRSLDDLerVKVAGGGRVDVTVGS 239


                 ....*.
gi 488164351 230 GVFHFG 235
Cdd:PLN02446 240 ALDIFG 245
ER_like_FMN cd02931
Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent ...
 183-226 3.30e-03

Enoate reductase (ER)-like FMN-binding domain. Enoate reductase catalyzes the NADH-dependent reduction of carbon-carbon double bonds of several molecules, including nonactivated 2-enoates, alpha,beta-unsaturated aldehydes, cyclic ketones, and methylketones. ERs are similar to 2,4-dienoyl-CoA reductase from E. coli and to the old yellow enzyme from Saccharomyces cerevisiae.


Pssm-ID: 239241 [Multi-domain]  Cd Length: 382  Bit Score: 38.26  E-value: 3.30e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 488164351 183 KQGFNLPLTRAVAEAVDIPVIASGGVGNVRHLIEGITEGKADAV 226
Cdd:cd02931  289 KKGMYLPYCKALKEVVDVPVIMAGRMEDPELASEAINEGIADMI 332
OYE_like_4_FMN cd04735
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ...
 53-115 4.76e-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: 37.58  E-value: 4.76e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488164351  53 ITASSDNRDTILHIIEEVAGQvfIPLTVGGGVRTVADIRRLLNAGADKVSINTAAVTRPDLID 115
Cdd:cd04735  264 RRGRDDNQTIMELVKERIAGR--LPLIAVGSINTPDDALEALETGADLVAIGRGLLVDPDWVE 324
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 175-226 5.18e-03

2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.


Pssm-ID: 240081 [Multi-domain]  Cd Length: 236  Bit Score: 37.08  E-value: 5.18e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488164351 175 TGMDRDGTkqgfnLPLTRAVAEAVDIPVIASGGVGNVRHLIEGITEGkADAV 226
Cdd:cd04730  137 RGTFDIGT-----FALVPEVRDAVDIPVIAAGGIADGRGIAAALALG-ADGV 182
NMO pfam03060
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ...
 50-230 5.66e-03

Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane dioxygenase (NPD) (EC:1.13.11.32), is an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and, in the case of the enzyme from Neurospora crassa, (neutral) nitroalkanes to the corresponding carbonyl compounds and nitrite. Previously classified as 2-nitropropane dioxygenase, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity. One atom of oxygen is incorporated into the carbonyl group of the aldehyde product. The reaction appears to involve the formation of an enzyme-bound nitronate radical and an a-peroxynitroethane species, which then decomposes, either in the active site of the enzyme or after release, to acetaldehyde and nitrite.


Pssm-ID: 367316 [Multi-domain]  Cd Length: 331  Bit Score: 37.49  E-value: 5.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351   50 FLDITASSDNRDTILHIIEEVAGQVFIPLtvggGVRTVADIRRLLNAGADKVSInTAAVTRPDLIDEAAgFFGSQAIVAA 129
Cdd:pfam03060  70 FLPKPDLADPAANYAKILGNNALGYNIEE----GVPDYGKVLVDLDEGVNVVSF-GFGLPPNDVVFRLH-FAGVALIPTI 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351  130 VDAKAvnpentrweifthggrnptgldavewAIEMQKRGAGEILLTGMDRDGTKQGFN------LPLTRAVAEAVDIPVI 203
Cdd:pfam03060 144 SSAKE--------------------------ARIAEARGADALIVQGPEAGGHQGTPEygdkglFRLVPQVPDAVDIPVI 197

                         170       180
                  ....*....|....*....|....*..
gi 488164351  204 ASGGVGNVRHLiegitegkaDAVLAAG 230
Cdd:pfam03060 198 AAGGIWDRRGV---------AAALALG 215
OYE_YqiM_FMN cd02932
Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress ...
 185-229 5.92e-03

Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress response of Bacillus subtilis. Like the other OYE members, each monomer of YqjM contains FMN as a non-covalently bound cofactor and uses NADPH as a reducing agent. The YqjM enzyme exists as a homotetramer that is assembled as a dimer of catalytically dependent dimers, while other OYE members exist only as monomers or dimers. Moreover, the protein displays a shared active site architecture where an arginine finger at the COOH terminus of one monomer extends into the active site of the adjacent monomer and is directly involved in substrate recognition. Another remarkable difference in the binding of the ligand in YqjM is represented by the contribution of the NH2-terminal tyrosine instead of a COOH-terminal tyrosine in OYE and its homologs.


Pssm-ID: 239242 [Multi-domain]  Cd Length: 336  Bit Score: 37.47  E-value: 5.92e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 488164351 185 GFNLPLTRAVAEAVDIPVIASGGVGNVRHLIEGITEGKADAVLAA 229
Cdd:cd02932  276 GYQVPFAERIRQEAGIPVIAVGLITDPEQAEAILESGRADLVALG 320
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 30-230 7.55e-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: 36.41  E-value: 7.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351  30 AGDPVEAAKRYNGEGADELTFLDITASSDNRDT-ILHIIEEVAGQVFIPLTVGGGVRTVADI-----RRLLNAGADKVSI 103
Cdd:cd04722   11 SGDPVELAKAAAEAGADAIIVGTRSSDPEEAETdDKEVLKEVAAETDLPLGVQLAINDAAAAvdiaaAAARAAGADGVEI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351 104 NTAAVTRPD----LIDEAAGFFGSQAIVAAVDakavnpentrweifthggrnPTGLDAVEWAIEmqkRGAGEILLTGMDR 179
Cdd:cd04722   91 HGAVGYLARedleLIRELREAVPDVKVVVKLS--------------------PTGELAAAAAEE---AGVDEVGLGNGGG 147

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488164351 180 DGTKQGFNLP---LTRAVAEAVDIPVIASGGVGNVRHLIEGITEGkADAVLAAG 230
Cdd:cd04722  148 GGGGRDAVPIadlLLILAKRGSKVPVIAGGGINDPEDAAEALALG-ADGVIVGS 200
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
 34-121 7.78e-03

tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439812 [Multi-domain]  Cd Length: 310  Bit Score: 37.00  E-value: 7.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488164351  34 VEAAKRYNGEGADELTflditassdnrdtiLH---------------IIEEVAGQVFIPLTVGGGVRTVADIRRLLNA-G 97
Cdd:COG0042  149 LEFARIAEDAGAAALT--------------VHgrtreqrykgpadwdAIARVKEAVSIPVIGNGDIFSPEDAKRMLEEtG 214

                         90       100
                 ....*....|....*....|....
gi 488164351  98 ADKVSINTAAVTRPDLIDEAAGFF 121
Cdd:COG0042  215 CDGVMIGRGALGNPWLFREIDAYL 238
GGGP-family TIGR01768
geranylgeranylglyceryl phosphate synthase family protein; This model represents a family of ...
 76-112 9.13e-03

geranylgeranylglyceryl phosphate synthase family protein; This model represents a family of sequences including geranylgeranylglyceryl phosphate synthase which catalyzes the first committed step in the synthesis of ether-linked membrane lipids in archaea. The clade of bacterial sequences may have the same function or a closely related function. This model supercedes TIGR00265, which has been retired.


Pssm-ID: 273794  Cd Length: 223  Bit Score: 36.31  E-value: 9.13e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 488164351   76 IPLTVGGGVRTVADIRRLLNAGADKVSINTAAVTRPD 112
Cdd:TIGR01768 180 ARLFVGGGIRSVEKAREMAEAGADTVVTGNVIEESVD 216
 
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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