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Conserved domains on  [gi|518776410|ref|WP_019933699|]
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imidazole glycerol phosphate synthase subunit HisF [Oceanimonas smirnovii]

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]; ...
 2-256 2.70e-143

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: 401.32  E-value: 2.70e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410   2 LARRIIPCLDVKDGQVVKGVKFRNHEIIGDIVPLAERYAAEGADELVFYDITASSQDRVVDKSWVSRVAEVIDIPFCVAG 81
Cdd:COG0107    1 LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410  82 GIKSVEDAARILEFGADKISINSPALSNPKLITQLADTFGVQCIVVGIDSYFDEaTGQYQVHQFTGDESrtqvTRWSTFD 161
Cdd:COG0107   81 GIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRVP-DGGWEVYTHGGRKP----TGLDAVE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410 162 WVQEVQQRGAGEIVLNVMNQDGVRQGYDIEQLLKVRAICDVPLIASGGAGEMVHFRDAFLEADVDGALAASVFHKGIINM 241
Cdd:COG0107  156 WAKEAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITI 235

                        250
                 ....*....|....*
gi 518776410 242 GELKQYLKQEGVVIR 256
Cdd:COG0107  236 AELKAYLAEAGIPVR 250
 
Name Accession Description Interval E-value
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 2-256 2.70e-143

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: 401.32  E-value: 2.70e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410   2 LARRIIPCLDVKDGQVVKGVKFRNHEIIGDIVPLAERYAAEGADELVFYDITASSQDRVVDKSWVSRVAEVIDIPFCVAG 81
Cdd:COG0107    1 LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410  82 GIKSVEDAARILEFGADKISINSPALSNPKLITQLADTFGVQCIVVGIDSYFDEaTGQYQVHQFTGDESrtqvTRWSTFD 161
Cdd:COG0107   81 GIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRVP-DGGWEVYTHGGRKP----TGLDAVE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410 162 WVQEVQQRGAGEIVLNVMNQDGVRQGYDIEQLLKVRAICDVPLIASGGAGEMVHFRDAFLEADVDGALAASVFHKGIINM 241
Cdd:COG0107  156 WAKEAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITI 235

                        250
                 ....*....|....*
gi 518776410 242 GELKQYLKQEGVVIR 256
Cdd:COG0107  236 AELKAYLAEAGIPVR 250
hisF TIGR00735
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ...
 1-256 8.16e-136

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


Pssm-ID: 273241  Cd Length: 254  Bit Score: 382.87  E-value: 8.16e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410    1 MLARRIIPCLDVKDGQVVKGVKFRNHEIIGDIVPLAERYAAEGADELVFYDITASSQDRVVDKSWVSRVAEVIDIPFCVA 80
Cdd:TIGR00735   1 MLAKRIIPCLDVRDGRVVKGVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410   81 GGIKSVEDAARILEFGADKISINSPALSNPKLITQLADTFGVQCIVVGIDSYFDEATGQ--YQVHQFTGDESrtqvTRWS 158
Cdd:TIGR00735  81 GGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRVYVNSYcwYEVYIYGGRES----TGLD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410  159 TFDWVQEVQQRGAGEIVLNVMNQDGVRQGYDIEQLLKVRAICDVPLIASGGAGEMVHFRDAFLEADVDGALAASVFHKGI 238
Cdd:TIGR00735 157 AVEWAKEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPEHFYEAFTKGKADAALAASVFHYRE 236

                         250
                  ....*....|....*...
gi 518776410  239 INMGELKQYLKQEGVVIR 256
Cdd:TIGR00735 237 ITIGEVKEYLAERGIPVR 254
HisF cd04731
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ...
 4-249 1.89e-122

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: 348.30  E-value: 1.89e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410   4 RRIIPCLDVKDGQVVKGVKFRNHEIIGDIVPLAERYAAEGADELVFYDITASSQDRVVDKSWVSRVAEVIDIPFCVAGGI 83
Cdd:cd04731    1 KRIIPCLDVKDGRVVKGVNFKNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410  84 KSVEDAARILEFGADKISINSPALSNPKLITQLADTFGVQCIVVGIDSYFDEAtGQYQVHqftgDESRTQVTRWSTFDWV 163
Cdd:cd04731   81 RSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAKRRGD-GGYEVY----THGGRKPTGLDAVEWA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410 164 QEVQQRGAGEIVLNVMNQDGVRQGYDIEQLLKVRAICDVPLIASGGAGEMVHFRDAFLEADVDGALAASVFHKGIINMGE 243
Cdd:cd04731  156 KEVEELGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEAFEEGGADAALAASIFHFGEYTIAE 235


                 ....*.
gi 518776410 244 LKQYLK 249
Cdd:cd04731  236 LKEYLA 241
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 5-240 1.12e-92

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: 272.43  E-value: 1.12e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410    5 RIIPCLDVKDGQVV---KGVKFRNHEIIGDIVPLAERYAAEGADELVFYDITASSQDRVVDKSWVSRVAEVIDIPFCVAG 81
Cdd:pfam00977   1 RIIPAIDLKDGRVVrlvKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410   82 GIKSVEDAARILEFGADKISINSPALSNPKLITQLADTFGVQCIVVGIDSYFDEatgqyqVHQFTGDEsrtqVTRWSTFD 161
Cdd:pfam00977  81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDARRGK------VAINGWRE----DTGIDAVE 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518776410  162 WVQEVQQRGAGEIVLNVMNQDGVRQGYDIEQLLKVRAICDVPLIASGGAGEMVHFRDAFlEADVDGALAASVFHKGIIN 240
Cdd:pfam00977 151 WAKELEELGAGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELF-TEGVDGVIAGSALYEGEIT 228
AglZ_HisF2_fam NF038364
AglZ/HisF2 family acetamidino modification protein;
2-236 1.44e-69

AglZ/HisF2 family acetamidino modification protein;


Pssm-ID: 439657  Cd Length: 248  Bit Score: 214.26  E-value: 1.44e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410   2 LARRIIPCLDVKDGQVVKGVKFRNHEIIGDivPL-AERYAAE-GADELVFYDITASSQDRVVDKSWVSRVAEVIDIPFCV 79
Cdd:NF038364   1 LRPRIIPCLLLHNGGLVKTVKFKDPKYVGD--PInAVRIFNEkEVDELIVLDIDATKEGREPDYELIEDLASECFMPLCY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410  80 AGGIKSVEDAARILEFGADKISINSPALSNPKLITQLADTFGVQCIVVGID---SYFdeatGQYQVHQFTGdesrTQVTR 156
Cdd:NF038364  79 GGGIKTLEQARRIFSLGVEKVALNSAALENPELITEAAEEFGSQSVVVSIDvkkNLF----GGYEVYTHNG----TKKTK 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410 157 WSTFDWVQEVQQRGAGEIVLNVMNQDGVRQGYDIEQLLKVRAICDVPLIASGGAGEMVHFRDAFLEADVDGALAAS--VF 234
Cdd:NF038364 151 LDPVEFAKELEALGAGEIVLNSIDRDGTMKGYDLELIKKVSSAVSIPVIALGGAGSLEDLKEAIKQAGASAVAAGSlfVF 230


                 ..
gi 518776410 235 HK 236
Cdd:NF038364 231 KG 232
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 2-256 7.63e-36

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 133.68  E-value: 7.63e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410   2 LARRIIPCLDVK-----DGQVVKGVKF--RNHEIIGDI------VPLAERYAAEGADELVFYDITASSQDRVVDKSWVS- 67
Cdd:PLN02617 226 LAKRVIACLDVRsndkgDLVVTKGDQYdvREHSEGREVrnlgkpVELAGQYYKDGADEVAFLNITGFRDFPLGDLPMLEv 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410  68 --RVAEVIDIPFCVAGGIKSVED-----------AARILEFGADKISINSPAL--------SNPKL----ITQLADTFGV 122
Cdd:PLN02617 306 lrRASENVFVPLTVGGGIRDFTDangryysslevASEYFRSGADKISIGSDAVyaaeeyiaSGVKTgktsIEQISRVYGN 385

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410 123 QCIVVGIDS---YFDEATG----------------QYQVHQFT---GDESRTqvtrWSTFDWVQEVQQRGAGEIVLNVMN 180
Cdd:PLN02617 386 QAVVVSIDPrrvYVKDPSDvpfktvkvtnpgpngeEYAWYQCTvkgGREGRP----IGAYELAKAVEELGAGEILLNCID 461

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518776410 181 QDGVRQGYDIEQllkVRAICD---VPLIASGGAGEMVHFRDAFLEADVDGALAASVFHKGIINMGELKQYLKQEGVVIR 256
Cdd:PLN02617 462 CDGQGKGFDIEL---VKLVSDavtIPVIASSGAGTPEHFSDVFSKTNASAALAAGIFHRKEVPISSVKEHLLEEGIETR 537
 
Name Accession Description Interval E-value
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 2-256 2.70e-143

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: 401.32  E-value: 2.70e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410   2 LARRIIPCLDVKDGQVVKGVKFRNHEIIGDIVPLAERYAAEGADELVFYDITASSQDRVVDKSWVSRVAEVIDIPFCVAG 81
Cdd:COG0107    1 LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410  82 GIKSVEDAARILEFGADKISINSPALSNPKLITQLADTFGVQCIVVGIDSYFDEaTGQYQVHQFTGDESrtqvTRWSTFD 161
Cdd:COG0107   81 GIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRVP-DGGWEVYTHGGRKP----TGLDAVE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410 162 WVQEVQQRGAGEIVLNVMNQDGVRQGYDIEQLLKVRAICDVPLIASGGAGEMVHFRDAFLEADVDGALAASVFHKGIINM 241
Cdd:COG0107  156 WAKEAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITI 235

                        250
                 ....*....|....*
gi 518776410 242 GELKQYLKQEGVVIR 256
Cdd:COG0107  236 AELKAYLAEAGIPVR 250
hisF TIGR00735
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ...
 1-256 8.16e-136

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


Pssm-ID: 273241  Cd Length: 254  Bit Score: 382.87  E-value: 8.16e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410    1 MLARRIIPCLDVKDGQVVKGVKFRNHEIIGDIVPLAERYAAEGADELVFYDITASSQDRVVDKSWVSRVAEVIDIPFCVA 80
Cdd:TIGR00735   1 MLAKRIIPCLDVRDGRVVKGVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410   81 GGIKSVEDAARILEFGADKISINSPALSNPKLITQLADTFGVQCIVVGIDSYFDEATGQ--YQVHQFTGDESrtqvTRWS 158
Cdd:TIGR00735  81 GGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRVYVNSYcwYEVYIYGGRES----TGLD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410  159 TFDWVQEVQQRGAGEIVLNVMNQDGVRQGYDIEQLLKVRAICDVPLIASGGAGEMVHFRDAFLEADVDGALAASVFHKGI 238
Cdd:TIGR00735 157 AVEWAKEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPEHFYEAFTKGKADAALAASVFHYRE 236

                         250
                  ....*....|....*...
gi 518776410  239 INMGELKQYLKQEGVVIR 256
Cdd:TIGR00735 237 ITIGEVKEYLAERGIPVR 254
HisF cd04731
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ...
 4-249 1.89e-122

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: 348.30  E-value: 1.89e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410   4 RRIIPCLDVKDGQVVKGVKFRNHEIIGDIVPLAERYAAEGADELVFYDITASSQDRVVDKSWVSRVAEVIDIPFCVAGGI 83
Cdd:cd04731    1 KRIIPCLDVKDGRVVKGVNFKNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410  84 KSVEDAARILEFGADKISINSPALSNPKLITQLADTFGVQCIVVGIDSYFDEAtGQYQVHqftgDESRTQVTRWSTFDWV 163
Cdd:cd04731   81 RSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAKRRGD-GGYEVY----THGGRKPTGLDAVEWA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410 164 QEVQQRGAGEIVLNVMNQDGVRQGYDIEQLLKVRAICDVPLIASGGAGEMVHFRDAFLEADVDGALAASVFHKGIINMGE 243
Cdd:cd04731  156 KEVEELGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEAFEEGGADAALAASIFHFGEYTIAE 235


                 ....*.
gi 518776410 244 LKQYLK 249
Cdd:cd04731  236 LKEYLA 241
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 5-240 1.12e-92

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: 272.43  E-value: 1.12e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410    5 RIIPCLDVKDGQVV---KGVKFRNHEIIGDIVPLAERYAAEGADELVFYDITASSQDRVVDKSWVSRVAEVIDIPFCVAG 81
Cdd:pfam00977   1 RIIPAIDLKDGRVVrlvKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410   82 GIKSVEDAARILEFGADKISINSPALSNPKLITQLADTFGVQCIVVGIDSYFDEatgqyqVHQFTGDEsrtqVTRWSTFD 161
Cdd:pfam00977  81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDARRGK------VAINGWRE----DTGIDAVE 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518776410  162 WVQEVQQRGAGEIVLNVMNQDGVRQGYDIEQLLKVRAICDVPLIASGGAGEMVHFRDAFlEADVDGALAASVFHKGIIN 240
Cdd:pfam00977 151 WAKELEELGAGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELF-TEGVDGVIAGSALYEGEIT 228
WbuZ TIGR03572
glycosyl amidation-associated protein WbuZ; This clade of sequences is highly similar to the ...
 1-235 3.80e-83

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: 248.34  E-value: 3.80e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410    1 MLARRIIPCLDVKDGQVVKGVKFRNHEIIGDIVPLAERYAAEGADELVFYDITASSQDRVVDKSWVSRVAEVIDIPFCVA 80
Cdd:TIGR03572   1 MLKKRIIPCLLLKDGRLVKTVQFKDPRYIGDPVNAARIYNAKGADELIVLDIDASKRGREPLFELISNLAEECFMPLTVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410   81 GGIKSVEDAARILEFGADKISINSPALSNPKLITQLADTFGVQCIVVGIDSYFDEATGQYQVHqftgDESRTQVTRWSTF 160
Cdd:TIGR03572  81 GGIRSLEDAKKLLSLGADKVSINTAALENPDLIEEAARRFGSQCVVVSIDVKKELDGSDYKVY----SDNGRRATGRDPV 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518776410  161 DWVQEVQQRGAGEIVLNVMNQDGVRQGYDIEQLLKVRAICDVPLIASGGAGEMVHFRDAFLEADVDGALAASVFH 235
Cdd:TIGR03572 157 EWAREAEQLGAGEILLNSIDRDGTMKGYDLELIKTVSDAVSIPVIALGGAGSLDDLVEVALEAGASAVAAASLFH 231
AglZ_HisF2_fam NF038364
AglZ/HisF2 family acetamidino modification protein;
2-236 1.44e-69

AglZ/HisF2 family acetamidino modification protein;


Pssm-ID: 439657  Cd Length: 248  Bit Score: 214.26  E-value: 1.44e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410   2 LARRIIPCLDVKDGQVVKGVKFRNHEIIGDivPL-AERYAAE-GADELVFYDITASSQDRVVDKSWVSRVAEVIDIPFCV 79
Cdd:NF038364   1 LRPRIIPCLLLHNGGLVKTVKFKDPKYVGD--PInAVRIFNEkEVDELIVLDIDATKEGREPDYELIEDLASECFMPLCY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410  80 AGGIKSVEDAARILEFGADKISINSPALSNPKLITQLADTFGVQCIVVGID---SYFdeatGQYQVHQFTGdesrTQVTR 156
Cdd:NF038364  79 GGGIKTLEQARRIFSLGVEKVALNSAALENPELITEAAEEFGSQSVVVSIDvkkNLF----GGYEVYTHNG----TKKTK 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410 157 WSTFDWVQEVQQRGAGEIVLNVMNQDGVRQGYDIEQLLKVRAICDVPLIASGGAGEMVHFRDAFLEADVDGALAAS--VF 234
Cdd:NF038364 151 LDPVEFAKELEALGAGEIVLNSIDRDGTMKGYDLELIKKVSSAVSIPVIALGGAGSLEDLKEAIKQAGASAVAAGSlfVF 230


                 ..
gi 518776410 235 HK 236
Cdd:NF038364 231 KG 232
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 2-256 7.63e-36

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 133.68  E-value: 7.63e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410   2 LARRIIPCLDVK-----DGQVVKGVKF--RNHEIIGDI------VPLAERYAAEGADELVFYDITASSQDRVVDKSWVS- 67
Cdd:PLN02617 226 LAKRVIACLDVRsndkgDLVVTKGDQYdvREHSEGREVrnlgkpVELAGQYYKDGADEVAFLNITGFRDFPLGDLPMLEv 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410  68 --RVAEVIDIPFCVAGGIKSVED-----------AARILEFGADKISINSPAL--------SNPKL----ITQLADTFGV 122
Cdd:PLN02617 306 lrRASENVFVPLTVGGGIRDFTDangryysslevASEYFRSGADKISIGSDAVyaaeeyiaSGVKTgktsIEQISRVYGN 385

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410 123 QCIVVGIDS---YFDEATG----------------QYQVHQFT---GDESRTqvtrWSTFDWVQEVQQRGAGEIVLNVMN 180
Cdd:PLN02617 386 QAVVVSIDPrrvYVKDPSDvpfktvkvtnpgpngeEYAWYQCTvkgGREGRP----IGAYELAKAVEELGAGEILLNCID 461

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518776410 181 QDGVRQGYDIEQllkVRAICD---VPLIASGGAGEMVHFRDAFLEADVDGALAASVFHKGIINMGELKQYLKQEGVVIR 256
Cdd:PLN02617 462 CDGQGKGFDIEL---VKLVSDavtIPVIASSGAGTPEHFSDVFSKTNASAALAAGIFHRKEVPISSVKEHLLEEGIETR 537
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 5-246 7.19e-32

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: 116.81  E-value: 7.19e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410   5 RIIPCLDVKDGQVV---KGVKFRNHEIIGDIVPLAERYAAEGADELVFYDITASSQDRVVDKSWVSRVAEVIDIPFCVAG 81
Cdd:cd04732    1 IIIPAIDLKDGKCVrlyQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410  82 GIKSVEDAARILEFGADKISINSPALSNPKLITQLADTFGVQCIVVGIDSYfdeaTGQYQVHQFtgdesrTQVTRWSTFD 161
Cdd:cd04732   81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLDAK----DGKVATKGW------LETSEVSLEE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410 162 WVQEVQQRGAGEIVLNVMNQDGVRQGYDIEQLLKVRAICDVPLIASGGAGEMVHFRdAFLEADVDGALAASVFHKGIINM 241
Cdd:cd04732  151 LAKRFEELGVKAIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDDIK-ALKELGVAGVIVGKALYEGKITL 229


                 ....*
gi 518776410 242 GELKQ 246
Cdd:cd04732  230 EEALA 234
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 5-249 3.18e-27

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: 104.73  E-value: 3.18e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410   5 RIIPCLDVKDGQVV---KGVKFRNHEIIGDIVPLAERYAAEGADEL--VfyDITASSQDRVVDKSWVSRVAEVIDIPFCV 79
Cdd:COG0106    1 IIIPAIDLKDGKCVrlvQGDYDQETVYSDDPVEVAKRWEDAGAEWLhlV--DLDGAFAGKPVNLELIEEIAKATGLPVQV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410  80 AGGIKSVEDAARILEFGADKISINSPALSNPKLITQLADTFGVQcIVVGIDSYfDE--ATgqyqvhqftgdESRTQVTRW 157
Cdd:COG0106   79 GGGIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPER-IVVGLDAR-DGkvAT-----------DGWQETSGV 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410 158 STFDWVQEVQQRGAGEIVLNVMNQDGVRQGYDIEQLLKVRAICDVPLIASGGAGEMVHFRdAFLEADVDGALAASVFHKG 237
Cdd:COG0106  146 DLEELAKRFEDAGVAAILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDLR-ALKELGVEGAIVGKALYEG 224

                        250
                 ....*....|..
gi 518776410 238 IINMGELKQYLK 249
Cdd:COG0106  225 KIDLEEALALAR 236
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 6-243 3.85e-26

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


Pssm-ID: 184165  Cd Length: 241  Bit Score: 102.29  E-value: 3.85e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410   6 IIPCLDVKDG---QVVKGVKFRNHEIIGDIVPLAERYAAEGADELVFYDITASSQDRVVDKSWVSRVAEVIDIPFCVAGG 82
Cdd:PRK13585   5 VIPAVDMKGGkcvQLVQGEPGTETVSYGDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEKIIEAVGVPVQLGGG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410  83 IKSVEDAARILEFGADKISINSPALSNPKLITQLADTFGVQCIVVGIDSyfdeATGQYQVHQFtgdesrTQVTRWSTFDW 162
Cdd:PRK13585  85 IRSAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEFGSERVMVSLDA----KDGEVVIKGW------TEKTGYTPVEA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410 163 VQEVQQRGAGEIVLNVMNQDGVRQGYDIEQLLKVRAICDVPLIASGGAGEMVHFRdAFLEADVDGALAASVFHKGIINMG 242
Cdd:PRK13585 155 AKRFEELGAGSILFTNVDVEGLLEGVNTEPVKELVDSVDIPVIASGGVTTLDDLR-ALKEAGAAGVVVGSALYKGKFTLE 233


                 .
gi 518776410 243 E 243
Cdd:PRK13585 234 E 234
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 6-243 7.54e-26

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: 101.12  E-value: 7.54e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410    6 IIPCLDVKDGQVVKGVK--FRNHEIIGD-IVPLAERYAAEGADELVFYDITASSQDRVVDKSWVSRVAEVIDIPFCVAGG 82
Cdd:TIGR00007   1 IIPAIDIKDGKCVRLYQgdYDKETVYGDdPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410   83 IKSVEDAARILEFGADKISINSPALSNPKLITQLADTFGVQCIVVGIDSYFDE-ATGqyqvhqftGDESRTQVTrwsTFD 161
Cdd:TIGR00007  81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSLDARGGEvAVK--------GWLEKSEVS---LEE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410  162 WVQEVQQRGAGEIVLNVMNQDGVRQGYDIEQLLKVRAICDVPLIASGGAGEMVHFRdAFLEADVDGALAASVFHKGIINM 241
Cdd:TIGR00007 150 LAKRLEELGLEGIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSIDDLI-ALKKLGVYGVIVGKALYEGKITL 228


                  ..
gi 518776410  242 GE 243
Cdd:TIGR00007 229 EE 230
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 5-246 1.35e-22

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: 92.72  E-value: 1.35e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410   5 RIIPCLDVKDGQVVKGVKFR---------NHEIIGDIVPLAERYAAEGADELVFYDITASsQDRVVDKSWVSRVAEVIDI 75
Cdd:cd04723    1 RIIPVIDLKDGVVVHGVGGDrdnyrpitsNLCSTSDPLDVARAYKELGFRGLYIADLDAI-MGRGDNDEAIRELAAAWPL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410  76 PFCVAGGIKSVEDAARILEFGADKISINSPALSNpKLITQLADTFGVQCIVVGIDsyfdeatgqyqvhqFTGDESRTQVT 155
Cdd:cd04723   80 GLWVDGGIRSLENAQEWLKRGASRVIVGTETLPS-DDDEDRLAALGEQRLVLSLD--------------FRGGQLLKPTD 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410 156 RWSTFDWVQEVQQRgAGEIVLNVMNQDGVRQGYDIEQLLKVRAICDVPLIASGGAGEMVHFRDAFlEADVDGALAASVFH 235
Cdd:cd04723  145 FIGPEELLRRLAKW-PEELIVLDIDRVGSGQGPDLELLERLAARADIPVIAAGGVRSVEDLELLK-KLGASGALVASALH 222

                        250
                 ....*....|.
gi 518776410 236 KGIINMGELKQ 246
Cdd:cd04723  223 DGGLTLEDVVR 233
PRK00748 PRK00748
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 6-228 1.98e-17

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


Pssm-ID: 179108  Cd Length: 233  Bit Score: 78.57  E-value: 1.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410   6 IIPCLDVKDGQVV---KGvKFRNHEIIG-DIVPLAERYAAEGADELVFYDITASSQDRVVDKSWVSRVAEVIDIPFCVAG 81
Cdd:PRK00748   3 IIPAIDLKDGKCVrlyQG-DYDQATVYSdDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410  82 GIKSVEDAARILEFGADKISINSPALSNPKLITQLADTFGVQcIVVGIDSYfdeaTGQYQVHQFTgDESRTQVTrwstfD 161
Cdd:PRK00748  82 GIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFPGK-IVVGLDAR----DGKVATDGWL-ETSGVTAE-----D 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518776410 162 WVQEVQQRGAGEIVLNVMNQDGVRQGYDIEQLLKVRAICDVPLIASGGAGEMVHFRDAFLEADVDGA 228
Cdd:PRK00748 151 LAKRFEDAGVKAIIYTDISRDGTLSGPNVEATRELAAAVPIPVIASGGVSSLDDIKALKGLGAVEGV 217
PRK14114 PRK14114
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 6-247 6.72e-10

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


Pssm-ID: 172604  Cd Length: 241  Bit Score: 57.72  E-value: 6.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410   6 IIPCLDVKDGQVVKGVKFRNHEII---GDIVPLAERYAAEGADELVFYDITASSQDRVVDKSWVSRVAEVIDiPFCVAGG 82
Cdd:PRK14114   3 VVPAIDLFRGKVARMVKGKKENTIfyeKDPAELVEKLIEEGFTLIHVVDLSKAIENSVENLPVLEKLSEFAE-HIQIGGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410  83 IKSVEDAARILEFGADKISINSPALSNPKLITQLADtfgvqcivVGIDSYFDEATGQYQVhQFTGDESRTQVTRWSTfdw 162
Cdd:PRK14114  82 IRSLDYAEKLRKLGYRRQIVSSKVLEDPSFLKFLKE--------IDVEPVFSLDTRGGKV-AFKGWLAEEEIDPVSL--- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410 163 VQEVQQRGAGEIVLNVMNQDGVRQGYDIEQLLKVRAICDVPLIASGG--------AGEMVHFRDAFLeadVDGALAASVF 234
Cdd:PRK14114 150 LKRLKEYGLEEIVHTEIEKDGTLQEHDFSLTRKIAIEAEVKVFAAGGissenslkTAQRVHRETNGL---LKGVIVGRAF 226

                        250
                 ....*....|...
gi 518776410 235 HKGIINMGELKQY 247
Cdd:PRK14114 227 LEGILTVEVMKRY 239
PRK13586 PRK13586
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 5-130 1.72e-07

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


Pssm-ID: 237439  Cd Length: 232  Bit Score: 50.51  E-value: 1.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410   5 RIIPCLDVKDGQVVKGVKFRNHE--IIGDIVPLAERYAAEGADELVFYDITASsqDRVVDKSWVsrVAEVIDIPFC---V 79
Cdd:PRK13586   3 KIIPSIDISLGKAVKRIRGVKGTglILGNPIEIASKLYNEGYTRIHVVDLDAA--EGVGNNEMY--IKEISKIGFDwiqV 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 518776410  80 AGGIKSVEDAARILEFGADKISINSPALSNPKLITQLADTFGVQCIVVGID 130
Cdd:PRK13586  79 GGGIRDIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGSNRVLVSID 129
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
 21-117 3.09e-07

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: 50.48  E-value: 3.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410  21 VKFRnheiIG------DIVPLAERYAAEGADELV--------FYDITAssqdrvvDKSWVSRVAEVIDIPFCVAGGIKSV 86
Cdd:COG0042  135 VKIR----LGwddddeNALEFARIAEDAGAAALTvhgrtreqRYKGPA-------DWDAIARVKEAVSIPVIGNGDIFSP 203

                         90       100       110
                 ....*....|....*....|....*....|..
gi 518776410  87 EDAARILE-FGADKISINSPALSNPKLITQLA 117
Cdd:COG0042  204 EDAKRMLEeTGCDGVMIGRGALGNPWLFREID 235
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 3-98 3.93e-06

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: 46.49  E-value: 3.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410   3 ARRIIPCLDVKDGQVVKGVKFRNHEiigDIVPLAERYAaegaDELVFYDITASSQDRVVDKSWVSRVAEVIDIPFCVAGG 82
Cdd:cd04723  125 EQRLVLSLDFRGGQLLKPTDFIGPE---ELLRRLAKWP----EELIVLDIDRVGSGQGPDLELLERLAARADIPVIAAGG 197

                         90
                 ....*....|....*.
gi 518776410  83 IKSVEDAARILEFGAD 98
Cdd:cd04723  198 VRSVEDLELLKKLGAS 213
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 5-104 8.80e-06

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


Pssm-ID: 184165  Cd Length: 241  Bit Score: 45.67  E-value: 8.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410   5 RIIPCLDVKDGQVVkgVKFRNHEIIGDIVPLAERYAAEGADELVFYDITASSQDRVVDKSWVSRVAEVIDIPFCVAGGIK 84
Cdd:PRK13585 126 RVMVSLDAKDGEVV--IKGWTEKTGYTPVEAAKRFEELGAGSILFTNVDVEGLLEGVNTEPVKELVDSVDIPVIASGGVT 203

                         90       100
                 ....*....|....*....|
gi 518776410  85 SVEDAARILEFGADKISINS 104
Cdd:PRK13585 204 TLDDLRALKEAGAAGVVVGS 223
PRK13587 PRK13587
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 51-209 1.30e-05

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


Pssm-ID: 172156  Cd Length: 234  Bit Score: 45.21  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410  51 DITASSQDRVVDKSWVSRVAEVIDIPFCVAGGIKSVEDAARILEFGADKISINSPALSNPKLITQLADTFGVQcIVVGID 130
Cdd:PRK13587  53 DLIGAKAQHAREFDYIKSLRRLTTKDIEVGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGR-IYLSVD 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518776410 131 SYFDEAtgqyQVHQFTGDesrtqvTRWSTFDWVQEVQQRGAGEIVLNVMNQDGVRQGYDIEQLLKVRAICDVPLIASGG 209
Cdd:PRK13587 132 AYGEDI----KVNGWEED------TELNLFSFVRQLSDIPLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGG 200
PRK04128 PRK04128
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 5-132 4.23e-05

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


Pssm-ID: 167709  Cd Length: 228  Bit Score: 43.61  E-value: 4.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410   5 RIIPCLDVKDGQVVKGVKFRNHEI--IGDIVPLAERYAaEGADELVFYDITASSQDRVVDKSWVSRVAEVIDIPFCVAGG 82
Cdd:PRK04128   3 RIYPAIDLMNGKAVRLYKGRKEEVkvYGDPVEIALRFS-EYVDKIHVVDLDGAFEGKPKNLDVVKNIIRETGLKVQVGGG 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 518776410  83 IKSVEDAARILEFGADKISINSPALsNPKLITQLADTFGvqCIVVGIDSY 132
Cdd:PRK04128  82 LRTYESIKDAYEIGVENVIIGTKAF-DLEFLEKVTSEFE--GITVSLDVK 128
Dus pfam01207
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ...
 21-115 6.45e-05

Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria.


Pssm-ID: 426126  Cd Length: 309  Bit Score: 43.47  E-value: 6.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410   21 VKFRN--HEIIGDIVPLAERYAAEGADELV--------FYDITAssqdrvvDKSWVSRVAEVIDIPFCVAGGIKSVEDAA 90
Cdd:pfam01207 127 VKIRIgwDDSHENAVEIAKIVEDAGAQALTvhgrtraqNYEGTA-------DWDAIKQVKQAVSIPVIANGDITDPEDAQ 199

                          90       100
                  ....*....|....*....|....*.
gi 518776410   91 RILEF-GADKISINSPALSNPKLITQ 115
Cdd:pfam01207 200 RCLAYtGADGVMIGRGALGNPWLFAE 225
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 61-120 7.15e-05

Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.


Pssm-ID: 239200 [Multi-domain]  Cd Length: 231  Bit Score: 42.87  E-value: 7.15e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518776410  61 VDKSWVSRVAEVIDIPFCVAGGIKSVEDAARILE-FGADKISINSPALSNPKLITQLADTF 120
Cdd:cd02801  170 ADWDYIAEIKEAVSIPVIANGDIFSLEDALRCLEqTGVDGVMIGRGALGNPWLFREIKELL 230
PcrB COG1646
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];
35-100 8.20e-05

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


Pssm-ID: 441252  Cd Length: 241  Bit Score: 42.84  E-value: 8.20e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518776410  35 LAERYAAegADEL----VFYdITASSQ-DRVVDKSWVSRVAEVI-DIPFCVAGGIKSVEDAARILEFGADKI 100
Cdd:COG1646  154 VAAAAAL--AEEYlgmpIVY-LEYGSGaGEPVDPEMVKAVKKALeDTPLIYGGGIRSPEKAREMAEAGADTI 222
OYE_like_FMN_family cd02803
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
 29-113 2.28e-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: 41.79  E-value: 2.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410  29 IGDIVPLAERYAAEGADelvFYDITASSQDR--------VVDKSW----VSRVAEVIDIPFCVAGGIKSVEDAARIL-EF 95
Cdd:cd02803  227 LEEAIEIAKALEEAGVD---ALHVSGGSYESpppiipppYVPEGYflelAEKIKKAVKIPVIAVGGIRDPEVAEEILaEG 303

                         90
                 ....*....|....*...
gi 518776410  96 GADKISINSPALSNPKLI 113
Cdd:cd02803  304 KADLVALGRALLADPDLP 321
PcrB_like cd02812
PcrB_like proteins. One member of this family, a protein from Archaeoglobus fulgidus, has been ...
 60-102 2.29e-04

PcrB_like proteins. One member of this family, a protein from Archaeoglobus fulgidus, has been characterized as a (S)-3-O-geranylgeranylglyceryl phosphate synthase (AfGGGPS). AfGGGPS catalyzes the formation of an ether linkage between sn-glycerol-1-phosphate (G1P) and geranylgeranyl diphosphate (GGPP), the committed step in archaeal lipid biosynthesis. Therefore, it has been proposed that PcrB-like proteins are either prenyltransferases or are involved in lipoteichoic acid biosynthesis although the exact function is still unknown.


Pssm-ID: 239206  Cd Length: 219  Bit Score: 41.07  E-value: 2.29e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 518776410  60 VVDKSWVSRVAEVI-DIPFCVAGGIKSVEDAARILEFGADKISI 102
Cdd:cd02812  160 YGPPEVVRAVKKVLgDTPLIVGGGIRSGEQAKEMAEAGADTIVV 203
FadH COG1902
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ...
 31-118 5.72e-04

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: 40.54  E-value: 5.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410  31 DIVPLAERYAAEGAD--ELV--FYDITASSQDRVVDKSWVS---RVAEVIDIPFCVAGGIKSVEDAARILEFG-ADKISI 102
Cdd:COG1902  237 ESVELAKALEEAGVDylHVSsgGYEPDAMIPTIVPEGYQLPfaaRIRKAVGIPVIAVGGITTPEQAEAALASGdADLVAL 316

                         90
                 ....*....|....*.
gi 518776410 103 NSPALSNPKLITQLAD 118
Cdd:COG1902  317 GRPLLADPDLPNKAAA 332
OYE_like_4_FMN cd04735
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ...
 58-137 1.64e-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: 39.12  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410  58 DRVVDKSWVSRVAEVID--IPFCVAGGIKSVEDAARILEFGADKISINSPALSNPKLITQLADTFGVQcivvgIDSYFDE 135
Cdd:cd04735  266 GRDDNQTIMELVKERIAgrLPLIAVGSINTPDDALEALETGADLVAIGRGLLVDPDWVEKIKEGREDE-----INLEIDP 340


                 ..
gi 518776410 136 AT 137
Cdd:cd04735  341 DD 342
GGGP-family TIGR01768
geranylgeranylglyceryl phosphate synthase family protein; This model represents a family of ...
 34-100 6.59e-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: 37.08  E-value: 6.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518776410   34 PLAERYAAEGADEL---VFYDITASSQDRVVDKSWVSRVAEVID-IPFCVAGGIKSVEDAARILEFGADKI 100
Cdd:TIGR01768 135 EDLAAYAAMAEEMLgmpIFYLEAGSGAPEPVPPELVAEVKKVLDkARLFVGGGIRSVEKAREMAEAGADTV 205
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 26-104 8.78e-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: 8.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518776410  26 HEIIGDIVPLAERYAAEGADE--LVFYDITASSQDRV-VDKSWVSRVAEVIDIPFCVAGGIKSVEDAARILEFGADKISI 102
Cdd:cd04722  119 VKLSPTGELAAAAAEEAGVDEvgLGNGGGGGGGRDAVpIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIV 198


                 ..
gi 518776410 103 NS 104
Cdd:cd04722  199 GS 200
 
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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