NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|490872571|ref|WP_004734577|]
View 

MULTISPECIES: imidazole glycerol phosphate synthase subunit HisF [Vibrio]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 2-257 2.44e-152

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: 424.44  E-value: 2.44e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   2 LAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAQRYAEEGADELVFYDITASSDGRVVDKSWVKRVAEVIDIPFCVAG 81
Cdd:COG0107    1 LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571  82 GIKSAEDAARILEFGADKVSINSPALANPQLITDLADKFGVQCIVVGIDSYFDkETGKYQVYQFTGdearTKATKWETKD 161
Cdd:COG0107   81 GIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRV-PDGGWEVYTHGG----RKPTGLDAVE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571 162 WVQEVQKRGAGEIVLNMMNQDGVRNGYDIDQLNMVRSVCNVPLIASGGAGAMEHFAEAYKKTNVDGALAASVFHKQVINI 241
Cdd:COG0107  156 WAKEAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITI 235

                        250
                 ....*....|....*.
gi 490872571 242 GELKQYLKQQDVEVRL 257
Cdd:COG0107  236 AELKAYLAEAGIPVRL 251
 
Name Accession Description Interval E-value
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 2-257 2.44e-152

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: 424.44  E-value: 2.44e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   2 LAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAQRYAEEGADELVFYDITASSDGRVVDKSWVKRVAEVIDIPFCVAG 81
Cdd:COG0107    1 LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571  82 GIKSAEDAARILEFGADKVSINSPALANPQLITDLADKFGVQCIVVGIDSYFDkETGKYQVYQFTGdearTKATKWETKD 161
Cdd:COG0107   81 GIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRV-PDGGWEVYTHGG----RKPTGLDAVE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571 162 WVQEVQKRGAGEIVLNMMNQDGVRNGYDIDQLNMVRSVCNVPLIASGGAGAMEHFAEAYKKTNVDGALAASVFHKQVINI 241
Cdd:COG0107  156 WAKEAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITI 235

                        250
                 ....*....|....*.
gi 490872571 242 GELKQYLKQQDVEVRL 257
Cdd:COG0107  236 AELKAYLAEAGIPVRL 251
hisF TIGR00735
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ...
 1-256 2.42e-144

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


Pssm-ID: 273241  Cd Length: 254  Bit Score: 404.44  E-value: 2.42e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571    1 MLAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAQRYAEEGADELVFYDITASSDGRVVDKSWVKRVAEVIDIPFCVA 80
Cdd:TIGR00735   1 MLAKRIIPCLDVRDGRVVKGVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   81 GGIKSAEDAARILEFGADKVSINSPALANPQLITDLADKFGVQCIVVGIDSYFDKET--GKYQVYQFTGDEartkATKWE 158
Cdd:TIGR00735  81 GGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRVYVNsyCWYEVYIYGGRE----STGLD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571  159 TKDWVQEVQKRGAGEIVLNMMNQDGVRNGYDIDQLNMVRSVCNVPLIASGGAGAMEHFAEAYKKTNVDGALAASVFHKQV 238
Cdd:TIGR00735 157 AVEWAKEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPEHFYEAFTKGKADAALAASVFHYRE 236

                         250
                  ....*....|....*...
gi 490872571  239 INIGELKQYLKQQDVEVR 256
Cdd:TIGR00735 237 ITIGEVKEYLAERGIPVR 254
HisF cd04731
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ...
 4-251 7.18e-130

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: 367.18  E-value: 7.18e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   4 KRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAQRYAEEGADELVFYDITASSDGRVVDKSWVKRVAEVIDIPFCVAGGI 83
Cdd:cd04731    1 KRIIPCLDVKDGRVVKGVNFKNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571  84 KSAEDAARILEFGADKVSINSPALANPQLITDLADKFGVQCIVVGIDSYFDKEtGKYQVYqftgDEARTKATKWETKDWV 163
Cdd:cd04731   81 RSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAKRRGD-GGYEVY----THGGRKPTGLDAVEWA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571 164 QEVQKRGAGEIVLNMMNQDGVRNGYDIDQLNMVRSVCNVPLIASGGAGAMEHFAEAYKKTNVDGALAASVFHKQVINIGE 243
Cdd:cd04731  156 KEVEELGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEAFEEGGADAALAASIFHFGEYTIAE 235


                 ....*...
gi 490872571 244 LKQYLKQQ 251
Cdd:cd04731  236 LKEYLAER 243
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 5-240 6.20e-96

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: 280.52  E-value: 6.20e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571    5 RIIPCLDVRDGQVV---KGVQFRNHEIIGDIVPLAQRYAEEGADELVFYDITASSDGRVVDKSWVKRVAEVIDIPFCVAG 81
Cdd:pfam00977   1 RIIPAIDLKDGRVVrlvKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   82 GIKSAEDAARILEFGADKVSINSPALANPQLITDLADKFGVQCIVVGIDSYFDKetgkyqVYQFTGDEartkATKWETKD 161
Cdd:pfam00977  81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDARRGK------VAINGWRE----DTGIDAVE 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490872571  162 WVQEVQKRGAGEIVLNMMNQDGVRNGYDIDQLNMVRSVCNVPLIASGGAGAMEHFAEAyKKTNVDGALAASVFHKQVIN 240
Cdd:pfam00977 151 WAKELEELGAGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKEL-FTEGVDGVIAGSALYEGEIT 228
AglZ_HisF2_fam NF038364
AglZ/HisF2 family acetamidino modification protein;
2-237 3.08e-76

AglZ/HisF2 family acetamidino modification protein;


Pssm-ID: 439657  Cd Length: 248  Bit Score: 231.21  E-value: 3.08e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   2 LAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAQRYAEEGADELVFYDITASSDGRVVDKSWVKRVAEVIDIPFCVAG 81
Cdd:NF038364   1 LRPRIIPCLLLHNGGLVKTVKFKDPKYVGDPINAVRIFNEKEVDELIVLDIDATKEGREPDYELIEDLASECFMPLCYGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571  82 GIKSAEDAARILEFGADKVSINSPALANPQLITDLADKFGVQCIVVGIDsyFDKE-TGKYQVYQFTGdearTKATKWETK 160
Cdd:NF038364  81 GIKTLEQARRIFSLGVEKVALNSAALENPELITEAAEEFGSQSVVVSID--VKKNlFGGYEVYTHNG----TKKTKLDPV 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490872571 161 DWVQEVQKRGAGEIVLNMMNQDGVRNGYDIDQLNMVRSVCNVPLIASGGAGAMEHFAEAYKKTNVDGALAAS--VFHKQ 237
Cdd:NF038364 155 EFAKELEALGAGEIVLNSIDRDGTMKGYDLELIKKVSSAVSIPVIALGGAGSLEDLKEAIKQAGASAVAAGSlfVFKGK 233
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 2-257 2.49e-48

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 167.20  E-value: 2.49e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   2 LAKRIIPCLDVR-----DGQVVKGVQF--RNHEIIGDI------VPLAQRYAEEGADELVFYDITASSDGRVVDKSWV-- 66
Cdd:PLN02617 226 LAKRVIACLDVRsndkgDLVVTKGDQYdvREHSEGREVrnlgkpVELAGQYYKDGADEVAFLNITGFRDFPLGDLPMLev 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571  67 -KRVAEVIDIPFCVAGGIKSAED-----------AARILEFGADKVSINSPAL--ANPQLITDLAD----------KFGV 122
Cdd:PLN02617 306 lRRASENVFVPLTVGGGIRDFTDangryysslevASEYFRSGADKISIGSDAVyaAEEYIASGVKTgktsieqisrVYGN 385

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571 123 QCIVVGIDSYfdketgkyQVYQFTGDEARTKATKWETKD-------WVQ-------------------EVQKRGAGEIVL 176
Cdd:PLN02617 386 QAVVVSIDPR--------RVYVKDPSDVPFKTVKVTNPGpngeeyaWYQctvkggregrpigayelakAVEELGAGEILL 457

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571 177 NMMNQDGVRNGYDIDQLNMVRSVCNVPLIASGGAGAMEHFAEAYKKTNVDGALAASVFHKQVINIGELKQYLKQQDVEVR 256
Cdd:PLN02617 458 NCIDCDGQGKGFDIELVKLVSDAVTIPVIASSGAGTPEHFSDVFSKTNASAALAAGIFHRKEVPISSVKEHLLEEGIETR 537


                 .
gi 490872571 257 L 257
Cdd:PLN02617 538 I 538
 
Name Accession Description Interval E-value
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 2-257 2.44e-152

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: 424.44  E-value: 2.44e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   2 LAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAQRYAEEGADELVFYDITASSDGRVVDKSWVKRVAEVIDIPFCVAG 81
Cdd:COG0107    1 LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571  82 GIKSAEDAARILEFGADKVSINSPALANPQLITDLADKFGVQCIVVGIDSYFDkETGKYQVYQFTGdearTKATKWETKD 161
Cdd:COG0107   81 GIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRV-PDGGWEVYTHGG----RKPTGLDAVE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571 162 WVQEVQKRGAGEIVLNMMNQDGVRNGYDIDQLNMVRSVCNVPLIASGGAGAMEHFAEAYKKTNVDGALAASVFHKQVINI 241
Cdd:COG0107  156 WAKEAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITI 235

                        250
                 ....*....|....*.
gi 490872571 242 GELKQYLKQQDVEVRL 257
Cdd:COG0107  236 AELKAYLAEAGIPVRL 251
hisF TIGR00735
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ...
 1-256 2.42e-144

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


Pssm-ID: 273241  Cd Length: 254  Bit Score: 404.44  E-value: 2.42e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571    1 MLAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAQRYAEEGADELVFYDITASSDGRVVDKSWVKRVAEVIDIPFCVA 80
Cdd:TIGR00735   1 MLAKRIIPCLDVRDGRVVKGVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   81 GGIKSAEDAARILEFGADKVSINSPALANPQLITDLADKFGVQCIVVGIDSYFDKET--GKYQVYQFTGDEartkATKWE 158
Cdd:TIGR00735  81 GGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRVYVNsyCWYEVYIYGGRE----STGLD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571  159 TKDWVQEVQKRGAGEIVLNMMNQDGVRNGYDIDQLNMVRSVCNVPLIASGGAGAMEHFAEAYKKTNVDGALAASVFHKQV 238
Cdd:TIGR00735 157 AVEWAKEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPEHFYEAFTKGKADAALAASVFHYRE 236

                         250
                  ....*....|....*...
gi 490872571  239 INIGELKQYLKQQDVEVR 256
Cdd:TIGR00735 237 ITIGEVKEYLAERGIPVR 254
HisF cd04731
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ...
 4-251 7.18e-130

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: 367.18  E-value: 7.18e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   4 KRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAQRYAEEGADELVFYDITASSDGRVVDKSWVKRVAEVIDIPFCVAGGI 83
Cdd:cd04731    1 KRIIPCLDVKDGRVVKGVNFKNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571  84 KSAEDAARILEFGADKVSINSPALANPQLITDLADKFGVQCIVVGIDSYFDKEtGKYQVYqftgDEARTKATKWETKDWV 163
Cdd:cd04731   81 RSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAKRRGD-GGYEVY----THGGRKPTGLDAVEWA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571 164 QEVQKRGAGEIVLNMMNQDGVRNGYDIDQLNMVRSVCNVPLIASGGAGAMEHFAEAYKKTNVDGALAASVFHKQVINIGE 243
Cdd:cd04731  156 KEVEELGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEAFEEGGADAALAASIFHFGEYTIAE 235


                 ....*...
gi 490872571 244 LKQYLKQQ 251
Cdd:cd04731  236 LKEYLAER 243
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 5-240 6.20e-96

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: 280.52  E-value: 6.20e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571    5 RIIPCLDVRDGQVV---KGVQFRNHEIIGDIVPLAQRYAEEGADELVFYDITASSDGRVVDKSWVKRVAEVIDIPFCVAG 81
Cdd:pfam00977   1 RIIPAIDLKDGRVVrlvKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   82 GIKSAEDAARILEFGADKVSINSPALANPQLITDLADKFGVQCIVVGIDSYFDKetgkyqVYQFTGDEartkATKWETKD 161
Cdd:pfam00977  81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDARRGK------VAINGWRE----DTGIDAVE 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490872571  162 WVQEVQKRGAGEIVLNMMNQDGVRNGYDIDQLNMVRSVCNVPLIASGGAGAMEHFAEAyKKTNVDGALAASVFHKQVIN 240
Cdd:pfam00977 151 WAKELEELGAGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKEL-FTEGVDGVIAGSALYEGEIT 228
WbuZ TIGR03572
glycosyl amidation-associated protein WbuZ; This clade of sequences is highly similar to the ...
 1-235 1.55e-86

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: 256.81  E-value: 1.55e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571    1 MLAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAQRYAEEGADELVFYDITASSDGRVVDKSWVKRVAEVIDIPFCVA 80
Cdd:TIGR03572   1 MLKKRIIPCLLLKDGRLVKTVQFKDPRYIGDPVNAARIYNAKGADELIVLDIDASKRGREPLFELISNLAEECFMPLTVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   81 GGIKSAEDAARILEFGADKVSINSPALANPQLITDLADKFGVQCIVVGIDSYFDKETGKYQVYQFTGdearTKATKWETK 160
Cdd:TIGR03572  81 GGIRSLEDAKKLLSLGADKVSINTAALENPDLIEEAARRFGSQCVVVSIDVKKELDGSDYKVYSDNG----RRATGRDPV 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490872571  161 DWVQEVQKRGAGEIVLNMMNQDGVRNGYDIDQLNMVRSVCNVPLIASGGAGAMEHFAEAYKKTNVDGALAASVFH 235
Cdd:TIGR03572 157 EWAREAEQLGAGEILLNSIDRDGTMKGYDLELIKTVSDAVSIPVIALGGAGSLDDLVEVALEAGASAVAAASLFH 231
AglZ_HisF2_fam NF038364
AglZ/HisF2 family acetamidino modification protein;
2-237 3.08e-76

AglZ/HisF2 family acetamidino modification protein;


Pssm-ID: 439657  Cd Length: 248  Bit Score: 231.21  E-value: 3.08e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   2 LAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAQRYAEEGADELVFYDITASSDGRVVDKSWVKRVAEVIDIPFCVAG 81
Cdd:NF038364   1 LRPRIIPCLLLHNGGLVKTVKFKDPKYVGDPINAVRIFNEKEVDELIVLDIDATKEGREPDYELIEDLASECFMPLCYGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571  82 GIKSAEDAARILEFGADKVSINSPALANPQLITDLADKFGVQCIVVGIDsyFDKE-TGKYQVYQFTGdearTKATKWETK 160
Cdd:NF038364  81 GIKTLEQARRIFSLGVEKVALNSAALENPELITEAAEEFGSQSVVVSID--VKKNlFGGYEVYTHNG----TKKTKLDPV 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490872571 161 DWVQEVQKRGAGEIVLNMMNQDGVRNGYDIDQLNMVRSVCNVPLIASGGAGAMEHFAEAYKKTNVDGALAAS--VFHKQ 237
Cdd:NF038364 155 EFAKELEALGAGEIVLNSIDRDGTMKGYDLELIKKVSSAVSIPVIALGGAGSLEDLKEAIKQAGASAVAAGSlfVFKGK 233
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 2-257 2.49e-48

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 167.20  E-value: 2.49e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   2 LAKRIIPCLDVR-----DGQVVKGVQF--RNHEIIGDI------VPLAQRYAEEGADELVFYDITASSDGRVVDKSWV-- 66
Cdd:PLN02617 226 LAKRVIACLDVRsndkgDLVVTKGDQYdvREHSEGREVrnlgkpVELAGQYYKDGADEVAFLNITGFRDFPLGDLPMLev 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571  67 -KRVAEVIDIPFCVAGGIKSAED-----------AARILEFGADKVSINSPAL--ANPQLITDLAD----------KFGV 122
Cdd:PLN02617 306 lRRASENVFVPLTVGGGIRDFTDangryysslevASEYFRSGADKISIGSDAVyaAEEYIASGVKTgktsieqisrVYGN 385

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571 123 QCIVVGIDSYfdketgkyQVYQFTGDEARTKATKWETKD-------WVQ-------------------EVQKRGAGEIVL 176
Cdd:PLN02617 386 QAVVVSIDPR--------RVYVKDPSDVPFKTVKVTNPGpngeeyaWYQctvkggregrpigayelakAVEELGAGEILL 457

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571 177 NMMNQDGVRNGYDIDQLNMVRSVCNVPLIASGGAGAMEHFAEAYKKTNVDGALAASVFHKQVINIGELKQYLKQQDVEVR 256
Cdd:PLN02617 458 NCIDCDGQGKGFDIELVKLVSDAVTIPVIASSGAGTPEHFSDVFSKTNASAALAAGIFHRKEVPISSVKEHLLEEGIETR 537


                 .
gi 490872571 257 L 257
Cdd:PLN02617 538 I 538
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 5-246 1.19e-33

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: 121.43  E-value: 1.19e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   5 RIIPCLDVRDGQVV---KGVQFRNHEIIGDIVPLAQRYAEEGADELVFYDITASSDGRVVDKSWVKRVAEVIDIPFCVAG 81
Cdd:cd04732    1 IIIPAIDLKDGKCVrlyQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571  82 GIKSAEDAARILEFGADKVSINSPALANPQLITDLADKFGVQCIVVGIDSYfdketGKYQVYQftGDEARTKATKWetkD 161
Cdd:cd04732   81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLDAK-----DGKVATK--GWLETSEVSLE---E 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571 162 WVQEVQKRGAGEIVLNMMNQDGVRNGYDIDQLNMVRSVCNVPLIASGGAGAMEHFAEAyKKTNVDGALAASVFHKQVINI 241
Cdd:cd04732  151 LAKRFEELGVKAIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDDIKAL-KELGVAGVIVGKALYEGKITL 229


                 ....*
gi 490872571 242 GELKQ 246
Cdd:cd04732  230 EEALA 234
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 6-243 4.39e-28

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


Pssm-ID: 184165  Cd Length: 241  Bit Score: 107.30  E-value: 4.39e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   6 IIPCLDVRDGQVVKGVQFR---NHEIIGDIVPLAQRYAEEGADELVFYDITASSDGRVVDKSWVKRVAEVIDIPFCVAGG 82
Cdd:PRK13585   5 VIPAVDMKGGKCVQLVQGEpgtETVSYGDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEKIIEAVGVPVQLGGG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571  83 IKSAEDAARILEFGADKVSINSPALANPQLITDLADKFGVQCIVVGIDSyfdkETGKYQVyqftgdEARTKATKWETKDW 162
Cdd:PRK13585  85 IRSAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEFGSERVMVSLDA----KDGEVVI------KGWTEKTGYTPVEA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571 163 VQEVQKRGAGEIVLNMMNQDGVRNGYDIDQL-NMVRSVcNVPLIASGGAGAMEHFAeAYKKTNVDGALAASVFHKQVINI 241
Cdd:PRK13585 155 AKRFEELGAGSILFTNVDVEGLLEGVNTEPVkELVDSV-DIPVIASGGVTTLDDLR-ALKEAGAAGVVVGSALYKGKFTL 232


                 ..
gi 490872571 242 GE 243
Cdd:PRK13585 233 EE 234
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 5-228 5.03e-28

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: 107.05  E-value: 5.03e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   5 RIIPCLDVRDGQVV---KGVQFRNHEIIGDIVPLAQRYAEEGADEL--VfyDITASSDGRVVDKSWVKRVAEVIDIPFCV 79
Cdd:COG0106    1 IIIPAIDLKDGKCVrlvQGDYDQETVYSDDPVEVAKRWEDAGAEWLhlV--DLDGAFAGKPVNLELIEEIAKATGLPVQV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571  80 AGGIKSAEDAARILEFGADKVSINSPALANPQLITDLADKFGVQcIVVGIDSYfdkeTGKYQVyqftgdEARTKATKWET 159
Cdd:COG0106   79 GGGIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPER-IVVGLDAR----DGKVAT------DGWQETSGVDL 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490872571 160 KDWVQEVQKRGAGEIVLNMMNQDGVRNGYDIDQLNMVRSVCNVPLIASGGAGAMEHFaEAYKKTNVDGA 228
Cdd:COG0106  148 EELAKRFEDAGVAAILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDL-RALKELGVEGA 215
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 6-243 3.85e-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: 101.89  E-value: 3.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571    6 IIPCLDVRDGQVVKGVQ--FRNHEIIGD-IVPLAQRYAEEGADELVFYDITASSDGRVVDKSWVKRVAEVIDIPFCVAGG 82
Cdd:TIGR00007   1 IIPAIDIKDGKCVRLYQgdYDKETVYGDdPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   83 IKSAEDAARILEFGADKVSINSPALANPQLITDLADKFGVQCIVVGIDSYFD-------KETGKYQVYQFtgdeartkat 155
Cdd:TIGR00007  81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSLDARGGevavkgwLEKSEVSLEEL---------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571  156 kwetkdwVQEVQKRGAGEIVLNMMNQDGVRNGYDIDQLNMVRSVCNVPLIASGGAGAMEHFAEAyKKTNVDGALAASVFH 235
Cdd:TIGR00007 151 -------AKRLEELGLEGIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSIDDLIAL-KKLGVYGVIVGKALY 222


                  ....*...
gi 490872571  236 KQVINIGE 243
Cdd:TIGR00007 223 EGKITLEE 230
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 5-246 3.30e-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: 91.56  E-value: 3.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   5 RIIPCLDVRDGQVVKGVQFR---------NHEIIGDIVPLAQRYAEEGADELVFYDITASSdGRVVDKSWVKRVAEVIDI 75
Cdd:cd04723    1 RIIPVIDLKDGVVVHGVGGDrdnyrpitsNLCSTSDPLDVARAYKELGFRGLYIADLDAIM-GRGDNDEAIRELAAAWPL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571  76 PFCVAGGIKSAEDAARILEFGADKVSINSPALANpQLITDLADKFGVQCIVVGIDsyfdketgkyqvyqFTGDEARTKAT 155
Cdd:cd04723   80 GLWVDGGIRSLENAQEWLKRGASRVIVGTETLPS-DDDEDRLAALGEQRLVLSLD--------------FRGGQLLKPTD 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571 156 KWETKDWVQEVQKRgAGEIVLNMMNQDGVRNGYDIDQLNMVRSVCNVPLIASGGAGAMEHFaEAYKKTNVDGALAASVFH 235
Cdd:cd04723  145 FIGPEELLRRLAKW-PEELIVLDIDRVGSGQGPDLELLERLAARADIPVIAAGGVRSVEDL-ELLKKLGASGALVASALH 222

                        250
                 ....*....|.
gi 490872571 236 KQVINIGELKQ 246
Cdd:cd04723  223 DGGLTLEDVVR 233
PRK00748 PRK00748
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 6-228 8.12e-22

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


Pssm-ID: 179108  Cd Length: 233  Bit Score: 90.51  E-value: 8.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   6 IIPCLDVRDGQVVKGVQ--FRNHEIIG-DIVPLAQRYAEEGADELVFYDITASSDGRVVDKSWVKRVAEVIDIPFCVAGG 82
Cdd:PRK00748   3 IIPAIDLKDGKCVRLYQgdYDQATVYSdDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGGG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571  83 IKSAEDAARILEFGADKVSINSPALANPQLITDLADKFGVQcIVVGIDsyfdketgkyqvyqftgdeARTK--ATK-WET 159
Cdd:PRK00748  83 IRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFPGK-IVVGLD-------------------ARDGkvATDgWLE 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490872571 160 K------DWVQEVQKRGAGEIVLNMMNQDGVRNGYDIDQLNMVRSVCNVPLIASGGAGAMEHFAEAYKKTNVDGA 228
Cdd:PRK00748 143 TsgvtaeDLAKRFEDAGVKAIIYTDISRDGTLSGPNVEATRELAAAVPIPVIASGGVSSLDDIKALKGLGAVEGV 217
PRK14024 PRK14024
phosphoribosyl isomerase A; Provisional
 6-229 1.59e-12

phosphoribosyl isomerase A; Provisional


Pssm-ID: 237589  Cd Length: 241  Bit Score: 65.36  E-value: 1.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   6 IIPCLDVRDGQVVKGVQFR--NHEIIGDIVPLAQRYAEEGADELVFYDITASSdGRVVDKSWVKRVAEVIDIPFCVAGGI 83
Cdd:PRK14024   6 LLPAVDVVDGQAVRLVQGEagSETSYGSPLDAALAWQRDGAEWIHLVDLDAAF-GRGSNRELLAEVVGKLDVKVELSGGI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571  84 KSAEDAARILEFGADKVSINSPALANPQLITDLADKFGVQcIVVGIDSyfdketgkyqvyqftgDEARTKATKWeTKD-- 161
Cdd:PRK14024  85 RDDESLEAALATGCARVNIGTAALENPEWCARVIAEHGDR-VAVGLDV----------------RGHTLAARGW-TRDgg 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490872571 162 --WvqEVQKR----GAGEIVLNMMNQDGVRNGYDIDQLNMVRSVCNVPLIASGGAGAMEHFAE--AYKKTNVDGAL 229
Cdd:PRK14024 147 dlW--EVLERldsaGCSRYVVTDVTKDGTLTGPNLELLREVCARTDAPVVASGGVSSLDDLRAlaELVPLGVEGAI 220
PRK13586 PRK13586
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 5-214 1.02e-08

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


Pssm-ID: 237439  Cd Length: 232  Bit Score: 54.36  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   5 RIIPCLDVRDGQVVKGVQFRNHE--IIGDIVPLAQRYAEEGADELVFYDITASsDGRVVDKSWVKRVAEVIDIPFCVAGG 82
Cdd:PRK13586   3 KIIPSIDISLGKAVKRIRGVKGTglILGNPIEIASKLYNEGYTRIHVVDLDAA-EGVGNNEMYIKEISKIGFDWIQVGGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571  83 IKSAEDAARILEFGADKVSINSPALANPQLITDLADKFGVQCIVVGIDsyFDketgkyqvyqftgDEARTKATKWETK-- 160
Cdd:PRK13586  82 IRDIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGSNRVLVSID--YD-------------NTKRVLIRGWKEKsm 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490872571 161 ---DWVQEVQKRGAGEIVLNMMNQDGVRNGYDIDQLNMVRSVCNVPLIAsGGAGAME 214
Cdd:PRK13586 147 eviDGIKKVNELELLGIIFTYISNEGTTKGIDYNVKDYARLIRGLKEYA-GGVSSDA 202
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
 31-120 2.04e-08

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: 53.94  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571  31 DIVPLAQRYAEEGADELV--------FYDITAssdgrvvDKSWVKRVAEVIDIPFCVAGGIKSAEDAARILE-FGADKVS 101
Cdd:COG0042  147 NALEFARIAEDAGAAALTvhgrtreqRYKGPA-------DWDAIARVKEAVSIPVIGNGDIFSPEDAKRMLEeTGCDGVM 219

                         90
                 ....*....|....*....
gi 490872571 102 INSPALANPQLITDLADKF 120
Cdd:COG0042  220 IGRGALGNPWLFREIDAYL 238
PRK14114 PRK14114
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 6-247 2.35e-08

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


Pssm-ID: 172604  Cd Length: 241  Bit Score: 53.09  E-value: 2.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   6 IIPCLDVRDGQVVKGVQFRNHEII---GDIVPLAQRYAEEGADELVFYDITASSDGRVVDKSWVKRVAEVIDiPFCVAGG 82
Cdd:PRK14114   3 VVPAIDLFRGKVARMVKGKKENTIfyeKDPAELVEKLIEEGFTLIHVVDLSKAIENSVENLPVLEKLSEFAE-HIQIGGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571  83 IKSAEDAARILEFGADKVSINSPALANPQLITDLadkfgvqcivvgidsyfdKETGKYQVYQFTGDEARTKATKWETKD- 161
Cdd:PRK14114  82 IRSLDYAEKLRKLGYRRQIVSSKVLEDPSFLKFL------------------KEIDVEPVFSLDTRGGKVAFKGWLAEEe 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571 162 -----WVQEVQKRGAGEIVLNMMNQDGVRNGYDIDQLNMVRSVCNVPLIASGGAG---AMEHFAEAYKKTN--VDGALAA 231
Cdd:PRK14114 144 idpvsLLKRLKEYGLEEIVHTEIEKDGTLQEHDFSLTRKIAIEAEVKVFAAGGISsenSLKTAQRVHRETNglLKGVIVG 223

                        250
                 ....*....|....*.
gi 490872571 232 SVFHKQVINIGELKQY 247
Cdd:PRK14114 224 RAFLEGILTVEVMKRY 239
OYE_like_FMN_family cd02803
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
 29-118 1.11e-06

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: 48.72  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571  29 IGDIVPLAQRYAEEGAD---------ELVFYDITASSDGRVVDKSWVKRVAEVIDIPFCVAGGIKSAEDAARIL-EFGAD 98
Cdd:cd02803  227 LEEAIEIAKALEEAGVDalhvsggsyESPPPIIPPPYVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILaEGKAD 306

                         90       100
                 ....*....|....*....|
gi 490872571  99 KVSINSPALANPQLITDLAD 118
Cdd:cd02803  307 LVALGRALLADPDLPNKARE 326
PRK04128 PRK04128
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 5-135 1.48e-06

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


Pssm-ID: 167709  Cd Length: 228  Bit Score: 47.84  E-value: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   5 RIIPCLDVRDGQVVKGVQFRNHEI--IGDIVPLAQRYAEEgADELVFYDITASSDGRVVDKSWVKRVAEVIDIPFCVAGG 82
Cdd:PRK04128   3 RIYPAIDLMNGKAVRLYKGRKEEVkvYGDPVEIALRFSEY-VDKIHVVDLDGAFEGKPKNLDVVKNIIRETGLKVQVGGG 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490872571  83 IKSAEDAARILEFGADKVSINSPALaNPQLITDLADKFGvqCIVVGIDSYFDK 135
Cdd:PRK04128  82 LRTYESIKDAYEIGVENVIIGTKAF-DLEFLEKVTSEFE--GITVSLDVKGGR 131
OYE_like_4_FMN cd04735
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ...
 58-137 1.80e-06

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: 48.36  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571  58 GRVVDKSWVKRVAEVID--IPFCVAGGIKSAEDAARILEFGADKVSINSPALANPQLITDLADKFGVQcivvgIDSYFDK 135
Cdd:cd04735  266 GRDDNQTIMELVKERIAgrLPLIAVGSINTPDDALEALETGADLVAIGRGLLVDPDWVEKIKEGREDE-----INLEIDP 340


                 ..
gi 490872571 136 ET 137
Cdd:cd04735  341 DD 342
FadH COG1902
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ...
 31-118 2.08e-06

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: 47.86  E-value: 2.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571  31 DIVPLAQRYAEEGAD--ELV--FYDITASSDGRVVDKSWV---KRVAEVIDIPFCVAGGIKSAEDAARILEFG-ADKVSI 102
Cdd:COG1902  237 ESVELAKALEEAGVDylHVSsgGYEPDAMIPTIVPEGYQLpfaARIRKAVGIPVIAVGGITTPEQAEAALASGdADLVAL 316

                         90
                 ....*....|....*.
gi 490872571 103 NSPALANPQLITDLAD 118
Cdd:COG1902  317 GRPLLADPDLPNKAAA 332
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 5-104 3.04e-06

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


Pssm-ID: 184165  Cd Length: 241  Bit Score: 46.82  E-value: 3.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   5 RIIPCLDVRDGQVV-KGVQfrnhEIIG-DIVPLAQRYAEEGADELVFYDItaSSDGRV--VDKSWVKRVAEVIDIPFCVA 80
Cdd:PRK13585 126 RVMVSLDAKDGEVViKGWT----EKTGyTPVEAAKRFEELGAGSILFTNV--DVEGLLegVNTEPVKELVDSVDIPVIAS 199

                         90       100
                 ....*....|....*....|....
gi 490872571  81 GGIKSAEDAARILEFGADKVSINS 104
Cdd:PRK13585 200 GGVTTLDDLRALKEAGAAGVVVGS 223
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 4-98 3.07e-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: 47.09  E-value: 3.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   4 KRIIPCLDVRDGQV-VKGVQfRNHEIigDIVPLAQRYAEEGADELVFYDItaSSDGRV--VDKSWVKRVAEVIDIPFCVA 80
Cdd:cd04732  122 ERIVVGLDAKDGKVaTKGWL-ETSEV--SLEELAKRFEELGVKAIIYTDI--SRDGTLsgPNFELYKELAAATGIPVIAS 196

                         90
                 ....*....|....*...
gi 490872571  81 GGIKSAEDAARILEFGAD 98
Cdd:cd04732  197 GGVSSLDDIKALKELGVA 214
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 3-104 3.79e-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: 3.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   3 AKRIIPCLDVRDGQVVKGVQF-RNHEIIgdivplaqRYAEEGADELVFYDITASSDGRVVDKSWVKRVAEVIDIPFCVAG 81
Cdd:cd04723  125 EQRLVLSLDFRGGQLLKPTDFiGPEELL--------RRLAKWPEELIVLDIDRVGSGQGPDLELLERLAARADIPVIAAG 196

                         90       100
                 ....*....|....*....|...
gi 490872571  82 GIKSAEDAARILEFGADKVSINS 104
Cdd:cd04723  197 GVRSVEDLELLKKLGASGALVAS 219
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 35-120 4.21e-06

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: 46.33  E-value: 4.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571  35 LAQRYAEEGADELVFYditassdGRV--------VDKSWVKRVAEVIDIPFCVAGGIKSAEDAARILE-FGADKVSINSP 105
Cdd:cd02801  143 LAKALEDAGASALTVH-------GRTreqrysgpADWDYIAEIKEAVSIPVIANGDIFSLEDALRCLEqTGVDGVMIGRG 215

                         90
                 ....*....|....*
gi 490872571 106 ALANPQLITDLADKF 120
Cdd:cd02801  216 ALGNPWLFREIKELL 230
PcrB COG1646
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];
44-98 1.11e-05

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


Pssm-ID: 441252  Cd Length: 241  Bit Score: 45.15  E-value: 1.11e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490872571  44 ADEL----VFYdITASSD-GRVVDKSWVKRVAEVI-DIPFCVAGGIKSAEDAARILEFGAD 98
Cdd:COG1646  161 AEEYlgmpIVY-LEYGSGaGEPVDPEMVKAVKKALeDTPLIYGGGIRSPEKAREMAEAGAD 220
Dus pfam01207
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ...
 31-113 1.42e-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: 45.39  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   31 DIVPLAQRYAEEGADELV--------FYDITAssdgrvvDKSWVKRVAEVIDIPFCVAGGIKSAEDAARILEF-GADKVS 101
Cdd:pfam01207 139 NAVEIAKIVEDAGAQALTvhgrtraqNYEGTA-------DWDAIKQVKQAVSIPVIANGDITDPEDAQRCLAYtGADGVM 211

                          90
                  ....*....|..
gi 490872571  102 INSPALANPQLI 113
Cdd:pfam01207 212 IGRGALGNPWLF 223
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 4-102 1.74e-05

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: 44.50  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571    4 KRIIPCLDVRDGQV-VKGvqFRNHEIIgDIVPLAQRYAEEGADELVFYDItaSSDGRV--VDKSWVKRVAEVIDIPFCVA 80
Cdd:TIGR00007 121 ERIVVSLDARGGEVaVKG--WLEKSEV-SLEELAKRLEELGLEGIIYTDI--SRDGTLsgPNFELTKELVKAVNVPVIAS 195

                          90       100
                  ....*....|....*....|..
gi 490872571   81 GGIKSAEDAARILEFGADKVSI 102
Cdd:TIGR00007 196 GGVSSIDDLIALKKLGVYGVIV 217
PcrB_like cd02812
PcrB_like proteins. One member of this family, a protein from Archaeoglobus fulgidus, has been ...
 58-102 1.12e-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: 42.23  E-value: 1.12e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 490872571  58 GRVVDKSWVKRVAEVI-DIPFCVAGGIKSAEDAARILEFGADKVSI 102
Cdd:cd02812  158 GAYGPPEVVRAVKKVLgDTPLIVGGGIRSGEQAKEMAEAGADTIVV 203
PLN02591 PLN02591
tryptophan synthase
 54-104 4.65e-04

tryptophan synthase


Pssm-ID: 178201  Cd Length: 250  Bit Score: 40.42  E-value: 4.65e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490872571  54 ASSDGRVvdKSWVKRVAEVIDIPFCVAGGIKSAEDAARILEFGADKVSINS 104
Cdd:PLN02591 171 ASVSGRV--ESLLQELKEVTDKPVAVGFGISKPEHAKQIAGWGADGVIVGS 219
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 66-114 5.22e-04

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


Pssm-ID: 240080 [Multi-domain]  Cd Length: 219  Bit Score: 40.25  E-value: 5.22e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 490872571  66 VKRVAEVIDIPFCVAGGIKSAEDAARILEFGADKVSINSpALANPQLIT 114
Cdd:cd04729  169 LKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVGS-AITRPEHIT 216
PRK13587 PRK13587
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 51-237 5.85e-04

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


Pssm-ID: 172156  Cd Length: 234  Bit Score: 40.20  E-value: 5.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571  51 DITASSDGRVVDKSWVKRVAEVIDIPFCVAGGIKSAEDAARILEFGADKVSINSPALANPQLITDLADKFGVQcIVVGID 130
Cdd:PRK13587  53 DLIGAKAQHAREFDYIKSLRRLTTKDIEVGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGR-IYLSVD 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571 131 SYFDKetgkyqvyqftgdearTKATKWETK------DWVQEVQKRGAGEIVLNMMNQDGVRNGYDIDQLNMVRSVCNVPL 204
Cdd:PRK13587 132 AYGED----------------IKVNGWEEDtelnlfSFVRQLSDIPLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPV 195

                        170       180       190
                 ....*....|....*....|....*....|...
gi 490872571 205 IASGGAGAMEHFAEaYKKTNVDGALAASVFHKQ 237
Cdd:PRK13587 196 IASGGIRHQQDIQR-LASLNVHAAIIGKAAHQA 227
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 39-104 9.57e-04

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: 39.11  E-value: 9.57e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490872571  39 YAEEGADELV---FYDITASSDGRVVDKSWVKRVAEVIDIPFCVAGGIKSAEDAARILEFGADKVSINS 104
Cdd:cd04722  132 AEEAGVDEVGlgnGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
PRK04169 PRK04169
heptaprenylglyceryl phosphate synthase;
48-98 2.47e-03

heptaprenylglyceryl phosphate synthase;


Pssm-ID: 235237  Cd Length: 232  Bit Score: 38.25  E-value: 2.47e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490872571  48 VFYdITASSD-GRVVDKSWVKRVAEVIDI-PFCVAGGIKSAEDAARILEFGAD 98
Cdd:PRK04169 157 IVY-LEYGGGaGDPVPPEMVKAVKKALDItPLIYGGGIRSPEQARELMAAGAD 208
DCR_FMN cd02930
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ...
 64-113 3.29e-03

2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur flavoenzyme which contains FMN, FAD, and a 4Fe-4S cluster. It is also a monomer, unlike that of its eukaryotic counterparts which form homotetramers and lack the flavin and iron-sulfur cofactors. Metabolism of unsaturated fatty acids requires auxiliary enzymes in addition to those used in b-oxidation. After a given number of cycles through the b-oxidation pathway, those unsaturated fatty acyl-CoAs with double bonds at even-numbered carbon positions contain 2-trans, 4-cis double bonds that can not be modified by enoyl-CoA hydratase. DCR utilizes NADPH to remove the C4-C5 double bond. DCR can catalyze the reduction of both natural fatty acids with cis double bonds, as well as substrates containing trans double bonds. The reaction is initiated by hybrid transfer from NADPH to FAD, which in turn transfers electrons, one at a time, to FMN via the 4Fe-4S cluster. The fully reduced FMN provides a hydrid ion to the C5 atom of substrate, and Tyr and His are proposed to form a catalytic dyad that protonates the C4 atom of the substrate and completes the reaction.


Pssm-ID: 239240 [Multi-domain]  Cd Length: 353  Bit Score: 38.42  E-value: 3.29e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490872571  64 SWV-KRVAEVIDIPFCVAGGIKSAEDAARILEFG-ADKVSINSPALANPQLI 113
Cdd:cd02930  265 AWAtAKLKRAVDIPVIASNRINTPEVAERLLADGdADMVSMARPFLADPDFV 316
PRK00748 PRK00748
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 5-97 5.11e-03

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


Pssm-ID: 179108  Cd Length: 233  Bit Score: 37.35  E-value: 5.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490872571   5 RIIPCLDVRDGQV-VKGVQfrnhEIIG-DIVPLAQRYAEEGADELVFYDItaSSDGRV--VDKSWVKRVAEVIDIPFCVA 80
Cdd:PRK00748 123 KIVVGLDARDGKVaTDGWL----ETSGvTAEDLAKRFEDAGVKAIIYTDI--SRDGTLsgPNVEATRELAAAVPIPVIAS 196

                         90
                 ....*....|....*..
gi 490872571  81 GGIKSAEDAARILEFGA 97
Cdd:PRK00748 197 GGVSSLDDIKALKGLGA 213
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
66-114 6.91e-03

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


Pssm-ID: 234907  Cd Length: 221  Bit Score: 36.66  E-value: 6.91e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 490872571  66 VKRVAEVIDIPFCVAGGIKSAEDAARILEFGADKVSINSpALANPQLIT 114
Cdd:PRK01130 165 LKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVGG-AITRPEEIT 212
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH