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Conserved domains on  [gi|1918169413|ref|WP_192971321|]
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MULTISPECIES: imidazole glycerol phosphate synthase subunit HisF [Enterobacter]

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 5.95e-150

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: 418.27  E-value: 5.95e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   2 LAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYADEGADELVFYDITASSDGRVVDKSWVARVAEVIDIPFCVAG 81
Cdd:COG0107     1 LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  82 GIKSADDAAKILSFGADKISINSPALAEPELITRLADRFGVQCIVVGIDTWFDaATGKYHVNQYTGDESrtrvTQWETLD 161
Cdd:COG0107    81 GIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRV-PDGGWEVYTHGGRKP----TGLDAVE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413 162 WVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVRAVCHVPLIASGGAGTMEHFLEALRDANVDGALAASVFHKQIINI 241
Cdd:COG0107   156 WAKEAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITI 235

                         250
                  ....*....|....*
gi 1918169413 242 GELKTYLADQGVEIR 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 5.95e-150

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: 418.27  E-value: 5.95e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   2 LAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYADEGADELVFYDITASSDGRVVDKSWVARVAEVIDIPFCVAG 81
Cdd:COG0107     1 LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  82 GIKSADDAAKILSFGADKISINSPALAEPELITRLADRFGVQCIVVGIDTWFDaATGKYHVNQYTGDESrtrvTQWETLD 161
Cdd:COG0107    81 GIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRV-PDGGWEVYTHGGRKP----TGLDAVE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413 162 WVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVRAVCHVPLIASGGAGTMEHFLEALRDANVDGALAASVFHKQIINI 241
Cdd:COG0107   156 WAKEAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITI 235

                         250
                  ....*....|....*
gi 1918169413 242 GELKTYLADQGVEIR 256
Cdd:COG0107   236 AELKAYLAEAGIPVR 250
hisF TIGR00735
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ...
 1-256 8.66e-150

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


Pssm-ID: 273241  Cd Length: 254  Bit Score: 417.92  E-value: 8.66e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   1 MLAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYADEGADELVFYDITASSDGRVVDKSWVARVAEVIDIPFCVA 80
Cdd:TIGR00735   1 MLAKRIIPCLDVRDGRVVKGVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  81 GGIKSADDAAKILSFGADKISINSPALAEPELITRLADRFGVQCIVVGIDTWFDAAT--GKYHVNQYTGDESrtrvTQWE 158
Cdd:TIGR00735  81 GGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRVYVNsyCWYEVYIYGGRES----TGLD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413 159 TLDWVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVRAVCHVPLIASGGAGTMEHFLEALRDANVDGALAASVFHKQI 238
Cdd:TIGR00735 157 AVEWAKEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPEHFYEAFTKGKADAALAASVFHYRE 236

                         250
                  ....*....|....*...
gi 1918169413 239 INIGELKTYLADQGVEIR 256
Cdd:TIGR00735 237 ITIGEVKEYLAERGIPVR 254
HisF cd04731
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ...
 4-251 1.95e-127

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: 361.01  E-value: 1.95e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   4 KRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYADEGADELVFYDITASSDGRVVDKSWVARVAEVIDIPFCVAGGI 83
Cdd:cd04731     1 KRIIPCLDVKDGRVVKGVNFKNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  84 KSADDAAKILSFGADKISINSPALAEPELITRLADRFGVQCIVVGIDtwfdaATGKYHVNQYTGDESRTRVTQWETLDWV 163
Cdd:cd04731    81 RSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSID-----AKRRGDGGYEVYTHGGRKPTGLDAVEWA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413 164 QEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVRAVCHVPLIASGGAGTMEHFLEALRDANVDGALAASVFHKQIINIGE 243
Cdd:cd04731   156 KEVEELGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEAFEEGGADAALAASIFHFGEYTIAE 235


                  ....*...
gi 1918169413 244 LKTYLADQ 251
Cdd:cd04731   236 LKEYLAER 243
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 5-240 2.45e-94

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


Pssm-ID: 425971  Cd Length: 228  Bit Score: 276.67  E-value: 2.45e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   5 RIIPCLDVRDGQVV---KGVQFRNHEIIGDIVPLAKRYADEGADELVFYDITASSDGRVVDKSWVARVAEVIDIPFCVAG 81
Cdd:pfam00977   1 RIIPAIDLKDGRVVrlvKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  82 GIKSADDAAKILSFGADKISINSPALAEPELITRLADRFGVQCIVVGIDTWFdaatGKyhVNQYTGDEsrtrVTQWETLD 161
Cdd:pfam00977  81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDARR----GK--VAINGWRE----DTGIDAVE 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1918169413 162 WVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVRAVCHVPLIASGGAGTMEHFLEaLRDANVDGALAASVFHKQIIN 240
Cdd:pfam00977 151 WAKELEELGAGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKE-LFTEGVDGVIAGSALYEGEIT 228
AglZ_HisF2_fam NF038364
AglZ/HisF2 family acetamidino modification protein;
2-237 1.51e-76

AglZ/HisF2 family acetamidino modification protein;


Pssm-ID: 439657  Cd Length: 248  Bit Score: 231.98  E-value: 1.51e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   2 LAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYADEGADELVFYDITASSDGRVVDKSWVARVAEVIDIPFCVAG 81
Cdd:NF038364    1 LRPRIIPCLLLHNGGLVKTVKFKDPKYVGDPINAVRIFNEKEVDELIVLDIDATKEGREPDYELIEDLASECFMPLCYGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  82 GIKSADDAAKILSFGADKISINSPALAEPELITRLADRFGVQCIVVGID---TWFdaatGKYHVnqYTgdESRTRVTQWE 158
Cdd:NF038364   81 GIKTLEQARRIFSLGVEKVALNSAALENPELITEAAEEFGSQSVVVSIDvkkNLF----GGYEV--YT--HNGTKKTKLD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413 159 TLDWVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVRAVCHVPLIASGGAGTMEHFLEALRDANVDGALAAS--VFHK 236
Cdd:NF038364  153 PVEFAKELEALGAGEIVLNSIDRDGTMKGYDLELIKKVSSAVSIPVIALGGAGSLEDLKEAIKQAGASAVAAGSlfVFKG 232


                  .
gi 1918169413 237 Q 237
Cdd:NF038364  233 K 233
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 2-257 2.93e-43

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 153.71  E-value: 2.93e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   2 LAKRIIPCLDVR-----DGQVVKGVQF--RNHEIIGDI------VPLAKRYADEGADELVFYDITASSDGRVVDKSWVA- 67
Cdd:PLN02617  226 LAKRVIACLDVRsndkgDLVVTKGDQYdvREHSEGREVrnlgkpVELAGQYYKDGADEVAFLNITGFRDFPLGDLPMLEv 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  68 --RVAEVIDIPFCVAGGIKSADD-----------AAKILSFGADKISINSPAL--AEPELITRLAD----------RFGV 122
Cdd:PLN02617  306 lrRASENVFVPLTVGGGIRDFTDangryysslevASEYFRSGADKISIGSDAVyaAEEYIASGVKTgktsieqisrVYGN 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413 123 QCIVVGIDTwfdaatGKYHVNQYTGDESRT-RVTQ----WETLDWVQ-------------------EVQKRGAGEIVLNM 178
Cdd:PLN02617  386 QAVVVSIDP------RRVYVKDPSDVPFKTvKVTNpgpnGEEYAWYQctvkggregrpigayelakAVEELGAGEILLNC 459

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1918169413 179 MNQDGVRNGYDLEQLKKVRAVCHVPLIASGGAGTMEHFLEALRDANVDGALAASVFHKQIINIGELKTYLADQGVEIRV 257
Cdd:PLN02617  460 IDCDGQGKGFDIELVKLVSDAVTIPVIASSGAGTPEHFSDVFSKTNASAALAAGIFHRKEVPISSVKEHLLEEGIETRI 538
 
Name Accession Description Interval E-value
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 2-256 5.95e-150

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: 418.27  E-value: 5.95e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   2 LAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYADEGADELVFYDITASSDGRVVDKSWVARVAEVIDIPFCVAG 81
Cdd:COG0107     1 LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  82 GIKSADDAAKILSFGADKISINSPALAEPELITRLADRFGVQCIVVGIDTWFDaATGKYHVNQYTGDESrtrvTQWETLD 161
Cdd:COG0107    81 GIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRV-PDGGWEVYTHGGRKP----TGLDAVE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413 162 WVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVRAVCHVPLIASGGAGTMEHFLEALRDANVDGALAASVFHKQIINI 241
Cdd:COG0107   156 WAKEAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITI 235

                         250
                  ....*....|....*
gi 1918169413 242 GELKTYLADQGVEIR 256
Cdd:COG0107   236 AELKAYLAEAGIPVR 250
hisF TIGR00735
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ...
 1-256 8.66e-150

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


Pssm-ID: 273241  Cd Length: 254  Bit Score: 417.92  E-value: 8.66e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   1 MLAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYADEGADELVFYDITASSDGRVVDKSWVARVAEVIDIPFCVA 80
Cdd:TIGR00735   1 MLAKRIIPCLDVRDGRVVKGVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  81 GGIKSADDAAKILSFGADKISINSPALAEPELITRLADRFGVQCIVVGIDTWFDAAT--GKYHVNQYTGDESrtrvTQWE 158
Cdd:TIGR00735  81 GGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRVYVNsyCWYEVYIYGGRES----TGLD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413 159 TLDWVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVRAVCHVPLIASGGAGTMEHFLEALRDANVDGALAASVFHKQI 238
Cdd:TIGR00735 157 AVEWAKEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPEHFYEAFTKGKADAALAASVFHYRE 236

                         250
                  ....*....|....*...
gi 1918169413 239 INIGELKTYLADQGVEIR 256
Cdd:TIGR00735 237 ITIGEVKEYLAERGIPVR 254
HisF cd04731
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ...
 4-251 1.95e-127

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: 361.01  E-value: 1.95e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   4 KRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYADEGADELVFYDITASSDGRVVDKSWVARVAEVIDIPFCVAGGI 83
Cdd:cd04731     1 KRIIPCLDVKDGRVVKGVNFKNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  84 KSADDAAKILSFGADKISINSPALAEPELITRLADRFGVQCIVVGIDtwfdaATGKYHVNQYTGDESRTRVTQWETLDWV 163
Cdd:cd04731    81 RSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSID-----AKRRGDGGYEVYTHGGRKPTGLDAVEWA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413 164 QEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVRAVCHVPLIASGGAGTMEHFLEALRDANVDGALAASVFHKQIINIGE 243
Cdd:cd04731   156 KEVEELGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEAFEEGGADAALAASIFHFGEYTIAE 235


                  ....*...
gi 1918169413 244 LKTYLADQ 251
Cdd:cd04731   236 LKEYLAER 243
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 5-240 2.45e-94

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


Pssm-ID: 425971  Cd Length: 228  Bit Score: 276.67  E-value: 2.45e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   5 RIIPCLDVRDGQVV---KGVQFRNHEIIGDIVPLAKRYADEGADELVFYDITASSDGRVVDKSWVARVAEVIDIPFCVAG 81
Cdd:pfam00977   1 RIIPAIDLKDGRVVrlvKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  82 GIKSADDAAKILSFGADKISINSPALAEPELITRLADRFGVQCIVVGIDTWFdaatGKyhVNQYTGDEsrtrVTQWETLD 161
Cdd:pfam00977  81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDARR----GK--VAINGWRE----DTGIDAVE 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1918169413 162 WVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVRAVCHVPLIASGGAGTMEHFLEaLRDANVDGALAASVFHKQIIN 240
Cdd:pfam00977 151 WAKELEELGAGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKE-LFTEGVDGVIAGSALYEGEIT 228
WbuZ TIGR03572
glycosyl amidation-associated protein WbuZ; This clade of sequences is highly similar to the ...
 1-235 8.28e-85

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: 252.58  E-value: 8.28e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   1 MLAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYADEGADELVFYDITASSDGRVVDKSWVARVAEVIDIPFCVA 80
Cdd:TIGR03572   1 MLKKRIIPCLLLKDGRLVKTVQFKDPRYIGDPVNAARIYNAKGADELIVLDIDASKRGREPLFELISNLAEECFMPLTVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  81 GGIKSADDAAKILSFGADKISINSPALAEPELITRLADRFGVQCIVVGIDTWFDAATGKYHVNQYTGdesrTRVTQWETL 160
Cdd:TIGR03572  81 GGIRSLEDAKKLLSLGADKVSINTAALENPDLIEEAARRFGSQCVVVSIDVKKELDGSDYKVYSDNG----RRATGRDPV 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1918169413 161 DWVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVRAVCHVPLIASGGAGTMEHFLEALRDANVDGALAASVFH 235
Cdd:TIGR03572 157 EWAREAEQLGAGEILLNSIDRDGTMKGYDLELIKTVSDAVSIPVIALGGAGSLDDLVEVALEAGASAVAAASLFH 231
AglZ_HisF2_fam NF038364
AglZ/HisF2 family acetamidino modification protein;
2-237 1.51e-76

AglZ/HisF2 family acetamidino modification protein;


Pssm-ID: 439657  Cd Length: 248  Bit Score: 231.98  E-value: 1.51e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   2 LAKRIIPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYADEGADELVFYDITASSDGRVVDKSWVARVAEVIDIPFCVAG 81
Cdd:NF038364    1 LRPRIIPCLLLHNGGLVKTVKFKDPKYVGDPINAVRIFNEKEVDELIVLDIDATKEGREPDYELIEDLASECFMPLCYGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  82 GIKSADDAAKILSFGADKISINSPALAEPELITRLADRFGVQCIVVGID---TWFdaatGKYHVnqYTgdESRTRVTQWE 158
Cdd:NF038364   81 GIKTLEQARRIFSLGVEKVALNSAALENPELITEAAEEFGSQSVVVSIDvkkNLF----GGYEV--YT--HNGTKKTKLD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413 159 TLDWVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVRAVCHVPLIASGGAGTMEHFLEALRDANVDGALAAS--VFHK 236
Cdd:NF038364  153 PVEFAKELEALGAGEIVLNSIDRDGTMKGYDLELIKKVSSAVSIPVIALGGAGSLEDLKEAIKQAGASAVAAGSlfVFKG 232


                  .
gi 1918169413 237 Q 237
Cdd:NF038364  233 K 233
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 2-257 2.93e-43

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 153.71  E-value: 2.93e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   2 LAKRIIPCLDVR-----DGQVVKGVQF--RNHEIIGDI------VPLAKRYADEGADELVFYDITASSDGRVVDKSWVA- 67
Cdd:PLN02617  226 LAKRVIACLDVRsndkgDLVVTKGDQYdvREHSEGREVrnlgkpVELAGQYYKDGADEVAFLNITGFRDFPLGDLPMLEv 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  68 --RVAEVIDIPFCVAGGIKSADD-----------AAKILSFGADKISINSPAL--AEPELITRLAD----------RFGV 122
Cdd:PLN02617  306 lrRASENVFVPLTVGGGIRDFTDangryysslevASEYFRSGADKISIGSDAVyaAEEYIASGVKTgktsieqisrVYGN 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413 123 QCIVVGIDTwfdaatGKYHVNQYTGDESRT-RVTQ----WETLDWVQ-------------------EVQKRGAGEIVLNM 178
Cdd:PLN02617  386 QAVVVSIDP------RRVYVKDPSDVPFKTvKVTNpgpnGEEYAWYQctvkggregrpigayelakAVEELGAGEILLNC 459

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1918169413 179 MNQDGVRNGYDLEQLKKVRAVCHVPLIASGGAGTMEHFLEALRDANVDGALAASVFHKQIINIGELKTYLADQGVEIRV 257
Cdd:PLN02617  460 IDCDGQGKGFDIELVKLVSDAVTIPVIASSGAGTPEHFSDVFSKTNASAALAAGIFHRKEVPISSVKEHLLEEGIETRI 538
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 5-244 2.72e-36

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: 128.37  E-value: 2.72e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   5 RIIPCLDVRDGQVV---KGVQFRNHEIIGDIVPLAKRYADEGADELVFYDITASSDGRVVDKSWVARVAEVIDIPFCVAG 81
Cdd:cd04732     1 IIIPAIDLKDGKCVrlyQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  82 GIKSADDAAKILSFGADKISINSPALAEPELITRLADRFGVQCIVVGIDTWfdaatgkyhvNQYTGDESRTRVTQWETLD 161
Cdd:cd04732    81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLDAK----------DGKVATKGWLETSEVSLEE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413 162 WVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVRAVCHVPLIASGGAGTMEHfLEALRDANVDGALAASVFHKQIINI 241
Cdd:cd04732   151 LAKRFEELGVKAIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDD-IKALKELGVAGVIVGKALYEGKITL 229


                  ...
gi 1918169413 242 GEL 244
Cdd:cd04732   230 EEA 232
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 5-228 5.16e-31

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: 114.75  E-value: 5.16e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   5 RIIPCLDVRDGQVV---KGVQFRNHEIIGDIVPLAKRYADEGADEL--VfyDITASSDGRVVDKSWVARVAEVIDIPFCV 79
Cdd:COG0106     1 IIIPAIDLKDGKCVrlvQGDYDQETVYSDDPVEVAKRWEDAGAEWLhlV--DLDGAFAGKPVNLELIEEIAKATGLPVQV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  80 AGGIKSADDAAKILSFGADKISINSPALAEPELITRLADRFGVQcIVVGIDT---------Wfdaatgkyhvnqytgdes 150
Cdd:COG0106    79 GGGIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPER-IVVGLDArdgkvatdgW------------------ 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1918169413 151 rTRVTQWETLDWVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVRAVCHVPLIASGGAGTMEHfLEALRDANVDGA 228
Cdd:COG0106   140 -QETSGVDLEELAKRFEDAGVAAILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDD-LRALKELGVEGA 215
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 6-243 2.64e-29

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


Pssm-ID: 184165  Cd Length: 241  Bit Score: 110.38  E-value: 2.64e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   6 IIPCLDVRDGQVVKGVQFR---NHEIIGDIVPLAKRYADEGADELVFYDITASSDGRVVDKSWVARVAEVIDIPFCVAGG 82
Cdd:PRK13585    5 VIPAVDMKGGKCVQLVQGEpgtETVSYGDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEKIIEAVGVPVQLGGG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  83 IKSADDAAKILSFGADKISINSPALAEPELITRLADRFGVQCIVVGIdtwfDAATGKYHVnqytgdESRTRVTQWETLDW 162
Cdd:PRK13585   85 IRSAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEFGSERVMVSL----DAKDGEVVI------KGWTEKTGYTPVEA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413 163 VQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVRAVCHVPLIASGGAGTMEHfLEALRDANVDGALAASVFHKQIINIG 242
Cdd:PRK13585  155 AKRFEELGAGSILFTNVDVEGLLEGVNTEPVKELVDSVDIPVIASGGVTTLDD-LRALKEAGAAGVVVGSALYKGKFTLE 233


                  .
gi 1918169413 243 E 243
Cdd:PRK13585  234 E 234
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 6-243 6.75e-27

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: 103.82  E-value: 6.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   6 IIPCLDVRDGQVVKGVQ--FRNHEIIGD-IVPLAKRYADEGADELVFYDITASSDGRVVDKSWVARVAEVIDIPFCVAGG 82
Cdd:TIGR00007   1 IIPAIDIKDGKCVRLYQgdYDKETVYGDdPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  83 IKSADDAAKILSFGADKISINSPALAEPELITRLADRFGVQCIVVGIdtwfDAATGKYHVNQYtgdesrTRVTQWETLDW 162
Cdd:TIGR00007  81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSL----DARGGEVAVKGW------LEKSEVSLEEL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413 163 VQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVRAVCHVPLIASGGAGTMEHfLEALRDANVDGALAASVFHKQIINIG 242
Cdd:TIGR00007 151 AKRLEELGLEGIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSIDD-LIALKKLGVYGVIVGKALYEGKITLE 229


                  .
gi 1918169413 243 E 243
Cdd:TIGR00007 230 E 230
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 5-245 2.08e-24

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: 97.34  E-value: 2.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   5 RIIPCLDVRDGQVVKGVQFR---------NHEIIGDIVPLAKRYADEGADELVFYDITASSdGRVVDKSWVARVAEVIDI 75
Cdd:cd04723     1 RIIPVIDLKDGVVVHGVGGDrdnyrpitsNLCSTSDPLDVARAYKELGFRGLYIADLDAIM-GRGDNDEAIRELAAAWPL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  76 PFCVAGGIKSADDAAKILSFGADKISINSpALAEPELITRLADRFGVQCIVVGIDtwfdaatgkyHVNQYTGDESRTRVT 155
Cdd:cd04723    80 GLWVDGGIRSLENAQEWLKRGASRVIVGT-ETLPSDDDEDRLAALGEQRLVLSLD----------FRGGQLLKPTDFIGP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413 156 QwetlDWVQEVQKRgAGEIVLNMMNQDGVRNGYDLEQLKKVRAVCHVPLIASGGAGTMEHfLEALRDANVDGALAASVFH 235
Cdd:cd04723   149 E----ELLRRLAKW-PEELIVLDIDRVGSGQGPDLELLERLAARADIPVIAAGGVRSVED-LELLKKLGASGALVASALH 222

                         250
                  ....*....|
gi 1918169413 236 KQIINIGELK 245
Cdd:cd04723   223 DGGLTLEDVV 232
PRK00748 PRK00748
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 6-228 2.74e-22

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


Pssm-ID: 179108  Cd Length: 233  Bit Score: 91.67  E-value: 2.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   6 IIPCLDVRDGQVVKGVQ--FRNHEIIG-DIVPLAKRYADEGADELVFYDITASSDGRVVDKSWVARVAEVIDIPFCVAGG 82
Cdd:PRK00748    3 IIPAIDLKDGKCVRLYQgdYDQATVYSdDPVAQAKAWEDQGAKWLHLVDLDGAKAGKPVNLELIEAIVKAVDIPVQVGGG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  83 IKSADDAAKILSFGADKISINSPALAEPELITRLADRFGVQcIVVGIDtwfdAATGKYHVNQYTgDESRTRVTqwetlDW 162
Cdd:PRK00748   83 IRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFPGK-IVVGLD----ARDGKVATDGWL-ETSGVTAE-----DL 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1918169413 163 VQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVRAVCHVPLIASGGAGTMEHfLEALRDA-NVDGA 228
Cdd:PRK00748  152 AKRFEDAGVKAIIYTDISRDGTLSGPNVEATRELAAAVPIPVIASGGVSSLDD-IKALKGLgAVEGV 217
PRK14024 PRK14024
phosphoribosyl isomerase A; Provisional
 6-229 1.04e-13

phosphoribosyl isomerase A; Provisional


Pssm-ID: 237589  Cd Length: 241  Bit Score: 68.45  E-value: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   6 IIPCLDVRDGQVVKGVQFR--NHEIIGDIVPLAKRYADEGADELVFYDITASSdGRVVDKSWVARVAEVIDIPFCVAGGI 83
Cdd:PRK14024    6 LLPAVDVVDGQAVRLVQGEagSETSYGSPLDAALAWQRDGAEWIHLVDLDAAF-GRGSNRELLAEVVGKLDVKVELSGGI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  84 KSADDAAKILSFGADKISINSPALAEPELITRLADRFGVQcIVVGIDT--WFDAATGkyhvnqYTGDESRTrvtqWETLD 161
Cdd:PRK14024   85 RDDESLEAALATGCARVNIGTAALENPEWCARVIAEHGDR-VAVGLDVrgHTLAARG------WTRDGGDL----WEVLE 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413 162 wvqEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVRAVCHVPLIASGGAGTMEHF--LEALRDANVDGAL 229
Cdd:PRK14024  154 ---RLDSAGCSRYVVTDVTKDGTLTGPNLELLREVCARTDAPVVASGGVSSLDDLraLAELVPLGVEGAI 220
PRK14114 PRK14114
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 6-247 1.61e-09

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


Pssm-ID: 172604  Cd Length: 241  Bit Score: 56.56  E-value: 1.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   6 IIPCLDVRDGQVVKGVQFRNHEII---GDIVPLAKRYADEGADELVFYDITASSDGRVVDKSWVARVAEVIDiPFCVAGG 82
Cdd:PRK14114    3 VVPAIDLFRGKVARMVKGKKENTIfyeKDPAELVEKLIEEGFTLIHVVDLSKAIENSVENLPVLEKLSEFAE-HIQIGGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  83 IKSADDAAKILSFGADKISINSPALAEPELITRLADrfgvqcivVGIDTWF--DAATGKYHVNQYTGDEsrtrvtQWETL 160
Cdd:PRK14114   82 IRSLDYAEKLRKLGYRRQIVSSKVLEDPSFLKFLKE--------IDVEPVFslDTRGGKVAFKGWLAEE------EIDPV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413 161 DWVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVRAVCHVPLIASGGAG---TMEHFLEALRDAN--VDGALAASVFH 235
Cdd:PRK14114  148 SLLKRLKEYGLEEIVHTEIEKDGTLQEHDFSLTRKIAIEAEVKVFAAGGISsenSLKTAQRVHRETNglLKGVIVGRAFL 227

                         250
                  ....*....|..
gi 1918169413 236 KQIINIGELKTY 247
Cdd:PRK14114  228 EGILTVEVMKRY 239
OYE_like_FMN_family cd02803
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
 29-118 7.95e-07

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: 49.11  E-value: 7.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  29 IGDIVPLAKRYADEGAD---------ELVFYDITASSDGRVVDKSWVARVAEVIDIPFCVAGGIKSADDAAKIL-SFGAD 98
Cdd:cd02803   227 LEEAIEIAKALEEAGVDalhvsggsyESPPPIIPPPYVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILaEGKAD 306

                          90       100
                  ....*....|....*....|
gi 1918169413  99 KISINSPALAEPELITRLAD 118
Cdd:cd02803   307 LVALGRALLADPDLPNKARE 326
PRK13586 PRK13586
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 5-218 4.97e-06

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


Pssm-ID: 237439  Cd Length: 232  Bit Score: 46.27  E-value: 4.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   5 RIIPCLDVRDGQVVKGVQFRNHE--IIGDIVPLAKRYADEGADELVFYDITASsDGRVVDKSWVARVAEVIDIPFCVAGG 82
Cdd:PRK13586    3 KIIPSIDISLGKAVKRIRGVKGTglILGNPIEIASKLYNEGYTRIHVVDLDAA-EGVGNNEMYIKEISKIGFDWIQVGGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  83 IKSADDAAKILSFGADKISINSPALAEPELITRLADRFGVQCIVVGIDtwFDaatgkyhvnqytgDESRTRVTQW----- 157
Cdd:PRK13586   82 IRDIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGSNRVLVSID--YD-------------NTKRVLIRGWkeksm 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1918169413 158 ETLDWVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVRAVCHVPLIAsGGAGTMEHFLE 218
Cdd:PRK13586  147 EVIDGIKKVNELELLGIIFTYISNEGTTKGIDYNVKDYARLIRGLKEYA-GGVSSDADLEY 206
FadH COG1902
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ...
 31-118 7.01e-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: 46.32  E-value: 7.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  31 DIVPLAKRYADEGAD--ELV--FYDITASSDGRVVDKSWV---ARVAEVIDIPFCVAGGIKSADDAAKILSFG-ADKISI 102
Cdd:COG1902   237 ESVELAKALEEAGVDylHVSsgGYEPDAMIPTIVPEGYQLpfaARIRKAVGIPVIAVGGITTPEQAEAALASGdADLVAL 316

                          90
                  ....*....|....*.
gi 1918169413 103 NSPALAEPELITRLAD 118
Cdd:COG1902   317 GRPLLADPDLPNKAAA 332
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 4-98 8.58e-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: 45.55  E-value: 8.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   4 KRIIPCLDVRDGQV-VKGVQfRNHEIigDIVPLAKRYADEGADELVFYDItaSSDGRV--VDKSWVARVAEVIDIPFCVA 80
Cdd:cd04732   122 ERIVVGLDAKDGKVaTKGWL-ETSEV--SLEELAKRFEELGVKAIIYTDI--SRDGTLsgPNFELYKELAAATGIPVIAS 196

                          90
                  ....*....|....*...
gi 1918169413  81 GGIKSADDAAKILSFGAD 98
Cdd:cd04732   197 GGVSSLDDIKALKELGVA 214
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
 31-102 1.23e-05

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: 45.47  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  31 DIVPLAKRYADEGADELV--------FYDITAssdgrvvDKSWVARVAEVIDIPFCVAGGIKSADDAAKILS-FGADKIS 101
Cdd:COG0042   147 NALEFARIAEDAGAAALTvhgrtreqRYKGPA-------DWDAIARVKEAVSIPVIGNGDIFSPEDAKRMLEeTGCDGVM 219


                  .
gi 1918169413 102 I 102
Cdd:COG0042   220 I 220
PRK13587 PRK13587
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 51-237 2.04e-05

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


Pssm-ID: 172156  Cd Length: 234  Bit Score: 44.44  E-value: 2.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  51 DITASSDGRVVDKSWVARVAEVIDIPFCVAGGIKSADDAAKILSFGADKISINSPALAEPELITRLADRFGVQcIVVGID 130
Cdd:PRK13587   53 DLIGAKAQHAREFDYIKSLRRLTTKDIEVGGGIRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGR-IYLSVD 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413 131 TWFDaatgKYHVNQYTGDesrtrvTQWETLDWVQEVQKRGAGEIVLNMMNQDGVRNGYDLEQLKKVRAVCHVPLIASGGA 210
Cdd:PRK13587  132 AYGE----DIKVNGWEED------TELNLFSFVRQLSDIPLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGGI 201

                         170       180
                  ....*....|....*....|....*..
gi 1918169413 211 GTMEHfLEALRDANVDGALAASVFHKQ 237
Cdd:PRK13587  202 RHQQD-IQRLASLNVHAAIIGKAAHQA 227
OYE_like_4_FMN cd04735
Old yellow enzyme (OYE)-related FMN binding domain, group 4. Each monomer of OYE contains FMN ...
 58-118 5.08e-05

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: 43.74  E-value: 5.08e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1918169413  58 GRVVDKSWVARVAEVID--IPFCVAGGIKSADDAAKILSFGADKISINSPALAEPELITRLAD 118
Cdd:cd04735   266 GRDDNQTIMELVKERIAgrLPLIAVGSINTPDDALEALETGADLVAIGRGLLVDPDWVEKIKE 328
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 5-104 6.21e-05

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


Pssm-ID: 184165  Cd Length: 241  Bit Score: 42.97  E-value: 6.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   5 RIIPCLDVRDGQVV-KGVQfrnhEIIG-DIVPLAKRYADEGADELVFYDItaSSDGRV--VDKSWVARVAEVIDIPFCVA 80
Cdd:PRK13585  126 RVMVSLDAKDGEVViKGWT----EKTGyTPVEAAKRFEELGAGSILFTNV--DVEGLLegVNTEPVKELVDSVDIPVIAS 199

                          90       100
                  ....*....|....*....|....
gi 1918169413  81 GGIKSADDAAKILSFGADKISINS 104
Cdd:PRK13585  200 GGVTTLDDLRALKEAGAAGVVVGS 223
PRK04128 PRK04128
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 5-245 7.66e-05

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


Pssm-ID: 167709  Cd Length: 228  Bit Score: 42.84  E-value: 7.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   5 RIIPCLDVRDGQVVKGVQFRNHEI--IGDIVPLAKRYAdEGADELVFYDITASSDGRVVDKSWVARVAEVIDIPFCVAGG 82
Cdd:PRK04128    3 RIYPAIDLMNGKAVRLYKGRKEEVkvYGDPVEIALRFS-EYVDKIHVVDLDGAFEGKPKNLDVVKNIIRETGLKVQVGGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  83 IKSADDAAKILSFGADKISINSPALaEPELITRLADRFGvqcivvGIDTWFDAATGKYHVNQYTGDESRTRVTQWETLdw 162
Cdd:PRK04128   82 LRTYESIKDAYEIGVENVIIGTKAF-DLEFLEKVTSEFE------GITVSLDVKGGRIAVKGWLEESSIKVEDAYEML-- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413 163 vqevqKRGAGEIVLNMMNQDGVRNGydLEQLKKVRAvcHVPLIASGGAGTMEHFLEALRDAnVDGALAASVFHKQIINIG 242
Cdd:PRK04128  153 -----KNYVNRFIYTSIERDGTLTG--IEEIERFWG--DEEFIYAGGVSSAEDVKKLAEIG-FSGVIIGKALYEGRISLE 222


                  ...
gi 1918169413 243 ELK 245
Cdd:PRK04128  223 ELL 225
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 4-88 1.05e-04

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: 42.19  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   4 KRIIPCLDVRDGQV-VKGvqFRNHEIIgDIVPLAKRYADEGADELVFYDItaSSDGRV--VDKSWVARVAEVIDIPFCVA 80
Cdd:TIGR00007 121 ERIVVSLDARGGEVaVKG--WLEKSEV-SLEELAKRLEELGLEGIIYTDI--SRDGTLsgPNFELTKELVKAVNVPVIAS 195


                  ....*...
gi 1918169413  81 GGIKSADD 88
Cdd:TIGR00007 196 GGVSSIDD 203
PcrB COG1646
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];
44-100 1.31e-04

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


Pssm-ID: 441252  Cd Length: 241  Bit Score: 42.07  E-value: 1.31e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1918169413  44 ADEL----VFYdITASSD-GRVVDKSWVARVAEVI-DIPFCVAGGIKSADDAAKILSFGADKI 100
Cdd:COG1646   161 AEEYlgmpIVY-LEYGSGaGEPVDPEMVKAVKKALeDTPLIYGGGIRSPEKAREMAEAGADTI 222
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 156-231 3.77e-04

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: 40.56  E-value: 3.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413 156 QWETLDWVQEVQKRGAGEIVL-----NMMNQDGVrngyDLEQLKKVRAVCHVPLIASGGAGTMEHFLEALRDANVDGALA 230
Cdd:cd02801   137 EEETLELAKALEDAGASALTVhgrtrEQRYSGPA----DWDYIAEIKEAVSIPVIANGDIFSLEDALRCLEQTGVDGVMI 212


                  .
gi 1918169413 231 A 231
Cdd:cd02801   213 G 213
PcrB_like cd02812
PcrB_like proteins. One member of this family, a protein from Archaeoglobus fulgidus, has been ...
 58-102 8.83e-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: 39.53  E-value: 8.83e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1918169413  58 GRVVDKSWVARVAEVI-DIPFCVAGGIKSADDAAKILSFGADKISI 102
Cdd:cd02812   158 GAYGPPEVVRAVKKVLgDTPLIVGGGIRSGEQAKEMAEAGADTIVV 203
DHOD_like cd04739
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ...
 35-134 1.18e-03

Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. This subgroup has the conserved FMN binding site, but lacks some catalytic residues and may therefore be inactive.


Pssm-ID: 240090  Cd Length: 325  Bit Score: 39.52  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  35 LAKRYADEGADELV----FY--DI-------------TASSDGRVVDKsWVARVAEVIDIPFCVAGGIKSADDAAKILSF 95
Cdd:cd04739   180 MAKQLDAAGADGLVlfnrFYqpDIdletlevvpnlllSSPAEIRLPLR-WIAILSGRVKASLAASGGVHDAEDVVKYLLA 258

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1918169413  96 GADKISINSPALAE-PELItrladrfgvQCIVVGIDTWFD 134
Cdd:cd04739   259 GADVVMTTSALLRHgPDYI---------GTLLAGLEAWME 289
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 26-104 2.88e-03

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


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 37.95  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  26 HEIIGDIVPLAKRYADEGADELV---FYDITASSDGRVVDKSWVARVAEVIDIPFCVAGGIKSADDAAKILSFGADKISI 102
Cdd:cd04722   119 VKLSPTGELAAAAAEEAGVDEVGlgnGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIV 198


                  ..
gi 1918169413 103 NS 104
Cdd:cd04722   199 GS 200
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 35-120 3.43e-03

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: 37.86  E-value: 3.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413  35 LAKRYADEGADELVFYditassdGRV--------VDKSWVARVAEVIDIPFCVAGGIKSADDAAKILS-FGADKISINSP 105
Cdd:cd02801   143 LAKALEDAGASALTVH-------GRTreqrysgpADWDYIAEIKEAVSIPVIANGDIFSLEDALRCLEqTGVDGVMIGRG 215

                          90
                  ....*....|....*
gi 1918169413 106 ALAEPELITRLADRF 120
Cdd:cd02801   216 ALGNPWLFREIKELL 230
PRK00748 PRK00748
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 5-97 3.76e-03

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


Pssm-ID: 179108  Cd Length: 233  Bit Score: 37.74  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1918169413   5 RIIPCLDVRDGQV-VKGVQfrnhEIIG-DIVPLAKRYADEGADELVFYDItaSSDGRV--VDKSWVARVAEVIDIPFCVA 80
Cdd:PRK00748  123 KIVVGLDARDGKVaTDGWL----ETSGvTAEDLAKRFEDAGVKAIIYTDI--SRDGTLsgPNVEATRELAAAVPIPVIAS 196

                          90
                  ....*....|....*..
gi 1918169413  81 GGIKSADDAAKILSFGA 97
Cdd:PRK00748  197 GGVSSLDDIKALKGLGA 213
PRK04169 PRK04169
heptaprenylglyceryl phosphate synthase;
48-100 7.26e-03

heptaprenylglyceryl phosphate synthase;


Pssm-ID: 235237  Cd Length: 232  Bit Score: 36.71  E-value: 7.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1918169413  48 VFYdITASSD-GRVVDKSWVARVAEVIDI-PFCVAGGIKSADDAAKILSFGADKI 100
Cdd:PRK04169  157 IVY-LEYGGGaGDPVPPEMVKAVKKALDItPLIYGGGIRSPEQARELMAAGADTI 210
DCR_FMN cd02930
2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur ...
 64-115 8.23e-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: 36.88  E-value: 8.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1918169413  64 SWVA-RVAEVIDIPFCVAGGIKSADDAAKILSFG-ADKISINSPALAEPELITR 115
Cdd:cd02930   265 AWATaKLKRAVDIPVIASNRINTPEVAERLLADGdADMVSMARPFLADPDFVAK 318
 
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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