NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|518491212|ref|WP_019661419|]
View 

MULTISPECIES: imidazole glycerol phosphate synthase subunit HisF [Stenotrophomonas]

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]; ...
 2-255 8.91e-139

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: 390.15  E-value: 8.91e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   2 LSRRIIPCLDVRDGRVVKGVRFRDHVDMGDIAELAQRYRDQGADELVFYDIGASPEARSVDVTWIERIARLIDIPFCVAG 81
Cdd:COG0107    1 LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  82 GIDSVETARRVLFAGADKVSINSPALGRPELITELADEFGVQCVVVGVDSVREADGQWRVRRFSGdpdkTQAVPLRTLDW 161
Cdd:COG0107   81 GIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRVPDGGWEVYTHGG----RKPTGLDAVEW 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212 162 IVEAQRRGAGEIVLNCMDSDGVRRGYDVVQLQQARALCQVPLIASGGAGAMEHFAEAFDQADVDGALAASVFHSGAIAIP 241
Cdd:COG0107  157 AKEAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITIA 236

                        250
                 ....*....|....
gi 518491212 242 ELKRYLRGQQIEVR 255
Cdd:COG0107  237 ELKAYLAEAGIPVR 250
 
Name Accession Description Interval E-value
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 2-255 8.91e-139

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: 390.15  E-value: 8.91e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   2 LSRRIIPCLDVRDGRVVKGVRFRDHVDMGDIAELAQRYRDQGADELVFYDIGASPEARSVDVTWIERIARLIDIPFCVAG 81
Cdd:COG0107    1 LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  82 GIDSVETARRVLFAGADKVSINSPALGRPELITELADEFGVQCVVVGVDSVREADGQWRVRRFSGdpdkTQAVPLRTLDW 161
Cdd:COG0107   81 GIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRVPDGGWEVYTHGG----RKPTGLDAVEW 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212 162 IVEAQRRGAGEIVLNCMDSDGVRRGYDVVQLQQARALCQVPLIASGGAGAMEHFAEAFDQADVDGALAASVFHSGAIAIP 241
Cdd:COG0107  157 AKEAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITIA 236

                        250
                 ....*....|....
gi 518491212 242 ELKRYLRGQQIEVR 255
Cdd:COG0107  237 ELKAYLAEAGIPVR 250
HisF cd04731
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ...
 4-250 7.49e-120

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: 341.75  E-value: 7.49e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   4 RRIIPCLDVRDGRVVKGVRFRDHVDMGDIAELAQRYRDQGADELVFYDIGASPEARSVDVTWIERIARLIDIPFCVAGGI 83
Cdd:cd04731    1 KRIIPCLDVKDGRVVKGVNFKNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  84 DSVETARRVLFAGADKVSINSPALGRPELITELADEFGVQCVVVGVDSVREADGQWRVrrfsGDPDKTQAVPLRTLDWIV 163
Cdd:cd04731   81 RSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAKRRGDGGYEV----YTHGGRKPTGLDAVEWAK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212 164 EAQRRGAGEIVLNCMDSDGVRRGYDVVQLQQARALCQVPLIASGGAGAMEHFAEAFDQADVDGALAASVFHSGAIAIPEL 243
Cdd:cd04731  157 EVEELGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEAFEEGGADAALAASIFHFGEYTIAEL 236


                 ....*..
gi 518491212 244 KRYLRGQ 250
Cdd:cd04731  237 KEYLAER 243
hisF TIGR00735
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ...
 1-255 1.84e-115

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


Pssm-ID: 273241  Cd Length: 254  Bit Score: 331.25  E-value: 1.84e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212    1 MLSRRIIPCLDVRDGRVVKGVRFRDHVDMGDIAELAQRYRDQGADELVFYDIGASPEARSVDVTWIERIARLIDIPFCVA 80
Cdd:TIGR00735   1 MLAKRIIPCLDVRDGRVVKGVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   81 GGIDSVETARRVLFAGADKVSINSPALGRPELITELADEFGVQCVVVGVDSVREADGQ---WRVRRFSGDpdktQAVPLR 157
Cdd:TIGR00735  81 GGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRVYVNSycwYEVYIYGGR----ESTGLD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  158 TLDWIVEAQRRGAGEIVLNCMDSDGVRRGYDVVQLQQARALCQVPLIASGGAGAMEHFAEAFDQADVDGALAASVFHSGA 237
Cdd:TIGR00735 157 AVEWAKEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPEHFYEAFTKGKADAALAASVFHYRE 236

                         250
                  ....*....|....*...
gi 518491212  238 IAIPELKRYLRGQQIEVR 255
Cdd:TIGR00735 237 ITIGEVKEYLAERGIPVR 254
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 5-238 1.09e-83

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: 249.70  E-value: 1.09e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212    5 RIIPCLDVRDGRVV---KGVRFRDHVDMGDIAELAQRYRDQGADELVFYDIGASPEARSVDVTWIERIARLIDIPFCVAG 81
Cdd:pfam00977   1 RIIPAIDLKDGRVVrlvKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   82 GIDSVETARRVLFAGADKVSINSPALGRPELITELADEFGVQCVVVGVDSVREadgqwRVRRFSGdpdkTQAVPLRTLDW 161
Cdd:pfam00977  81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDARRG-----KVAINGW----REDTGIDAVEW 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518491212  162 IVEAQRRGAGEIVLNCMDSDGVRRGYDVVQLQQARALCQVPLIASGGAGAMEHFAEAFDQAdVDGALAASVFHSGAI 238
Cdd:pfam00977 152 AKELEELGAGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTEG-VDGVIAGSALYEGEI 227
AglZ_HisF2_fam NF038364
AglZ/HisF2 family acetamidino modification protein;
2-234 3.32e-70

AglZ/HisF2 family acetamidino modification protein;


Pssm-ID: 439657  Cd Length: 248  Bit Score: 216.18  E-value: 3.32e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   2 LSRRIIPCLDVRDGRVVKGVRFRDHVDMGDIAELAQRYRDQGADELVFYDIGASPEARSVDVTWIERIARLIDIPFCVAG 81
Cdd:NF038364   1 LRPRIIPCLLLHNGGLVKTVKFKDPKYVGDPINAVRIFNEKEVDELIVLDIDATKEGREPDYELIEDLASECFMPLCYGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  82 GIDSVETARRVLFAGADKVSINSPALGRPELITELADEFGVQCVVVGVDSVREADGQWRVRRFSGdpdkTQAVPLRTLDW 161
Cdd:NF038364  81 GIKTLEQARRIFSLGVEKVALNSAALENPELITEAAEEFGSQSVVVSIDVKKNLFGGYEVYTHNG----TKKTKLDPVEF 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518491212 162 IVEAQRRGAGEIVLNCMDSDGVRRGYDVVQLQQARALCQVPLIASGGAGAMEHFAEAFDQADVDGALAAS--VFH 234
Cdd:NF038364 157 AKELEALGAGEIVLNSIDRDGTMKGYDLELIKKVSSAVSIPVIALGGAGSLEDLKEAIKQAGASAVAAGSlfVFK 231
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 2-255 2.86e-35

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 132.14  E-value: 2.86e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   2 LSRRIIPCLDVR-----DGRVVKGVRF--RDHVDMGDI------AELAQRYRDQGADELVFYDIGASPEARSVDVTWIE- 67
Cdd:PLN02617 226 LAKRVIACLDVRsndkgDLVVTKGDQYdvREHSEGREVrnlgkpVELAGQYYKDGADEVAFLNITGFRDFPLGDLPMLEv 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  68 --RIARLIDIPFCVAGGI-----------DSVETARRVLFAGADKVSINSPALGRPEL------------ITELADEFGV 122
Cdd:PLN02617 306 lrRASENVFVPLTVGGGIrdftdangryySSLEVASEYFRSGADKISIGSDAVYAAEEyiasgvktgktsIEQISRVYGN 385

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212 123 QCVVVGVDSVREadgqwrvrrFSGDPDKTQAVPLRT---------LDW---IVEAQRR----------------GAGEIV 174
Cdd:PLN02617 386 QAVVVSIDPRRV---------YVKDPSDVPFKTVKVtnpgpngeeYAWyqcTVKGGREgrpigayelakaveelGAGEIL 456

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212 175 LNCMDSDGVRRGYDVVQLQQARALCQVPLIASGGAGAMEHFAEAFDQADVDGALAASVFHSGAIAIPELKRYLRGQQIEV 254
Cdd:PLN02617 457 LNCIDCDGQGKGFDIELVKLVSDAVTIPVIASSGAGTPEHFSDVFSKTNASAALAAGIFHRKEVPISSVKEHLLEEGIET 536


                 .
gi 518491212 255 R 255
Cdd:PLN02617 537 R 537
 
Name Accession Description Interval E-value
HisF COG0107
Imidazole glycerol phosphate synthase subunit HisF [Amino acid transport and metabolism]; ...
 2-255 8.91e-139

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: 390.15  E-value: 8.91e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   2 LSRRIIPCLDVRDGRVVKGVRFRDHVDMGDIAELAQRYRDQGADELVFYDIGASPEARSVDVTWIERIARLIDIPFCVAG 81
Cdd:COG0107    1 LAKRIIPCLDVKDGRVVKGVNFVNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRKTMLDVVRRVAEEVFIPLTVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  82 GIDSVETARRVLFAGADKVSINSPALGRPELITELADEFGVQCVVVGVDSVREADGQWRVRRFSGdpdkTQAVPLRTLDW 161
Cdd:COG0107   81 GIRSVEDARRLLRAGADKVSINSAAVKNPELITEAAERFGSQCIVVAIDAKRVPDGGWEVYTHGG----RKPTGLDAVEW 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212 162 IVEAQRRGAGEIVLNCMDSDGVRRGYDVVQLQQARALCQVPLIASGGAGAMEHFAEAFDQADVDGALAASVFHSGAIAIP 241
Cdd:COG0107  157 AKEAEELGAGEILLTSMDRDGTKDGYDLELTRAVSEAVSIPVIASGGAGTLEHFVEVFTEGGADAALAASIFHFGEITIA 236

                        250
                 ....*....|....
gi 518491212 242 ELKRYLRGQQIEVR 255
Cdd:COG0107  237 ELKAYLAEAGIPVR 250
HisF cd04731
The cyclase subunit of imidazoleglycerol phosphate synthase (HisF). Imidazole glycerol ...
 4-250 7.49e-120

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: 341.75  E-value: 7.49e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   4 RRIIPCLDVRDGRVVKGVRFRDHVDMGDIAELAQRYRDQGADELVFYDIGASPEARSVDVTWIERIARLIDIPFCVAGGI 83
Cdd:cd04731    1 KRIIPCLDVKDGRVVKGVNFKNLRDAGDPVELAKRYNEQGADELVFLDITASSEGRETMLDVVERVAEEVFIPLTVGGGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  84 DSVETARRVLFAGADKVSINSPALGRPELITELADEFGVQCVVVGVDSVREADGQWRVrrfsGDPDKTQAVPLRTLDWIV 163
Cdd:cd04731   81 RSLEDARRLLRAGADKVSINSAAVENPELIREIAKRFGSQCVVVSIDAKRRGDGGYEV----YTHGGRKPTGLDAVEWAK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212 164 EAQRRGAGEIVLNCMDSDGVRRGYDVVQLQQARALCQVPLIASGGAGAMEHFAEAFDQADVDGALAASVFHSGAIAIPEL 243
Cdd:cd04731  157 EVEELGAGEILLTSMDRDGTKKGYDLELIRAVSSAVNIPVIASGGAGKPEHFVEAFEEGGADAALAASIFHFGEYTIAEL 236


                 ....*..
gi 518491212 244 KRYLRGQ 250
Cdd:cd04731  237 KEYLAER 243
hisF TIGR00735
imidazoleglycerol phosphate synthase, cyclase subunit; [Amino acid biosynthesis, Histidine ...
 1-255 1.84e-115

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


Pssm-ID: 273241  Cd Length: 254  Bit Score: 331.25  E-value: 1.84e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212    1 MLSRRIIPCLDVRDGRVVKGVRFRDHVDMGDIAELAQRYRDQGADELVFYDIGASPEARSVDVTWIERIARLIDIPFCVA 80
Cdd:TIGR00735   1 MLAKRIIPCLDVRDGRVVKGVQFLNLRDAGDPVELAQRYDEEGADELVFLDITASSEGRTTMIDVVERTAETVFIPLTVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   81 GGIDSVETARRVLFAGADKVSINSPALGRPELITELADEFGVQCVVVGVDSVREADGQ---WRVRRFSGDpdktQAVPLR 157
Cdd:TIGR00735  81 GGIKSIEDVDKLLRAGADKVSINTAAVKNPELIYELADRFGSQCIVVAIDAKRVYVNSycwYEVYIYGGR----ESTGLD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  158 TLDWIVEAQRRGAGEIVLNCMDSDGVRRGYDVVQLQQARALCQVPLIASGGAGAMEHFAEAFDQADVDGALAASVFHSGA 237
Cdd:TIGR00735 157 AVEWAKEVEKLGAGEILLTSMDKDGTKSGYDLELTKAVSEAVKIPVIASGGAGKPEHFYEAFTKGKADAALAASVFHYRE 236

                         250
                  ....*....|....*...
gi 518491212  238 IAIPELKRYLRGQQIEVR 255
Cdd:TIGR00735 237 ITIGEVKEYLAERGIPVR 254
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 5-238 1.09e-83

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: 249.70  E-value: 1.09e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212    5 RIIPCLDVRDGRVV---KGVRFRDHVDMGDIAELAQRYRDQGADELVFYDIGASPEARSVDVTWIERIARLIDIPFCVAG 81
Cdd:pfam00977   1 RIIPAIDLKDGRVVrlvKGDYFQNTVYAGDPVELAKRYEEEGADELHFVDLDAAKEGRPVNLDVVEEIAEEVFIPVQVGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   82 GIDSVETARRVLFAGADKVSINSPALGRPELITELADEFGVQCVVVGVDSVREadgqwRVRRFSGdpdkTQAVPLRTLDW 161
Cdd:pfam00977  81 GIRSLEDVERLLSAGADRVIIGTAAVKNPELIKEAAEKFGSQCIVVAIDARRG-----KVAINGW----REDTGIDAVEW 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518491212  162 IVEAQRRGAGEIVLNCMDSDGVRRGYDVVQLQQARALCQVPLIASGGAGAMEHFAEAFDQAdVDGALAASVFHSGAI 238
Cdd:pfam00977 152 AKELEELGAGEILLTDIDRDGTLSGPDLELTRELAEAVNIPVIASGGVGSLEDLKELFTEG-VDGVIAGSALYEGEI 227
WbuZ TIGR03572
glycosyl amidation-associated protein WbuZ; This clade of sequences is highly similar to the ...
 1-234 2.51e-76

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: 231.00  E-value: 2.51e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212    1 MLSRRIIPCLDVRDGRVVKGVRFRDHVDMGDIAELAQRYRDQGADELVFYDIGASPEARSVDVTWIERIARLIDIPFCVA 80
Cdd:TIGR03572   1 MLKKRIIPCLLLKDGRLVKTVQFKDPRYIGDPVNAARIYNAKGADELIVLDIDASKRGREPLFELISNLAEECFMPLTVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   81 GGIDSVETARRVLFAGADKVSINSPALGRPELITELADEFGVQCVVVGVDSVREADG-QWRVRRFSGdpdkTQAVPLRTL 159
Cdd:TIGR03572  81 GGIRSLEDAKKLLSLGADKVSINTAALENPDLIEEAARRFGSQCVVVSIDVKKELDGsDYKVYSDNG----RRATGRDPV 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518491212  160 DWIVEAQRRGAGEIVLNCMDSDGVRRGYDVVQLQQARALCQVPLIASGGAGAMEHFAEAFDQADVDGALAASVFH 234
Cdd:TIGR03572 157 EWAREAEQLGAGEILLNSIDRDGTMKGYDLELIKTVSDAVSIPVIALGGAGSLDDLVEVALEAGASAVAAASLFH 231
AglZ_HisF2_fam NF038364
AglZ/HisF2 family acetamidino modification protein;
2-234 3.32e-70

AglZ/HisF2 family acetamidino modification protein;


Pssm-ID: 439657  Cd Length: 248  Bit Score: 216.18  E-value: 3.32e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   2 LSRRIIPCLDVRDGRVVKGVRFRDHVDMGDIAELAQRYRDQGADELVFYDIGASPEARSVDVTWIERIARLIDIPFCVAG 81
Cdd:NF038364   1 LRPRIIPCLLLHNGGLVKTVKFKDPKYVGDPINAVRIFNEKEVDELIVLDIDATKEGREPDYELIEDLASECFMPLCYGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  82 GIDSVETARRVLFAGADKVSINSPALGRPELITELADEFGVQCVVVGVDSVREADGQWRVRRFSGdpdkTQAVPLRTLDW 161
Cdd:NF038364  81 GIKTLEQARRIFSLGVEKVALNSAALENPELITEAAEEFGSQSVVVSIDVKKNLFGGYEVYTHNG----TKKTKLDPVEF 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518491212 162 IVEAQRRGAGEIVLNCMDSDGVRRGYDVVQLQQARALCQVPLIASGGAGAMEHFAEAFDQADVDGALAAS--VFH 234
Cdd:NF038364 157 AKELEALGAGEIVLNSIDRDGTMKGYDLELIKKVSSAVSIPVIALGGAGSLEDLKEAIKQAGASAVAAGSlfVFK 231
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 2-255 2.86e-35

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 132.14  E-value: 2.86e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   2 LSRRIIPCLDVR-----DGRVVKGVRF--RDHVDMGDI------AELAQRYRDQGADELVFYDIGASPEARSVDVTWIE- 67
Cdd:PLN02617 226 LAKRVIACLDVRsndkgDLVVTKGDQYdvREHSEGREVrnlgkpVELAGQYYKDGADEVAFLNITGFRDFPLGDLPMLEv 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  68 --RIARLIDIPFCVAGGI-----------DSVETARRVLFAGADKVSINSPALGRPEL------------ITELADEFGV 122
Cdd:PLN02617 306 lrRASENVFVPLTVGGGIrdftdangryySSLEVASEYFRSGADKISIGSDAVYAAEEyiasgvktgktsIEQISRVYGN 385

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212 123 QCVVVGVDSVREadgqwrvrrFSGDPDKTQAVPLRT---------LDW---IVEAQRR----------------GAGEIV 174
Cdd:PLN02617 386 QAVVVSIDPRRV---------YVKDPSDVPFKTVKVtnpgpngeeYAWyqcTVKGGREgrpigayelakaveelGAGEIL 456

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212 175 LNCMDSDGVRRGYDVVQLQQARALCQVPLIASGGAGAMEHFAEAFDQADVDGALAASVFHSGAIAIPELKRYLRGQQIEV 254
Cdd:PLN02617 457 LNCIDCDGQGKGFDIELVKLVSDAVTIPVIASSGAGTPEHFSDVFSKTNASAALAAGIFHRKEVPISSVKEHLLEEGIET 536


                 .
gi 518491212 255 R 255
Cdd:PLN02617 537 R 537
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 5-245 4.26e-28

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: 107.18  E-value: 4.26e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   5 RIIPCLDVRDGRVV---KGVRFRDHVDMGDIAELAQRYRDQGADELVFYDIGASPEARSVDVTWIERIARLIDIPFCVAG 81
Cdd:cd04732    1 IIIPAIDLKDGKCVrlyQGDYDKKTVYSDDPVEVAKKWEEAGAKWLHVVDLDGAKGGEPVNLELIEEIVKAVGIPVQVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  82 GIDSVETARRVLFAGADKVSINSPALGRPELITELADEFGVQCVVVGVDsVRE---ADGQWrvrrfsgdpdkTQAVPLRT 158
Cdd:cd04732   81 GIRSLEDIERLLDLGVSRVIIGTAAVKNPELVKELLKEYGGERIVVGLD-AKDgkvATKGW-----------LETSEVSL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212 159 LDWIVEAQRRGAGEIVLNCMDSDGVRRGYDVVQLQQARALCQVPLIASGGAGAMEHFAEAfDQADVDGALAASVFHSGAI 238
Cdd:cd04732  149 EELAKRFEELGVKAIIYTDISRDGTLSGPNFELYKELAAATGIPVIASGGVSSLDDIKAL-KELGVAGVIVGKALYEGKI 227


                 ....*..
gi 518491212 239 AIPELKR 245
Cdd:cd04732  228 TLEEALA 234
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 6-242 8.71e-27

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


Pssm-ID: 184165  Cd Length: 241  Bit Score: 103.83  E-value: 8.71e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   6 IIPCLDVRDGRVVK---GVRFRDHVDMGDIAELAQRYRDQGADELVFYDIGASPEARSVDVTWIERIARLIDIPFCVAGG 82
Cdd:PRK13585   5 VIPAVDMKGGKCVQlvqGEPGTETVSYGDPVEVAKRWVDAGAETLHLVDLDGAFEGERKNAEAIEKIIEAVGVPVQLGGG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  83 IDSVETARRVLFAGADKVSINSPALGRPELITELADEFGVQCVVVGVDSvreADGQWRVrrfSGDPDKTQAVPlrtLDWI 162
Cdd:PRK13585  85 IRSAEDAASLLDLGVDRVILGTAAVENPEIVRELSEEFGSERVMVSLDA---KDGEVVI---KGWTEKTGYTP---VEAA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212 163 VEAQRRGAGEIVLNCMDSDGVRRGYDVVQLQQARALCQVPLIASGGAGAMEHFAeAFDQADVDGALAASVFHSGAIAIPE 242
Cdd:PRK13585 156 KRFEELGAGSILFTNVDVEGLLEGVNTEPVKELVDSVDIPVIASGGVTTLDDLR-ALKEAGAAGVVVGSALYKGKFTLEE 234
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 5-248 1.70e-25

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: 100.11  E-value: 1.70e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   5 RIIPCLDVRDGRVV---KGVRFRDHVDMGDIAELAQRYRDQGADELVFYDIGASPEARSVDVTWIERIARLIDIPFCVAG 81
Cdd:COG0106    1 IIIPAIDLKDGKCVrlvQGDYDQETVYSDDPVEVAKRWEDAGAEWLHLVDLDGAFAGKPVNLELIEEIAKATGLPVQVGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  82 GIDSVETARRVLFAGADKVSINSPALGRPELITELADEFGVQcVVVGVDsVReaDGQWRVRRFsgdpdkTQAVPLRTLDW 161
Cdd:COG0106   81 GIRSLEDIERLLDAGASRVILGTAAVKDPELVKEALEEFPER-IVVGLD-AR--DGKVATDGW------QETSGVDLEEL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212 162 IVEAQRRGAGEIVLNCMDSDGVRRGYDVVQLQQARALCQVPLIASGGAGAMEHFaEAFDQADVDGALAASVFHSGAIAIP 241
Cdd:COG0106  151 AKRFEDAGVAAILYTDISRDGTLQGPNLELYRELAAATGIPVIASGGVSSLDDL-RALKELGVEGAIVGKALYEGKIDLE 229


                 ....*..
gi 518491212 242 ELKRYLR 248
Cdd:COG0106  230 EALALAR 236
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 5-245 4.81e-25

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: 98.88  E-value: 4.81e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   5 RIIPCLDVRDGRVVKGVRF-RDH--------VDMGDIAELAQRYRDQGADELVFYDIGASpEARSVDVTWIERIARLIDI 75
Cdd:cd04723    1 RIIPVIDLKDGVVVHGVGGdRDNyrpitsnlCSTSDPLDVARAYKELGFRGLYIADLDAI-MGRGDNDEAIRELAAAWPL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  76 PFCVAGGIDSVETARRVLFAGADKVSINSPALgRPELITELADEFGVQCVVVGVDsvreadgqwrvrrFSGDPDKTQAVP 155
Cdd:cd04723   80 GLWVDGGIRSLENAQEWLKRGASRVIVGTETL-PSDDDEDRLAALGEQRLVLSLD-------------FRGGQLLKPTDF 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212 156 LRTLDWIVEAQRRgAGEIVLNCMDSDGVRRGYDVVQLQQARALCQVPLIASGGAGAMEHFAEAfDQADVDGALAASVFHS 235
Cdd:cd04723  146 IGPEELLRRLAKW-PEELIVLDIDRVGSGQGPDLELLERLAARADIPVIAAGGVRSVEDLELL-KKLGASGALVASALHD 223

                        250
                 ....*....|
gi 518491212 236 GAIAIPELKR 245
Cdd:cd04723  224 GGLTLEDVVR 233
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 6-242 1.38e-22

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: 92.26  E-value: 1.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212    6 IIPCLDVRDGRVV---KGVRFRDHVDMGDIAELAQRYRDQGADELVFYDIGASPEARSVDVTWIERIARLIDIPFCVAGG 82
Cdd:TIGR00007   1 IIPAIDIKDGKCVrlyQGDYDKETVYGDDPVEAAKKWEEEGAERIHVVDLDGAKEGGPVNLPVIKKIVRETGVPVQVGGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   83 IDSVETARRVLFAGADKVSINSPALGRPELITELADEFGVQCVVVGVDSvreadgqwRVRR--FSGDPDKTQAVPlrtLD 160
Cdd:TIGR00007  81 IRSLEDVEKLLDLGVDRVIIGTAAVENPDLVKELLKEYGPERIVVSLDA--------RGGEvaVKGWLEKSEVSL---EE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  161 WIVEAQRRGAGEIVLNCMDSDGVRRGYDVVQLQQARALCQVPLIASGGAGAMEHFaEAFDQADVDGALAASVFHSGAIAI 240
Cdd:TIGR00007 150 LAKRLEELGLEGIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASGGVSSIDDL-IALKKLGVYGVIVGKALYEGKITL 228


                  ..
gi 518491212  241 PE 242
Cdd:TIGR00007 229 EE 230
PRK00748 PRK00748
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 6-242 3.12e-16

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


Pssm-ID: 179108  Cd Length: 233  Bit Score: 75.49  E-value: 3.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   6 IIPCLDVRDGRVV---KGvrfrdhvDMG-------DIAELAQRYRDQGADELVFYDI-GA-SPEARSVDVtwIERIARLI 73
Cdd:PRK00748   3 IIPAIDLKDGKCVrlyQG-------DYDqatvysdDPVAQAKAWEDQGAKWLHLVDLdGAkAGKPVNLEL--IEAIVKAV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  74 DIPFCVAGGIDSVETARRVLFAGADKVSINSPALGRPELITELADEFGVQcVVVGVDsVReaDGQWRVRRFSGDPDKTqa 153
Cdd:PRK00748  74 DIPVQVGGGIRSLETVEALLDAGVSRVIIGTAAVKNPELVKEACKKFPGK-IVVGLD-AR--DGKVATDGWLETSGVT-- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212 154 vplrTLDWIVEAQRRGAGEIVlnCMD--SDGVRRGydvVQLQQARALCQ---VPLIASGGAGAMEHFAEAFDQADVDGAL 228
Cdd:PRK00748 148 ----AEDLAKRFEDAGVKAII--YTDisRDGTLSG---PNVEATRELAAavpIPVIASGGVSSLDDIKALKGLGAVEGVI 218

                        250
                 ....*....|....
gi 518491212 229 AASVFHSGAIAIPE 242
Cdd:PRK00748 219 VGRALYEGKFDLAE 232
PRK14024 PRK14024
phosphoribosyl isomerase A; Provisional
 6-242 1.96e-08

phosphoribosyl isomerase A; Provisional


Pssm-ID: 237589  Cd Length: 241  Bit Score: 53.42  E-value: 1.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   6 IIPCLDVRDGRVVKGVRFRD--HVDMGDIAELAQRYRDQGADELVFYDIGASpEARSVDVTWIERIARLIDIPFCVAGGI 83
Cdd:PRK14024   6 LLPAVDVVDGQAVRLVQGEAgsETSYGSPLDAALAWQRDGAEWIHLVDLDAA-FGRGSNRELLAEVVGKLDVKVELSGGI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  84 DSVETARRVLFAGADKVSINSPALGRPELITELADEFGVQcVVVGVDSvreadGQWRVR-----RFSGDPDKTqavpLRT 158
Cdd:PRK14024  85 RDDESLEAALATGCARVNIGTAALENPEWCARVIAEHGDR-VAVGLDV-----RGHTLAargwtRDGGDLWEV----LER 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212 159 LDwiveaqRRGAGEIVLNCMDSDGVRRGYDVVQLQQARALCQVPLIASGGAGAMEHFAE--AFDQADVDGALAASVFHSG 236
Cdd:PRK14024 155 LD------SAGCSRYVVTDVTKDGTLTGPNLELLREVCARTDAPVVASGGVSSLDDLRAlaELVPLGVEGAIVGKALYAG 228


                 ....*.
gi 518491212 237 AIAIPE 242
Cdd:PRK14024 229 AFTLPE 234
PRK14114 PRK14114
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 6-248 4.15e-08

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


Pssm-ID: 172604  Cd Length: 241  Bit Score: 52.71  E-value: 4.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   6 IIPCLDVRDGRVVKGVRFRDHVDM---GDIAELAQRYRDQGADELVFYDIGASPEARSVDVTWIERIARLIDiPFCVAGG 82
Cdd:PRK14114   3 VVPAIDLFRGKVARMVKGKKENTIfyeKDPAELVEKLIEEGFTLIHVVDLSKAIENSVENLPVLEKLSEFAE-HIQIGGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  83 IDSVETARRVLFAGADKVSINSPALGRPELITELADefgvqcvvVGVDSVREADGQWRVRRFSGDPDKTQAVPLRTLDWI 162
Cdd:PRK14114  82 IRSLDYAEKLRKLGYRRQIVSSKVLEDPSFLKFLKE--------IDVEPVFSLDTRGGKVAFKGWLAEEEIDPVSLLKRL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212 163 VEAqrrGAGEIVLNCMDSDGVRRGYDVVQLQQARALCQVPLIASGGAGAMEHFAEAFD-----QADVDGALAASVFHSGA 237
Cdd:PRK14114 154 KEY---GLEEIVHTEIEKDGTLQEHDFSLTRKIAIEAEVKVFAAGGISSENSLKTAQRvhretNGLLKGVIVGRAFLEGI 230

                        250
                 ....*....|.
gi 518491212 238 IAIPELKRYLR 248
Cdd:PRK14114 231 LTVEVMKRYAR 241
PRK13586 PRK13586
1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ...
 5-130 2.49e-07

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


Pssm-ID: 237439  Cd Length: 232  Bit Score: 50.12  E-value: 2.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   5 RIIPCLDVRDGRVVKGVRFRDH--VDMGDIAELAQRYRDQGADELVFYDIGASpEARSVDVTWIERIARLIDIPFCVAGG 82
Cdd:PRK13586   3 KIIPSIDISLGKAVKRIRGVKGtgLILGNPIEIASKLYNEGYTRIHVVDLDAA-EGVGNNEMYIKEISKIGFDWIQVGGG 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 518491212  83 IDSVETARRVLFAGADKVSINSPALGRPELITELADEFGVQCVVVGVD 130
Cdd:PRK13586  82 IRDIEKAKRLLSLDVNALVFSTIVFTNFNLFHDIVREIGSNRVLVSID 129
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
 31-120 1.75e-06

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: 48.17  E-value: 1.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  31 DIAELAQRYRDQGADELV--------FYdigaSPEArsvDVTWIERIARLIDIPFCVAGGIDSVETARRVL-FAGADKVS 101
Cdd:COG0042  147 NALEFARIAEDAGAAALTvhgrtreqRY----KGPA---DWDAIARVKEAVSIPVIGNGDIFSPEDAKRMLeETGCDGVM 219

                         90
                 ....*....|....*....
gi 518491212 102 INSPALGRPELITELADEF 120
Cdd:COG0042  220 IGRGALGNPWLFREIDAYL 238
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 3-97 2.53e-06

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: 47.19  E-value: 2.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212    3 SRRIIPCLDVRDGRV-VKGVRFRDHVdmgDIAELAQRYRDQGADELVFYDIGASPEARSVDVTWIERIARLIDIPFCVAG 81
Cdd:TIGR00007 120 PERIVVSLDARGGEVaVKGWLEKSEV---SLEELAKRLEELGLEGIIYTDISRDGTLSGPNFELTKELVKAVNVPVIASG 196

                          90
                  ....*....|....*....
gi 518491212   82 GI---DSVETARRVLFAGA 97
Cdd:TIGR00007 197 GVssiDDLIALKKLGVYGV 215
pyrD_sub1_fam TIGR01037
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ...
 28-119 2.71e-04

dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 dihydroorotate dehydrogenases while excluding the closely related subfamily 2 (TIGR01036). This family also includes a number of uncharacterized proteins and a domain of dihydropyrimidine dehydrogenase. The uncharacterized proteins might all be dihydroorotate dehydrogenase.


Pssm-ID: 130109 [Multi-domain]  Cd Length: 300  Bit Score: 41.64  E-value: 2.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   28 DMGDIAELAQRYRDQGADELVF--------YDI------------GAS-PEARSVDVTWIERIARLIDIPFCVAGGIDSV 86
Cdd:TIGR01037 167 NVTDITEIAKAAEEAGADGLTLintlrgmkIDIktgkpilanktgGLSgPAIKPIALRMVYDVYKMVDIPIIGVGGITSF 246

                          90       100       110
                  ....*....|....*....|....*....|...
gi 518491212   87 ETARRVLFAGADKVSINSPALGRPELITELADE 119
Cdd:TIGR01037 247 EDALEFLMAGASAVQVGTAVYYRGFAFKKIIEG 279
Dus pfam01207
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ...
 17-115 2.95e-04

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: 41.54  E-value: 2.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   17 VVKGVRFRDHVDMGDIAELAQRYRDQGADELVFYdiGASPEARS---VDVTWIERIARLIDIPFCVAGGIDSVETARRVL 93
Cdd:pfam01207 125 VTVKIRIGWDDSHENAVEIAKIVEDAGAQALTVH--GRTRAQNYegtADWDAIKQVKQAVSIPVIANGDITDPEDAQRCL 202

                          90       100
                  ....*....|....*....|...
gi 518491212   94 -FAGADKVSINSPALGRPELITE 115
Cdd:pfam01207 203 aYTGADGVMIGRGALGNPWLFAE 225
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 29-115 3.69e-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: 40.64  E-value: 3.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  29 MGDIAELAQRYRdqgADELVFYDIG--------ASPEARSVDVTWIERIARLIDIPFCVAGGIDSVETARRVLFAGADKV 100
Cdd:cd04729  127 MADISTLEEALN---AAKLGFDIIGttlsgyteETAKTEDPDFELLKELRKALGIPVIAEGRINSPEQAAKALELGADAV 203

                         90
                 ....*....|....*
gi 518491212 101 SINSpALGRPELITE 115
Cdd:cd04729  204 VVGS-AITRPEHITG 217
PcrB COG1646
Glycerol-1-phosphate heptaprenyltransferase [Lipid transport and metabolism];
59-98 4.11e-04

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


Pssm-ID: 441252  Cd Length: 241  Bit Score: 40.53  E-value: 4.11e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 518491212  59 RSVDVTWIERIAR-LIDIPFCVAGGIDSVETARRVLFAGAD 98
Cdd:COG1646  180 EPVDPEMVKAVKKaLEDTPLIYGGGIRSPEKAREMAEAGAD 220
PRK13587 PRK13587
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide ...
 8-208 4.43e-04

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


Pssm-ID: 172156  Cd Length: 234  Bit Score: 40.58  E-value: 4.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   8 PCLDVRDG---RVVKGvRFRDHVDMGDIAELAQRYRDQ--GADELVFYDIGASPEARSVDVTWIERIARLIDIPFCVAGG 82
Cdd:PRK13587   6 PAIDLIGStsvRLTEG-KYDSEEKMSRSAEESIAYYSQfeCVNRIHIVDLIGAKAQHAREFDYIKSLRRLTTKDIEVGGG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  83 IDSVETARRVLFAGADKVSINSPALGRPELITELADEFGVQcVVVGVDSVREadgQWRVRRFSGDPDktqavpLRTLDWI 162
Cdd:PRK13587  85 IRTKSQIMDYFAAGINYCIVGTKGIQDTDWLKEMAHTFPGR-IYLSVDAYGE---DIKVNGWEEDTE------LNLFSFV 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 518491212 163 VEAQRRGAGEIVLNCMDSDGVRRGYDVVQLQQARALCQVPLIASGG 208
Cdd:PRK13587 155 RQLSDIPLGGIIYTDIAKDGKMSGPNFELTGQLVKATTIPVIASGG 200
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 3-97 6.25e-04

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: 40.16  E-value: 6.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   3 SRRIIPCLDVRDGRV-VKGVRFRDHVdmgDIAELAQRYRDQGADELVFYDIGASPEARSVDVTWIERIARLIDIPFCVAG 81
Cdd:cd04732  121 GERIVVGLDAKDGKVaTKGWLETSEV---SLEELAKRFEELGVKAIIYTDISRDGTLSGPNFELYKELAAATGIPVIASG 197

                         90
                 ....*....|....*....
gi 518491212  82 GI---DSVETARRVLFAGA 97
Cdd:cd04732  198 GVsslDDIKALKELGVAGV 216
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 3-104 9.92e-04

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


Pssm-ID: 184165  Cd Length: 241  Bit Score: 39.51  E-value: 9.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   3 SRRIIPCLDVRDGRVV-KGvrFRDHVDMgDIAELAQRYRDQGADELVFYDIGASPEARSVDVTWIERIARLIDIPFCVAG 81
Cdd:PRK13585 124 SERVMVSLDAKDGEVViKG--WTEKTGY-TPVEAAKRFEELGAGSILFTNVDVEGLLEGVNTEPVKELVDSVDIPVIASG 200

                         90       100
                 ....*....|....*....|...
gi 518491212  82 GIDSVETARRVLFAGADKVSINS 104
Cdd:PRK13585 201 GVTTLDDLRALKEAGAAGVVVGS 223
PRK07565 PRK07565
dihydroorotate dehydrogenase-like protein;
32-119 1.97e-03

dihydroorotate dehydrogenase-like protein;


Pssm-ID: 236051  Cd Length: 334  Bit Score: 39.08  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  32 IAELAQRYRDQGADELV----FY--DIG------------ASPEARSVDVTWIERIARLIDIPFCVAGGIDSVETARRVL 93
Cdd:PRK07565 179 LANMAKRLDAAGADGLVlfnrFYqpDIDletlevvpglvlSTPAELRLPLRWIAILSGRVGADLAATTGVHDAEDVIKML 258

                         90       100
                 ....*....|....*....|....*...
gi 518491212  94 FAGADKVSINSpALGR--PELITELADE 119
Cdd:PRK07565 259 LAGADVVMIAS-ALLRhgPDYIGTILRG 285
FadH COG1902
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ...
 14-119 2.00e-03

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: 39.00  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  14 DGRVvkGVRF--RDHVDMG----DIAELAQRYRDQGADelvFYDIGA------------SPEARSVDVTwiERIARLIDI 75
Cdd:COG1902  216 DFPV--GVRLspTDFVEGGltleESVELAKALEEAGVD---YLHVSSggyepdamiptiVPEGYQLPFA--ARIRKAVGI 288

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 518491212  76 PFCVAGGIDSVETARRVLFAG-ADKVSINSPALGRPELITELADE 119
Cdd:COG1902  289 PVIAVGGITTPEQAEAALASGdADLVALGRPLLADPDLPNKAAAG 333
OYE_like_FMN_family cd02803
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
 23-113 2.47e-03

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


Pssm-ID: 239201 [Multi-domain]  Cd Length: 327  Bit Score: 38.71  E-value: 2.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  23 FRDHVDMGDIAELAQRYRDQGAD---------ELVFYDIGASPEARSVDVTWIERIARLIDIPFCVAGGIDSVETARRVL 93
Cdd:cd02803  221 VPGGLTLEEAIEIAKALEEAGVDalhvsggsyESPPPIIPPPYVPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEIL 300

                         90       100
                 ....*....|....*....|.
gi 518491212  94 FAG-ADKVSINSPALGRPELI 113
Cdd:cd02803  301 AEGkADLVALGRALLADPDLP 321
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 34-120 3.76e-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: 37.47  E-value: 3.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  34 ELAQRYRDQGADELVFYdiGASPEARS---VDVTWIERIARLIDIPFCVAGGIDSVETARRVL-FAGADKVSINSPALGR 109
Cdd:cd02801  142 ELAKALEDAGASALTVH--GRTREQRYsgpADWDYIAEIKEAVSIPVIANGDIFSLEDALRCLeQTGVDGVMIGRGALGN 219

                         90
                 ....*....|.
gi 518491212 110 PELITELADEF 120
Cdd:cd02801  220 PWLFREIKELL 230
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 3-119 4.08e-03

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: 37.63  E-value: 4.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212   3 SRRIIPCLDVRDGRVVKGVRFRDHVdmgDIAELAQRYrdqgADELVFYDIGASPEARSVDVTWIERIARLIDIPFCVAGG 82
Cdd:cd04723  125 EQRLVLSLDFRGGQLLKPTDFIGPE---ELLRRLAKW----PEELIVLDIDRVGSGQGPDLELLERLAARADIPVIAAGG 197

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 518491212  83 IDSVETARRVLFAGADKVSINSpALGRPELITELADE 119
Cdd:cd04723  198 VRSVEDLELLKKLGASGALVAS-ALHDGGLTLEDVVR 233
DHOD_like cd04739
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ...
 32-119 5.67e-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: 37.59  E-value: 5.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  32 IAELAQRYRDQGADELV----FY--DIG------------ASPEARSVDVTWIERIARLIDIPFCVAGGIDSVETARRVL 93
Cdd:cd04739  177 LAHMAKQLDAAGADGLVlfnrFYqpDIDletlevvpnlllSSPAEIRLPLRWIAILSGRVKASLAASGGVHDAEDVVKYL 256

                         90       100
                 ....*....|....*....|....*...
gi 518491212  94 FAGADKVSINSpALGR--PELITELADE 119
Cdd:cd04739  257 LAGADVVMTTS-ALLRhgPDYIGTLLAG 283
PcrB_like cd02812
PcrB_like proteins. One member of this family, a protein from Archaeoglobus fulgidus, has been ...
 61-102 7.03e-03

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: 36.83  E-value: 7.03e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 518491212  61 VDVTWIERIARLI-DIPFCVAGGIDSVETARRVLFAGADKVSI 102
Cdd:cd02812  161 GPPEVVRAVKKVLgDTPLIVGGGIRSGEQAKEMAEAGADTIVV 203
OYE_like_3_FMN cd04734
Old yellow enzyme (OYE)-related FMN binding domain, group 3. Each monomer of OYE contains FMN ...
 12-118 9.17e-03

Old yellow enzyme (OYE)-related FMN binding domain, group 3. 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. One member of this subgroup, the Sinorhizobium meliloti stachydrine utilization protein stcD, has been idenified as a putative N-methylproline demethylase.


Pssm-ID: 240085 [Multi-domain]  Cd Length: 343  Bit Score: 36.82  E-value: 9.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518491212  12 VRDGRVVkGVRF------RDHVDMGDIAELAQRYRDQGADELV------FYDIGAS---------PEARSVDVTwiERIA 70
Cdd:cd04734  205 VGPDFIV-GIRIsgdedtEGGLSPDEALEIAARLAAEGLIDYVnvsagsYYTLLGLahvvpsmgmPPGPFLPLA--ARIK 281

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 518491212  71 RLIDIPFCVAGGIDSVETARRVLFAG-ADKVSINSPALGRPELITELAD 118
Cdd:cd04734  282 QAVDLPVFHAGRIRDPAEAEQALAAGhADMVGMTRAHIADPHLVAKARE 330
 
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