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Conserved domains on  [gi|1604577489|gb|TFG52414|]
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bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase, partial [Hyphomicrobiales bacterium]

Protein Classification

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase( domain architecture ID 10001245)

bifunctional enzyme, phosphomethylpyrimidine (HMP-P) kinase/hydroxymethylpyrimidine (HMP) kinase; bifunctional hydroxymethylpyrimidine (HMP) kinase/phosphomethylpyrimidine (HMP-P) kinase catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P

CATH:  3.40.1190.20
EC:  2.7.4.7|2.7.1.49
Gene Symbol:  thiD
Gene Ontology:  GO:0005524|GO:0016310|GO:0042724|GO:0008902|GO:0008972|GO:0009228|GO:0005829
PubMed:  8382990|11839308
SCOP:  3001268

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 1-154 1.78e-61

Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase is part of the Pathway/BioSystem: Thiamine biosynthesis


:

Pssm-ID: 440120 [Multi-domain]  Cd Length: 254  Bit Score: 189.86  E-value: 1.78e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489   1 VMFAKGGAALLDGGGVAALKELLLPRAELVTPNAPEAAMLTGIRVETPDDLVQAGQALIALGARAALVKGGHLQGPMVTD 80
Cdd:COG0351   101 VMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLELGAKAVLVKGGHLPGDEAVD 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604577489  81 ALVTAFDVHLFEAWRMDTVSTHGTGCTLASACAAGIAQGMELFDAVARAHRYVQDAIATAPGFGKGSGPLNHMH 154
Cdd:COG0351   181 VLYDGDGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQAIRAALRLGMGHGPVNHFA 254
 
Name Accession Description Interval E-value
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 1-154 1.78e-61

Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440120 [Multi-domain]  Cd Length: 254  Bit Score: 189.86  E-value: 1.78e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489   1 VMFAKGGAALLDGGGVAALKELLLPRAELVTPNAPEAAMLTGIRVETPDDLVQAGQALIALGARAALVKGGHLQGPMVTD 80
Cdd:COG0351   101 VMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLELGAKAVLVKGGHLPGDEAVD 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604577489  81 ALVTAFDVHLFEAWRMDTVSTHGTGCTLASACAAGIAQGMELFDAVARAHRYVQDAIATAPGFGKGSGPLNHMH 154
Cdd:COG0351   181 VLYDGDGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQAIRAALRLGMGHGPVNHFA 254
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 1-151 9.94e-55

Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.


Pssm-ID: 430062 [Multi-domain]  Cd Length: 246  Bit Score: 172.67  E-value: 9.94e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489   1 VMFAKGGAALLDGGGVAALKELLLPRAELVTPNAPEAAMLTGIRVETPDDLVQAGQALIALGARAALVKGGHLQGP--MV 78
Cdd:pfam08543  94 VMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKGGHLEGEeaVV 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604577489  79 TDALVTAFDVHLFEAWRMDTVSTHGTGCTLASACAAGIAQGMELFDAVARAHRYVQDAIATAPGFGKGSGPLN 151
Cdd:pfam08543 174 TDVLYDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVTEAIRDALNLGKGHGPVN 246
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 1-140 2.21e-49

4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two consecutive phosphorylation steps in the thiamine phosphate biosynthesis pathway, leading to the synthesis of vitamin B1. The first step is the phosphorylation of the hydroxyl group of HMP to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate (HMP-P) and then the phophorylation of HMP-P to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine pyrophosphate (HMP-PP), which is the substrate for the thiamine synthase coupling reaction.


Pssm-ID: 238574 [Multi-domain]  Cd Length: 242  Bit Score: 158.82  E-value: 2.21e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489   1 VMFAKGGAALLDGGGVAALKELLLPRAELVTPNAPEAAMLTGIRVETPDDLVQAGQALIALGARAALVKGGHLQGPMVTD 80
Cdd:cd01169   103 VMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTGLEIATEEDMMKAAKALLALGAKAVLIKGGHLPGDEAVD 182

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489  81 ALVTAFDVHLFEAWRMDTVSTHGTGCTLASACAAGIAQGMELFDAVARAHRYVQDAIATA 140
Cdd:cd01169   183 VLYDGGGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQAIRNA 242
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 1-154 3.82e-48

bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 156.44  E-value: 3.82e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489   1 VMFAKGGAALLDGGGVAALKELLLPRAELVTPNAPEAAMLTGIRVETPDD-LVQAGQALIALGARAALVKGGH-LQGPMV 78
Cdd:PRK06427  108 VMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTGLPIADTEDeMKAAARALHALGCKAVLIKGGHlLDGEES 187

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604577489  79 TDALVTAFDVHLFEAWRMDTVSTHGTGCTLASACAAGIAQGMELFDAVARAHRYVQDAIATAPGFGKGSGPLNHMH 154
Cdd:PRK06427  188 VDWLFDGEGEERFSAPRIPTKNTHGTGCTLSAAIAAELAKGASLLDAVQTAKDYVTRAIRHALEIGQGHGPVNHFA 263
HMP-P_kinase TIGR00097
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ...
 1-152 1.15e-45

hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a bifunctional enzyme, phosphomethylpyrimidine kinase (EC 2.7.4.7)/Hydroxymethylpyrimidine kinase (EC 2.7.1.49), the ThiD/J protein of thiamine biosynthesis. The protein is commonly observed within operons containing other thiamine biosynthesis genes. Numerous examples are fusion proteins with other thiamine-biosynthetic domains. Saccaromyces has three recent paralogs, two of which are isofunctional and score above the trusted cutoff. The third shows a longer branch length in a phylogenetic tree and scores below the trusted cutoff, as do putative second copies in a number of species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 272904 [Multi-domain]  Cd Length: 254  Bit Score: 149.75  E-value: 1.15e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489   1 VMFAKGGAALLDGGGVAALKELLLPRAELVTPNAPEAAMLTGIRVETPDDLVQAGQALIALGARAALVKGGHLQGPMVTD 80
Cdd:TIGR00097 102 VMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGTKIRTEQDMIKAAKKLRELGPKAVLIKGGHLEGDQAVD 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604577489  81 ALVTAFDVHLFEAWRMDTVSTHGTGCTLASACAAGIAQGMELFDAVARAHRYVQDAIATAPGFGKGSGPLNH 152
Cdd:TIGR00097 182 VLFDGGEIHILKAPRIETKNTHGTGCTLSAAIAANLAKGLSLKEAVKEAKEFVTGAIRYGLNIGHGHGPLNH 253
 
Name Accession Description Interval E-value
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 1-154 1.78e-61

Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440120 [Multi-domain]  Cd Length: 254  Bit Score: 189.86  E-value: 1.78e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489   1 VMFAKGGAALLDGGGVAALKELLLPRAELVTPNAPEAAMLTGIRVETPDDLVQAGQALIALGARAALVKGGHLQGPMVTD 80
Cdd:COG0351   101 VMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLELGAKAVLVKGGHLPGDEAVD 180

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604577489  81 ALVTAFDVHLFEAWRMDTVSTHGTGCTLASACAAGIAQGMELFDAVARAHRYVQDAIATAPGFGKGSGPLNHMH 154
Cdd:COG0351   181 VLYDGDGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQAIRAALRLGMGHGPVNHFA 254
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 1-151 9.94e-55

Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.


Pssm-ID: 430062 [Multi-domain]  Cd Length: 246  Bit Score: 172.67  E-value: 9.94e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489   1 VMFAKGGAALLDGGGVAALKELLLPRAELVTPNAPEAAMLTGIRVETPDDLVQAGQALIALGARAALVKGGHLQGP--MV 78
Cdd:pfam08543  94 VMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKGGHLEGEeaVV 173

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604577489  79 TDALVTAFDVHLFEAWRMDTVSTHGTGCTLASACAAGIAQGMELFDAVARAHRYVQDAIATAPGFGKGSGPLN 151
Cdd:pfam08543 174 TDVLYDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVTEAIRDALNLGKGHGPVN 246
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 1-140 2.21e-49

4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two consecutive phosphorylation steps in the thiamine phosphate biosynthesis pathway, leading to the synthesis of vitamin B1. The first step is the phosphorylation of the hydroxyl group of HMP to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate (HMP-P) and then the phophorylation of HMP-P to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine pyrophosphate (HMP-PP), which is the substrate for the thiamine synthase coupling reaction.


Pssm-ID: 238574 [Multi-domain]  Cd Length: 242  Bit Score: 158.82  E-value: 2.21e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489   1 VMFAKGGAALLDGGGVAALKELLLPRAELVTPNAPEAAMLTGIRVETPDDLVQAGQALIALGARAALVKGGHLQGPMVTD 80
Cdd:cd01169   103 VMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTGLEIATEEDMMKAAKALLALGAKAVLIKGGHLPGDEAVD 182

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489  81 ALVTAFDVHLFEAWRMDTVSTHGTGCTLASACAAGIAQGMELFDAVARAHRYVQDAIATA 140
Cdd:cd01169   183 VLYDGGGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQAIRNA 242
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 1-154 3.82e-48

bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 156.44  E-value: 3.82e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489   1 VMFAKGGAALLDGGGVAALKELLLPRAELVTPNAPEAAMLTGIRVETPDD-LVQAGQALIALGARAALVKGGH-LQGPMV 78
Cdd:PRK06427  108 VMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTGLPIADTEDeMKAAARALHALGCKAVLIKGGHlLDGEES 187

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1604577489  79 TDALVTAFDVHLFEAWRMDTVSTHGTGCTLASACAAGIAQGMELFDAVARAHRYVQDAIATAPGFGKGSGPLNHMH 154
Cdd:PRK06427  188 VDWLFDGEGEERFSAPRIPTKNTHGTGCTLSAAIAAELAKGASLLDAVQTAKDYVTRAIRHALEIGQGHGPVNHFA 263
HMP-P_kinase TIGR00097
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ...
 1-152 1.15e-45

hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a bifunctional enzyme, phosphomethylpyrimidine kinase (EC 2.7.4.7)/Hydroxymethylpyrimidine kinase (EC 2.7.1.49), the ThiD/J protein of thiamine biosynthesis. The protein is commonly observed within operons containing other thiamine biosynthesis genes. Numerous examples are fusion proteins with other thiamine-biosynthetic domains. Saccaromyces has three recent paralogs, two of which are isofunctional and score above the trusted cutoff. The third shows a longer branch length in a phylogenetic tree and scores below the trusted cutoff, as do putative second copies in a number of species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 272904 [Multi-domain]  Cd Length: 254  Bit Score: 149.75  E-value: 1.15e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489   1 VMFAKGGAALLDGGGVAALKELLLPRAELVTPNAPEAAMLTGIRVETPDDLVQAGQALIALGARAALVKGGHLQGPMVTD 80
Cdd:TIGR00097 102 VMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGTKIRTEQDMIKAAKKLRELGPKAVLIKGGHLEGDQAVD 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604577489  81 ALVTAFDVHLFEAWRMDTVSTHGTGCTLASACAAGIAQGMELFDAVARAHRYVQDAIATAPGFGKGSGPLNH 152
Cdd:TIGR00097 182 VLFDGGEIHILKAPRIETKNTHGTGCTLSAAIAANLAKGLSLKEAVKEAKEFVTGAIRYGLNIGHGHGPLNH 253
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 1-153 4.48e-37

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 132.97  E-value: 4.48e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489   1 VMFAKGGAALLDGGGVAALKELLLPRAELVTPNAPEA-AMLTGIRVETPDDLVQAGQALIALGARAALVKGGHLQGPM-V 78
Cdd:PLN02898  113 VMVSTSGDVLAGPSILSALREELLPLATIVTPNVKEAsALLGGDPLETVADMRSAAKELHKLGPRYVLVKGGHLPDSLdA 192

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604577489  79 TDALVTAFDVHLFEAWRMDTVSTHGTGCTLASACAAGIAQGMELFDAVARAHRYVQDAIATAPGFGKGS---GPLNHM 153
Cdd:PLN02898  193 VDVLYDGTEFHELRSSRIKTRNTHGTGCTLASCIAAELAKGSDMLSAVKVAKRYVETALEYSKDIGIGNgaqGPFNHL 270
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
1-153 1.44e-36

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 130.62  E-value: 1.44e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489   1 VMFAKGGAALLDGGGVAALKELLLPRAELVTPNAPEAAMLTGIRVETPDDLVQAGQALIA-LGARAALVKGGHLQGPMVT 79
Cdd:PRK08573  105 VMIAKSGAPLLREDAVDALIKRLLPLATVVTPNRPEAEKLTGMKIRSVEDARKAAKYIVEeLGAEAVVVKGGHLEGEEAV 184

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604577489  80 DALVTAFDVHLFEAWRMDTVSTHGTGCTLASACAAGIAQGMELFDAVARAHRYVQDAIATAPGFGKGSGPLNHM 153
Cdd:PRK08573  185 DVLYHNGTFREFRAPRVESGCTHGTGCSFSAAIAAGLAKGLDPEEAIKTAKKFITMAIKYGVKIGKGHCPVNPM 258
PRK14713 PRK14713
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
17-157 2.25e-27

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 237797 [Multi-domain]  Cd Length: 530  Bit Score: 106.41  E-value: 2.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489  17 AALKELLlPRAELVTPNAPEAAMLTGI-RVETPDDLVQAGQALIALGARAALVKGGHLQGPMVTDALV-TAFDVHLFEAW 94
Cdd:PRK14713  149 AALRELV-PRADLITPNLPELAVLLGEpPATTWEEALAQARRLAAETGTTVLVKGGHLDGQRAPDALVgPDGAVTEVPGP 227

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1604577489  95 RMDTVSTHGTGCTLASACAAGIAQGMELFDAVARAHRYVQDAIATAPGF--GKGSGPLNHMHNFR 157
Cdd:PRK14713  228 RVDTRNTHGTGCSLSSALATRLGRGGDWAAALRWATAWLHGAIAAGAALqvGTGNGPVDHFHRAR 292
PRK12412 PRK12412
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
1-152 1.82e-25

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183512 [Multi-domain]  Cd Length: 268  Bit Score: 98.12  E-value: 1.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489   1 VMFAKGGAALLDGGGVAALKELLLPRAELVTPNAPEAAMLTGIRVETPDDLVQAGQALIALGARAALVKGGH-LQGPMVT 79
Cdd:PRK12412  107 VMVCKGADEALHPETNDCLRDVLVPKALVVTPNLFEAYQLSGVKINSLEDMKEAAKKIHALGAKYVLIKGGSkLGTETAI 186

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1604577489  80 DALVTAFDVHLFEAWRMDTVSTHGTGCTLASACAAGIAQGMELFDAVARAHRYVQDAIATAPGFGKGSGPLNH 152
Cdd:PRK12412  187 DVLYDGETFDLLESEKIDTTNTHGAGCTYSAAITAELAKGKPVKEAVKTAKEFITAAIRYSFKINEYVGPTHH 259
PTZ00347 PTZ00347
phosphomethylpyrimidine kinase; Provisional
 16-155 1.56e-22

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240375 [Multi-domain]  Cd Length: 504  Bit Score: 92.72  E-value: 1.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489  16 VAALKELLLPRAELVTPNAPEAAMLTGIR-VETPDDLVQAGQALIALGARAALVKGGHLQ--GPMVTDALV--TAFDVHL 90
Cdd:PTZ00347  350 LAMYKERIFPMATIITPNIPEAERILGRKeITGVYEARAAAQALAQYGSRYVLVKGGHDLidPEACRDVLYdrEKDRFYE 429

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1604577489  91 FEAWRMDTVSTHGTGCTLASACAAGIAQGMELFDAVARAHRYVQDAIATA--PGFGKGS-GPLNHMHN 155
Cdd:PTZ00347  430 FTANRIATINTHGTGCTLASAISSFLARGYTVPDAVERAIGYVHEAIVRScgVPLGQGTnRPLVHSLN 497
PRK12616 PRK12616
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
1-152 3.21e-20

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183624  Cd Length: 270  Bit Score: 84.33  E-value: 3.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489   1 VMFAKGGAALLDGGGVAALKELLLPRAELVTPNAPEAAMLTGI-RVETPDDLVQAGQALIALGARAALVKGG-HLQGPMV 78
Cdd:PRK12616  109 VMVCKGANEVLYPEHAEALREQLAPLATVITPNLFEAGQLSGMgEIKTVEQMKEAAKKIHELGAQYVVITGGgKLKHEKA 188

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1604577489  79 TDALVTAFDVHLFEAWRMDTVSTHGTGCTLASACAAGIAQGMELFDAVARAHRYVQDAIATAPGFGKGSGPLNH 152
Cdd:PRK12616  189 VDVLYDGETAEVLESEMIDTPYTHGAGCTFSAAVTAELAKGSEVKEAIYAAKEFITAAIKESFPLNQYVGPTKH 262
PRK09517 PRK09517
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ...
 1-157 3.60e-20

multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 169939 [Multi-domain]  Cd Length: 755  Bit Score: 86.18  E-value: 3.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489   1 VMFAKGGAALLDGGGVAALKELLlPRAELVTPNAPEAAMLTGIR-VETPDDLVQAGQALIALGARAALVKGGHLQGPMVT 79
Cdd:PRK09517  345 VMVATSGDRLLDADATEALRRLA-VHVDVVTPNIPELAVLCGEApAITMDEAIAQARGFARTHGTIVIVKGGHLTGDLAD 423

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489  80 DALVTA-FDVHLFEAWRMDTVSTHGTGCTLASACAAGIAQGMELFDAVARAHRYVQDAIATAP--GFGKGSGPLNHMHNF 156
Cdd:PRK09517  424 NAVVRPdGSVHQVENPRVNTTNSHGTGCSLSAALATLIAAGESVEKALEWATRWLNEALRHADhlAVGSGNGPVDHGHLA 503


                  .
gi 1604577489 157 R 157
Cdd:PRK09517  504 R 504
COG1992 COG1992
Predicted transcriptional regulator fused phosphomethylpyrimidine kinase (thiamin biosynthesis) ...
 1-159 6.66e-20

Predicted transcriptional regulator fused phosphomethylpyrimidine kinase (thiamin biosynthesis) [General function prediction only];


Pssm-ID: 441595 [Multi-domain]  Cd Length: 432  Bit Score: 84.81  E-value: 6.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489   1 VMFAKGGAALLDGGGVAALKELLLPRAELVTPNAPEA-AMLTGIRVETPDDLVQAGQALIALGARAALVKGGHLQGPMVT 79
Cdd:COG1992    92 VPVAVAAAGLGLLLAEAELAKLLLPLLATVTPNEPEVeELLLPTIRSLLAEARAARLALQEEGADALGVKGGHVSGDAVV 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489  80 DALVTAFDVHLFEAWRMDTVSTHGTGCTLASACAAGIAQGMELFDAVARAHRYVQDAIATAPGFGKGSGPLNHMHNFRLE 159
Cdd:COG1992   172 DVLEDERDVETFRHPRLVTEATHGSGCTFSAAIAALLAKGLSLEEAVRGAKLFLLHAIRYGLLVGKGVGPVNHLADLRLE 251
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
16-144 8.13e-20

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 82.80  E-value: 8.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489  16 VAALKELLL---PRAELVTPNAPEAAMLTGIRVETPDDLVQAGQALIALGARAALVKGGH-LQGPMVTDALVTAFDVHLF 91
Cdd:PRK12413  116 VSELRQELIqffPYVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVIKGGNrLSQKKAIDLFYDGKEFVIL 195

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1604577489  92 EAWRMDTVSThGTGCTLASACAAGIAQGMELFDAVARAHRYVQDAIATAPGFG 144
Cdd:PRK12413  196 ESPVLEKNNI-GAGCTFASSIASQLVKGKSPLEAVKNSKDFVYQAIQQSDQYG 247
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 16-144 2.05e-17

Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal/pyridoxine/pyridoxamine kinase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 441841 [Multi-domain]  Cd Length: 272  Bit Score: 76.73  E-value: 2.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489  16 VAALKELLLPRAELVTPNAPEAAMLTGIRVETPDDLVQAGQALIALGARAALVKGGHLQGPM---VTDALVTAFDVHLFE 92
Cdd:COG2240   128 AEFIMRRLVPLADIITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVTSVPLDDTPadkIGNLAVTADGAWLVE 207

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1604577489  93 AWRMDtVSTHGTGCTLASACAAGIAQGMELFDAVARAHRYVQDAIATAPGFG 144
Cdd:COG2240   208 TPLLP-FSPNGTGDLFAALLLAHLLRGKSLEEALERAAAFVYEVLERTAAAG 258
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 16-139 2.83e-17

Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.


Pssm-ID: 238578 [Multi-domain]  Cd Length: 254  Bit Score: 76.08  E-value: 2.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489  16 VAALKELLLPRAELVTPNAPEAAMLTGIRVETPDDLVQAGQALIALGARAALVKGGHLQGPMVTDALVTAFDvhlfEAWR 95
Cdd:cd01173   126 VPVYRDLLVPLADIITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTSVELADDDRIEMLGSTAT----EAWL 201

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1604577489  96 MDT------VSTHGTGCTLASACAAGIAQGMELFDAVARAHRYVQDAIAT 139
Cdd:cd01173   202 VQRpkipfpAYFNGTGDLFAALLLARLLKGKSLAEALEKALNFVHEVLEA 251
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
16-138 1.18e-14

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 69.30  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489  16 VAALKELLLPRAELVTPNAPEAAMLTGIRVETPDDLVQAGQALIALGARAALVKGGHLQGP--MVTDALVTAFDVHLFEA 93
Cdd:PRK08176  142 PEAYRQHLLPLAQGLTPNIFELEILTGKPCRTLDSAIAAAKSLLSDTLKWVVITSAAGNEEnqEMQVVVVTADSVNVISH 221

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1604577489  94 WRMDTvSTHGTGCTLASACAAGIAQGMELFDAVARAHRYVQDAIA 138
Cdd:PRK08176  222 PRVDT-DLKGTGDLFCAELVSGLLKGKALTDAAHRAGLRVLEVMR 265
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
17-129 1.50e-11

1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 60.92  E-value: 1.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489  17 AALKELLLPRAELVTPNAPEAAMLTGIRVETPDDLVQAGQALIALGARAALV---KGGHLqgpmvtdaLVTAFDVHLFEA 93
Cdd:COG1105   168 EALKAALEAGPDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVslgADGAL--------LVTEDGVYRAKP 239

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1604577489  94 WRMDTVSTHGTG-CTLAsACAAGIAQGMELFDAVARA 129
Cdd:COG1105   240 PKVEVVSTVGAGdSMVA-GFLAGLARGLDLEEALRLA 275
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 16-132 7.21e-10

Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.


Pssm-ID: 238579 [Multi-domain]  Cd Length: 292  Bit Score: 56.02  E-value: 7.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489  16 VAALKELLLPRAELVTPNAPEAAMLTGIRVETPDDLVQAGQALIALGARAALVKGGHlQGpmvtDALVTAFDVHLFEAWR 95
Cdd:cd01174   165 ARPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGA-KG----ALLASGGEVEHVPAFK 239

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1604577489  96 MDTVSTHGTGCTLASACAAGIAQGMELFDAVARAHRY 132
Cdd:cd01174   240 VKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAA 276
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 23-131 1.95e-09

pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 54.66  E-value: 1.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489  23 LLPRAELVTPNAPEAAMLTGIRVETPDDLVQAGQALIALGARAALVKgghlQGPMVTDALVTAFDVHLFEAWRMDTVSTH 102
Cdd:pfam00294 177 LLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVT----LGADGALVVEGDGEVHVPAVPKVKVVDTT 252

                          90       100
                  ....*....|....*....|....*....
gi 1604577489 103 GTGCTLASACAAGIAQGMELFDAVARAHR 131
Cdd:pfam00294 253 GAGDSFVGGFLAGLLAGKSLEEALRFANA 281
PRK05756 PRK05756
pyridoxal kinase PdxY;
17-69 1.17e-07

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 49.48  E-value: 1.17e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1604577489  17 AALKELLLPRAELVTPNAPEAAMLTGIRVETPDDLVQAGQALIALGARAALVK 69
Cdd:PRK05756  129 EFLRDRALPAADIITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVT 181
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 23-117 3.03e-07

ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).


Pssm-ID: 238177 [Multi-domain]  Cd Length: 196  Bit Score: 47.86  E-value: 3.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489  23 LLPRAELVTPNAPEAAMLTGIRVETPDDLVQAGQALIALGARAALVKGGHLQGPMVTdalvTAFDVHLFEAWRMDTVSTH 102
Cdd:cd00287   106 LLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVAT----RGGTEVHVPAFPVKVVDTT 181

                          90
                  ....*....|....*
gi 1604577489 103 GTGCTLASACAAGIA 117
Cdd:cd00287   182 GAGDAFLAALAAGLA 196
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
 17-69 6.37e-07

pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal/pyridoxamine kinase, but mutants lacking PdxK activity retain a specific pyridoxal kinase, PdxY. PdxY acts in the salvage pathway of pyridoxal 5'-phosphate biosynthesis. Mammalian forms of pyridoxal kinase are more similar to PdxY than to PdxK. The PdxK isozyme is omitted from the seed alignment but scores above the trusted cutoff.ThiD and related proteins form an outgroup. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]


Pssm-ID: 273221 [Multi-domain]  Cd Length: 287  Bit Score: 47.52  E-value: 6.37e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1604577489  17 AALKELLLPRAELVTPNAPEAAMLTGIRVETPDDLVQAGQALIALGARAALVK 69
Cdd:TIGR00687 129 EVYREKAIPVADIITPNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVT 181
PRK11142 PRK11142
ribokinase; Provisional
 23-131 6.88e-07

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 47.56  E-value: 6.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489  23 LLPRAELVTPNAPEAAMLTGIRVETPDDLVQAGQAL---------IALGARAALVKGGHLQGpmvtdaLVTAFDVhlfea 93
Cdd:PRK11142  175 LLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLhqkgietvlITLGSRGVWLSENGEGQ------RVPGFRV----- 243

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1604577489  94 wrmDTVSTHGTGCTLASACAAGIAQGMELFDAVARAHR 131
Cdd:PRK11142  244 ---QAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHA 278
PTZ00493 PTZ00493
phosphomethylpyrimidine kinase; Provisional
 82-153 9.30e-07

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240440  Cd Length: 321  Bit Score: 47.30  E-value: 9.30e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1604577489  82 LVTAFDVHLFEAWRMDTVSTHGTGCTLASACAAGIAQGMELFDAVARAHRYVQDAIATAPGFGKGSGPLNHM 153
Cdd:PTZ00493  228 VTYLYDVYKLRSKRKPGKDIHGTGCTLSTAIACYLAKKHNILQSCIESKKYIYNCIRYAYPFGSKSQGLNHL 299
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 23-131 2.48e-06

Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 440290 [Multi-domain]  Cd Length: 301  Bit Score: 46.03  E-value: 2.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489  23 LLPRAELVTPNAPEAAMLTGIrvetpDDLVQAGQALIALGARAALVKGGHlQGPMVtdalVTAFDVHLFEAWRMDTVSTH 102
Cdd:COG0524   182 LLALVDILFPNEEEAELLTGE-----TDPEEAAAALLARGVKLVVVTLGA-EGALL----YTGGEVVHVPAFPVEVVDTT 251

                          90       100
                  ....*....|....*....|....*....
gi 1604577489 103 GTGCTLASACAAGIAQGMELFDAVARAHR 131
Cdd:COG0524   252 GAGDAFAAGFLAGLLEGLDLEEALRFANA 280
PLN02978 PLN02978
pyridoxal kinase
 16-62 3.65e-06

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 45.50  E-value: 3.65e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1604577489  16 VAALKELLLPRAELVTPNAPEAAMLTGIRVETPDDLVQAGQALIALG 62
Cdd:PLN02978  139 VPVYREKVVPLATMLTPNQFEAEQLTGIRIVTEEDAREACAILHAAG 185
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 16-151 5.16e-05

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 41.99  E-value: 5.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489  16 VAALKELLlPRAELVTPNAPEAAMLTGIRVETPDDLVQAGQALialgaraalvkggHLQGPMVTdaLVTAFdvhlfeawR 95
Cdd:PTZ00344  130 VDAYRELI-PYADVITPNQFEASLLSGVEVKDLSDALEAIDWF-------------HEQGIPVV--VITSF--------R 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489  96 MDTVSTH------------------------------GTGCTLASACAA-GIAQGMELfdAVARAHRYVQDAI-ATAPGF 143
Cdd:PTZ00344  186 EDEDPTHlrfllscrdkdtknnkrftgkvpyiegrytGTGDLFAALLLAfSHQHPMDL--AVGKAMGVLQDIIkATRESG 263


                  ....*...
gi 1604577489 144 GKGSGPLN 151
Cdd:PTZ00344  264 GSGSSSLM 271
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
 26-125 1.24e-04

RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.


Pssm-ID: 238577 [Multi-domain]  Cd Length: 304  Bit Score: 41.01  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489  26 RAELVTPNAPEAAMLTGIRVETPDDLVQAGQALIA-LGARAALVKGGHlQGpmvtdalVTAFDVHLfEAWRMDTVSTH-- 102
Cdd:cd01172   181 GATLLTPNEKEAREALGDEINDDDELEAAGEKLLElLNLEALLVTLGE-EG-------MTLFERDG-EVQHIPALAKEvy 251

                          90       100
                  ....*....|....*....|....*.
gi 1604577489 103 ---GTGCTLASACAAGIAQGMELFDA 125
Cdd:cd01172   252 dvtGAGDTVIATLALALAAGADLEEA 277
PRK10294 PRK10294
6-phosphofructokinase 2; Provisional
 28-126 1.92e-04

6-phosphofructokinase 2; Provisional


Pssm-ID: 182361 [Multi-domain]  Cd Length: 309  Bit Score: 40.54  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489  28 ELVTPNAPEAAMLTGIRVETPDDLVQAGQALIALGARAALVKGGHLQGPMVTDAlvtafdvhlfEAW------RMDTVST 101
Cdd:PRK10294  182 ELVKPNQKELSALVNRDLTQPDDVRKAAQELVNSGKAKRVVVSLGPQGALGVDS----------ENCiqvvppPVKSQST 251

                          90       100
                  ....*....|....*....|....*
gi 1604577489 102 HGTGCTLASACAAGIAQGMELFDAV 126
Cdd:PRK10294  252 VGAGDSMVGAMTLKLAENASLEEMV 276
PTZ00292 PTZ00292
ribokinase; Provisional
 23-142 8.33e-04

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 38.56  E-value: 8.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489  23 LLPRAELVTPNAPEAAMLTGIRVETPDDLVQAGQALIALGARAALVK-GGHLQGPMVTDALvtafDVHLfEAWRMDTVST 101
Cdd:PTZ00292  195 FLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITlGANGCLIVEKENE----PVHV-PGKRVKAVDT 269

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1604577489 102 HGTGCTLASACAAGIAQGMELFDAVARAHRYVQDAIaTAPG 142
Cdd:PTZ00292  270 TGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISV-TRHG 309
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 29-130 8.85e-04

YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238916 [Multi-domain]  Cd Length: 288  Bit Score: 38.45  E-value: 8.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489  29 LVTPNAPEAAMLTGIRVETPDDLVQAGQALIALGARAALVKGGHlQGPMVTDALVTAFDVHLFEAWRMDTVSTHGTGCTL 108
Cdd:cd01941   179 LLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGA-KGVLLSSREGGVETKLFPAPQPETVVNVTGAGDAF 257

                          90       100
                  ....*....|....*....|..
gi 1604577489 109 ASACAAGIAQGMELFDAVARAH 130
Cdd:cd01941   258 VAGLVAGLLEGMSLDDSLRFAQ 279
PRK07105 PRK07105
pyridoxamine kinase; Validated
 27-143 1.49e-03

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 37.59  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489  27 AELVTPNAPEAAMLTGIRVETPD----DLVQAGQALIALGARAALVKGGHLQGPMVTdalVTAFDVHLFEAWRMDT--VS 100
Cdd:PRK07105  138 ADVITPNLTEACLLLDKPYLEKSyseeEIKQLLRKLADLGPKIVIITSVPFEDGKIG---VAYYDRATDRFWKVFCkyIP 214

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1604577489 101 TH--GTGCTLASACAAGIAQGMELFDAVARAHRYVQDAIATAPGF 143
Cdd:PRK07105  215 AHypGTGDIFTSVITGSLLQGDSLPIALDRAVQFIEKGIRATLGL 259
YegV_kinase_like cd01944
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ...
 23-131 3.02e-03

YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238919 [Multi-domain]  Cd Length: 289  Bit Score: 37.02  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489  23 LLPRAELVTPNAPEAAMLTgirvETPDDLVQAGQALIALGARAALV-----KGGHLQGPMVTDALVTAFDVHLfeawrmd 97
Cdd:cd01944   178 LMAKRPIWSCNREEAAIFA----ERGDPAAEASALRIYAKTAAPVVvrlgsNGAWIRLPDGNTHIIPGFKVKA------- 246

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1604577489  98 tVSTHGTGCTLASACAAGIAQGMELFDAVARAHR 131
Cdd:cd01944   247 -VDTIGAGDTHAGGMLAGLAKGMSLADAVLLANA 279
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 16-142 9.73e-03

B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of the ATP binding site, the substrate binding site and the Mg2+binding site and structural homology this group is a member of the ribokinase-like superfamily.


Pssm-ID: 238576  Cd Length: 254  Bit Score: 35.28  E-value: 9.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1604577489  16 VAALKELLLPRAELV-TPNAPEAAMLTGIRVETP-DDLVQAGQALIALGARAALVKGghlQGPMVTDALVTAFDVHLFEA 93
Cdd:cd01171   117 LADEPSLIKRYGPVVlTPHPGEFARLLGALVEEIqADRLAAAREAAAKLGATVVLKG---AVTVIADPDGRVYVNPTGNP 193

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1604577489  94 WRmdtvSTHGTGCTLASACAAGIAQGMELFDAV---ARAHRYVQDAIATAPG 142
Cdd:cd01171   194 GL----ATGGSGDVLAGIIAALLAQGLSPLEAAalaVYLHGLAGDLAAKKKG 241
 
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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