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Conserved domains on  [gi|739394763|ref|WP_037255333|]
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hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Roseobacter sp. SK209-2-6]

Protein Classification

hydroxymethylpyrimidine/phosphomethylpyrimidine kinase( domain architecture ID 10100230)

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:  2.7.1.49|2.7.4.7
Gene Ontology:  GO:0005524|GO:0008902|GO:0008972|GO:0009228|GO:0009229
PubMed:  8382990
SCOP:  4000759

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 3-235 1.24e-69

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: 213.52  E-value: 1.24e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763   3 HILAIGGTDSSGGAGLTRDTAMAAKLGCSLSPVVTAVTAQTNANVQEIHPVPAKIIEVQLLAALDPAspKPKAIKIGMIG 82
Cdd:cd01169    1 VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDI--PVDAIKIGMLG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763  83 SPAAADLLCKHLP--ANMPIVLDPVLKSTSGKRLMTKETL----TPLLQRVSLLTPNLPESHLLSGGgASGERLDHRPLA 156
Cdd:cd01169   79 SAEIIEAVAEALKdyPDIPVVLDPVMVAKSGDSLLDDDAIealrELLLPLATLITPNLPEAELLTGL-EIATEEDMMKAA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763 157 EALLSLGPKAVLIKGGHDQGESCVDHLWVGTDHHQFDALRL-PHSKRGTGCSLATAIACSLAQGASLVEACRRAKADVHK 235
Cdd:cd01169  158 KALLALGAKAVLIKGGHLPGDEAVDVLYDGGGFFEFESPRIdTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQ 237
 
Name Accession Description Interval E-value
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 3-235 1.24e-69

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: 213.52  E-value: 1.24e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763   3 HILAIGGTDSSGGAGLTRDTAMAAKLGCSLSPVVTAVTAQTNANVQEIHPVPAKIIEVQLLAALDPAspKPKAIKIGMIG 82
Cdd:cd01169    1 VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDI--PVDAIKIGMLG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763  83 SPAAADLLCKHLP--ANMPIVLDPVLKSTSGKRLMTKETL----TPLLQRVSLLTPNLPESHLLSGGgASGERLDHRPLA 156
Cdd:cd01169   79 SAEIIEAVAEALKdyPDIPVVLDPVMVAKSGDSLLDDDAIealrELLLPLATLITPNLPEAELLTGL-EIATEEDMMKAA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763 157 EALLSLGPKAVLIKGGHDQGESCVDHLWVGTDHHQFDALRL-PHSKRGTGCSLATAIACSLAQGASLVEACRRAKADVHK 235
Cdd:cd01169  158 KALLALGAKAVLIKGGHLPGDEAVDVLYDGGGFFEFESPRIdTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQ 237
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 5-235 6.09e-69

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: 212.21  E-value: 6.09e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763   5 LAIGGTDSSGGAGLTRDTAMAAKLGCSLSPVVTAVTAQTNANVQEIHPVPAKIIEVQLLAALDpaSPKPKAIKIGMIGSP 84
Cdd:COG0351    1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLE--DIPVDAIKIGMLGSA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763  85 AA----ADLLCKHLPAnmPIVLDPVLKSTSGKRLMTKETL----TPLLQRVSLLTPNLPESHLLSGGGASGErLDHRPLA 156
Cdd:COG0351   79 EIieavAEILADYPLV--PVVLDPVMVAKSGDRLLDEDAVealrELLLPLATVVTPNLPEAEALLGIEITTL-DDMREAA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763 157 EALLSLGPKAVLIKGGHDQGESCVDHLWVGTDHHQFDALRLP-HSKRGTGCSLATAIACSLAQGASLVEACRRAKADVHK 235
Cdd:COG0351  156 KALLELGAKAVLVKGGHLPGDEAVDVLYDGDGVREFSAPRIDtGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQ 235
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 11-234 9.92e-62

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: 193.47  E-value: 9.92e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763   11 DSSGGAGLTRDTAMAAKLGCSLSPVVTAVTAQTNANVQEIHPVPAKIIEVQLLAALDpaSPKPKAIKIGMIGSPAAADLL 90
Cdd:pfam08543   1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLE--DIPVDAVKTGMLGSAEIIEAV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763   91 CKHLP-ANMPIVLDPVLKSTSGKRLMTKETL----TPLLQRVSLLTPNLPESHLLSGGGASGERlDHRPLAEALLSLGPK 165
Cdd:pfam08543  79 AEKLDkYGVPVVLDPVMVAKSGDSLLDDEAIealkEELLPLATLITPNLPEAEALTGRKIKTLE-DMKEAAKKLLALGAK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739394763  166 AVLIKGGHDQGES--CVDHLWVGTDHHQFDALRLP-HSKRGTGCSLATAIACSLAQGASLVEACRRAKADVH 234
Cdd:pfam08543 158 AVLIKGGHLEGEEavVTDVLYDGGGFYTLEAPRIPtKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVT 229
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 5-231 9.91e-58

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 184.17  E-value: 9.91e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763   5 LAIGGTDSSGGAGLTRD-TAMAAkLGCSLSPVVTAVTAQTNANVQEIHPVPAKIIEVQLLAALdpASPKPKAIKIGMIGS 83
Cdd:PRK06427   8 LTIAGSDSGGGAGIQADlKTFQA-LGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVF--SDIRIDAVKIGMLAS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763  84 P----AAADLLCKHLPAnmPIVLDPVLKSTSGKRLMTKETLTP----LLQRVSLLTPNLPESHLLSGGGASGERLDHRPL 155
Cdd:PRK06427  85 AeiieTVAEALKRYPIP--PVVLDPVMIAKSGDPLLADDAVAAlrerLLPLATLITPNLPEAEALTGLPIADTEDEMKAA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763 156 AEALLSLGPKAVLIKGGHD-QGESCVDHLWVGTDHHQFDALRLP----HskrGTGCSLATAIACSLAQGASLVEACRRAK 230
Cdd:PRK06427 163 ARALHALGCKAVLIKGGHLlDGEESVDWLFDGEGEERFSAPRIPtkntH---GTGCTLSAAIAAELAKGASLLDAVQTAK 239


                 .
gi 739394763 231 A 231
Cdd:PRK06427 240 D 240
HMP-P_kinase TIGR00097
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ...
 4-231 1.97e-50

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: 165.16  E-value: 1.97e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763    4 ILAIGGTDSSGGAGLTRDTAMAAKLGCSLSPVVTAVTAQTNANVQEIHPVPAKIIEVQLLAALDPAspKPKAIKIGMIGS 83
Cdd:TIGR00097   1 ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDI--PVDAAKTGMLAS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763   84 PAAADLLCKHL---PANmPIVLDPVLKSTSGKRLMTKETL----TPLLQRVSLLTPNLPESHLLSGGGASGERlDHRPLA 156
Cdd:TIGR00097  79 AEIVEAVARKLreyPVR-PLVVDPVMVAKSGAPLLEEEAIealrKRLLPLATLITPNLPEAEALLGTKIRTEQ-DMIKAA 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739394763  157 EALLSLGPKAVLIKGGHDQGESCVDHLWVGTDHHQFDALRL--PHSkRGTGCSLATAIACSLAQGASLVEACRRAKA 231
Cdd:TIGR00097 157 KKLRELGPKAVLIKGGHLEGDQAVDVLFDGGEIHILKAPRIetKNT-HGTGCTLSAAIAANLAKGLSLKEAVKEAKE 232
 
Name Accession Description Interval E-value
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 3-235 1.24e-69

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: 213.52  E-value: 1.24e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763   3 HILAIGGTDSSGGAGLTRDTAMAAKLGCSLSPVVTAVTAQTNANVQEIHPVPAKIIEVQLLAALDPAspKPKAIKIGMIG 82
Cdd:cd01169    1 VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDI--PVDAIKIGMLG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763  83 SPAAADLLCKHLP--ANMPIVLDPVLKSTSGKRLMTKETL----TPLLQRVSLLTPNLPESHLLSGGgASGERLDHRPLA 156
Cdd:cd01169   79 SAEIIEAVAEALKdyPDIPVVLDPVMVAKSGDSLLDDDAIealrELLLPLATLITPNLPEAELLTGL-EIATEEDMMKAA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763 157 EALLSLGPKAVLIKGGHDQGESCVDHLWVGTDHHQFDALRL-PHSKRGTGCSLATAIACSLAQGASLVEACRRAKADVHK 235
Cdd:cd01169  158 KALLALGAKAVLIKGGHLPGDEAVDVLYDGGGFFEFESPRIdTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQ 237
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 5-235 6.09e-69

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: 212.21  E-value: 6.09e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763   5 LAIGGTDSSGGAGLTRDTAMAAKLGCSLSPVVTAVTAQTNANVQEIHPVPAKIIEVQLLAALDpaSPKPKAIKIGMIGSP 84
Cdd:COG0351    1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLE--DIPVDAIKIGMLGSA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763  85 AA----ADLLCKHLPAnmPIVLDPVLKSTSGKRLMTKETL----TPLLQRVSLLTPNLPESHLLSGGGASGErLDHRPLA 156
Cdd:COG0351   79 EIieavAEILADYPLV--PVVLDPVMVAKSGDRLLDEDAVealrELLLPLATVVTPNLPEAEALLGIEITTL-DDMREAA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763 157 EALLSLGPKAVLIKGGHDQGESCVDHLWVGTDHHQFDALRLP-HSKRGTGCSLATAIACSLAQGASLVEACRRAKADVHK 235
Cdd:COG0351  156 KALLELGAKAVLVKGGHLPGDEAVDVLYDGDGVREFSAPRIDtGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQ 235
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 11-234 9.92e-62

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: 193.47  E-value: 9.92e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763   11 DSSGGAGLTRDTAMAAKLGCSLSPVVTAVTAQTNANVQEIHPVPAKIIEVQLLAALDpaSPKPKAIKIGMIGSPAAADLL 90
Cdd:pfam08543   1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLE--DIPVDAVKTGMLGSAEIIEAV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763   91 CKHLP-ANMPIVLDPVLKSTSGKRLMTKETL----TPLLQRVSLLTPNLPESHLLSGGGASGERlDHRPLAEALLSLGPK 165
Cdd:pfam08543  79 AEKLDkYGVPVVLDPVMVAKSGDSLLDDEAIealkEELLPLATLITPNLPEAEALTGRKIKTLE-DMKEAAKKLLALGAK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739394763  166 AVLIKGGHDQGES--CVDHLWVGTDHHQFDALRLP-HSKRGTGCSLATAIACSLAQGASLVEACRRAKADVH 234
Cdd:pfam08543 158 AVLIKGGHLEGEEavVTDVLYDGGGFYTLEAPRIPtKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVT 229
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 5-231 9.91e-58

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 184.17  E-value: 9.91e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763   5 LAIGGTDSSGGAGLTRD-TAMAAkLGCSLSPVVTAVTAQTNANVQEIHPVPAKIIEVQLLAALdpASPKPKAIKIGMIGS 83
Cdd:PRK06427   8 LTIAGSDSGGGAGIQADlKTFQA-LGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVF--SDIRIDAVKIGMLAS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763  84 P----AAADLLCKHLPAnmPIVLDPVLKSTSGKRLMTKETLTP----LLQRVSLLTPNLPESHLLSGGGASGERLDHRPL 155
Cdd:PRK06427  85 AeiieTVAEALKRYPIP--PVVLDPVMIAKSGDPLLADDAVAAlrerLLPLATLITPNLPEAEALTGLPIADTEDEMKAA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763 156 AEALLSLGPKAVLIKGGHD-QGESCVDHLWVGTDHHQFDALRLP----HskrGTGCSLATAIACSLAQGASLVEACRRAK 230
Cdd:PRK06427 163 ARALHALGCKAVLIKGGHLlDGEESVDWLFDGEGEERFSAPRIPtkntH---GTGCTLSAAIAAELAKGASLLDAVQTAK 239


                 .
gi 739394763 231 A 231
Cdd:PRK06427 240 D 240
HMP-P_kinase TIGR00097
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ...
 4-231 1.97e-50

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: 165.16  E-value: 1.97e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763    4 ILAIGGTDSSGGAGLTRDTAMAAKLGCSLSPVVTAVTAQTNANVQEIHPVPAKIIEVQLLAALDPAspKPKAIKIGMIGS 83
Cdd:TIGR00097   1 ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDI--PVDAAKTGMLAS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763   84 PAAADLLCKHL---PANmPIVLDPVLKSTSGKRLMTKETL----TPLLQRVSLLTPNLPESHLLSGGGASGERlDHRPLA 156
Cdd:TIGR00097  79 AEIVEAVARKLreyPVR-PLVVDPVMVAKSGAPLLEEEAIealrKRLLPLATLITPNLPEAEALLGTKIRTEQ-DMIKAA 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739394763  157 EALLSLGPKAVLIKGGHDQGESCVDHLWVGTDHHQFDALRL--PHSkRGTGCSLATAIACSLAQGASLVEACRRAKA 231
Cdd:TIGR00097 157 KKLRELGPKAVLIKGGHLEGDQAVDVLFDGGEIHILKAPRIetKNT-HGTGCTLSAAIAANLAKGLSLKEAVKEAKE 232
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 3-237 1.42e-46

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 161.09  E-value: 1.42e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763   3 HILAIGGTDSSGGAGLTRDTAMAAKLGCSLSPVVTAVTAQTNANVQEIHPVPAKIIEVQLLAALDPASpkPKAIKIGMIG 82
Cdd:PLN02898  11 HVLTVAGSDSGAGAGIQADIKACAARGVYCTTAITAVTAQNTVGVQGVHAVPLDFVAEQLKSVLSDMP--VDVVKTGMLP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763  83 SPAAADLLC---KHLPANmPIVLDPVLKSTSGKRLMTKETLTPLLQRV----SLLTPNLPESHLLSGGGASGERLDHRPL 155
Cdd:PLN02898  89 SAEIVKVLCqalKEFPVK-ALVVDPVMVSTSGDVLAGPSILSALREELlplaTIVTPNVKEASALLGGDPLETVADMRSA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763 156 AEALLSLGPKAVLIKGGHDQGES-CVDHLWVGTDHHQFDALRL-PHSKRGTGCSLATAIACSLAQGASLVEACRRAKADV 233
Cdd:PLN02898 168 AKELHKLGPRYVLVKGGHLPDSLdAVDVLYDGTEFHELRSSRIkTRNTHGTGCTLASCIAAELAKGSDMLSAVKVAKRYV 247


                 ....
gi 739394763 234 HKWL 237
Cdd:PLN02898 248 ETAL 251
PRK14713 PRK14713
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
4-237 3.47e-36

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 237797 [Multi-domain]  Cd Length: 530  Bit Score: 133.76  E-value: 3.47e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763   4 ILAIGGTDSSGGAGLTRDTAMAAKLGCSLSPVVTAVTAQTNANVQEIHPVPAKIIEVQLLAALDPASPKpkAIKIGMIGS 83
Cdd:PRK14713  32 VLSIAGTDPSGGAGIQADLKSIAAAGGYGMAVITALVAQNTRGVRAVHVPPADFLRAQLDAVSDDVTVD--AVKIGMLGD 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763  84 PAAADLLCKHLPANMP--IVLDPVLKSTSGKRLMTKET---LTPLLQRVSLLTPNLPESHLLSGGGASGERLDHRPLAEA 158
Cdd:PRK14713 110 AEVIDAVRTWLAEHRPpvVVLDPVMVATSGDRLLEEDAeaaLRELVPRADLITPNLPELAVLLGEPPATTWEEALAQARR 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763 159 LLSLGPKAVLIKGGHDQGESCvDHLWVGTDH--HQFDALRL-PHSKRGTGCSLATAIACSLAQGASLVEACRRAKAdvhk 235
Cdd:PRK14713 190 LAAETGTTVLVKGGHLDGQRA-PDALVGPDGavTEVPGPRVdTRNTHGTGCSLSSALATRLGRGGDWAAALRWATA---- 264


                 ..
gi 739394763 236 WL 237
Cdd:PRK14713 265 WL 266
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
5-230 1.63e-34

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 127.92  E-value: 1.63e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763   5 LAIGGTDSSGGAGLTRDTAMAAKLGCSLSPVVTAVTAQTNANVQEIHPVPAKIIEVQLLAALDPASpkPKAIKIGMIGS- 83
Cdd:PRK08573   6 LTIAGSDSGGGAGIEADLKTFAALGVHGAVAITSVTAQNTYEVRAIHDLPPEVVAAQIEAVWEDMG--IDAAKTGMLSNr 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763  84 ---PAAADLLCKHlpaNMPIVLDPVLKSTSGKRLMTKETLTPLLQRV----SLLTPNLPESHLLSGGGASGERlDHRPLA 156
Cdd:PRK08573  84 eiiEAVAKTVSKY---GFPLVVDPVMIAKSGAPLLREDAVDALIKRLlplaTVVTPNRPEAEKLTGMKIRSVE-DARKAA 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739394763 157 EALL-SLGPKAVLIKGGHDQGESCVDHLWVGTDHHQFDALRLPH-SKRGTGCSLATAIACSLAQGASLVEACRRAK 230
Cdd:PRK08573 160 KYIVeELGAEAVVVKGGHLEGEEAVDVLYHNGTFREFRAPRVESgCTHGTGCSFSAAIAAGLAKGLDPEEAIKTAK 235
PTZ00347 PTZ00347
phosphomethylpyrimidine kinase; Provisional
 4-235 4.76e-34

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240375 [Multi-domain]  Cd Length: 504  Bit Score: 127.77  E-value: 4.76e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763   4 ILAIGGTDSSGGAGLTRDTAMAAKLGCSLSPVVTAVTAQTNANVQEIHPVPAKIIEVQLLAALdpASPKPKAIKIGMIGS 83
Cdd:PTZ00347 233 VLTVSGSDSGGGAGHQADLKTLEALGVYSTSALTSLTAQNTKGVQQIQVVNEDFFAAQIDSVM--SDFNISVVKLGLVPT 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763  84 PAAADLLCKHLpANMPIVLDPVLKSTSGKRLMTKETLTPLLQ--------RVSLLTPNLPES-HLLSGGGASGERLDhRP 154
Cdd:PTZ00347 311 ARQLEIVIEKL-KNLPMVVDPVLVATSGDDLVAQKNADDVLAmykerifpMATIITPNIPEAeRILGRKEITGVYEA-RA 388

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763 155 LAEALLSLGPKAVLIKGGHDQ--GESCVDHLWvGTDHHQFDALrlpHSKR-------GTGCSLATAIACSLAQGASLVEA 225
Cdd:PTZ00347 389 AAQALAQYGSRYVLVKGGHDLidPEACRDVLY-DREKDRFYEF---TANRiatinthGTGCTLASAISSFLARGYTVPDA 464

                        250
                 ....*....|
gi 739394763 226 CRRAKADVHK 235
Cdd:PTZ00347 465 VERAIGYVHE 474
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
4-235 4.60e-28

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 107.07  E-value: 4.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763   4 ILAIGGTDSSGGAGLTRDTAMAAKLGCSLSPVVTAVTAQTnANVQEIHPVPAKIIEVQLLAALD-PASpkpkAIKIGMIG 82
Cdd:PRK12413   6 ILAISGNDIFSGGGLHADLATYTRNGLHGFVAVTCLTAMT-EKGFEVFPVDKEIFQQQLDSLKDvPFS----AIKIGLLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763  83 SPAAADLLCKHLPA--NMPIVLDPVL--KSTSGKRLMT-KETLTPLLQRVSLLTPNLPESHLLSGGGASGERlDHRPLAE 157
Cdd:PRK12413  81 NVEIAEQALDFIKGhpGIPVVLDPVLvcKETHDVEVSElRQELIQFFPYVTVITPNLVEAELLSGKEIKTLE-DMKEAAK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763 158 ALLSLGPKAVLIKGGH--DQgESCVDHLWVGTDHHQFDALRLPHSKRGTGCSLATAIACSLAQGASLVEACRRAKADVHK 235
Cdd:PRK12413 160 KLYDLGAKAVVIKGGNrlSQ-KKAIDLFYDGKEFVILESPVLEKNNIGAGCTFASSIASQLVKGKSPLEAVKNSKDFVYQ 238
PRK09517 PRK09517
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ...
 4-237 1.20e-26

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


Pssm-ID: 169939 [Multi-domain]  Cd Length: 755  Bit Score: 107.75  E-value: 1.20e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763   4 ILAIGGTDSSGGAGLTRDTAMAAKLGCSLSPVVTAVTAQTNANVQEIHPVPAKIIEVQLLAALDPASpkPKAIKIGMIGS 83
Cdd:PRK09517 244 VLSIAGTDPTGGAGIQADLKSIAAGGGYGMCVVTALVAQNTHGVNTIHTPPLTFLEEQLEAVFSDVT--VDAVKLGMLGS 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763  84 PAAADLLCKHLPANM--PIVLDPVLKSTSGKRLM---TKETLTPLLQRVSLLTPNLPESHLLSGGGASGERLDHRPLAEA 158
Cdd:PRK09517 322 ADTVDLVASWLGSHEhgPVVLDPVMVATSGDRLLdadATEALRRLAVHVDVVTPNIPELAVLCGEAPAITMDEAIAQARG 401

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763 159 LLSLGPKAVLIKGGHDQGESCVDHL-WVGTDHHQFDALRL-PHSKRGTGCSLATAIACSLAQGASLVEACRRAKAdvhkW 236
Cdd:PRK09517 402 FARTHGTIVIVKGGHLTGDLADNAVvRPDGSVHQVENPRVnTTNSHGTGCSLSAALATLIAAGESVEKALEWATR----W 477


                 .
gi 739394763 237 L 237
Cdd:PRK09517 478 L 478
PRK12412 PRK12412
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
1-231 2.84e-20

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183512 [Multi-domain]  Cd Length: 268  Bit Score: 86.56  E-value: 2.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763   1 MSHILAIGGTDSSGGAGLTRDTAMAAKLGC-SLSPVVTAVTAQT-NANVQEIHPVPAKIIEVQLLAALDPASpkPKAIKI 78
Cdd:PRK12412   1 LNKALTIAGSDTSGGAGIQADLKTFQELGVyGMTSLTTIVTMDPhNGWAHNVFPIPASTLKPQLETTIEGVG--VDALKT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763  79 GMIGS----PAAADLLCKHLPANmpIVLDPVLKSTSGKRLMTKETLT----PLLQRVSLLTPNLPESHLLSGGGASGERl 150
Cdd:PRK12412  79 GMLGSveiiEMVAETIEKHNFKN--VVVDPVMVCKGADEALHPETNDclrdVLVPKALVVTPNLFEAYQLSGVKINSLE- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763 151 DHRPLAEALLSLGPKAVLIKGGHDQG-ESCVDHLWVGTDHHQFDALRLPHS-KRGTGCSLATAIACSLAQGASLVEACRR 228
Cdd:PRK12412 156 DMKEAAKKIHALGAKYVLIKGGSKLGtETAIDVLYDGETFDLLESEKIDTTnTHGAGCTYSAAITAELAKGKPVKEAVKT 235


                 ...
gi 739394763 229 AKA 231
Cdd:PRK12412 236 AKE 238
PRK12616 PRK12616
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
1-231 5.64e-20

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183624  Cd Length: 270  Bit Score: 85.87  E-value: 5.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763   1 MSHILAIGGTDSSGGAGLTRDTAMAAK---LGCSLSPVVTAVTAQTNANVQeIHPVPAKIIEVQLLAALDPASPKpkAIK 77
Cdd:PRK12616   3 MHKALTIAGSDSSGGAGIQADLKTFQEknvYGMTALTVVVAMDPENSWDHQ-VFPIDTDTIRAQLSTIVDGIGVD--AMK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763  78 IGMIGS----PAAADLLCKHLPANmpIVLDPVLKSTSGKRLM-------TKETLTPLlqrVSLLTPNLPESHLLSGGGAS 146
Cdd:PRK12616  80 TGMLPTvdiiELAADTIKEKQLKN--VVIDPVMVCKGANEVLypehaeaLREQLAPL---ATVITPNLFEAGQLSGMGEI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763 147 GERLDHRPLAEALLSLGPKAVLIKGGHD-QGESCVDHLWVGTDHHQFDALRL--PHSkRGTGCSLATAIACSLAQGASLV 223
Cdd:PRK12616 155 KTVEQMKEAAKKIHELGAQYVVITGGGKlKHEKAVDVLYDGETAEVLESEMIdtPYT-HGAGCTFSAAVTAELAKGSEVK 233


                 ....*...
gi 739394763 224 EACRRAKA 231
Cdd:PRK12616 234 EAIYAAKE 241
PTZ00493 PTZ00493
phosphomethylpyrimidine kinase; Provisional
 2-230 1.34e-15

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240440  Cd Length: 321  Bit Score: 74.65  E-value: 1.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763   2 SHILAIGGTDSSGGAGLTRDTAMAAKLGCSLSPVVTAVTAQTNANVQEIHPVPAKIIEVQLLAALdpASPKPKAIKIGMI 81
Cdd:PTZ00493   5 SNILSIAGSDSCGGAGMQADIKTAMGLGCHCCTALVVLTAQNTKEVKRIVEIEEKFIVEQLDSIF--ADVTIDVVKLGVL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763  82 GSPAAADLLCKHLpANMP--------IVLDPVLKSTSGKRLM-----TKETLTPLLQRVSLLTPNLPESHLLSgggasgE 148
Cdd:PTZ00493  83 YSKKIISLVHNYI-TNMNkkrgkkllVVFDPVFVSSSGCLLVenleyIKFALDLICPISCIITPNFYECKVIL------E 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763 149 RLD-HRPLAEALLS---------LGPKAVLIKG---GHDQGES----CVDHLWV----------------GTDHHQFDAL 195
Cdd:PTZ00493 156 ALDcQMDLSKANMTelcklvtekLNINACLFKScnvGENSAEEnevyAVDHLCIrnvgsyptgekqqidaGGVTYLYDVY 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 739394763 196 RLpHSKR-------GTGCSLATAIACSLAQGASLVEACRRAK 230
Cdd:PTZ00493 236 KL-RSKRkpgkdihGTGCTLSTAIACYLAKKHNILQSCIESK 276
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 75-235 8.99e-08

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: 51.43  E-value: 8.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763  75 AIKIGMIGSPAAADLLC------KHLPANMPIVLDPVLkSTSGKRLMTKETLTP-----LLQRVSLLTPNLPESHLLSGG 143
Cdd:cd01173   75 AVLTGYLGSAEQVEAVAeivkrlKEKNPNLLYVCDPVM-GDNGKLYVVAEEIVPvyrdlLVPLADIITPNQFELELLTGK 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763 144 GASGERlDHRPLAEALLSLGPKAVLIKGGHDQGEscvDHLW-VGTDHHQFDALRLPHSKR-----GTGCSLATAIACSLA 217
Cdd:cd01173  154 KINDLE-DAKAAARALHAKGPKTVVVTSVELADD---DRIEmLGSTATEAWLVQRPKIPFpayfnGTGDLFAALLLARLL 229

                        170
                 ....*....|....*...
gi 739394763 218 QGASLVEACRRAKADVHK 235
Cdd:cd01173  230 KGKSLAEALEKALNFVHE 247
PRK07105 PRK07105
pyridoxamine kinase; Validated
 75-229 1.09e-07

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 51.45  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763  75 AIKIGMIGSPAAADLLCKHLPA----NMPIVLDPVLkSTSGK------RLMTKEtLTPLLQRVSLLTPNLPESHLLSGGG 144
Cdd:PRK07105  78 AIYSGYLGSPRQIQIVSDFIKYfkkkDLLVVVDPVM-GDNGKlyqgfdQEMVEE-MRKLIQKADVITPNLTEACLLLDKP 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763 145 ASGERLDHRPLAEALLSL---GPKAVLIKGGHDQGE--------SCVDHLWvgtdhhQFDALRLPHSKRGTGCSLATAIA 213
Cdd:PRK07105 156 YLEKSYSEEEIKQLLRKLadlGPKIVIITSVPFEDGkigvayydRATDRFW------KVFCKYIPAHYPGTGDIFTSVIT 229

                        170
                 ....*....|....*.
gi 739394763 214 CSLAQGASLVEACRRA 229
Cdd:PRK07105 230 GSLLQGDSLPIALDRA 245
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 96-229 6.80e-07

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: 49.11  E-value: 6.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763  96 ANMPIVLDPVLKSTSGKRlmTKETLTPLLQRVSLLTPNLPESHLLSGggasgeRLDHRPLAEALLSLGPKAVLIKGGhdq 175
Cdd:COG0524  157 AGVPVSLDPNYRPALWEP--ARELLRELLALVDILFPNEEEAELLTG------ETDPEEAAAALLARGVKLVVVTLG--- 225

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 739394763 176 GESCVdhLWVGTDHHQFDALRLpHSKRGTGC--SLATAIACSLAQGASLVEACRRA 229
Cdd:COG0524  226 AEGAL--LYTGGEVVHVPAFPV-EVVDTTGAgdAFAAGFLAGLLEGLDLEEALRFA 278
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
74-229 8.13e-05

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 42.72  E-value: 8.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763  74 KAIKIGMIGSPAAADLLCKHLPA------NMPIVLDPVLKST-SG---KRLMTKETLTPLLQRVSLLTPNLPESHLLSGg 143
Cdd:PRK08176  90 RAVTTGYMGSASQIKILAEWLTAlradhpDLLIMVDPVIGDIdSGiyvKPDLPEAYRQHLLPLAQGLTPNIFELEILTG- 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763 144 gASGERLDHR-PLAEALLSLGPKAVLIKGGHDQGESCVDHLWVGT--DHHQFDALRLPHSKRGTGCSLATAIACSLAQGA 220
Cdd:PRK08176 169 -KPCRTLDSAiAAAKSLLSDTLKWVVITSAAGNEENQEMQVVVVTadSVNVISHPRVDTDLKGTGDLFCAELVSGLLKGK 247


                 ....*....
gi 739394763 221 SLVEACRRA 229
Cdd:PRK08176 248 ALTDAAHRA 256
PTZ00292 PTZ00292
ribokinase; Provisional
 105-229 5.81e-04

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 40.49  E-value: 5.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763 105 VLKSTSGKRLMTKETLTPLLQRVSLLTPNLPESHLLSGG----GASGERLdhrplAEALLSLGPKAVLIKGGhDQGESCV 180
Cdd:PTZ00292 177 VFNPAPAPKLAEVEIIKPFLKYVSLFCVNEVEAALITGMevtdTESAFKA-----SKELQQLGVENVIITLG-ANGCLIV 250

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 739394763 181 DHlwvGTDHHQFDALRLPH-SKRGTGCSLATAIACSLAQGASLVEACRRA 229
Cdd:PTZ00292 251 EK---ENEPVHVPGKRVKAvDTTGAGDCFVGSMAYFMSRGKDLKESCKRA 297
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
 48-227 1.29e-03

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: 39.08  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763  48 QEIHPVPAKIiEVQLLAALDPASPKPKAIKI-----GMIgSPAAADLLCKHLPA-NMPIVLDPVLKSTSGKRlmtketlt 121
Cdd:cd01172  111 EDDSPLSAEE-EQRLIERIAERLPEADVVILsdygkGVL-TPRVIEALIAAARElGIPVLVDPKGRDYSKYR-------- 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763 122 pllqRVSLLTPNLPESHLLSGGGAsGERLDHRPLAEALLS-LGPKAVLIKGGhDQGESCVDhlwvGTDHHQfdalRLP-H 199
Cdd:cd01172  181 ----GATLLTPNEKEAREALGDEI-NDDDELEAAGEKLLElLNLEALLVTLG-EEGMTLFE----RDGEVQ----HIPaL 246

                        170       180       190
                 ....*....|....*....|....*....|...
gi 739394763 200 SKR-----GTGCSLATAIACSLAQGASLVEACR 227
Cdd:cd01172  247 AKEvydvtGAGDTVIATLALALAAGADLEEAAF 279
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 3-174 1.41e-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: 38.75  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763   3 HILAIGGTDSSGGAGLTrdTAMAA-KLGCSLSPVVTavtaqTNANVQEIHPVPAKII----EVQLLAALDPASPKPKAIK 77
Cdd:cd01171   10 RVLVIGGSRGYTGAAYL--AALAAlRAGAGLVTVAT-----PPEAAAVIKSYSPELMvhplLETDIEELLELLERADAVV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763  78 IGM-IG-SPAAADLLCKHLPANMPIVLDpvlksTSGKRLMTKETLTPLLQRVSLLTPNLPESHLLSGGGASGERLDHRPL 155
Cdd:cd01171   83 IGPgLGrDEEAAEILEKALAKDKPLVLD-----ADALNLLADEPSLIKRYGPVVLTPHPGEFARLLGALVEEIQADRLAA 157

                        170
                 ....*....|....*....
gi 739394763 156 AEALLSLGPKAVLIKGGHD 174
Cdd:cd01171  158 AREAAAKLGATVVLKGAVT 176
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 90-231 9.73e-03

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 36.55  E-value: 9.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739394763   90 LCKHLPANMPIVLDPVLKstsgkrlmTKETLTPLLQRVSLLTPNLPESHLLSGggASGERLDH-RPLAEALLSLGPKAVL 168
Cdd:pfam00294 152 AAKNGGTFDPNLLDPLGA--------AREALLELLPLADLLKPNEEELEALTG--AKLDDIEEaLAALHKLLAKGIKTVI 221

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739394763  169 IKGGhDQGESCVDHlwVGTDHHQFDALRLPHSKRGTGCSLATAIACSLAQGASLVEACRRAKA 231
Cdd:pfam00294 222 VTLG-ADGALVVEG--DGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANA 281
 
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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