NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|489739578|ref|WP_003643660|]
View 

MULTISPECIES: bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase [Lactobacillaceae]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 9-263 2.00e-111

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: 321.60  E-value: 2.00e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578   9 TIAGTDSGGGAGVMADLKTMQARHVFGTAVVVAVTAQNTLGVQDFMAMPTKLIDEQFASLAADLDIRACKTGMLADAEHV 88
Cdd:COG0351    2 TIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSAEII 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  89 HAVVENLKRVDFGPLTVDPVMIAKGGAALLAADAIKTVRDELIPLATVVTPNLPEAERLTGQAITSNQAMVTAGHALQGL 168
Cdd:COG0351   82 EAVAEILADYPLVPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLEL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 169 GADNVIIKGGHGDNPDLANdfVLLADGTAFWLSAPRIDTVRTHGTGDTLSACITAELAKGRSMAAAIKTAKAYVAGTIQD 248
Cdd:COG0351  162 GAKAVLVKGGHLPGDEAVD--VLYDGDGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQAIRA 239

                        250
                 ....*....|....*
gi 489739578 249 GIQVGHGHGPLNHWA 263
Cdd:COG0351  240 ALRLGMGHGPVNHFA 254
 
Name Accession Description Interval E-value
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 9-263 2.00e-111

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: 321.60  E-value: 2.00e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578   9 TIAGTDSGGGAGVMADLKTMQARHVFGTAVVVAVTAQNTLGVQDFMAMPTKLIDEQFASLAADLDIRACKTGMLADAEHV 88
Cdd:COG0351    2 TIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSAEII 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  89 HAVVENLKRVDFGPLTVDPVMIAKGGAALLAADAIKTVRDELIPLATVVTPNLPEAERLTGQAITSNQAMVTAGHALQGL 168
Cdd:COG0351   82 EAVAEILADYPLVPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLEL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 169 GADNVIIKGGHGDNPDLANdfVLLADGTAFWLSAPRIDTVRTHGTGDTLSACITAELAKGRSMAAAIKTAKAYVAGTIQD 248
Cdd:COG0351  162 GAKAVLVKGGHLPGDEAVD--VLYDGDGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQAIRA 239

                        250
                 ....*....|....*
gi 489739578 249 GIQVGHGHGPLNHWA 263
Cdd:COG0351  240 ALRLGMGHGPVNHFA 254
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 1-263 4.10e-106

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 308.59  E-value: 4.10e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578   1 MNEFPQVATIAGTDSGGGAGVMADLKTMQARHVFGTAVVVAVTAQNTLGVQDFMAMPTKLIDEQFASLAADLDIRACKTG 80
Cdd:PRK06427   1 MMKRPIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  81 MLADAEHVHAVVENLKRVDFGPLTVDPVMIAKGGAALLAADAIKTVRDELIPLATVVTPNLPEAERLTGQAI-TSNQAMV 159
Cdd:PRK06427  81 MLASAEIIETVAEALKRYPIPPVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTGLPIaDTEDEMK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 160 TAGHALQGLGADNVIIKGGHGDNPDLANDfvLLADGTAFW-LSAPRIDTVRTHGTGDTLSACITAELAKGRSMAAAIKTA 238
Cdd:PRK06427 161 AAARALHALGCKAVLIKGGHLLDGEESVD--WLFDGEGEErFSAPRIPTKNTHGTGCTLSAAIAAELAKGASLLDAVQTA 238

                        250       260
                 ....*....|....*....|....*
gi 489739578 239 KAYVAGTIQDGIQVGHGHGPLNHWA 263
Cdd:PRK06427 239 KDYVTRAIRHALEIGQGHGPVNHFA 263
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 14-260 7.80e-105

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: 304.40  E-value: 7.80e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578   14 DSGGGAGVMADLKTMQARHVFGTAVVVAVTAQNTLGVQDFMAMPTKLIDEQFASLAADLDIRACKTGMLADAEHVHAVVE 93
Cdd:pfam08543   1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLGSAEIIEAVAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578   94 NLKRVDFgPLTVDPVMIAKGGAALLAADAIKTVRDELIPLATVVTPNLPEAERLTGQAITSNQAMVTAGHALQGLGADNV 173
Cdd:pfam08543  81 KLDKYGV-PVVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  174 IIKGGHGDNPDLANDFVLLADGTAFWLSAPRIDTVRTHGTGDTLSACITAELAKGRSMAAAIKTAKAYVAGTIQDGIQVG 253
Cdd:pfam08543 160 LIKGGHLEGEEAVVTDVLYDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVTEAIRDALNLG 239


                  ....*..
gi 489739578  254 HGHGPLN 260
Cdd:pfam08543 240 KGHGPVN 246
HMP-P_kinase TIGR00097
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ...
 7-262 1.16e-104

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: 304.60  E-value: 1.16e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578    7 VATIAGTDSGGGAGVMADLKTMQARHVFGTAVVVAVTAQNTLGVQDFMAMPTKLIDEQFASLAADLDIRACKTGMLADAE 86
Cdd:TIGR00097   1 ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLASAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578   87 HVHAVVENLKRVDFGPLTVDPVMIAKGGAALLAADAIKTVRDELIPLATVVTPNLPEAERLTGQAITSNQAMVTAGHALQ 166
Cdd:TIGR00097  81 IVEAVARKLREYPVRPLVVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGTKIRTEQDMIKAAKKLR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  167 GLGADNVIIKGGHGDNpDLANDfVLLADGTAFWLSAPRIDTVRTHGTGDTLSACITAELAKGRSMAAAIKTAKAYVAGTI 246
Cdd:TIGR00097 161 ELGPKAVLIKGGHLEG-DQAVD-VLFDGGEIHILKAPRIETKNTHGTGCTLSAAIAANLAKGLSLKEAVKEAKEFVTGAI 238

                         250
                  ....*....|....*.
gi 489739578  247 QDGIQVGHGHGPLNHW 262
Cdd:TIGR00097 239 RYGLNIGHGHGPLNHF 254
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 6-249 1.14e-101

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: 296.34  E-value: 1.14e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578   6 QVATIAGTDSGGGAGVMADLKTMQARHVFGTAVVVAVTAQNTLGVQDFMAMPTKLIDEQFASLAADLDIRACKTGMLADA 85
Cdd:cd01169    1 VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLGSA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  86 EHVHAVVENLKRVDFGPLTVDPVMIAKGGAALLAADAIKTVRDELIPLATVVTPNLPEAERLTGQAITSNQAMVTAGHAL 165
Cdd:cd01169   81 EIIEAVAEALKDYPDIPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTGLEIATEEDMMKAAKAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 166 QGLGADNVIIKGGHGdNPDLANDfVLLADGTAFWLSAPRIDTVRTHGTGDTLSACITAELAKGRSMAAAIKTAKAYVAGT 245
Cdd:cd01169  161 LALGAKAVLIKGGHL-PGDEAVD-VLYDGGGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQA 238


                 ....
gi 489739578 246 IQDG 249
Cdd:cd01169  239 IRNA 242
 
Name Accession Description Interval E-value
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 9-263 2.00e-111

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: 321.60  E-value: 2.00e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578   9 TIAGTDSGGGAGVMADLKTMQARHVFGTAVVVAVTAQNTLGVQDFMAMPTKLIDEQFASLAADLDIRACKTGMLADAEHV 88
Cdd:COG0351    2 TIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSAEII 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  89 HAVVENLKRVDFGPLTVDPVMIAKGGAALLAADAIKTVRDELIPLATVVTPNLPEAERLTGQAITSNQAMVTAGHALQGL 168
Cdd:COG0351   82 EAVAEILADYPLVPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLEL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 169 GADNVIIKGGHGDNPDLANdfVLLADGTAFWLSAPRIDTVRTHGTGDTLSACITAELAKGRSMAAAIKTAKAYVAGTIQD 248
Cdd:COG0351  162 GAKAVLVKGGHLPGDEAVD--VLYDGDGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQAIRA 239

                        250
                 ....*....|....*
gi 489739578 249 GIQVGHGHGPLNHWA 263
Cdd:COG0351  240 ALRLGMGHGPVNHFA 254
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 1-263 4.10e-106

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 308.59  E-value: 4.10e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578   1 MNEFPQVATIAGTDSGGGAGVMADLKTMQARHVFGTAVVVAVTAQNTLGVQDFMAMPTKLIDEQFASLAADLDIRACKTG 80
Cdd:PRK06427   1 MMKRPIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  81 MLADAEHVHAVVENLKRVDFGPLTVDPVMIAKGGAALLAADAIKTVRDELIPLATVVTPNLPEAERLTGQAI-TSNQAMV 159
Cdd:PRK06427  81 MLASAEIIETVAEALKRYPIPPVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTGLPIaDTEDEMK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 160 TAGHALQGLGADNVIIKGGHGDNPDLANDfvLLADGTAFW-LSAPRIDTVRTHGTGDTLSACITAELAKGRSMAAAIKTA 238
Cdd:PRK06427 161 AAARALHALGCKAVLIKGGHLLDGEESVD--WLFDGEGEErFSAPRIPTKNTHGTGCTLSAAIAAELAKGASLLDAVQTA 238

                        250       260
                 ....*....|....*....|....*
gi 489739578 239 KAYVAGTIQDGIQVGHGHGPLNHWA 263
Cdd:PRK06427 239 KDYVTRAIRHALEIGQGHGPVNHFA 263
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 14-260 7.80e-105

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: 304.40  E-value: 7.80e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578   14 DSGGGAGVMADLKTMQARHVFGTAVVVAVTAQNTLGVQDFMAMPTKLIDEQFASLAADLDIRACKTGMLADAEHVHAVVE 93
Cdd:pfam08543   1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLGSAEIIEAVAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578   94 NLKRVDFgPLTVDPVMIAKGGAALLAADAIKTVRDELIPLATVVTPNLPEAERLTGQAITSNQAMVTAGHALQGLGADNV 173
Cdd:pfam08543  81 KLDKYGV-PVVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  174 IIKGGHGDNPDLANDFVLLADGTAFWLSAPRIDTVRTHGTGDTLSACITAELAKGRSMAAAIKTAKAYVAGTIQDGIQVG 253
Cdd:pfam08543 160 LIKGGHLEGEEAVVTDVLYDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVTEAIRDALNLG 239


                  ....*..
gi 489739578  254 HGHGPLN 260
Cdd:pfam08543 240 KGHGPVN 246
HMP-P_kinase TIGR00097
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ...
 7-262 1.16e-104

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: 304.60  E-value: 1.16e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578    7 VATIAGTDSGGGAGVMADLKTMQARHVFGTAVVVAVTAQNTLGVQDFMAMPTKLIDEQFASLAADLDIRACKTGMLADAE 86
Cdd:TIGR00097   1 ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLASAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578   87 HVHAVVENLKRVDFGPLTVDPVMIAKGGAALLAADAIKTVRDELIPLATVVTPNLPEAERLTGQAITSNQAMVTAGHALQ 166
Cdd:TIGR00097  81 IVEAVARKLREYPVRPLVVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGTKIRTEQDMIKAAKKLR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  167 GLGADNVIIKGGHGDNpDLANDfVLLADGTAFWLSAPRIDTVRTHGTGDTLSACITAELAKGRSMAAAIKTAKAYVAGTI 246
Cdd:TIGR00097 161 ELGPKAVLIKGGHLEG-DQAVD-VLFDGGEIHILKAPRIETKNTHGTGCTLSAAIAANLAKGLSLKEAVKEAKEFVTGAI 238

                         250
                  ....*....|....*.
gi 489739578  247 QDGIQVGHGHGPLNHW 262
Cdd:TIGR00097 239 RYGLNIGHGHGPLNHF 254
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 6-249 1.14e-101

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: 296.34  E-value: 1.14e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578   6 QVATIAGTDSGGGAGVMADLKTMQARHVFGTAVVVAVTAQNTLGVQDFMAMPTKLIDEQFASLAADLDIRACKTGMLADA 85
Cdd:cd01169    1 VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLGSA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  86 EHVHAVVENLKRVDFGPLTVDPVMIAKGGAALLAADAIKTVRDELIPLATVVTPNLPEAERLTGQAITSNQAMVTAGHAL 165
Cdd:cd01169   81 EIIEAVAEALKDYPDIPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTGLEIATEEDMMKAAKAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 166 QGLGADNVIIKGGHGdNPDLANDfVLLADGTAFWLSAPRIDTVRTHGTGDTLSACITAELAKGRSMAAAIKTAKAYVAGT 245
Cdd:cd01169  161 LALGAKAVLIKGGHL-PGDEAVD-VLYDGGGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQA 238


                 ....
gi 489739578 246 IQDG 249
Cdd:cd01169  239 IRNA 242
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 5-261 3.92e-75

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 237.36  E-value: 3.92e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578   5 PQVATIAGTDSGGGAGVMADLKTMQARHVFGTAVVVAVTAQNTLGVQDFMAMPTKLIDEQFASLAADLDIRACKTGMLAD 84
Cdd:PLN02898  10 PHVLTVAGSDSGAGAGIQADIKACAARGVYCTTAITAVTAQNTVGVQGVHAVPLDFVAEQLKSVLSDMPVDVVKTGMLPS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  85 AEHVHAVVENLKRVDFGPLTVDPVMIAKGGAALLAADAIKTVRDELIPLATVVTPNLPEAERLTG-QAITSNQAMVTAGH 163
Cdd:PLN02898  90 AEIVKVLCQALKEFPVKALVVDPVMVSTSGDVLAGPSILSALREELLPLATIVTPNVKEASALLGgDPLETVADMRSAAK 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 164 ALQGLGADNVIIKGGHgdNPDLANDFVLLADGTAFW-LSAPRIDTVRTHGTGDTLSACITAELAKGRSMAAAIKTAKAYV 242
Cdd:PLN02898 170 ELHKLGPRYVLVKGGH--LPDSLDAVDVLYDGTEFHeLRSSRIKTRNTHGTGCTLASCIAAELAKGSDMLSAVKVAKRYV 247

                        250       260
                 ....*....|....*....|..
gi 489739578 243 AGTIQ--DGIQVGHG-HGPLNH 261
Cdd:PLN02898 248 ETALEysKDIGIGNGaQGPFNH 269
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
9-260 2.33e-72

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 228.46  E-value: 2.33e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578   9 TIAGTDSGGGAGVMADLKTMQARHVFGTAVVVAVTAQNTLGVQDFMAMPTKLIDEQFASLAADLDIRACKTGMLADAEHV 88
Cdd:PRK08573   7 TIAGSDSGGGAGIEADLKTFAALGVHGAVAITSVTAQNTYEVRAIHDLPPEVVAAQIEAVWEDMGIDAAKTGMLSNREII 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  89 HAVVENLKRVDFgPLTVDPVMIAKGGAALLAADAIKTVRDELIPLATVVTPNLPEAERLTGQAITS-NQAMVTAGHALQG 167
Cdd:PRK08573  87 EAVAKTVSKYGF-PLVVDPVMIAKSGAPLLREDAVDALIKRLLPLATVVTPNRPEAEKLTGMKIRSvEDARKAAKYIVEE 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 168 LGADNVIIKGGHGDNPDlANDfVLLADGTAFWLSAPRIDTVRTHGTGDTLSACITAELAKGRSMAAAIKTAKAYVAGTIQ 247
Cdd:PRK08573 166 LGAEAVVVKGGHLEGEE-AVD-VLYHNGTFREFRAPRVESGCTHGTGCSFSAAIAAGLAKGLDPEEAIKTAKKFITMAIK 243

                        250
                 ....*....|...
gi 489739578 248 DGIQVGHGHGPLN 260
Cdd:PRK08573 244 YGVKIGKGHCPVN 256
PTZ00347 PTZ00347
phosphomethylpyrimidine kinase; Provisional
 5-266 4.76e-56

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240375 [Multi-domain]  Cd Length: 504  Bit Score: 187.86  E-value: 4.76e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578   5 PQVATIAGTDSGGGAGVMADLKTMQARHVFGTAVVVAVTAQNTLGVQDFMAMPTKLIDEQFASLAADLDIRACKTGMLAD 84
Cdd:PTZ00347 231 PTVLTVSGSDSGGGAGHQADLKTLEALGVYSTSALTSLTAQNTKGVQQIQVVNEDFFAAQIDSVMSDFNISVVKLGLVPT 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  85 AEHVHAVVENLKRVdfgPLTVDPVMIAKGGAALLAADAIKTV----RDELIPLATVVTPNLPEAERLTGQA-ITSNQAMV 159
Cdd:PTZ00347 311 ARQLEIVIEKLKNL---PMVVDPVLVATSGDDLVAQKNADDVlamyKERIFPMATIITPNIPEAERILGRKeITGVYEAR 387

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 160 TAGHALQGLGADNVIIKGGHGD-NPDLANDFVLLADGTAFW-LSAPRIDTVRTHGTGDTLSACITAELAKGRSMAAAIKT 237
Cdd:PTZ00347 388 AAAQALAQYGSRYVLVKGGHDLiDPEACRDVLYDREKDRFYeFTANRIATINTHGTGCTLASAISSFLARGYTVPDAVER 467

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 489739578 238 AKAYVAGTIQDGIQVGHG---HGPLNH-----WATPS 266
Cdd:PTZ00347 468 AIGYVHEAIVRSCGVPLGqgtNRPLVHslnsvWANYV 504
PRK14713 PRK14713
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
5-261 1.66e-52

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 237797 [Multi-domain]  Cd Length: 530  Bit Score: 178.83  E-value: 1.66e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578   5 PQVATIAGTDSGGGAGVMADLKTMQARHVFGTAVVVAVTAQNTLGVQDFMAMPTKLIDEQFASLAADLDIRACKTGMLAD 84
Cdd:PRK14713  30 PRVLSIAGTDPSGGAGIQADLKSIAAAGGYGMAVITALVAQNTRGVRAVHVPPADFLRAQLDAVSDDVTVDAVKIGMLGD 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  85 AEHVHAVVENLKRVDFGPLTVDPVMIAKGGAALLAADAIKTVRdELIPLATVVTPNLPEAERLTGQ-AITSNQAMVTAGH 163
Cdd:PRK14713 110 AEVIDAVRTWLAEHRPPVVVLDPVMVATSGDRLLEEDAEAALR-ELVPRADLITPNLPELAVLLGEpPATTWEEALAQAR 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 164 ALQGLGADNVIIKGGHGDNPDlANDFVLLADGTAFWLSAPRIDTVRTHGTGDTLSACITAELAKGRSMAAAIKTAKAYVA 243
Cdd:PRK14713 189 RLAAETGTTVLVKGGHLDGQR-APDALVGPDGAVTEVPGPRVDTRNTHGTGCSLSSALATRLGRGGDWAAALRWATAWLH 267

                        250       260
                 ....*....|....*....|
gi 489739578 244 GTIQ--DGIQVGHGHGPLNH 261
Cdd:PRK14713 268 GAIAagAALQVGTGNGPVDH 287
PRK12616 PRK12616
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
9-263 1.83e-49

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183624  Cd Length: 270  Bit Score: 164.45  E-value: 1.83e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578   9 TIAGTDSGGGAGVMADLKTMQARHVFG-TA--VVVAVTAQNTLGVQDFmAMPTKLIDEQFASLAADLDIRACKTGMLADA 85
Cdd:PRK12616   8 TIAGSDSSGGAGIQADLKTFQEKNVYGmTAltVVVAMDPENSWDHQVF-PIDTDTIRAQLSTIVDGIGVDAMKTGMLPTV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  86 EHVHAVVENLKRVDFGPLTVDPVMIAKGGAALLAADAIKTVRDELIPLATVVTPNLPEAERLTG-QAITSNQAMVTAGHA 164
Cdd:PRK12616  87 DIIELAADTIKEKQLKNVVIDPVMVCKGANEVLYPEHAEALREQLAPLATVITPNLFEAGQLSGmGEIKTVEQMKEAAKK 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 165 LQGLGADNVIIKGGHGDNPDLANDfvLLADG-TAFWLSAPRIDTVRTHGTGDTLSACITAELAKGRSMAAAIKTAKAYVA 243
Cdd:PRK12616 167 IHELGAQYVVITGGGKLKHEKAVD--VLYDGeTAEVLESEMIDTPYTHGAGCTFSAAVTAELAKGSEVKEAIYAAKEFIT 244

                        250       260
                 ....*....|....*....|
gi 489739578 244 GTIQDGIQVGHGHGPLNHWA 263
Cdd:PRK12616 245 AAIKESFPLNQYVGPTKHSA 264
PRK12412 PRK12412
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
5-263 1.96e-49

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183512 [Multi-domain]  Cd Length: 268  Bit Score: 164.37  E-value: 1.96e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578   5 PQVATIAGTDSGGGAGVMADLKTMQARHVFG-TAV--VVAVTAQNTLGVQDFmAMPTKLIDEQFASLAADLDIRACKTGM 81
Cdd:PRK12412   2 NKALTIAGSDTSGGAGIQADLKTFQELGVYGmTSLttIVTMDPHNGWAHNVF-PIPASTLKPQLETTIEGVGVDALKTGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  82 LADAEHVHAVVENLKRVDFGPLTVDPVMIAKGGAALLAADAIKTVRDELIPLATVVTPNLPEAERLTGQAITSNQAMVTA 161
Cdd:PRK12412  81 LGSVEIIEMVAETIEKHNFKNVVVDPVMVCKGADEALHPETNDCLRDVLVPKALVVTPNLFEAYQLSGVKINSLEDMKEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 162 GHALQGLGADNVIIKGGHGDNPDLANDfvLLADGTAF-WLSAPRIDTVRTHGTGDTLSACITAELAKGRSMAAAIKTAKA 240
Cdd:PRK12412 161 AKKIHALGAKYVLIKGGSKLGTETAID--VLYDGETFdLLESEKIDTTNTHGAGCTYSAAITAELAKGKPVKEAVKTAKE 238

                        250       260
                 ....*....|....*....|...
gi 489739578 241 YVAGTIQDGIQVGHGHGPLNHWA 263
Cdd:PRK12412 239 FITAAIRYSFKINEYVGPTHHGA 261
PRK09517 PRK09517
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ...
 5-263 7.68e-45

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


Pssm-ID: 169939 [Multi-domain]  Cd Length: 755  Bit Score: 160.91  E-value: 7.68e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578   5 PQVATIAGTDSGGGAGVMADLKTMQARHVFGTAVVVAVTAQNTLGVQDFMAMPTKLIDEQFASLAADLDIRACKTGMLAD 84
Cdd:PRK09517 242 PRVLSIAGTDPTGGAGIQADLKSIAAGGGYGMCVVTALVAQNTHGVNTIHTPPLTFLEEQLEAVFSDVTVDAVKLGMLGS 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  85 AEHVHAVVENLKRVDFGPLTVDPVMIAKGGAALLAADAIKTVRdELIPLATVVTPNLPEAERLTGQ--AITSNQAMVTAg 162
Cdd:PRK09517 322 ADTVDLVASWLGSHEHGPVVLDPVMVATSGDRLLDADATEALR-RLAVHVDVVTPNIPELAVLCGEapAITMDEAIAQA- 399

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 163 halQGLGADN---VIIKGGHGDNPDlANDFVLLADGTAFWLSAPRIDTVRTHGTGDTLSACITAELAKGRSMAAAIKTAK 239
Cdd:PRK09517 400 ---RGFARTHgtiVIVKGGHLTGDL-ADNAVVRPDGSVHQVENPRVNTTNSHGTGCSLSAALATLIAAGESVEKALEWAT 475

                        250       260
                 ....*....|....*....|....*.
gi 489739578 240 AYVAGTIQ--DGIQVGHGHGPLNHWA 263
Cdd:PRK09517 476 RWLNEALRhaDHLAVGSGNGPVDHGH 501
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
7-253 1.87e-37

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 132.49  E-value: 1.87e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578   7 VATIAGTDSGGGAGVMADLKTMQARHVFGtavVVAVTAQNTLGVQDFMAMPT--KLIDEQFASLAaDLDIRACKTGMLAD 84
Cdd:PRK12413   6 ILAISGNDIFSGGGLHADLATYTRNGLHG---FVAVTCLTAMTEKGFEVFPVdkEIFQQQLDSLK-DVPFSAIKIGLLPN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  85 AEHVHAVVENLKRVDFGPLTVDPVMIAKGGAALLaadaIKTVRDELI---PLATVVTPNLPEAERLTGQAITSNQAMVTA 161
Cdd:PRK12413  82 VEIAEQALDFIKGHPGIPVVLDPVLVCKETHDVE----VSELRQELIqffPYVTVITPNLVEAELLSGKEIKTLEDMKEA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 162 GHALQGLGADNVIIKGGHGDNPDLANDfvLLADGTAFW-LSAPRIDTVRThGTGDTLSACITAELAKGRSMAAAIKTAKA 240
Cdd:PRK12413 158 AKKLYDLGAKAVVIKGGNRLSQKKAID--LFYDGKEFViLESPVLEKNNI-GAGCTFASSIASQLVKGKSPLEAVKNSKD 234

                        250
                 ....*....|...
gi 489739578 241 YVAGTIQDGIQVG 253
Cdd:PRK12413 235 FVYQAIQQSDQYG 247
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 39-247 8.81e-29

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: 110.24  E-value: 8.81e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  39 VVAV-TAQ--NTLGVQDF--MAMPTKLIDEQFASLA---ADLDIRACKTGMLADAEHVHAVVENLKRV----DFGPLTVD 106
Cdd:COG2240   32 VWPLpTVLlsNHTGYGTFtgRDLPTDDIADILDGWKelgVLLEFDAVLSGYLGSAEQGDIIADFVARVkaanPDALYLCD 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 107 PVMIAKGGAALLAADAIKTVRDELIPLATVVTPNLPEAERLTGQAITSNQAMVTAGHALQGLGADNVIIKG-GHGDNPDL 185
Cdd:COG2240  112 PVMGDNGKGYYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVTSvPLDDTPAD 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489739578 186 ANDFVLLADGTAFWLSAPRIDtVRTHGTGDTLSACITAELAKGRSMAAAIKTAKAYVAGTIQ 247
Cdd:COG2240  192 KIGNLAVTADGAWLVETPLLP-FSPNGTGDLFAALLLAHLLRGKSLEEALERAAAFVYEVLE 252
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 79-247 1.22e-20

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: 88.03  E-value: 1.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  79 TGMLADAEHVHAVVENLKRV--DFGPLT--VDPVMIAKGGAALLAADAIKTVRDELIPLATVVTPNLPEAERLTGQAITS 154
Cdd:cd01173   78 TGYLGSAEQVEAVAEIVKRLkeKNPNLLyvCDPVMGDNGKLYVVAEEIVPVYRDLLVPLADIITPNQFELELLTGKKIND 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 155 NQAMVTAGHALQGLGADNVIIKGGHGDNPDLANdfVLLADGTAFWLSA-PRIDTVRT-HGTGDTLSACITAELAKGRSMA 232
Cdd:cd01173  158 LEDAKAAARALHAKGPKTVVVTSVELADDDRIE--MLGSTATEAWLVQrPKIPFPAYfNGTGDLFAALLLARLLKGKSLA 235

                        170
                 ....*....|....*
gi 489739578 233 AAIKTAKAYVAGTIQ 247
Cdd:cd01173  236 EALEKALNFVHEVLE 250
PTZ00493 PTZ00493
phosphomethylpyrimidine kinase; Provisional
 1-261 1.31e-17

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240440  Cd Length: 321  Bit Score: 80.81  E-value: 1.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578   1 MNEFPQVATIAGTDSGGGAGVMADLKTMQARHVFGTAVVVAVTAQNTLGVQDFMAMPTKLIDEQFASLAADLDIRACKTG 80
Cdd:PTZ00493   1 MEGVSNILSIAGSDSCGGAGMQADIKTAMGLGCHCCTALVVLTAQNTKEVKRIVEIEEKFIVEQLDSIFADVTIDVVKLG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  81 MLADAE---HVHAVVENLKRVDFGPLTV--DPVMIAKGG-AALLAADAIKTVRDELIPLATVVTPNLPEAE--------- 145
Cdd:PTZ00493  81 VLYSKKiisLVHNYITNMNKKRGKKLLVvfDPVFVSSSGcLLVENLEYIKFALDLICPISCIITPNFYECKvilealdcq 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 146 ------------RLTGQAITSNQAMVTAGHALQGLGADNVIIKGGH------GDNPD------LANDFVLLADgtAFWLS 201
Cdd:PTZ00493 161 mdlskanmtelcKLVTEKLNINACLFKSCNVGENSAEENEVYAVDHlcirnvGSYPTgekqqiDAGGVTYLYD--VYKLR 238

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 202 APRIDTVRTHGTGDTLSACITAELAKGRSMAAAIKTAKAYVAGTIQDGIQVGHGHGPLNH 261
Cdd:PTZ00493 239 SKRKPGKDIHGTGCTLSTAIACYLAKKHNILQSCIESKKYIYNCIRYAYPFGSKSQGLNH 298
PRK05756 PRK05756
pyridoxal kinase PdxY;
54-242 3.36e-14

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 70.67  E-value: 3.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  54 MAMPtkliDEQFASLAADLD-------IRACKTGMLADAEHVHAVVENLKRV-DFGPLTV---DPVMIAKGGAALLAADA 122
Cdd:PRK05756  52 CVMP----PSHLTEIVQGIAdigwlgeCDAVLSGYLGSAEQGEAILDAVRRVkAANPQALyfcDPVMGDPEKGCIVAPGV 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 123 IKTVRDELIPLATVVTPNLPEAERLTGQAITSNQAMVTAGHALQGLGADNVIIKggHGDNPDLANDF--VLLADGTAFWL 200
Cdd:PRK05756 128 AEFLRDRALPAADIITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVT--SLARAGYPADRfeMLLVTADGAWH 205

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 489739578 201 -SAPRIDTVR-THGTGDTLSACITAELAKGRSMAAAIKTAKAYV 242
Cdd:PRK05756 206 iSRPLVDFMRqPVGVGDLTSALFLARLLQGGSLEEALEHTTAAV 249
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
62-242 6.49e-13

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 66.99  E-value: 6.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  62 DEQFASLAADL-------DIRACKTGMLADAEHVHAVVENLKRV--DFGPLT--VDPVMIAKGGAALLAADAIKTVRDEL 130
Cdd:PRK08176  70 DEWFSGYLRALqerdalrQLRAVTTGYMGSASQIKILAEWLTALraDHPDLLimVDPVIGDIDSGIYVKPDLPEAYRQHL 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 131 IPLATVVTPNLPEAERLTGQAITSNQAMVTAGHALQGLGADNVIIKGGHGDNPDLANDFVLLADGTAFWLSAPRIDTVrT 210
Cdd:PRK08176 150 LPLAQGLTPNIFELEILTGKPCRTLDSAIAAAKSLLSDTLKWVVITSAAGNEENQEMQVVVVTADSVNVISHPRVDTD-L 228

                        170       180       190
                 ....*....|....*....|....*....|..
gi 489739578 211 HGTGDTLSACITAELAKGRSMAAAIKTAKAYV 242
Cdd:PRK08176 229 KGTGDLFCAELVSGLLKGKALTDAAHRAGLRV 260
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 128-247 1.70e-12

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 66.21  E-value: 1.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  128 DELIPLATVVTPNLPEAERLTGQAITSNQAMVTAGHALQGLGADNVIIKggHGDNPDLANDfvllADGTAFWLSAPRIDT 207
Cdd:pfam00294 175 LELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVT--LGADGALVVE----GDGEVHVPAVPKVKV 248

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 489739578  208 VRTHGTGDTLSACITAELAKGRSMAAAIKTAKAYVAGTIQ 247
Cdd:pfam00294 249 VDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQ 288
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 124-247 3.02e-12

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: 65.26  E-value: 3.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 124 KTVRDELIPLATVVTPNLPEAERLTGQAITSNQAMVTAGHALQGLGADNVIIK-GGHGDnpdlandfVLLADGTAFWLSA 202
Cdd:cd01174  166 RPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTlGAKGA--------LLASGGEVEHVPA 237

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489739578 203 PRIDTVRTHGTGDTLSACITAELAKGRSMAAAIKTAKAYVAGTIQ 247
Cdd:cd01174  238 FKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVT 282
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
 54-253 3.23e-12

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: 65.24  E-value: 3.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578   54 MAMPTKLIDEQFASLAADLDIRACK---TGMLADAEHVHAVVENLKRVDFG-PLTV---DPVMIAKGGAALLAADAIKTV 126
Cdd:TIGR00687  52 QVLPPDELHELVEGLEAINKLNQCDavlSGYLGSAEQVAMVVGIVRQVKQAnPQALyvcDPVMGDPWKGCYVAPDLLEVY 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  127 RDELIPLATVVTPNLPEAERLTGQAITSNQAMVTAGHALQGLGADNVIIKG-GHGDNPDLANDFVLLADGTAFW-LSAPR 204
Cdd:TIGR00687 132 REKAIPVADIITPNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVTHlIRAGSQRDRSFEGLVATQEGRWhISRPL 211

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 489739578  205 IDTVRTH-GTGDTLSACITAELAKGRSMAAAIKTAKAYVAGTIQDGIQVG 253
Cdd:TIGR00687 212 AVFDPPPvGTGDLIAALLLATLLHGNSLKEALEKTVSAVYHVLRTTIQLG 261
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 129-232 5.15e-11

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 61.64  E-value: 5.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 129 ELIPLATVVTPNLPEAERLTGQAITSNQAMVTAGHALQGLGADNVIIKGGHGDNPDLANDFVLL------ADGTAFWLSA 202
Cdd:PTZ00344 135 ELIPYADVITPNQFEASLLSGVEVKDLSDALEAIDWFHEQGIPVVVITSFREDEDPTHLRFLLScrdkdtKNNKRFTGKV 214

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489739578 203 PRIDTVRThGTGDTLSACITA-------ELAKGRSMA 232
Cdd:PTZ00344 215 PYIEGRYT-GTGDLFAALLLAfshqhpmDLAVGKAMG 250
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
135-241 6.87e-11

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 61.30  E-value: 6.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 135 TVVTPNLPEAERLTGQAITSNQAMVTAGHALQGLGADNVII-KGGHGDnpdlandfVLLADGTAFWLSAPRIDTVRTHGT 213
Cdd:COG1105  179 DLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVsLGADGA--------LLVTEDGVYRAKPPKVEVVSTVGA 250

                         90       100
                 ....*....|....*....|....*...
gi 489739578 214 GDTLSACITAELAKGRSMAAAIKTAKAY 241
Cdd:COG1105  251 GDSMVAGFLAGLARGLDLEEALRLAVAA 278
PLN02978 PLN02978
pyridoxal kinase
 127-253 9.02e-11

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 61.29  E-value: 9.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 127 RDELIPLATVVTPNLPEAERLTGQAITSNQAMVTAGHALQGLGADNVIIKgghgdNPDLANDFVLLAD--------GTAF 198
Cdd:PLN02978 143 REKVVPLATMLTPNQFEAEQLTGIRIVTEEDAREACAILHAAGPSKVVIT-----SIDIDGKLLLVGShrkekgarPEQF 217

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 199 WLSAPRIDTVRThGTGDTLSACITAELAK-----GRSMAAAIKTAKAYVAGTIQDGIQVG 253
Cdd:PLN02978 218 KIVIPKIPAYFT-GTGDLMAALLLGWSHKypdnlDKAAELAVSSLQAVLRRTLADYKRAG 276
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
 135-247 4.52e-10

1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.


Pssm-ID: 238570 [Multi-domain]  Cd Length: 289  Bit Score: 59.08  E-value: 4.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 135 TVVTPNLPEAERLTGQAITSNQAMVTAGHALQGLGADNVIIKgghgdnpdLANDFVLLADGTAFWL-SAPRIDTVRTHGT 213
Cdd:cd01164  179 FLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVS--------LGADGALLVTKDGVYRaSPPKVKVVSTVGA 250

                         90       100       110
                 ....*....|....*....|....*....|....
gi 489739578 214 GDTLSACITAELAKGRSMAAAIKTAKAYVAGTIQ 247
Cdd:cd01164  251 GDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAF 284
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 128-238 9.60e-09

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: 54.89  E-value: 9.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 128 DELIPLATVVTPNLPEAERLTGQAitsnqAMVTAGHALQGLGADNVIIK-GGHGdnpdlandFVLLADGTAFWLSAPRID 206
Cdd:COG0524  180 RELLALVDILFPNEEEAELLTGET-----DPEEAAAALLARGVKLVVVTlGAEG--------ALLYTGGEVVHVPAFPVE 246

                         90       100       110
                 ....*....|....*....|....*....|..
gi 489739578 207 TVRTHGTGDTLSACITAELAKGRSMAAAIKTA 238
Cdd:COG0524  247 VVDTTGAGDAFAAGFLAGLLEGLDLEEALRFA 278
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 135-247 8.06e-08

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: 52.32  E-value: 8.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 135 TVVTPNLPEAERLTGQAITSNQAMVTAGHALQGLGADNVIIKggHGDNPDLANDfvlLADGTAFWLSAPRI--DTVRTHG 212
Cdd:cd01941  178 DLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVT--LGAKGVLLSS---REGGVETKLFPAPQpeTVVNVTG 252

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489739578 213 TGDTLSACITAELAKGRSMAAAIKTAKAYVAGTIQ 247
Cdd:cd01941  253 AGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTLE 287
PRK11142 PRK11142
ribokinase; Provisional
 128-243 1.49e-06

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 48.33  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 128 DELIPLATVVTPNLPEAERLTGQAITSNQAMVTAGHALQGLGADNVIIKGGhgdnpdlandfvllADGTafWLS------ 201
Cdd:PRK11142 173 DELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLG--------------SRGV--WLSengegq 236

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489739578 202 ---APRIDTVRTHGTGDTLS-ACITAELAkGRSMAAAIKTAKAYVA 243
Cdd:PRK11142 237 rvpGFRVQAVDTIAAGDTFNgALVTALLE-GKPLPEAIRFAHAAAA 281
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 129-226 3.00e-06

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: 46.70  E-value: 3.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 129 ELIPLATVVTPNLPEAERLTGQAITSNQAMVTAGHALQGLGADNVIIKGGHGdnpdlaNDFVLLADGTAFWLSAPRIDTV 208
Cdd:cd00287  105 KLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEK------GAIVATRGGTEVHVPAFPVKVV 178

                         90
                 ....*....|....*...
gi 489739578 209 RTHGTGDTLSACITAELA 226
Cdd:cd00287  179 DTTGAGDAFLAALAAGLA 196
PTZ00292 PTZ00292
ribokinase; Provisional
 129-247 1.40e-05

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 45.50  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 129 ELIPLATVVTPNLPEAERLTGQAITSNQAMVTAGHALQGLGADNVIIKGGhgdnpdlANDFVLLADGTA-FWLSAPRIDT 207
Cdd:PTZ00292 194 PFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLG-------ANGCLIVEKENEpVHVPGKRVKA 266

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489739578 208 VRTHGTGDTLSACITAELAKGRSMAAAIKTAKAYVAGTIQ 247
Cdd:PTZ00292 267 VDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVT 306
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
 134-234 2.12e-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: 41.78  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 134 ATVVTPNLPEAERLTGQAITSNQAMVTAGHALQG-LGADNVIIK-GGHGdnpdlandFVLLADGTAFW----LSAPRIDT 207
Cdd:cd01172  182 ATLLTPNEKEAREALGDEINDDDELEAAGEKLLElLNLEALLVTlGEEG--------MTLFERDGEVQhipaLAKEVYDV 253

                         90       100
                 ....*....|....*....|....*..
gi 489739578 208 VrthGTGDTLSACITAELAKGRSMAAA 234
Cdd:cd01172  254 T---GAGDTVIATLALALAAGADLEEA 277
PRK07105 PRK07105
pyridoxamine kinase; Validated
 71-247 8.84e-04

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 39.90  E-value: 8.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  71 DLDIRACKTGMLADAEHVHAVVENLK--RVDFGPLTVDPVMIAKGGAALLAADAIKTVRDELIPLATVVTPNLPEAERLT 148
Cdd:PRK07105  73 NLKFDAIYSGYLGSPRQIQIVSDFIKyfKKKDLLVVVDPVMGDNGKLYQGFDQEMVEEMRKLIQKADVITPNLTEACLLL 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 149 GQAIT----SNQAMVTAGHALQGLGADNVIIKGghgdNPDLANDFVLLA---DGTAFWL-SAPRIDTvrtH--GTGDTLS 218
Cdd:PRK07105 153 DKPYLeksySEEEIKQLLRKLADLGPKIVIITS----VPFEDGKIGVAYydrATDRFWKvFCKYIPA---HypGTGDIFT 225

                        170       180
                 ....*....|....*....|....*....
gi 489739578 219 ACITAELAKGRSMAAAIKTAKAYVAGTIQ 247
Cdd:PRK07105 226 SVITGSLLQGDSLPIALDRAVQFIEKGIR 254
fruK PRK09513
1-phosphofructokinase; Provisional
 137-243 1.39e-03

1-phosphofructokinase; Provisional


Pssm-ID: 181923 [Multi-domain]  Cd Length: 312  Bit Score: 39.29  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 137 VTPNLPEAERLTGQAITSNQAMVTAGHALQGLGADNVIIKGGhgdnpdlandfvllADGtAFWLSA--------PRIDTV 208
Cdd:PRK09513 184 VKPNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLG--------------AEG-ALWVNAsgewiakpPACDVV 248

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489739578 209 RTHGTGDTLSACITAELAKGRSMAAAIKTAKAYVA 243
Cdd:PRK09513 249 STVGAGDSMVGGLIYGLLMRESSEHTLRLATAVSA 283
YegV_kinase_like cd01944
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ...
 124-247 2.51e-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: 38.56  E-value: 2.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 124 KTVRDELIPLATVVTPNLPEAERLTGQAITSNQAMVTAGHALQGLGadnVIIKGGHgdnpdlANDFVLLADGTAFWLSAP 203
Cdd:cd01944  172 DTILQALMAKRPIWSCNREEAAIFAERGDPAAEASALRIYAKTAAP---VVVRLGS------NGAWIRLPDGNTHIIPGF 242

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489739578 204 RIDTVRTHGTGDTLSACITAELAKGRSMAAAIKTAKAYVAGTIQ 247
Cdd:cd01944  243 KVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVT 286
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 135-240 2.75e-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: 38.36  E-value: 2.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578 135 TVVTPNLPEAERLTGQAITSNQA-MVTAGHALQGLGADNVIIKGghgdnpdlANDFVLLADGTAFWLSA--PRidtVRTH 211
Cdd:cd01171  130 VVLTPHPGEFARLLGALVEEIQAdRLAAAREAAAKLGATVVLKG--------AVTVIADPDGRVYVNPTgnPG---LATG 198

                         90       100       110
                 ....*....|....*....|....*....|
gi 489739578 212 GTGDTLSACITAELAKGRS-MAAAIKTAKA 240
Cdd:cd01171  199 GSGDVLAGIIAALLAQGLSpLEAAALAVYL 228
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 134-248 5.04e-03

Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also is a carbohydrate kinase. (personal obs Yeats C).


Pssm-ID: 396007  Cd Length: 242  Bit Score: 37.34  E-value: 5.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489739578  134 ATVVTPNLPEAERLTGQAITSNQAMVTAGHAL-QGLGAdNVIIKGGHGDNPDLANDFVLLADGTAfWLsapridtvRTHG 212
Cdd:pfam01256 117 PTVLTPHPGEFERLCGLAGILGDDRLEAARELaQKLNG-TILLKGNVTVIAAPGGEVWINSTGNS-AL--------AKGG 186

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 489739578  213 TGDTLSACITAELAKGRSMAAAIKTAkAYVAGTIQD 248
Cdd:pfam01256 187 SGDVLAGLIGGLLAQNEDPYDAAIAA-AWLHGAASD 221
 
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