NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|521289071|ref|WP_020453339|]
View 

MULTISPECIES: bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase [Bacillus]

Protein Classification

carbohydrate kinase family protein( domain architecture ID 399)

carbohydrate kinase family protein that accepts a wide variety of substrates, including carbohydrates and aromatic small molecules, all being phosphorylated at a hydroxyl group; belongs to the ribokinase/pfkB sugar kinase superfamily

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ribokinase_pfkB_like super family cl00192
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 1-270 0e+00

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).


The actual alignment was detected with superfamily member PRK12616:

Pssm-ID: 469648  Cd Length: 270  Bit Score: 534.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071   1 MTMHKALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPENNWNHQVFPVDTEVIRAQLSTIVDGIGVDAMKT 80
Cdd:PRK12616   1 MSMHKALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPENSWDHQVFPIDTDTIRAQLSTIVDGIGVDAMKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  81 GMLPTVDIIELAADTIKKHSMKNVVIDPVMVCKGANEVLYPEHAKALRELLAPLATVITPNLFEAGQLSGLGEIKTVEQM 160
Cdd:PRK12616  81 GMLPTVDIIELAADTIKEKQLKNVVIDPVMVCKGANEVLYPEHAEALREQLAPLATVITPNLFEAGQLSGMGEIKTVEQM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 161 KEAAKVIHGLGAEHVLITGGGKLNHEKAVDVLFDGRDAEVIEGERIETPYTHGAGCTYSAAITAELAKGSNVKEAIYSAK 240
Cdd:PRK12616 161 KEAAKKIHELGAQYVVITGGGKLKHEKAVDVLYDGETAEVLESEMIDTPYTHGAGCTFSAAVTAELAKGSEVKEAIYAAK 240

                        250       260       270
                 ....*....|....*....|....*....|
gi 521289071 241 TFITEAIRESFRLNQYVGPTKHSALRLSGK 270
Cdd:PRK12616 241 EFITAAIKESFPLNQYVGPTKHSALRLSGK 270
 
Name Accession Description Interval E-value
PRK12616 PRK12616
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
1-270 0e+00

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183624  Cd Length: 270  Bit Score: 534.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071   1 MTMHKALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPENNWNHQVFPVDTEVIRAQLSTIVDGIGVDAMKT 80
Cdd:PRK12616   1 MSMHKALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPENSWDHQVFPIDTDTIRAQLSTIVDGIGVDAMKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  81 GMLPTVDIIELAADTIKKHSMKNVVIDPVMVCKGANEVLYPEHAKALRELLAPLATVITPNLFEAGQLSGLGEIKTVEQM 160
Cdd:PRK12616  81 GMLPTVDIIELAADTIKEKQLKNVVIDPVMVCKGANEVLYPEHAEALREQLAPLATVITPNLFEAGQLSGMGEIKTVEQM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 161 KEAAKVIHGLGAEHVLITGGGKLNHEKAVDVLFDGRDAEVIEGERIETPYTHGAGCTYSAAITAELAKGSNVKEAIYSAK 240
Cdd:PRK12616 161 KEAAKKIHELGAQYVVITGGGKLKHEKAVDVLYDGETAEVLESEMIDTPYTHGAGCTFSAAVTAELAKGSEVKEAIYAAK 240

                        250       260       270
                 ....*....|....*....|....*....|
gi 521289071 241 TFITEAIRESFRLNQYVGPTKHSALRLSGK 270
Cdd:PRK12616 241 EFITAAIKESFPLNQYVGPTKHSALRLSGK 270
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 7-264 8.32e-122

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: 347.80  E-value: 8.32e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071   7 LTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPENNwnHQVFPVDTEVIRAQLSTIVDGIGVDAMKTGMLPTV 86
Cdd:COG0351    1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGV--TGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  87 DIIELAADTIKKHSMKNVVIDPVMVCKGANEVLYPEHAKALRELLAPLATVITPNLFEAGQLSGLgEIKTVEQMKEAAKV 166
Cdd:COG0351   79 EIIEAVAEILADYPLVPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGI-EITTLDDMREAAKA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 167 IHGLGAEHVLITGGGkLNHEKAVDVLFDGRDAEVIEGERIETPYTHGAGCTYSAAITAELAKGSNVKEAIYSAKTFITEA 246
Cdd:COG0351  158 LLELGAKAVLVKGGH-LPGDEAVDVLYDGDGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQA 236

                        250
                 ....*....|....*...
gi 521289071 247 IRESFRLNQYVGPTKHSA 264
Cdd:COG0351  237 IRAALRLGMGHGPVNHFA 254
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 13-260 6.71e-116

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: 332.52  E-value: 6.71e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071   13 DSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPenNWNHQVFPVDTEVIRAQLSTIVDGIGVDAMKTGMLPTVDIIELA 92
Cdd:pfam08543   1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNT--LGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLGSAEIIEAV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071   93 ADTIKKHSMkNVVIDPVMVCKGANEVLYPEHAKALRELLAPLATVITPNLFEAGQLSGLgEIKTVEQMKEAAKVIHGLGA 172
Cdd:pfam08543  79 AEKLDKYGV-PVVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGR-KIKTLEDMKEAAKKLLALGA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  173 EHVLITGGgKLNHEKAV--DVLFDGRDAEVIEGERIETPYTHGAGCTYSAAITAELAKGSNVKEAIYSAKTFITEAIRES 250
Cdd:pfam08543 157 KAVLIKGG-HLEGEEAVvtDVLYDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVTEAIRDA 235

                         250
                  ....*....|
gi 521289071  251 FRLNQYVGPT 260
Cdd:pfam08543 236 LNLGKGHGPV 245
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 5-250 2.47e-115

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: 331.00  E-value: 2.47e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071   5 KALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPenNWNHQVFPVDTEVIRAQLSTIVDGIGVDAMKTGMLP 84
Cdd:cd01169    1 VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNT--LGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  85 TVDIIELAADTIKKHSMKNVVIDPVMVCKGANEVLYPEHAKALRELLAPLATVITPNLFEAGQLSGLgEIKTVEQMKEAA 164
Cdd:cd01169   79 SAEIIEAVAEALKDYPDIPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTGL-EIATEEDMMKAA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 165 KVIHGLGAEHVLITGGGkLNHEKAVDVLFDGRDAEVIEGERIETPYTHGAGCTYSAAITAELAKGSNVKEAIYSAKTFIT 244
Cdd:cd01169  158 KALLALGAKAVLIKGGH-LPGDEAVDVLYDGGGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVT 236


                 ....*.
gi 521289071 245 EAIRES 250
Cdd:cd01169  237 QAIRNA 242
HMP-P_kinase TIGR00097
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ...
 6-262 1.71e-94

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: 278.41  E-value: 1.71e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071    6 ALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAmdpENNWN-HQVFPVDTEVIRAQLSTIVDGIGVDAMKTGMLP 84
Cdd:TIGR00097   1 ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTA---QNTRGvTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071   85 TVDIIELAADTIKKHSMKNVVIDPVMVCKGANEVLYPEHAKALRELLAPLATVITPNLFEAGQLSGLgEIKTVEQMKEAA 164
Cdd:TIGR00097  78 SAEIVEAVARKLREYPVRPLVVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGT-KIRTEQDMIKAA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  165 KVIHGLGAEHVLITgGGKLNHEKAVDVLFDGRDAEVIEGERIETPYTHGAGCTYSAAITAELAKGSNVKEAIYSAKTFIT 244
Cdd:TIGR00097 157 KKLRELGPKAVLIK-GGHLEGDQAVDVLFDGGEIHILKAPRIETKNTHGTGCTLSAAIAANLAKGLSLKEAVKEAKEFVT 235

                         250
                  ....*....|....*...
gi 521289071  245 EAIRESFRLNQYVGPTKH 262
Cdd:TIGR00097 236 GAIRYGLNIGHGHGPLNH 253
 
Name Accession Description Interval E-value
PRK12616 PRK12616
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
1-270 0e+00

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183624  Cd Length: 270  Bit Score: 534.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071   1 MTMHKALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPENNWNHQVFPVDTEVIRAQLSTIVDGIGVDAMKT 80
Cdd:PRK12616   1 MSMHKALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPENSWDHQVFPIDTDTIRAQLSTIVDGIGVDAMKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  81 GMLPTVDIIELAADTIKKHSMKNVVIDPVMVCKGANEVLYPEHAKALRELLAPLATVITPNLFEAGQLSGLGEIKTVEQM 160
Cdd:PRK12616  81 GMLPTVDIIELAADTIKEKQLKNVVIDPVMVCKGANEVLYPEHAEALREQLAPLATVITPNLFEAGQLSGMGEIKTVEQM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 161 KEAAKVIHGLGAEHVLITGGGKLNHEKAVDVLFDGRDAEVIEGERIETPYTHGAGCTYSAAITAELAKGSNVKEAIYSAK 240
Cdd:PRK12616 161 KEAAKKIHELGAQYVVITGGGKLKHEKAVDVLYDGETAEVLESEMIDTPYTHGAGCTFSAAVTAELAKGSEVKEAIYAAK 240

                        250       260       270
                 ....*....|....*....|....*....|
gi 521289071 241 TFITEAIRESFRLNQYVGPTKHSALRLSGK 270
Cdd:PRK12616 241 EFITAAIKESFPLNQYVGPTKHSALRLSGK 270
PRK12412 PRK12412
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
3-266 1.29e-148

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183512 [Multi-domain]  Cd Length: 268  Bit Score: 416.29  E-value: 1.29e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071   3 MHKALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPENNWNHQVFPVDTEVIRAQLSTIVDGIGVDAMKTGM 82
Cdd:PRK12412   1 LNKALTIAGSDTSGGAGIQADLKTFQELGVYGMTSLTTIVTMDPHNGWAHNVFPIPASTLKPQLETTIEGVGVDALKTGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  83 LPTVDIIELAADTIKKHSMKNVVIDPVMVCKGANEVLYPEHAKALRELLAPLATVITPNLFEAGQLSGLgEIKTVEQMKE 162
Cdd:PRK12412  81 LGSVEIIEMVAETIEKHNFKNVVVDPVMVCKGADEALHPETNDCLRDVLVPKALVVTPNLFEAYQLSGV-KINSLEDMKE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 163 AAKVIHGLGAEHVLITGGGKLNHEKAVDVLFDGRDAEVIEGERIETPYTHGAGCTYSAAITAELAKGSNVKEAIYSAKTF 242
Cdd:PRK12412 160 AAKKIHALGAKYVLIKGGSKLGTETAIDVLYDGETFDLLESEKIDTTNTHGAGCTYSAAITAELAKGKPVKEAVKTAKEF 239

                        250       260
                 ....*....|....*....|....
gi 521289071 243 ITEAIRESFRLNQYVGPTKHSALR 266
Cdd:PRK12412 240 ITAAIRYSFKINEYVGPTHHGAYR 263
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 7-264 8.32e-122

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: 347.80  E-value: 8.32e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071   7 LTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPENNwnHQVFPVDTEVIRAQLSTIVDGIGVDAMKTGMLPTV 86
Cdd:COG0351    1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGV--TGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  87 DIIELAADTIKKHSMKNVVIDPVMVCKGANEVLYPEHAKALRELLAPLATVITPNLFEAGQLSGLgEIKTVEQMKEAAKV 166
Cdd:COG0351   79 EIIEAVAEILADYPLVPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGI-EITTLDDMREAAKA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 167 IHGLGAEHVLITGGGkLNHEKAVDVLFDGRDAEVIEGERIETPYTHGAGCTYSAAITAELAKGSNVKEAIYSAKTFITEA 246
Cdd:COG0351  158 LLELGAKAVLVKGGH-LPGDEAVDVLYDGDGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQA 236

                        250
                 ....*....|....*...
gi 521289071 247 IRESFRLNQYVGPTKHSA 264
Cdd:COG0351  237 IRAALRLGMGHGPVNHFA 254
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 1-262 1.07e-118

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 340.18  E-value: 1.07e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071   1 MTMHKALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPENNwnHQVFPVDTEVIRAQLSTIVDGIGVDAMKT 80
Cdd:PRK06427   2 MKRPIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGV--QRVHPIPPEFVAAQLDAVFSDIRIDAVKI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  81 GMLPTVDIIELAADTIKKHSMKNVVIDPVMVCKGANEVLYPEHAKALRELLAPLATVITPNLFEAGQLSGLGEIKTVEQM 160
Cdd:PRK06427  80 GMLASAEIIETVAEALKRYPIPPVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTGLPIADTEDEM 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 161 KEAAKVIHGLGAEHVLITGGGKLNHEKAVDVLFDGRDAEVIEGERIETPYTHGAGCTYSAAITAELAKGSNVKEAIYSAK 240
Cdd:PRK06427 160 KAAARALHALGCKAVLIKGGHLLDGEESVDWLFDGEGEERFSAPRIPTKNTHGTGCTLSAAIAAELAKGASLLDAVQTAK 239

                        250       260
                 ....*....|....*....|..
gi 521289071 241 TFITEAIRESFRLNQYVGPTKH 262
Cdd:PRK06427 240 DYVTRAIRHALEIGQGHGPVNH 261
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 13-260 6.71e-116

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: 332.52  E-value: 6.71e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071   13 DSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPenNWNHQVFPVDTEVIRAQLSTIVDGIGVDAMKTGMLPTVDIIELA 92
Cdd:pfam08543   1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNT--LGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLGSAEIIEAV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071   93 ADTIKKHSMkNVVIDPVMVCKGANEVLYPEHAKALRELLAPLATVITPNLFEAGQLSGLgEIKTVEQMKEAAKVIHGLGA 172
Cdd:pfam08543  79 AEKLDKYGV-PVVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGR-KIKTLEDMKEAAKKLLALGA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  173 EHVLITGGgKLNHEKAV--DVLFDGRDAEVIEGERIETPYTHGAGCTYSAAITAELAKGSNVKEAIYSAKTFITEAIRES 250
Cdd:pfam08543 157 KAVLIKGG-HLEGEEAVvtDVLYDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVTEAIRDA 235

                         250
                  ....*....|
gi 521289071  251 FRLNQYVGPT 260
Cdd:pfam08543 236 LNLGKGHGPV 245
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 5-250 2.47e-115

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: 331.00  E-value: 2.47e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071   5 KALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPenNWNHQVFPVDTEVIRAQLSTIVDGIGVDAMKTGMLP 84
Cdd:cd01169    1 VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNT--LGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  85 TVDIIELAADTIKKHSMKNVVIDPVMVCKGANEVLYPEHAKALRELLAPLATVITPNLFEAGQLSGLgEIKTVEQMKEAA 164
Cdd:cd01169   79 SAEIIEAVAEALKDYPDIPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTGL-EIATEEDMMKAA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 165 KVIHGLGAEHVLITGGGkLNHEKAVDVLFDGRDAEVIEGERIETPYTHGAGCTYSAAITAELAKGSNVKEAIYSAKTFIT 244
Cdd:cd01169  158 KALLALGAKAVLIKGGH-LPGDEAVDVLYDGGGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVT 236


                 ....*.
gi 521289071 245 EAIRES 250
Cdd:cd01169  237 QAIRNA 242
HMP-P_kinase TIGR00097
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ...
 6-262 1.71e-94

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: 278.41  E-value: 1.71e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071    6 ALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAmdpENNWN-HQVFPVDTEVIRAQLSTIVDGIGVDAMKTGMLP 84
Cdd:TIGR00097   1 ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTA---QNTRGvTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071   85 TVDIIELAADTIKKHSMKNVVIDPVMVCKGANEVLYPEHAKALRELLAPLATVITPNLFEAGQLSGLgEIKTVEQMKEAA 164
Cdd:TIGR00097  78 SAEIVEAVARKLREYPVRPLVVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGT-KIRTEQDMIKAA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  165 KVIHGLGAEHVLITgGGKLNHEKAVDVLFDGRDAEVIEGERIETPYTHGAGCTYSAAITAELAKGSNVKEAIYSAKTFIT 244
Cdd:TIGR00097 157 KKLRELGPKAVLIK-GGHLEGDQAVDVLFDGGEIHILKAPRIETKNTHGTGCTLSAAIAANLAKGLSLKEAVKEAKEFVT 235

                         250
                  ....*....|....*...
gi 521289071  245 EAIRESFRLNQYVGPTKH 262
Cdd:TIGR00097 236 GAIRYGLNIGHGHGPLNH 253
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 1-262 8.76e-78

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 243.91  E-value: 8.76e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071   1 MTMHKALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAmdpENNWN-HQVFPVDTEVIRAQLSTIVDGIGVDAMK 79
Cdd:PLN02898   7 MKVPHVLTVAGSDSGAGAGIQADIKACAARGVYCTTAITAVTA---QNTVGvQGVHAVPLDFVAEQLKSVLSDMPVDVVK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  80 TGMLPTVDIIELAADTIKKHSMKNVVIDPVMVCKGANEVLYPEHAKALRELLAPLATVITPNLFEAGQLSGLGEIKTVEQ 159
Cdd:PLN02898  84 TGMLPSAEIVKVLCQALKEFPVKALVVDPVMVSTSGDVLAGPSILSALREELLPLATIVTPNVKEASALLGGDPLETVAD 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 160 MKEAAKVIHGLGAEHVLITGGGKLNHEKAVDVLFDGRDAEVIEGERIETPYTHGAGCTYSAAITAELAKGSNVKEAIYSA 239
Cdd:PLN02898 164 MRSAAKELHKLGPRYVLVKGGHLPDSLDAVDVLYDGTEFHELRSSRIKTRNTHGTGCTLASCIAAELAKGSDMLSAVKVA 243

                        250       260
                 ....*....|....*....|....*.
gi 521289071 240 KTFITEAIRESFRL---NQYVGPTKH 262
Cdd:PLN02898 244 KRYVETALEYSKDIgigNGAQGPFNH 269
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
1-256 2.94e-74

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 226.87  E-value: 2.94e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071   1 MTMHKALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDpENNWnhQVFPVDTEVIRAQLSTIVDgIGVDAMKT 80
Cdd:PRK12413   1 MKTNYILAISGNDIFSGGGLHADLATYTRNGLHGFVAVTCLTAMT-EKGF--EVFPVDKEIFQQQLDSLKD-VPFSAIKI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  81 GMLPTVDIIELAADTIKKHSMKNVVIDPVMVCKGANEVLYPEHAKALRELLaPLATVITPNLFEAGQLSGLgEIKTVEQM 160
Cdd:PRK12413  77 GLLPNVEIAEQALDFIKGHPGIPVVLDPVLVCKETHDVEVSELRQELIQFF-PYVTVITPNLVEAELLSGK-EIKTLEDM 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 161 KEAAKVIHGLGAEHVLITGGGKLNHEKAVDVLFDGRDAEVIEGERIETPYThGAGCTYSAAITAELAKGSNVKEAIYSAK 240
Cdd:PRK12413 155 KEAAKKLYDLGAKAVVIKGGNRLSQKKAIDLFYDGKEFVILESPVLEKNNI-GAGCTFASSIASQLVKGKSPLEAVKNSK 233

                        250
                 ....*....|....*.
gi 521289071 241 TFITEAIRESfrlNQY 256
Cdd:PRK12413 234 DFVYQAIQQS---DQY 246
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
5-248 4.61e-74

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 232.70  E-value: 4.61e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071   5 KALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAmdpENNWN-HQVFPVDTEVIRAQLSTIVDGIGVDAMKTGML 83
Cdd:PRK08573   4 VALTIAGSDSGGGAGIEADLKTFAALGVHGAVAITSVTA---QNTYEvRAIHDLPPEVVAAQIEAVWEDMGIDAAKTGML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  84 PTVDIIELAADTIKKHSMKnVVIDPVMVCKGANEVLYPEHAKALRELLAPLATVITPNLFEAGQLSGLgEIKTVEQMKEA 163
Cdd:PRK08573  81 SNREIIEAVAKTVSKYGFP-LVVDPVMIAKSGAPLLREDAVDALIKRLLPLATVVTPNRPEAEKLTGM-KIRSVEDARKA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 164 AKVIH-GLGAEhVLITGGGKLNHEKAVDVLFDGRDAEVIEGERIETPYTHGAGCTYSAAITAELAKGSNVKEAIYSAKTF 242
Cdd:PRK08573 159 AKYIVeELGAE-AVVVKGGHLEGEEAVDVLYHNGTFREFRAPRVESGCTHGTGCSFSAAIAAGLAKGLDPEEAIKTAKKF 237


                 ....*.
gi 521289071 243 ITEAIR 248
Cdd:PRK08573 238 ITMAIK 243
PTZ00347 PTZ00347
phosphomethylpyrimidine kinase; Provisional
 1-264 3.11e-57

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240375 [Multi-domain]  Cd Length: 504  Bit Score: 190.56  E-value: 3.11e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071   1 MTMHKALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPENnwNHQVFPVDTEVIRAQLSTIVDGIGVDAMKT 80
Cdd:PTZ00347 228 MKIPTVLTVSGSDSGGGAGHQADLKTLEALGVYSTSALTSLTAQNTKG--VQQIQVVNEDFFAAQIDSVMSDFNISVVKL 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  81 GMLPTVDIIELAADTIKKHSMknvVIDPVMVCKGANEVLYPEHAKAL----RELLAPLATVITPNLFEAGQLSGLGEIKT 156
Cdd:PTZ00347 306 GLVPTARQLEIVIEKLKNLPM---VVDPVLVATSGDDLVAQKNADDVlamyKERIFPMATIITPNIPEAERILGRKEITG 382

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 157 VEQMKEAAKVIHGLGAEHVLITGGGKL-NHEKAVDVLFDGRDAEVIE--GERIETPYTHGAGCTYSAAITAELAKGSNVK 233
Cdd:PTZ00347 383 VYEARAAAQALAQYGSRYVLVKGGHDLiDPEACRDVLYDREKDRFYEftANRIATINTHGTGCTLASAISSFLARGYTVP 462

                        250       260       270
                 ....*....|....*....|....*....|....
gi 521289071 234 EAIYSAKTFITEAIRESFR--LNQYV-GPTKHSA 264
Cdd:PTZ00347 463 DAVERAIGYVHEAIVRSCGvpLGQGTnRPLVHSL 496
PRK14713 PRK14713
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
7-264 5.28e-52

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 237797 [Multi-domain]  Cd Length: 530  Bit Score: 177.29  E-value: 5.28e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071   7 LTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPENNwnHQVFPVDTEVIRAQLSTIVDGIGVDAMKTGMLPTV 86
Cdd:PRK14713  33 LSIAGTDPSGGAGIQADLKSIAAAGGYGMAVITALVAQNTRGV--RAVHVPPADFLRAQLDAVSDDVTVDAVKIGMLGDA 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  87 DIIELAADTIKKHSMKNVVIDPVMVCKGANEVLYPEHAKALRELLaPLATVITPNLFEAGQLSGLGEIKTVEQMKEAAKV 166
Cdd:PRK14713 111 EVIDAVRTWLAEHRPPVVVLDPVMVATSGDRLLEEDAEAALRELV-PRADLITPNLPELAVLLGEPPATTWEEALAQARR 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 167 IHGLGAEHVLITgGGKLNHEKAVDVLF--DGRDAEViEGERIETPYTHGAGCTYSAAITAELAKGSNVKEAIYSAKTFIT 244
Cdd:PRK14713 190 LAAETGTTVLVK-GGHLDGQRAPDALVgpDGAVTEV-PGPRVDTRNTHGTGCSLSSALATRLGRGGDWAAALRWATAWLH 267

                        250       260
                 ....*....|....*....|..
gi 521289071 245 EAIRESFRLN--QYVGPTKHSA 264
Cdd:PRK14713 268 GAIAAGAALQvgTGNGPVDHFH 289
PRK09517 PRK09517
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ...
 5-265 2.74e-41

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


Pssm-ID: 169939 [Multi-domain]  Cd Length: 755  Bit Score: 150.89  E-value: 2.74e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071   5 KALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPENNWNHQVFPVDteVIRAQLSTIVDGIGVDAMKTGMLP 84
Cdd:PRK09517 243 RVLSIAGTDPTGGAGIQADLKSIAAGGGYGMCVVTALVAQNTHGVNTIHTPPLT--FLEEQLEAVFSDVTVDAVKLGMLG 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  85 TVDIIELAADTIKKHSMKNVVIDPVMVCKGANEVLYPEHAKALRElLAPLATVITPNLFEAGQLSGLGEIKTVEQMKEAA 164
Cdd:PRK09517 321 SADTVDLVASWLGSHEHGPVVLDPVMVATSGDRLLDADATEALRR-LAVHVDVVTPNIPELAVLCGEAPAITMDEAIAQA 399

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 165 KvihGLGAEH--VLITGGGKLNHEKAVD-VLFDGRDAEVIEGERIETPYTHGAGCTYSAAITAELAKGSNVKEAIYSAKT 241
Cdd:PRK09517 400 R---GFARTHgtIVIVKGGHLTGDLADNaVVRPDGSVHQVENPRVNTTNSHGTGCSLSAALATLIAAGESVEKALEWATR 476

                        250       260
                 ....*....|....*....|....*.
gi 521289071 242 FITEAIR--ESFRLNQYVGPTKHSAL 265
Cdd:PRK09517 477 WLNEALRhaDHLAVGSGNGPVDHGHL 502
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 32-256 4.59e-34

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: 124.10  E-value: 4.59e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  32 VYGMTALTVVV----AMdpennwNHQVFPVDTevirAQLST-------------------IVDGI-------GVDAMKTG 81
Cdd:COG2240   12 VYGHVGNSAAVpplsAL------GVEVWPLPT----VLLSNhtgygtftgrdlptddiadILDGWkelgvllEFDAVLSG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  82 MLPTVDIIELAADTIKKHSMKN----VVIDPVMvckGANEVLY---PEHAKALRELLAPLATVITPNLFEAGQLSGLgEI 154
Cdd:COG2240   82 YLGSAEQGDIIADFVARVKAANpdalYLCDPVM---GDNGKGYyvfPGIAEFIMRRLVPLADIITPNLTELALLTGR-PY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 155 KTVEQMKEAAKVIHGLGAEHVLITG---GGKLNHEKAVdVLFDGRDAEVIEGERIETPYtHGAGCTYSAAITAELAKGSN 231
Cdd:COG2240  158 ETLEEALAAARALLALGPKIVVVTSvplDDTPADKIGN-LAVTADGAWLVETPLLPFSP-NGTGDLFAALLLAHLLRGKS 235

                        250       260
                 ....*....|....*....|....*
gi 521289071 232 VKEAIYSAKTFITEAIRESFRLNQY 256
Cdd:COG2240  236 LEEALERAAAFVYEVLERTAAAGSD 260
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 65-252 1.93e-32

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: 119.61  E-value: 1.93e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  65 QLSTIVDGIG-------VDAMKTGMLPTVDIIELAADTIKKHSMKN----VVIDPVMvckGANEVLY---PEHAKALREL 130
Cdd:cd01173   56 ELEDLLEGLEalgllleYDAVLTGYLGSAEQVEAVAEIVKRLKEKNpnllYVCDPVM---GDNGKLYvvaEEIVPVYRDL 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 131 LAPLATVITPNLFEAGQLSGLgEIKTVEQMKEAAKVIHGLGAEHVLITGGGKLNHEKAVDVLFDGRDAEVIEGERIETP- 209
Cdd:cd01173  133 LVPLADIITPNQFELELLTGK-KINDLEDAKAAARALHAKGPKTVVVTSVELADDDRIEMLGSTATEAWLVQRPKIPFPa 211

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 521289071 210 YTHGAGCTYSAAITAELAKGSNVKEAIYSAKTFITEAIRESFR 252
Cdd:cd01173  212 YFNGTGDLFAALLLARLLKGKSLAEALEKALNFVHEVLEATYE 254
COG1992 COG1992
Predicted transcriptional regulator fused phosphomethylpyrimidine kinase (thiamin biosynthesis) ...
 15-264 1.88e-26

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


Pssm-ID: 441595 [Multi-domain]  Cd Length: 432  Bit Score: 106.76  E-value: 1.88e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  15 SGGAGIQADLKTFQEKNVYGMTALTVVVAMdpeNNWNHQVFPVDT-EVIRAQLSTIVDGIGVDAMKTGMLPTVDIIELAA 93
Cdd:COG1992    1 GGGGGGGADAKTAAALGAGGGGTTTAVTVT---ATTTVTGVGSDPpPPVEVQQQAVAADDDVDDAKTGMLMTATIVEVVA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  94 DTIKKHSMKNVVIDPVMVCKGANEvLYPEHAKALRELLAPLATVITPNLFEAGQLSGLgEIKTVEQMKEAAKVIHGLGAE 173
Cdd:COG1992   78 VVVKSRDKPLVVVVVPVAVAAAGL-GLLLAEAELAKLLLPLLATVTPNEPEVEELLLP-TIRSLLAEARAARLALQEEGA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 174 HVLITGGGKLNHEKAVDVLFDGRDAEVIEGERIETPYTHGAGCTYSAAITAELAKGSNVKEAIYSAKTFITEAIRESFRL 253
Cdd:COG1992  156 DALGVKGGHVSGDAVVDVLEDERDVETFRHPRLVTEATHGSGCTFSAAIAALLAKGLSLEEAVRGAKLFLLHAIRYGLLV 235

                        250
                 ....*....|.
gi 521289071 254 NQYVGPTKHSA 264
Cdd:COG1992  236 GKGVGPVNHLA 246
PTZ00493 PTZ00493
phosphomethylpyrimidine kinase; Provisional
 5-253 1.15e-21

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240440  Cd Length: 321  Bit Score: 91.98  E-value: 1.15e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071   5 KALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPENnwNHQVFPVDTEVIRAQLSTIVDGIGVDAMKTGMLP 84
Cdd:PTZ00493   6 NILSIAGSDSCGGAGMQADIKTAMGLGCHCCTALVVLTAQNTKE--VKRIVEIEEKFIVEQLDSIFADVTIDVVKLGVLY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  85 TVDIIELAADTIKKHSMKN-----VVIDPVMV-CKGANEVLYPEHAKALRELLAPLATVITPNLFEAGQ-LSGLG---EI 154
Cdd:PTZ00493  84 SKKIISLVHNYITNMNKKRgkkllVVFDPVFVsSSGCLLVENLEYIKFALDLICPISCIITPNFYECKViLEALDcqmDL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 155 KTVEQMKEAAKVIHGLGAEHVLITG------GGKLNHEKAVDVLFDGRDAEVIEGERI-----ETPY------------- 210
Cdd:PTZ00493 164 SKANMTELCKLVTEKLNINACLFKScnvgenSAEENEVYAVDHLCIRNVGSYPTGEKQqidagGVTYlydvyklrskrkp 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 521289071 211 ---THGAGCTYSAAITAELAKGSNVKEAIYSAKTFITEAIRESFRL 253
Cdd:PTZ00493 244 gkdIHGTGCTLSTAIACYLAKKHNILQSCIESKKYIYNCIRYAYPF 289
PRK07105 PRK07105
pyridoxamine kinase; Validated
 72-254 6.74e-19

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 83.81  E-value: 6.74e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  72 GIGVDAMKTGMLPTVDIIELAADTIKKHSMKN--VVIDPVMvckGANEVLY----PEHAKALRELLApLATVITPNLFEA 145
Cdd:PRK07105  73 NLKFDAIYSGYLGSPRQIQIVSDFIKYFKKKDllVVVDPVM---GDNGKLYqgfdQEMVEEMRKLIQ-KADVITPNLTEA 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 146 GQLSG---LGEIKTVEQMKEAAKVIHGLGAEHVLITGGGKLNHEKAVdVLFDGRDAEV--IEGERIETPYtHGAGCTYSA 220
Cdd:PRK07105 149 CLLLDkpyLEKSYSEEEIKQLLRKLADLGPKIVIITSVPFEDGKIGV-AYYDRATDRFwkVFCKYIPAHY-PGTGDIFTS 226

                        170       180       190
                 ....*....|....*....|....*....|....
gi 521289071 221 AITAELAKGSNVKEAIYSAKTFITEAIRESFRLN 254
Cdd:PRK07105 227 VITGSLLQGDSLPIALDRAVQFIEKGIRATLGLK 260
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
77-248 1.02e-17

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 80.47  E-value: 1.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  77 AMKTGMLPTVDIIELAADTIKK----HSMKNVVIDPVMVCKGANEVLYPEHAKALRELLAPLATVITPNLFEAGQLSGLg 152
Cdd:PRK08176  91 AVTTGYMGSASQIKILAEWLTAlradHPDLLIMVDPVIGDIDSGIYVKPDLPEAYRQHLLPLAQGLTPNIFELEILTGK- 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 153 EIKTVEQMKEAAKVIHGLGAEHVLITGG-GKLNHEKAVDVLFDGRDAEVIEGERIET-PYthGAGCTYSAAITAELAKGS 230
Cdd:PRK08176 170 PCRTLDSAIAAAKSLLSDTLKWVVITSAaGNEENQEMQVVVVTADSVNVISHPRVDTdLK--GTGDLFCAELVSGLLKGK 247

                        170
                 ....*....|....*...
gi 521289071 231 NVKEAIYSAKTFITEAIR 248
Cdd:PRK08176 248 ALTDAAHRAGLRVLEVMR 265
PRK05756 PRK05756
pyridoxal kinase PdxY;
50-256 3.02e-15

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 73.75  E-value: 3.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  50 WNHQVFPVDteviraQLSTIVDGIG-------VDAMKTGMLPTVDIIELAADTIKKHSMKN----VVIDPVM--VCKGan 116
Cdd:PRK05756  49 WTGCVMPPS------HLTEIVQGIAdigwlgeCDAVLSGYLGSAEQGEAILDAVRRVKAANpqalYFCDPVMgdPEKG-- 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 117 evLY--PEHAKALRELLAPLATVITPNLFEAGQLSGLgEIKTVEQMKEAAKVIHGLGAEHVLITgggKLNH-EKAVD--- 190
Cdd:PRK05756 121 --CIvaPGVAEFLRDRALPAADIITPNLFELEWLSGR-PVETLEDAVAAARALIARGPKIVLVT---SLARaGYPADrfe 194

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521289071 191 -VLFDGRDAEVIEGERIETPY-THGAGCTYSAAITAELAKGSNVKEAIYSAKTFITEAIRESFRLNQY 256
Cdd:PRK05756 195 mLLVTADGAWHISRPLVDFMRqPVGVGDLTSALFLARLLQGGSLEEALEHTTAAVYEVMARTKERGSY 262
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 51-251 7.05e-15

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 72.81  E-value: 7.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  51 NHQVFPVdtevIRAQ------LSTIVDGI-------GVDAMKTGMLPTVDIIELAADTIK--KHSMKNVVI--DPVMvck 113
Cdd:PTZ00344  45 NHTGYPV----IKGHrldlneLITLMDGLrannllsDYTYVLTGYINSADILREVLATVKeiKELRPKLIFlcDPVM--- 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 114 GANEVLY-PEHA-KALRELLaPLATVITPNLFEAGQLSGLgEIKTVEQMKEAAKVIHGLGAEHVLITGGGKLNHEKAVDV 191
Cdd:PTZ00344 118 GDDGKLYvKEEVvDAYRELI-PYADVITPNQFEASLLSGV-EVKDLSDALEAIDWFHEQGIPVVVITSFREDEDPTHLRF 195

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521289071 192 LFDGRDAEVIEGER-------IETPYThGAGCTYSAAITAELAKGSNvKEAIYSAKTFITEAIRESF 251
Cdd:PTZ00344 196 LLSCRDKDTKNNKRftgkvpyIEGRYT-GTGDLFAALLLAFSHQHPM-DLAVGKAMGVLQDIIKATR 260
PLN02978 PLN02978
pyridoxal kinase
 49-178 1.60e-13

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 69.00  E-value: 1.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  49 NWNHQVFPVDteviraQLSTIVDGIGVDAMK------TGMLPTVDIIELAADTIKK---HSMKNV-VIDPVMvckGANEV 118
Cdd:PLN02978  61 TFKGQVLDGE------QLWALIEGLEANGLLfythllTGYIGSVSFLRTVLRVVKKlrsVNPNLTyVCDPVL---GDEGK 131

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 521289071 119 LY--PEHAKALRELLAPLATVITPNLFEAGQLSGLgEIKTVEQMKEAAKVIHGLGAEHVLIT 178
Cdd:PLN02978 132 LYvpPELVPVYREKVVPLATMLTPNQFEAEQLTGI-RIVTEEDAREACAILHAAGPSKVVIT 192
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
 50-256 4.86e-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: 64.47  E-value: 4.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071   50 WNHQVFPVDteviraQLSTIVDGIG-------VDAMKTGMLPTVDIIELAADTIKKHSMKN----VVIDPVMVCKGANEV 118
Cdd:TIGR00687  49 WTGQVLPPD------ELHELVEGLEainklnqCDAVLSGYLGSAEQVAMVVGIVRQVKQANpqalYVCDPVMGDPWKGCY 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  119 LYPEHAKALRELLAPLATVITPNLFEAGQLSGLgEIKTVEQMKEAAKVIHGLGAEHVLITGGGKLNHEKavDVLFDGRDA 198
Cdd:TIGR00687 123 VAPDLLEVYREKAIPVADIITPNQFELELLTGR-RINTEEEALAAADALIAMGPDIVLVTHLIRAGSQR--DRSFEGLVA 199

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521289071  199 EVIEGERIETP------YTHGAGCTYSAAITAELAKGSNVKEAIYSAKTFITEAIRESFRLNQY 256
Cdd:TIGR00687 200 TQEGRWHISRPlavfdpPPVGTGDLIAALLLATLLHGNSLKEALEKTVSAVYHVLRTTIQLGKY 263
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 86-236 2.64e-10

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 59.66  E-value: 2.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071   86 VDIIELAADTIKKHS-MKNVVIDPVmvckganevlyPEHAKALRELLaPLATVITPNLFEAGQLSGLgEIKTVEQMKEAA 164
Cdd:pfam00294 143 EATLEELIEAAKNGGtFDPNLLDPL-----------GAAREALLELL-PLADLLKPNEEELEALTGA-KLDDIEEALAAL 209

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 521289071  165 KVIHGLGAEHVLITGGGKlnhekavDVLFDGRDAEV-IEGERIETPY-THGAGCTYSAAITAELAKGSNVKEAI 236
Cdd:pfam00294 210 HKLLAKGIKTVIVTLGAD-------GALVVEGDGEVhVPAVPKVKVVdTTGAGDSFVGGFLAGLLAGKSLEEAL 276
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
 125-236 6.35e-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: 58.31  E-value: 6.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 125 KALRELLAPLATVITPNLFEAGQLSGLgEIKTVEQMKEAAKVIHGLGAEHVLITGGGKlnhekaVDVLFDGRDAEVIEGE 204
Cdd:cd01164  168 EALLAALAAKPFLIKPNREELEELFGR-PLGDEEDVIAAARKLIERGAENVLVSLGAD------GALLVTKDGVYRASPP 240

                         90       100       110
                 ....*....|....*....|....*....|..
gi 521289071 205 RIETPYTHGAGCTYSAAITAELAKGSNVKEAI 236
Cdd:cd01164  241 KVKVVSTVGAGDSMVAGFVAGLAQGLSLEEAL 272
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 73-227 2.24e-09

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: 55.95  E-value: 2.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  73 IGVDAMKTGML-PTVDIIELAADTIKKHSMKnVVIDPVMVckganevLYPEHAKALRELLaPLATVITPNLFEAGQLSGl 151
Cdd:cd00287   56 VGADAVVISGLsPAPEAVLDALEEARRRGVP-VVLDPGPR-------AVRLDGEELEKLL-PGVDILTPNEEEAEALTG- 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 521289071 152 GEIKTVEQMKEAAKVIHGLGAEHVLITGGGKlnhekaVDVLFDGRDAEVIEGERIETPY-THGAGCTYSAAITAELA 227
Cdd:cd00287  126 RRDLEVKEAAEAAALLLSKGPKVVIVTLGEK------GAIVATRGGTEVHVPAFPVKVVdTTGAGDAFLAALAAGLA 196
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 124-236 2.82e-09

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


Pssm-ID: 238579 [Multi-domain]  Cd Length: 292  Bit Score: 56.40  E-value: 2.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 124 AKALRELLAPLATVITPNLFEAGQLSGLgEIKTVEQMKEAAKVIHGLGAEHVLITGGgklnhEKAVdVLFDGRDAEVIEG 203
Cdd:cd01174  165 ARPLPAELLALVDILVPNETEAALLTGI-EVTDEEDAEKAARLLLAKGVKNVIVTLG-----AKGA-LLASGGEVEHVPA 237

                         90       100       110
                 ....*....|....*....|....*....|...
gi 521289071 204 ERIETPYTHGAGCTYSAAITAELAKGSNVKEAI 236
Cdd:cd01174  238 FKVKAVDTTGAGDTFIGALAAALARGLSLEEAI 270
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
125-236 2.94e-09

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 56.68  E-value: 2.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 125 KALRELLAPLATVITPNLFEAGQLSGLgEIKTVEQMKEAAKVIHGLGAEHVLITGGGklnhEKAvdVLFDGRDAEVIEGE 204
Cdd:COG1105  168 EALKAALEAGPDLIKPNLEELEELLGR-PLETLEDIIAAARELLERGAENVVVSLGA----DGA--LLVTEDGVYRAKPP 240

                         90       100       110
                 ....*....|....*....|....*....|..
gi 521289071 205 RIETPYTHGAGCTYSAAITAELAKGSNVKEAI 236
Cdd:COG1105  241 KVEVVSTVGAGDSMVAGFLAGLARGLDLEEAL 272
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 84-236 3.18e-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: 56.43  E-value: 3.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  84 PTVDIIELAADTIKKHSMKnVVIDPvmvckGANEVLYPEHAKALRELLaPLATVITPNLFEAGQLSGLGEIktveqmKEA 163
Cdd:COG0524  142 PPREALLAALEAARAAGVP-VSLDP-----NYRPALWEPARELLRELL-ALVDILFPNEEEAELLTGETDP------EEA 208

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521289071 164 AKVIHGLGAEHVLITGGgklnhEKAVdVLFDGRDAEVIEGERIETPYTHGAGCTYSAAITAELAKGSNVKEAI 236
Cdd:COG0524  209 AAALLARGVKLVVVTLG-----AEGA-LLYTGGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEAL 275
PRK11142 PRK11142
ribokinase; Provisional
 89-236 9.91e-08

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 52.18  E-value: 9.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  89 IELAADTIKKHsmknvvidpvmvckGANEVLYPEHAKAL-RELLApLATVITPNLFEAGQLSGLgEIKTVEQMKEAAKVI 167
Cdd:PRK11142 147 VLAAAKIAKQH--------------GTKVILNPAPARELpDELLA-LVDIITPNETEAEKLTGI-RVEDDDDAAKAAQVL 210

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 521289071 168 HGLGAEHVLITGGgklnhEKAVDVLFDGRdAEVIEGERIETPYTHGAGCTYSAAITAELAKGSNVKEAI 236
Cdd:PRK11142 211 HQKGIETVLITLG-----SRGVWLSENGE-GQRVPGFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAI 273
RfaE COG2870
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ...
 135-237 1.28e-06

ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442117 [Multi-domain]  Cd Length: 321  Bit Score: 48.65  E-value: 1.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 135 ATVITPNLFEAGQLSGLgEIKTVEQMKEAA-KVIHGLGAEHVLITGGgklnhEKAVdVLFDGRDAEVIEGERIETPY--T 211
Cdd:COG2870  199 ATLLTPNLKEAEAAVGI-PIADEEELVAAAaELLERLGLEALLVTRG-----EEGM-TLFDADGPPHHLPAQAREVFdvT 271

                         90       100
                 ....*....|....*....|....*.
gi 521289071 212 hGAGCTYSAAITAELAKGSNVKEAIY 237
Cdd:COG2870  272 -GAGDTVIATLALALAAGASLEEAAE 296
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 59-236 3.11e-06

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: 47.31  E-value: 3.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  59 TEVIRAQLSTIVDG-IGVDAMKTgmlptvdIIELAADTIKKhsmknVVIDPVMVCKganevlypehAKALRELLAPLATv 137
Cdd:cd01941  123 REALKEAKPIVVDAnLPEEALEY-------LLALAAKHGVP-----VAFEPTSAPK----------LKKLFYLLHAIDL- 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 138 ITPNLFEAGQLSGLGeIKTVEQMKEAAKVIHGLGAEHVLITGGGKlnhekavDVLFDGRDAEVIegERIETPYT------ 211
Cdd:cd01941  180 LTPNRAELEALAGAL-IENNEDENKAAKILLLPGIKNVIVTLGAK-------GVLLSSREGGVE--TKLFPAPQpetvvn 249

                        170       180
                 ....*....|....*....|....*.
gi 521289071 212 -HGAGCTYSAAITAELAKGSNVKEAI 236
Cdd:cd01941  250 vTGAGDAFVAGLVAGLLEGMSLDDSL 275
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
 51-237 6.16e-05

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: 43.70  E-value: 6.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071  51 NHQVFPVDTE---------------VIRAQLSTiVDG-IGVDAMKtGMLpTVDIIELAADTIKKHSmKNVVIDPvmvcKG 114
Cdd:cd01172  102 NQQLLRVDREddsplsaeeeqrlieRIAERLPE-ADVvILSDYGK-GVL-TPRVIEALIAAARELG-IPVLVDP----KG 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 115 ANEVLYPEhakalrellaplATVITPNLFEAGQLSGLgEIKTVEQMKEAA-KVIHGLGAEHVLITGGgklnhEKAVdVLF 193
Cdd:cd01172  174 RDYSKYRG------------ATLLTPNEKEAREALGD-EINDDDELEAAGeKLLELLNLEALLVTLG-----EEGM-TLF 234

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 521289071 194 DGrdaeviEGERIETPYTH-------GAGCTYSAAITAELAKGSNVKEAIY 237
Cdd:cd01172  235 ER------DGEVQHIPALAkevydvtGAGDTVIATLALALAAGADLEEAAF 279
PTZ00292 PTZ00292
ribokinase; Provisional
 133-239 3.76e-03

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 38.18  E-value: 3.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521289071 133 PLATVITPNLFEAGQLSGlGEIKTVEQMKEAAKVIHGLGAEHVLITGGGklnheKAVDVLFDGRDAEVIEGERIETPYTH 212
Cdd:PTZ00292 197 KYVSLFCVNEVEAALITG-MEVTDTESAFKASKELQQLGVENVIITLGA-----NGCLIVEKENEPVHVPGKRVKAVDTT 270

                         90       100
                 ....*....|....*....|....*..
gi 521289071 213 GAGCTYSAAITAELAKGSNVKEAIYSA 239
Cdd:PTZ00292 271 GAGDCFVGSMAYFMSRGKDLKESCKRA 297
 
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