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Conserved domains on  [gi|489753028|ref|WP_003657026|]
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MULTISPECIES: hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Moraxella]

Protein Classification

hydroxymethylpyrimidine/phosphomethylpyrimidine kinase( domain architecture ID 10100230)

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

CATH:  3.40.1190.20
EC:  2.7.1.49|2.7.4.7
Gene Ontology:  GO:0005524|GO:0008902|GO:0008972|GO:0009228|GO:0009229
PubMed:  8382990
SCOP:  4000759

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 9-248 4.17e-85

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: 253.97  E-value: 4.17e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028   9 TVLCFSGLDPSGGAGIQADIESIGASGAHAAIACTALTIQNSQKVFGFEPVCHQLLKAQAQAVLDDLPVRAIKSGMMGTL 88
Cdd:cd01169    1 VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLGSA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  89 ENIIALTELFETCtiKHIPYVLDPVLVANSGGILGDVKTLAQAFSRLLPYATLITPNTHEIRALSGQQ-----DLHDAAK 163
Cdd:cd01169   81 EIIEAVAEALKDY--PDIPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTGLEiateeDMMKAAK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028 164 ALNDQGANAVLVKTSHdFNTGDIEQFLYINGRIHHTSIVPRLTGEFHGSGCSLASHIAGRLAMGDDIIDAITAADAWIHQ 243
Cdd:cd01169  159 ALLALGAKAVLIKGGH-LPGDEAVDVLYDGGGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQ 237


                 ....*
gi 489753028 244 TLIHA 248
Cdd:cd01169  238 AIRNA 242
 
Name Accession Description Interval E-value
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 9-248 4.17e-85

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: 253.97  E-value: 4.17e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028   9 TVLCFSGLDPSGGAGIQADIESIGASGAHAAIACTALTIQNSQKVFGFEPVCHQLLKAQAQAVLDDLPVRAIKSGMMGTL 88
Cdd:cd01169    1 VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLGSA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  89 ENIIALTELFETCtiKHIPYVLDPVLVANSGGILGDVKTLAQAFSRLLPYATLITPNTHEIRALSGQQ-----DLHDAAK 163
Cdd:cd01169   81 EIIEAVAEALKDY--PDIPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTGLEiateeDMMKAAK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028 164 ALNDQGANAVLVKTSHdFNTGDIEQFLYINGRIHHTSIVPRLTGEFHGSGCSLASHIAGRLAMGDDIIDAITAADAWIHQ 243
Cdd:cd01169  159 ALLALGAKAVLIKGGH-LPGDEAVDVLYDGGGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQ 237


                 ....*
gi 489753028 244 TLIHA 248
Cdd:cd01169  238 AIRNA 242
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 11-248 4.74e-80

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: 241.48  E-value: 4.74e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  11 LCFSGLDPSGGAGIQADIESIGASGAHAAIACTALTIQNSQKVFGFEPVCHQLLKAQAQAVLDDLPVRAIKSGMMGTLEN 90
Cdd:COG0351    1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSAEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  91 IIALTELFEtcTIKHIPYVLDPVLVANSGGILGDVKTLAQAFSRLLPYATLITPNTHEIRALSGQ-----QDLHDAAKAL 165
Cdd:COG0351   81 IEAVAEILA--DYPLVPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGIeittlDDMREAAKAL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028 166 NDQGANAVLVKTSHdFNTGDIEQFLYINGRIHHTSiVPRL-TGEFHGSGCSLASHIAGRLAMGDDIIDAITAADAWIHQT 244
Cdd:COG0351  159 LELGAKAVLVKGGH-LPGDEAVDVLYDGDGVREFS-APRIdTGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQA 236


                 ....
gi 489753028 245 LIHA 248
Cdd:COG0351  237 IRAA 240
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 17-251 2.18e-73

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: 224.28  E-value: 2.18e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028   17 DPSGGAGIQADIESIGASGAHAAIACTALTIQNSQKVFGFEPVCHQLLKAQAQAVLDDLPVRAIKSGMMGTLENIIALTE 96
Cdd:pfam08543   1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLGSAEIIEAVAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028   97 LFETCtikHIPYVLDPVLVANSGGILGDVKTLAQAFSRLLPYATLITPNTHEIRALSGQ-----QDLHDAAKALNDQGAN 171
Cdd:pfam08543  81 KLDKY---GVPVVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRkiktlEDMKEAAKKLLALGAK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  172 AVLVKTSH-DFNTGDIEQFLYINGRIHHTSiVPRL-TGEFHGSGCSLASHIAGRLAMGDDIIDAITAADAWIHQTLIHAD 249
Cdd:pfam08543 158 AVLIKGGHlEGEEAVVTDVLYDGGGFYTLE-APRIpTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVTEAIRDAL 236


                  ..
gi 489753028  250 KP 251
Cdd:pfam08543 237 NL 238
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 5-248 3.98e-70

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 216.53  E-value: 3.98e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028   5 QMRPTVLCFSGLDPSGGAGIQADIESIGASGAHAAIACTALTIQNSQKVFGFEPVCHQLLKAQAQAVLDDLPVRAIKSGM 84
Cdd:PRK06427   2 MKRPIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  85 MGTLENIIALTELFETCTIKHIpyVLDPVLVANSGGILGDVKTLAQAFSRLLPYATLITPNTHEIRALSG------QQDL 158
Cdd:PRK06427  82 LASAEIIETVAEALKRYPIPPV--VLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTGlpiadtEDEM 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028 159 HDAAKALNDQGANAVLVKTSHDFNTGDIEQFLYiNGRIHHTSIVPRL-TGEFHGSGCSLASHIAGRLAMGDDIIDAITAA 237
Cdd:PRK06427 160 KAAARALHALGCKAVLIKGGHLLDGEESVDWLF-DGEGEERFSAPRIpTKNTHGTGCTLSAAIAAELAKGASLLDAVQTA 238

                        250
                 ....*....|.
gi 489753028 238 DAWIHQTLIHA 248
Cdd:PRK06427 239 KDYVTRAIRHA 249
HMP-P_kinase TIGR00097
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ...
 10-248 1.91e-54

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: 176.33  E-value: 1.91e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028   10 VLCFSGLDPSGGAGIQADIESIGASGAHAAIACTALTIQNSQKVFGFEPVCHQLLKAQAQAVLDDLPVRAIKSGMMGTLE 89
Cdd:TIGR00097   1 ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLASAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028   90 NIIALTELFETCTIKHIpyVLDPVLVANSGGILGDVKTLAQAFSRLLPYATLITPNTHEIRALSG-----QQDLHDAAKA 164
Cdd:TIGR00097  81 IVEAVARKLREYPVRPL--VVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGtkirtEQDMIKAAKK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  165 LNDQGANAVLVKTSH--DFNTGDIeqfLYINGRIHHTSiVPRL-TGEFHGSGCSLASHIAGRLAMGDDIIDAITAADAWI 241
Cdd:TIGR00097 159 LRELGPKAVLIKGGHleGDQAVDV---LFDGGEIHILK-APRIeTKNTHGTGCTLSAAIAANLAKGLSLKEAVKEAKEFV 234


                  ....*..
gi 489753028  242 HQTLIHA 248
Cdd:TIGR00097 235 TGAIRYG 241
 
Name Accession Description Interval E-value
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 9-248 4.17e-85

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: 253.97  E-value: 4.17e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028   9 TVLCFSGLDPSGGAGIQADIESIGASGAHAAIACTALTIQNSQKVFGFEPVCHQLLKAQAQAVLDDLPVRAIKSGMMGTL 88
Cdd:cd01169    1 VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLGSA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  89 ENIIALTELFETCtiKHIPYVLDPVLVANSGGILGDVKTLAQAFSRLLPYATLITPNTHEIRALSGQQ-----DLHDAAK 163
Cdd:cd01169   81 EIIEAVAEALKDY--PDIPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTGLEiateeDMMKAAK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028 164 ALNDQGANAVLVKTSHdFNTGDIEQFLYINGRIHHTSIVPRLTGEFHGSGCSLASHIAGRLAMGDDIIDAITAADAWIHQ 243
Cdd:cd01169  159 ALLALGAKAVLIKGGH-LPGDEAVDVLYDGGGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQ 237


                 ....*
gi 489753028 244 TLIHA 248
Cdd:cd01169  238 AIRNA 242
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 11-248 4.74e-80

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: 241.48  E-value: 4.74e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  11 LCFSGLDPSGGAGIQADIESIGASGAHAAIACTALTIQNSQKVFGFEPVCHQLLKAQAQAVLDDLPVRAIKSGMMGTLEN 90
Cdd:COG0351    1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSAEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  91 IIALTELFEtcTIKHIPYVLDPVLVANSGGILGDVKTLAQAFSRLLPYATLITPNTHEIRALSGQ-----QDLHDAAKAL 165
Cdd:COG0351   81 IEAVAEILA--DYPLVPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGIeittlDDMREAAKAL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028 166 NDQGANAVLVKTSHdFNTGDIEQFLYINGRIHHTSiVPRL-TGEFHGSGCSLASHIAGRLAMGDDIIDAITAADAWIHQT 244
Cdd:COG0351  159 LELGAKAVLVKGGH-LPGDEAVDVLYDGDGVREFS-APRIdTGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQA 236


                 ....
gi 489753028 245 LIHA 248
Cdd:COG0351  237 IRAA 240
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 17-251 2.18e-73

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: 224.28  E-value: 2.18e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028   17 DPSGGAGIQADIESIGASGAHAAIACTALTIQNSQKVFGFEPVCHQLLKAQAQAVLDDLPVRAIKSGMMGTLENIIALTE 96
Cdd:pfam08543   1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLGSAEIIEAVAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028   97 LFETCtikHIPYVLDPVLVANSGGILGDVKTLAQAFSRLLPYATLITPNTHEIRALSGQ-----QDLHDAAKALNDQGAN 171
Cdd:pfam08543  81 KLDKY---GVPVVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRkiktlEDMKEAAKKLLALGAK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  172 AVLVKTSH-DFNTGDIEQFLYINGRIHHTSiVPRL-TGEFHGSGCSLASHIAGRLAMGDDIIDAITAADAWIHQTLIHAD 249
Cdd:pfam08543 158 AVLIKGGHlEGEEAVVTDVLYDGGGFYTLE-APRIpTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVTEAIRDAL 236


                  ..
gi 489753028  250 KP 251
Cdd:pfam08543 237 NL 238
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 5-248 3.98e-70

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 216.53  E-value: 3.98e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028   5 QMRPTVLCFSGLDPSGGAGIQADIESIGASGAHAAIACTALTIQNSQKVFGFEPVCHQLLKAQAQAVLDDLPVRAIKSGM 84
Cdd:PRK06427   2 MKRPIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  85 MGTLENIIALTELFETCTIKHIpyVLDPVLVANSGGILGDVKTLAQAFSRLLPYATLITPNTHEIRALSG------QQDL 158
Cdd:PRK06427  82 LASAEIIETVAEALKRYPIPPV--VLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTGlpiadtEDEM 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028 159 HDAAKALNDQGANAVLVKTSHDFNTGDIEQFLYiNGRIHHTSIVPRL-TGEFHGSGCSLASHIAGRLAMGDDIIDAITAA 237
Cdd:PRK06427 160 KAAARALHALGCKAVLIKGGHLLDGEESVDWLF-DGEGEERFSAPRIpTKNTHGTGCTLSAAIAAELAKGASLLDAVQTA 238

                        250
                 ....*....|.
gi 489753028 238 DAWIHQTLIHA 248
Cdd:PRK06427 239 KDYVTRAIRHA 249
HMP-P_kinase TIGR00097
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ...
 10-248 1.91e-54

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: 176.33  E-value: 1.91e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028   10 VLCFSGLDPSGGAGIQADIESIGASGAHAAIACTALTIQNSQKVFGFEPVCHQLLKAQAQAVLDDLPVRAIKSGMMGTLE 89
Cdd:TIGR00097   1 ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLASAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028   90 NIIALTELFETCTIKHIpyVLDPVLVANSGGILGDVKTLAQAFSRLLPYATLITPNTHEIRALSG-----QQDLHDAAKA 164
Cdd:TIGR00097  81 IVEAVARKLREYPVRPL--VVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGtkirtEQDMIKAAKK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  165 LNDQGANAVLVKTSH--DFNTGDIeqfLYINGRIHHTSiVPRL-TGEFHGSGCSLASHIAGRLAMGDDIIDAITAADAWI 241
Cdd:TIGR00097 159 LRELGPKAVLIKGGHleGDQAVDV---LFDGGEIHILK-APRIeTKNTHGTGCTLSAAIAANLAKGLSLKEAVKEAKEFV 234


                  ....*..
gi 489753028  242 HQTLIHA 248
Cdd:TIGR00097 235 TGAIRYG 241
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 7-247 5.06e-48

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 166.10  E-value: 5.06e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028   7 RPTVLCFSGLDPSGGAGIQADIESIGASGAHAAIACTALTIQNSQKVFGFEPVCHQLLKAQAQAVLDDLPVRAIKSGMMG 86
Cdd:PLN02898   9 VPHVLTVAGSDSGAGAGIQADIKACAARGVYCTTAITAVTAQNTVGVQGVHAVPLDFVAEQLKSVLSDMPVDVVKTGMLP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  87 TLENIIALTELFETCTIKHIpyVLDPVLVANSGGILGDVKTLAQAFSRLLPYATLITPNTHEIRALSGQ------QDLHD 160
Cdd:PLN02898  89 SAEIVKVLCQALKEFPVKAL--VVDPVMVSTSGDVLAGPSILSALREELLPLATIVTPNVKEASALLGGdpletvADMRS 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028 161 AAKALNDQGANAVLVKTSHDFNTGDIEQFLYiNGRIHHTSIVPRL-TGEFHGSGCSLASHIAGRLAMGDDIIDAITAADA 239
Cdd:PLN02898 167 AAKELHKLGPRYVLVKGGHLPDSLDAVDVLY-DGTEFHELRSSRIkTRNTHGTGCTLASCIAAELAKGSDMLSAVKVAKR 245


                 ....*...
gi 489753028 240 WIHQTLIH 247
Cdd:PLN02898 246 YVETALEY 253
PRK14713 PRK14713
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
6-250 1.75e-47

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 237797 [Multi-domain]  Cd Length: 530  Bit Score: 165.35  E-value: 1.75e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028   6 MRPTVLCFSGLDPSGGAGIQADIESIGASGAHAAIACTALTIQNSQKVFGFEPVCHQLLKAQAQAVLDDLPVRAIKSGMM 85
Cdd:PRK14713  28 ATPRVLSIAGTDPSGGAGIQADLKSIAAAGGYGMAVITALVAQNTRGVRAVHVPPADFLRAQLDAVSDDVTVDAVKIGML 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  86 GTLENIIALTELFEtctiKHIP--YVLDPVLVANSGGILGDvKTLAQAFSRLLPYATLITPNTHEIRALSG---QQDLHD 160
Cdd:PRK14713 108 GDAEVIDAVRTWLA----EHRPpvVVLDPVMVATSGDRLLE-EDAEAALRELVPRADLITPNLPELAVLLGeppATTWEE 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028 161 A---AKALNDQGANAVLVKTSHDFNTGDIEQFLYINGRIHHTSiVPRL-TGEFHGSGCSLASHIAGRLAMGDDIIDAITA 236
Cdd:PRK14713 183 AlaqARRLAAETGTTVLVKGGHLDGQRAPDALVGPDGAVTEVP-GPRVdTRNTHGTGCSLSSALATRLGRGGDWAAALRW 261

                        250
                 ....*....|....
gi 489753028 237 ADAWIHQTLIHADK 250
Cdd:PRK14713 262 ATAWLHGAIAAGAA 275
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
6-241 3.78e-46

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 159.89  E-value: 3.78e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028   6 MRPTVLCFSGLDPSGGAGIQADIESIGASGAHAAIACTALTIQNSQKVFGFEPVCHQLLKAQAQAVLDDLPVRAIKSGMM 85
Cdd:PRK08573   1 LIPVALTIAGSDSGGGAGIEADLKTFAALGVHGAVAITSVTAQNTYEVRAIHDLPPEVVAAQIEAVWEDMGIDAAKTGML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  86 GTLENIIALTElfetcTIKHI--PYVLDPVLVANSGGIL---GDVKTLAQafsRLLPYATLITPNTHEIRALSGQQ--DL 158
Cdd:PRK08573  81 SNREIIEAVAK-----TVSKYgfPLVVDPVMIAKSGAPLlreDAVDALIK---RLLPLATVVTPNRPEAEKLTGMKirSV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028 159 HDAAKA----LNDQGANAVLVKTSHdFNTGDIEQFLYINGRIHHTSiVPRLT-GEFHGSGCSLASHIAGRLAMGDDIIDA 233
Cdd:PRK08573 153 EDARKAakyiVEELGAEAVVVKGGH-LEGEEAVDVLYHNGTFREFR-APRVEsGCTHGTGCSFSAAIAAGLAKGLDPEEA 230


                 ....*...
gi 489753028 234 ITAADAWI 241
Cdd:PRK08573 231 IKTAKKFI 238
PTZ00347 PTZ00347
phosphomethylpyrimidine kinase; Provisional
 8-257 2.93e-39

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240375 [Multi-domain]  Cd Length: 504  Bit Score: 142.79  E-value: 2.93e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028   8 PTVLCFSGLDPSGGAGIQADIESIGASGAHAAIACTALTIQNSQKVFGFEPVCHQLLKAQAQAVLDDLPVRAIKSGMMGT 87
Cdd:PTZ00347 231 PTVLTVSGSDSGGGAGHQADLKTLEALGVYSTSALTSLTAQNTKGVQQIQVVNEDFFAAQIDSVMSDFNISVVKLGLVPT 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  88 LENIIALTElfetcTIKHIPYVLDPVLVANSGGILGDVKT----LAQAFSRLLPYATLITPNTHEIRALSGQQDL----- 158
Cdd:PTZ00347 311 ARQLEIVIE-----KLKNLPMVVDPVLVATSGDDLVAQKNaddvLAMYKERIFPMATIITPNIPEAERILGRKEItgvye 385

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028 159 -HDAAKALNDQGANAVLVKTSHDF-NTGDIEQFLYINGRIHHTSIVPRL--TGEFHGSGCSLASHIAGRLAMGDDIIDAI 234
Cdd:PTZ00347 386 aRAAAQALAQYGSRYVLVKGGHDLiDPEACRDVLYDREKDRFYEFTANRiaTINTHGTGCTLASAISSFLARGYTVPDAV 465

                        250       260
                 ....*....|....*....|...
gi 489753028 235 TAADAWIHQTLIHADKPHQSDNT 257
Cdd:PTZ00347 466 ERAIGYVHEAIVRSCGVPLGQGT 488
PRK09517 PRK09517
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ...
 8-249 8.92e-38

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


Pssm-ID: 169939 [Multi-domain]  Cd Length: 755  Bit Score: 140.49  E-value: 8.92e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028   8 PTVLCFSGLDPSGGAGIQADIESIGASGAHAAIACTALTIQNSQKVFGFEPVCHQLLKAQAQAVLDDLPVRAIKSGMMGT 87
Cdd:PRK09517 242 PRVLSIAGTDPTGGAGIQADLKSIAAGGGYGMCVVTALVAQNTHGVNTIHTPPLTFLEEQLEAVFSDVTVDAVKLGMLGS 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  88 LENIIALTELFEtcTIKHIPYVLDPVLVANSGGILGDVKTlAQAFSRLLPYATLITPNTHEIRALSGQQ--DLHDAAKA- 164
Cdd:PRK09517 322 ADTVDLVASWLG--SHEHGPVVLDPVMVATSGDRLLDADA-TEALRRLAVHVDVVTPNIPELAVLCGEApaITMDEAIAq 398

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028 165 ---LNDQGANAVLVKTSHdfNTGDI--EQFLYINGRIHHTSiVPRL-TGEFHGSGCSLASHIAGRLAMGDDIIDAITAAD 238
Cdd:PRK09517 399 argFARTHGTIVIVKGGH--LTGDLadNAVVRPDGSVHQVE-NPRVnTTNSHGTGCSLSAALATLIAAGESVEKALEWAT 475

                        250
                 ....*....|.
gi 489753028 239 AWIHQTLIHAD 249
Cdd:PRK09517 476 RWLNEALRHAD 486
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
10-250 2.18e-33

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 121.71  E-value: 2.18e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  10 VLCFSGLDPSGGAGIQADIESIGASGAHAAIACTALTIQnSQKVFGFEPVCHQLLKAQAQAvLDDLPVRAIKSGMMGTLE 89
Cdd:PRK12413   6 ILAISGNDIFSGGGLHADLATYTRNGLHGFVAVTCLTAM-TEKGFEVFPVDKEIFQQQLDS-LKDVPFSAIKIGLLPNVE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  90 nIIALTELFETcTIKHIPYVLDPVLVANSGGILgDVKTLAQAFSRLLPYATLITPNTHEIRALSGQ-----QDLHDAAKA 164
Cdd:PRK12413  84 -IAEQALDFIK-GHPGIPVVLDPVLVCKETHDV-EVSELRQELIQFFPYVTVITPNLVEAELLSGKeiktlEDMKEAAKK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028 165 LNDQGANAVLVKTSHDFNTGDIEQFLYiNGRIHHTSIVPRLTGEFHGSGCSLASHIAGRLAMGDDIIDAITAADAWIHQT 244
Cdd:PRK12413 161 LYDLGAKAVVIKGGNRLSQKKAIDLFY-DGKEFVILESPVLEKNNIGAGCTFASSIASQLVKGKSPLEAVKNSKDFVYQA 239


                 ....*.
gi 489753028 245 LIHADK 250
Cdd:PRK12413 240 IQQSDQ 245
PRK12412 PRK12412
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
8-253 1.80e-26

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183512 [Multi-domain]  Cd Length: 268  Bit Score: 103.90  E-value: 1.80e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028   8 PTVLCFSGLDPSGGAGIQADIESIGASGAHAAIACTALTIQN-----SQKVFgfePVCHQLLKAQAQAVLDDLPVRAIKS 82
Cdd:PRK12412   2 NKALTIAGSDTSGGAGIQADLKTFQELGVYGMTSLTTIVTMDphngwAHNVF---PIPASTLKPQLETTIEGVGVDALKT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  83 GMMGTLENIIALTELFETCTIKHIpyVLDPVLVANSGGILGDVKTLAQAFSRLLPYATLITPNTHEIRALSGQ-----QD 157
Cdd:PRK12412  79 GMLGSVEIIEMVAETIEKHNFKNV--VVDPVMVCKGADEALHPETNDCLRDVLVPKALVVTPNLFEAYQLSGVkinslED 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028 158 LHDAAKALNDQGANAVLVKTSHDFNTGDIEQFLYiNGRIHHTSIVPRLTGEF-HGSGCSLASHIAGRLAMGDDIIDAITA 236
Cdd:PRK12412 157 MKEAAKKIHALGAKYVLIKGGSKLGTETAIDVLY-DGETFDLLESEKIDTTNtHGAGCTYSAAITAELAKGKPVKEAVKT 235

                        250
                 ....*....|....*..
gi 489753028 237 ADAWIHQTLIHADKPHQ 253
Cdd:PRK12412 236 AKEFITAAIRYSFKINE 252
PRK12616 PRK12616
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
1-241 2.36e-25

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183624  Cd Length: 270  Bit Score: 100.89  E-value: 2.36e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028   1 MQIHQmrptVLCFSGLDPSGGAGIQADIESIGASGAHAAIACT---ALTIQNS--QKVFgfePVCHQLLKAQAQAVLDDL 75
Cdd:PRK12616   1 MSMHK----ALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTvvvAMDPENSwdHQVF---PIDTDTIRAQLSTIVDGI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  76 PVRAIKSGMMGTLENIIALTELFETCTIKHIpyVLDPVLVANsggilGDVKTL----AQAFSRLL-PYATLITPNTHEIR 150
Cdd:PRK12616  74 GVDAMKTGMLPTVDIIELAADTIKEKQLKNV--VIDPVMVCK-----GANEVLypehAEALREQLaPLATVITPNLFEAG 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028 151 ALSGQ------QDLHDAAKALNDQGANAVLVKTSHDFNTGDIEQFLYiNGRIHHTSIVPRLTGEF-HGSGCSLASHIAGR 223
Cdd:PRK12616 147 QLSGMgeiktvEQMKEAAKKIHELGAQYVVITGGGKLKHEKAVDVLY-DGETAEVLESEMIDTPYtHGAGCTFSAAVTAE 225

                        250
                 ....*....|....*...
gi 489753028 224 LAMGDDIIDAITAADAWI 241
Cdd:PRK12616 226 LAKGSEVKEAIYAAKEFI 243
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 77-245 8.63e-18

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: 80.58  E-value: 8.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  77 VRAIKSGMMGTLENIIALTELFETCTIKH--IPYVLDPVLVANSGGILGDVKTLAQAFSRLLPYATLITPNTHEIRALSG 154
Cdd:COG2240   75 FDAVLSGYLGSAEQGDIIADFVARVKAANpdALYLCDPVMGDNGKGYYVFPGIAEFIMRRLVPLADIITPNLTELALLTG 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028 155 Q-----QDLHDAAKALNDQGANAVLVK--TSHDFNTGDIEQFLYINGRIHHTSiVPRLTGEFHGSGCSLASHIAGRLAMG 227
Cdd:COG2240  155 RpyetlEEALAAARALLALGPKIVVVTsvPLDDTPADKIGNLAVTADGAWLVE-TPLLPFSPNGTGDLFAALLLAHLLRG 233

                        170
                 ....*....|....*...
gi 489753028 228 DDIIDAITAADAWIHQTL 245
Cdd:COG2240  234 KSLEEALERAAAFVYEVL 251
PTZ00493 PTZ00493
phosphomethylpyrimidine kinase; Provisional
 8-248 2.62e-17

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240440  Cd Length: 321  Bit Score: 80.04  E-value: 2.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028   8 PTVLCFSGLDPSGGAGIQADIESIGASGAHAAIACTALTIQNSQKVFGFEPVCHQLLKAQAQAVLDDLPVRAIKSGMMGT 87
Cdd:PTZ00493   5 SNILSIAGSDSCGGAGMQADIKTAMGLGCHCCTALVVLTAQNTKEVKRIVEIEEKFIVEQLDSIFADVTIDVVKLGVLYS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  88 lENIIALTELFETCTI----KHIPYVLDPVLVANSGGIL-GDVKTLAQAFSRLLPYATLITPNTHE----IRALSGQQDL 158
Cdd:PTZ00493  85 -KKIISLVHNYITNMNkkrgKKLLVVFDPVFVSSSGCLLvENLEYIKFALDLICPISCIITPNFYEckviLEALDCQMDL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028 159 HDA---------AKALNdqgANAVLVKTSH-DFNTGDIEQFLYIN--------------------GRIHHTSIVPRLTG- 207
Cdd:PTZ00493 164 SKAnmtelcklvTEKLN---INACLFKSCNvGENSAEENEVYAVDhlcirnvgsyptgekqqidaGGVTYLYDVYKLRSk 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 489753028 208 -----EFHGSGCSLASHIAGRLAMGDDIIDAITAADAWIHQTLIHA 248
Cdd:PTZ00493 241 rkpgkDIHGTGCTLSTAIACYLAKKHNILQSCIESKKYIYNCIRYA 286
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 77-245 1.83e-13

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: 67.99  E-value: 1.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  77 VRAIKSGMMGTLENIIALTELFETCTIKH--IPYVLDPVLVANSGGILGDVKTLAQAFSRLLPYATLITPNTHEIRALSG 154
Cdd:cd01173   73 YDAVLTGYLGSAEQVEAVAEIVKRLKEKNpnLLYVCDPVMGDNGKLYVVAEEIVPVYRDLLVPLADIITPNQFELELLTG 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028 155 -----QQDLHDAAKALNDQGANAVLVKTSHDFNTGDIEQFLYINGRIHHTSIvPRLTGE--FHGSGCSLASHIAGRLAMG 227
Cdd:cd01173  153 kkindLEDAKAAARALHAKGPKTVVVTSVELADDDRIEMLGSTATEAWLVQR-PKIPFPayFNGTGDLFAALLLARLLKG 231

                        170
                 ....*....|....*...
gi 489753028 228 DDIIDAITAADAWIHQTL 245
Cdd:cd01173  232 KSLAEALEKALNFVHEVL 249
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 108-263 3.30e-09

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 56.24  E-value: 3.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028 108 YVLDPVLVANsgGILGDVKTLAQAFSRLLPYATLITPNTHEIRALSGQ--QDLHDAAKALN---DQGANAVLVkTSHDFN 182
Cdd:PTZ00344 111 FLCDPVMGDD--GKLYVKEEVVDAYRELIPYADVITPNQFEASLLSGVevKDLSDALEAIDwfhEQGIPVVVI-TSFRED 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028 183 TGDIEQFLYI-------NGRIHHTSIVPRLTGEFHGSGCSLASHIAGrLAMGDDIIDAITAADAWIhQTLIHADKPHQSD 255
Cdd:PTZ00344 188 EDPTHLRFLLscrdkdtKNNKRFTGKVPYIEGRYTGTGDLFAALLLA-FSHQHPMDLAVGKAMGVL-QDIIKATRESGGS 265


                 ....*...
gi 489753028 256 NTQLIPNR 263
Cdd:PTZ00344 266 GSSSLMSR 273
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 93-239 1.26e-06

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 48.49  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028   93 ALTELFETCTI--KHIPYVLDPVLVAnsggilgdvktlAQAFSRLLPYATLITPNTHEIRALSGQQ-----DLHDAAKAL 165
Cdd:pfam00294 145 TLEELIEAAKNggTFDPNLLDPLGAA------------REALLELLPLADLLKPNEEELEALTGAKlddieEALAALHKL 212

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489753028  166 NDQGANAVLVKTShdfntGDIEQFLYINGRIHHTSIVPRLTGEFHGSGCSLASHIAGRLAMGDDIIDAITAADA 239
Cdd:pfam00294 213 LAKGIKTVIVTLG-----ADGALVVEGDGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANA 281
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 93-176 1.58e-06

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


Pssm-ID: 440290 [Multi-domain]  Cd Length: 301  Bit Score: 48.34  E-value: 1.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  93 ALTELFETCTIKHIPYVLDPVLVANsggilgDVKTLAQAFSRLLPYATLITPNTHEIRALSGQQDLHDAAKALNDQGANA 172
Cdd:COG0524  146 ALLAALEAARAAGVPVSLDPNYRPA------LWEPARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKL 219


                 ....
gi 489753028 173 VLVK 176
Cdd:COG0524  220 VVVT 223
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
77-237 2.99e-06

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 47.34  E-value: 2.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  77 VRAIKSGMMGTLENIIALTELFETCTIKHiPYVL---DPVLvansggilGDVKT-------LAQAFSR-LLPYATLITPN 145
Cdd:PRK08176  89 LRAVTTGYMGSASQIKILAEWLTALRADH-PDLLimvDPVI--------GDIDSgiyvkpdLPEAYRQhLLPLAQGLTPN 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028 146 THEIRALSGQ-----QDLHDAAKALNDQGANAVLVkTSHDFNTGdieqflyiNGRIH---------HTSIVPRLTGEFHG 211
Cdd:PRK08176 160 IFELEILTGKpcrtlDSAIAAAKSLLSDTLKWVVI-TSAAGNEE--------NQEMQvvvvtadsvNVISHPRVDTDLKG 230

                        170       180
                 ....*....|....*....|....*.
gi 489753028 212 SGCSLASHIAGRLAMGDDIIDAITAA 237
Cdd:PRK08176 231 TGDLFCAELVSGLLKGKALTDAAHRA 256
THZ_kinase cd01170
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ...
 85-237 3.26e-06

4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the hydroxylgroup of Thz. A reaction that allows cells to recycle Thz into the thiamine biosynthesis pathway, as an alternative to its synthesis from cysteine, tyrosine and 1-deoxy-D-xylulose-5-phosphate.


Pssm-ID: 238575 [Multi-domain]  Cd Length: 242  Bit Score: 47.15  E-value: 3.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  85 MGTL--ENIIALTELFETCTIKHIPYVLDPVLVANSGGILGDVKTLAQAFsrllpYATLITPNTHEIRALSGQQ------ 156
Cdd:cd01170   57 IGTLtsEQIEAMLKAGKAANQLGKPVVLDPVGVGATSFRTEVAKELLAEG-----QPTVIRGNASEIAALAGLTglgkgv 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028 157 --------DLHDAAKALNDQGANAVLVKTSHDFNTGDIEQFLYINGrihhTSIVPRLTGefhgSGCSLASHIAGRLAMGD 228
Cdd:cd01170  132 dssssdeeDALELAKALARKYGAVVVVTGEVDYITDGERVVVVKNG----HPLLTKITG----TGCLLGAVIAAFLAVGD 203


                 ....*....
gi 489753028 229 DIIDAITAA 237
Cdd:cd01170  204 DPLEAAVSA 212
PRK05756 PRK05756
pyridoxal kinase PdxY;
134-245 5.63e-06

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 46.40  E-value: 5.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028 134 RLLPYATLITPNTHEIRALSGQ-----QDLHDAAKALNDQGANAVLVKTSH--DFNTGDIEQFLYINGRIHHTSiVPRLT 206
Cdd:PRK05756 134 RALPAADIITPNLFELEWLSGRpvetlEDAVAAARALIARGPKIVLVTSLAraGYPADRFEMLLVTADGAWHIS-RPLVD 212

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 489753028 207 GEF--HGSGCSLASHIAGRLAMGDDIIDAITAADAWIHQTL 245
Cdd:PRK05756 213 FMRqpVGVGDLTSALFLARLLQGGSLEEALEHTTAAVYEVM 253
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 104-225 1.24e-05

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: 44.78  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028 104 KHIPYVLDPVLVANSGGilgdvktlAQAFSRLLPYATLITPNTHEIRALSGQQDLHD-----AAKALNDQGANAVLVKTS 178
Cdd:cd00287   83 RGVPVVLDPGPRAVRLD--------GEELEKLLPGVDILTPNEEEAEALTGRRDLEVkeaaeAAALLLSKGPKVVIVTLG 154

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489753028 179 HDfntGDIeqFLYINGRIHHTSIVPRLTGEFHGSGCSLASHIAGRLA 225
Cdd:cd00287  155 EK---GAI--VATRGGTEVHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
PRK07105 PRK07105
pyridoxamine kinase; Validated
 74-234 2.67e-05

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 44.52  E-value: 2.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028  74 DLPVRAIKSGMMGTLENIIALTELFETCTIKHIPYVLDPVlvansggiLGDVKTLAQAFS--------RLLPYATLITPN 145
Cdd:PRK07105  73 NLKFDAIYSGYLGSPRQIQIVSDFIKYFKKKDLLVVVDPV--------MGDNGKLYQGFDqemveemrKLIQKADVITPN 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489753028 146 THEIRALSG---------QQDLHDAAKALNDQGANAVLVkTSHDFNTGDIeQFLYINGRIHHTSIV--PRLTGEFHGSGC 214
Cdd:PRK07105 145 LTEACLLLDkpyleksysEEEIKQLLRKLADLGPKIVII-TSVPFEDGKI-GVAYYDRATDRFWKVfcKYIPAHYPGTGD 222

                        170       180
                 ....*....|....*....|
gi 489753028 215 SLASHIAGRLAMGDDIIDAI 234
Cdd:PRK07105 223 IFTSVITGSLLQGDSLPIAL 242
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
140-175 9.96e-03

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 36.65  E-value: 9.96e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 489753028 140 TLITPNTHEIRALSGQ-----QDLHDAAKALNDQGANAVLV 175
Cdd:COG1105  179 DLIKPNLEELEELLGRpletlEDIIAAARELLERGAENVVV 219
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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