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Conserved domains on  [gi|582524153|gb|EVY16211|]
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hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Staphylococcus aureus F83272]

Protein Classification

hydroxymethylpyrimidine/phosphomethylpyrimidine kinase( domain architecture ID 10792784)

bifunctional enzyme, phosphomethylpyrimidine (HMP-P) kinase/hydroxymethylpyrimidine (HMP) kinase

EC:  2.7.4.7|2.7.1.49
Gene Ontology:  GO:0008902|GO:0008972|GO:0009228|GO:0005829
PubMed:  11839308

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 1-266 1.96e-151

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


:

Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 423.38  E-value: 1.96e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153   1 MIKPKIALTIAGTDPTGGAGVMADLKSFHSCGVYGMGVVTSIVAQNTLGVQHIHNLNHQWVDEQLDSVFNDTLPHAIKTG 80
Cdd:PRK06427   1 MMKRPIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  81 MIATADTMETIRHYLMQHESIPYVIDPVMLAKSGDSLMDNDTKQNLQHTLLPLADVVTPNLPEAEEITGLTIDSEEKIMQ 160
Cdd:PRK06427  81 MLASAEIIETVAEALKRYPIPPVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTGLPIADTEDEMK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 161 AGRIFINEIGSKGVIIKGGHSNDTDIAKDYLFTNEGVQTFENERFKTKHTHGTGCTFSAVITAELAKGRPLFEAVHKAKK 240
Cdd:PRK06427 161 AAARALHALGCKAVLIKGGHLLDGEESVDWLFDGEGEERFSAPRIPTKNTHGTGCTLSAAIAAELAKGASLLDAVQTAKD 240

                        250       260
                 ....*....|....*....|....*.
gi 582524153 241 FISMSIQYTPEIGRGRGPVNHFAYLK 266
Cdd:PRK06427 241 YVTRAIRHALEIGQGHGPVNHFAYLW 266
 
Name Accession Description Interval E-value
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 1-266 1.96e-151

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 423.38  E-value: 1.96e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153   1 MIKPKIALTIAGTDPTGGAGVMADLKSFHSCGVYGMGVVTSIVAQNTLGVQHIHNLNHQWVDEQLDSVFNDTLPHAIKTG 80
Cdd:PRK06427   1 MMKRPIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  81 MIATADTMETIRHYLMQHESIPYVIDPVMLAKSGDSLMDNDTKQNLQHTLLPLADVVTPNLPEAEEITGLTIDSEEKIMQ 160
Cdd:PRK06427  81 MLASAEIIETVAEALKRYPIPPVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTGLPIADTEDEMK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 161 AGRIFINEIGSKGVIIKGGHSNDTDIAKDYLFTNEGVQTFENERFKTKHTHGTGCTFSAVITAELAKGRPLFEAVHKAKK 240
Cdd:PRK06427 161 AAARALHALGCKAVLIKGGHLLDGEESVDWLFDGEGEERFSAPRIPTKNTHGTGCTLSAAIAAELAKGASLLDAVQTAKD 240

                        250       260
                 ....*....|....*....|....*.
gi 582524153 241 FISMSIQYTPEIGRGRGPVNHFAYLK 266
Cdd:PRK06427 241 YVTRAIRHALEIGQGHGPVNHFAYLW 266
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 14-260 1.29e-125

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: 357.18  E-value: 1.29e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153   14 DPTGGAGVMADLKSFHSCGVYGMGVVTSIVAQNTLGVQHIHNLNHQWVDEQLDSVFNDTLPHAIKTGMIATADTMETIRH 93
Cdd:pfam08543   1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLGSAEIIEAVAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153   94 YLmQHESIPYVIDPVMLAKSGDSLMDNDTKQNLQHTLLPLADVVTPNLPEAEEITGLTIDSEEKIMQAGRIfINEIGSKG 173
Cdd:pfam08543  81 KL-DKYGVPVVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKK-LLALGAKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  174 VIIKGGHSN-DTDIAKDYLFTNEGVQTFENERFKTKHTHGTGCTFSAVITAELAKGRPLFEAVHKAKKFISMSIQYTPEI 252
Cdd:pfam08543 159 VLIKGGHLEgEEAVVTDVLYDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVTEAIRDALNL 238


                  ....*...
gi 582524153  253 GRGRGPVN 260
Cdd:pfam08543 239 GKGHGPVN 246
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 8-263 1.37e-125

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: 357.43  E-value: 1.37e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153   8 LTIAGTDPTGGAGVMADLKSFHSCGVYGMGVVTSIVAQNTLGVQHIHNLNHQWVDEQLDSVFNDTLPHAIKTGMIATADT 87
Cdd:COG0351    1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSAEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  88 METIRHYLMQHESIPYVIDPVMLAKSGDSLMDNDTKQNLQHTLLPLADVVTPNLPEAEEITGLTIDSEEKIMQAGRIfIN 167
Cdd:COG0351   81 IEAVAEILADYPLVPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKA-LL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 168 EIGSKGVIIKGGHSNDTDiAKDYLFTNEGVQTFENERFKTKHTHGTGCTFSAVITAELAKGRPLFEAVHKAKKFISMSIQ 247
Cdd:COG0351  160 ELGAKAVLVKGGHLPGDE-AVDVLYDGDGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQAIR 238

                        250
                 ....*....|....*.
gi 582524153 248 YTPEIGRGRGPVNHFA 263
Cdd:COG0351  239 AALRLGMGHGPVNHFA 254
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 6-248 2.96e-117

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: 336.01  E-value: 2.96e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153   6 IALTIAGTDPTGGAGVMADLKSFHSCGVYGMGVVTSIVAQNTLGVQHIHNLNHQWVDEQLDSVFNDTLPHAIKTGMIATA 85
Cdd:cd01169    1 VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLGSA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  86 DTMETIRHYLMQHESIPYVIDPVMLAKSGDSLMDNDTKQNLQHTLLPLADVVTPNLPEAEEITGLTIDSEEKIMQAGRIf 165
Cdd:cd01169   81 EIIEAVAEALKDYPDIPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTGLEIATEEDMMKAAKA- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 166 INEIGSKGVIIKGGHSNDtDIAKDYLFTNEGVQTFENERFKTKHTHGTGCTFSAVITAELAKGRPLFEAVHKAKKFISMS 245
Cdd:cd01169  160 LLALGAKAVLIKGGHLPG-DEAVDVLYDGGGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQA 238


                 ...
gi 582524153 246 IQY 248
Cdd:cd01169  239 IRN 241
HMP-P_kinase TIGR00097
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ...
 7-262 5.27e-106

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: 308.07  E-value: 5.27e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153    7 ALTIAGTDPTGGAGVMADLKSFHSCGVYGMGVVTSIVAQNTLGVQHIHNLNHQWVDEQLDSVFNDTLPHAIKTGMIATAD 86
Cdd:TIGR00097   1 ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLASAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153   87 TMETIRHYLMQHESIPYVIDPVMLAKSGDSLMDNDTKQNLQHTLLPLADVVTPNLPEAEEITGLTIDSEEKIMQAGRIfI 166
Cdd:TIGR00097  81 IVEAVARKLREYPVRPLVVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGTKIRTEQDMIKAAKK-L 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  167 NEIGSKGVIIKGGHSNDtDIAKDYLFTNEGVQTFENERFKTKHTHGTGCTFSAVITAELAKGRPLFEAVHKAKKFISMSI 246
Cdd:TIGR00097 160 RELGPKAVLIKGGHLEG-DQAVDVLFDGGEIHILKAPRIETKNTHGTGCTLSAAIAANLAKGLSLKEAVKEAKEFVTGAI 238

                         250
                  ....*....|....*.
gi 582524153  247 QYTPEIGRGRGPVNHF 262
Cdd:TIGR00097 239 RYGLNIGHGHGPLNHF 254
 
Name Accession Description Interval E-value
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 1-266 1.96e-151

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 423.38  E-value: 1.96e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153   1 MIKPKIALTIAGTDPTGGAGVMADLKSFHSCGVYGMGVVTSIVAQNTLGVQHIHNLNHQWVDEQLDSVFNDTLPHAIKTG 80
Cdd:PRK06427   1 MMKRPIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  81 MIATADTMETIRHYLMQHESIPYVIDPVMLAKSGDSLMDNDTKQNLQHTLLPLADVVTPNLPEAEEITGLTIDSEEKIMQ 160
Cdd:PRK06427  81 MLASAEIIETVAEALKRYPIPPVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTGLPIADTEDEMK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 161 AGRIFINEIGSKGVIIKGGHSNDTDIAKDYLFTNEGVQTFENERFKTKHTHGTGCTFSAVITAELAKGRPLFEAVHKAKK 240
Cdd:PRK06427 161 AAARALHALGCKAVLIKGGHLLDGEESVDWLFDGEGEERFSAPRIPTKNTHGTGCTLSAAIAAELAKGASLLDAVQTAKD 240

                        250       260
                 ....*....|....*....|....*.
gi 582524153 241 FISMSIQYTPEIGRGRGPVNHFAYLK 266
Cdd:PRK06427 241 YVTRAIRHALEIGQGHGPVNHFAYLW 266
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 14-260 1.29e-125

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: 357.18  E-value: 1.29e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153   14 DPTGGAGVMADLKSFHSCGVYGMGVVTSIVAQNTLGVQHIHNLNHQWVDEQLDSVFNDTLPHAIKTGMIATADTMETIRH 93
Cdd:pfam08543   1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLGSAEIIEAVAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153   94 YLmQHESIPYVIDPVMLAKSGDSLMDNDTKQNLQHTLLPLADVVTPNLPEAEEITGLTIDSEEKIMQAGRIfINEIGSKG 173
Cdd:pfam08543  81 KL-DKYGVPVVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKK-LLALGAKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  174 VIIKGGHSN-DTDIAKDYLFTNEGVQTFENERFKTKHTHGTGCTFSAVITAELAKGRPLFEAVHKAKKFISMSIQYTPEI 252
Cdd:pfam08543 159 VLIKGGHLEgEEAVVTDVLYDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVTEAIRDALNL 238


                  ....*...
gi 582524153  253 GRGRGPVN 260
Cdd:pfam08543 239 GKGHGPVN 246
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 8-263 1.37e-125

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: 357.43  E-value: 1.37e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153   8 LTIAGTDPTGGAGVMADLKSFHSCGVYGMGVVTSIVAQNTLGVQHIHNLNHQWVDEQLDSVFNDTLPHAIKTGMIATADT 87
Cdd:COG0351    1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSAEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  88 METIRHYLMQHESIPYVIDPVMLAKSGDSLMDNDTKQNLQHTLLPLADVVTPNLPEAEEITGLTIDSEEKIMQAGRIfIN 167
Cdd:COG0351   81 IEAVAEILADYPLVPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKA-LL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 168 EIGSKGVIIKGGHSNDTDiAKDYLFTNEGVQTFENERFKTKHTHGTGCTFSAVITAELAKGRPLFEAVHKAKKFISMSIQ 247
Cdd:COG0351  160 ELGAKAVLVKGGHLPGDE-AVDVLYDGDGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQAIR 238

                        250
                 ....*....|....*.
gi 582524153 248 YTPEIGRGRGPVNHFA 263
Cdd:COG0351  239 AALRLGMGHGPVNHFA 254
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 6-248 2.96e-117

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: 336.01  E-value: 2.96e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153   6 IALTIAGTDPTGGAGVMADLKSFHSCGVYGMGVVTSIVAQNTLGVQHIHNLNHQWVDEQLDSVFNDTLPHAIKTGMIATA 85
Cdd:cd01169    1 VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLGSA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  86 DTMETIRHYLMQHESIPYVIDPVMLAKSGDSLMDNDTKQNLQHTLLPLADVVTPNLPEAEEITGLTIDSEEKIMQAGRIf 165
Cdd:cd01169   81 EIIEAVAEALKDYPDIPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTGLEIATEEDMMKAAKA- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 166 INEIGSKGVIIKGGHSNDtDIAKDYLFTNEGVQTFENERFKTKHTHGTGCTFSAVITAELAKGRPLFEAVHKAKKFISMS 245
Cdd:cd01169  160 LLALGAKAVLIKGGHLPG-DEAVDVLYDGGGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQA 238


                 ...
gi 582524153 246 IQY 248
Cdd:cd01169  239 IRN 241
HMP-P_kinase TIGR00097
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ...
 7-262 5.27e-106

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: 308.07  E-value: 5.27e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153    7 ALTIAGTDPTGGAGVMADLKSFHSCGVYGMGVVTSIVAQNTLGVQHIHNLNHQWVDEQLDSVFNDTLPHAIKTGMIATAD 86
Cdd:TIGR00097   1 ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLASAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153   87 TMETIRHYLMQHESIPYVIDPVMLAKSGDSLMDNDTKQNLQHTLLPLADVVTPNLPEAEEITGLTIDSEEKIMQAGRIfI 166
Cdd:TIGR00097  81 IVEAVARKLREYPVRPLVVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGTKIRTEQDMIKAAKK-L 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  167 NEIGSKGVIIKGGHSNDtDIAKDYLFTNEGVQTFENERFKTKHTHGTGCTFSAVITAELAKGRPLFEAVHKAKKFISMSI 246
Cdd:TIGR00097 160 RELGPKAVLIKGGHLEG-DQAVDVLFDGGEIHILKAPRIETKNTHGTGCTLSAAIAANLAKGLSLKEAVKEAKEFVTGAI 238

                         250
                  ....*....|....*.
gi 582524153  247 QYTPEIGRGRGPVNHF 262
Cdd:TIGR00097 239 RYGLNIGHGHGPLNHF 254
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
5-265 1.89e-86

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 265.05  E-value: 1.89e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153   5 KIALTIAGTDPTGGAGVMADLKSFHSCGVYGMGVVTSIVAQNTLGVQHIHNLNHQWVDEQLDSVFNDTLPHAIKTGMIAT 84
Cdd:PRK08573   3 PVALTIAGSDSGGGAGIEADLKTFAALGVHGAVAITSVTAQNTYEVRAIHDLPPEVVAAQIEAVWEDMGIDAAKTGMLSN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  85 ADTMETIRHYLMQHEsIPYVIDPVMLAKSGDSLMDNDTKQNLQHTLLPLADVVTPNLPEAEEITGLTIDSEEKIMQAGRI 164
Cdd:PRK08573  83 REIIEAVAKTVSKYG-FPLVVDPVMIAKSGAPLLREDAVDALIKRLLPLATVVTPNRPEAEKLTGMKIRSVEDARKAAKY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 165 FINEIGSKGVIIKGGHSnDTDIAKDYLFTNEGVQTFENERFKTKHTHGTGCTFSAVITAELAKGRPLFEAVHKAKKFISM 244
Cdd:PRK08573 162 IVEELGAEAVVVKGGHL-EGEEAVDVLYHNGTFREFRAPRVESGCTHGTGCSFSAAIAAGLAKGLDPEEAIKTAKKFITM 240

                        250       260
                 ....*....|....*....|.
gi 582524153 245 SIQYTPEIGRGRGPVNHFAYL 265
Cdd:PRK08573 241 AIKYGVKIGKGHCPVNPMAWI 261
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 1-267 7.10e-82

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 254.69  E-value: 7.10e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153   1 MIKPKIaLTIAGTDPTGGAGVMADLKSFHSCGVYGMGVVTSIVAQNTLGVQHIHNLNHQWVDEQLDSVFNDTLPHAIKTG 80
Cdd:PLN02898   7 MKVPHV-LTVAGSDSGAGAGIQADIKACAARGVYCTTAITAVTAQNTVGVQGVHAVPLDFVAEQLKSVLSDMPVDVVKTG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  81 MIATADTMETIRHYLMQHESIPYVIDPVMLAKSGDSLMDNDTKQNLQHTLLPLADVVTPNLPEAEEITGLtiDSEEKI-- 158
Cdd:PLN02898  86 MLPSAEIVKVLCQALKEFPVKALVVDPVMVSTSGDVLAGPSILSALREELLPLATIVTPNVKEASALLGG--DPLETVad 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 159 MQAGRIFINEIGSKGVIIKGGHSNDTDIAKDYLFTNEGVQTFENERFKTKHTHGTGCTFSAVITAELAKGRPLFEAVHKA 238
Cdd:PLN02898 164 MRSAAKELHKLGPRYVLVKGGHLPDSLDAVDVLYDGTEFHELRSSRIKTRNTHGTGCTLASCIAAELAKGSDMLSAVKVA 243

                        250       260       270
                 ....*....|....*....|....*....|..
gi 582524153 239 KKFISMSIQYTPEIGRG---RGPVNHFAYLKK 267
Cdd:PLN02898 244 KRYVETALEYSKDIGIGngaQGPFNHLFFLKS 275
PRK14713 PRK14713
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
8-271 1.81e-70

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 237797 [Multi-domain]  Cd Length: 530  Bit Score: 226.21  E-value: 1.81e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153   8 LTIAGTDPTGGAGVMADLKSFHSCGVYGMGVVTSIVAQNTLGVQHIHNLNHQWVDEQLDSVFNDTLPHAIKTGMIATADT 87
Cdd:PRK14713  33 LSIAGTDPSGGAGIQADLKSIAAAGGYGMAVITALVAQNTRGVRAVHVPPADFLRAQLDAVSDDVTVDAVKIGMLGDAEV 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  88 METIRHYLMQHESIPYVIDPVMLAKSGDSLMDNDTKQNLQhTLLPLADVVTPNLPEAEEITG--LTIDSEEKIMQAGRIf 165
Cdd:PRK14713 113 IDAVRTWLAEHRPPVVVLDPVMVATSGDRLLEEDAEAALR-ELVPRADLITPNLPELAVLLGepPATTWEEALAQARRL- 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 166 INEIGSKgVIIKGGHSNDtDIAKDYLFTNEGVQT-FENERFKTKHTHGTGCTFSAVITAELAKGRPLFEAVHKAKKFISM 244
Cdd:PRK14713 191 AAETGTT-VLVKGGHLDG-QRAPDALVGPDGAVTeVPGPRVDTRNTHGTGCSLSSALATRLGRGGDWAAALRWATAWLHG 268

                        250       260
                 ....*....|....*....|....*....
gi 582524153 245 SIQY--TPEIGRGRGPVNHFAYLKKEGLD 271
Cdd:PRK14713 269 AIAAgaALQVGTGNGPVDHFHRARRLAAD 297
PRK09517 PRK09517
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ...
 4-267 2.80e-68

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


Pssm-ID: 169939 [Multi-domain]  Cd Length: 755  Bit Score: 224.85  E-value: 2.80e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153   4 PKIaLTIAGTDPTGGAGVMADLKSFHSCGVYGMGVVTSIVAQNTLGVQHIHNLNHQWVDEQLDSVFNDTLPHAIKTGMIA 83
Cdd:PRK09517 242 PRV-LSIAGTDPTGGAGIQADLKSIAAGGGYGMCVVTALVAQNTHGVNTIHTPPLTFLEEQLEAVFSDVTVDAVKLGMLG 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  84 TADTMETIRHYLMQHESIPYVIDPVMLAKSGDSLMDNDTKQNLQHtLLPLADVVTPNLPEAEEITG-LTIDSEEKIMQAG 162
Cdd:PRK09517 321 SADTVDLVASWLGSHEHGPVVLDPVMVATSGDRLLDADATEALRR-LAVHVDVVTPNIPELAVLCGeAPAITMDEAIAQA 399

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 163 RIFINEIGSKgVIIKGGHSNdTDIAKDYLFTNEG-VQTFENERFKTKHTHGTGCTFSAVITAELAKGRPLFEAVHKAKKF 241
Cdd:PRK09517 400 RGFARTHGTI-VIVKGGHLT-GDLADNAVVRPDGsVHQVENPRVNTTNSHGTGCSLSAALATLIAAGESVEKALEWATRW 477

                        250       260
                 ....*....|....*....|....*...
gi 582524153 242 ISMSIQYTP--EIGRGRGPVNHFAYLKK 267
Cdd:PRK09517 478 LNEALRHADhlAVGSGNGPVDHGHLARR 505
PRK12412 PRK12412
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
7-266 8.21e-67

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183512 [Multi-domain]  Cd Length: 268  Bit Score: 208.67  E-value: 8.21e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153   7 ALTIAGTDPTGGAGVMADLKSFHSCGVYGMGVVTSIVAQNTLGvQHIHNLNHQ---WVDEQLDSVFNDTLPHAIKTGMIA 83
Cdd:PRK12412   4 ALTIAGSDTSGGAGIQADLKTFQELGVYGMTSLTTIVTMDPHN-GWAHNVFPIpasTLKPQLETTIEGVGVDALKTGMLG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  84 TADTMETIRHYLMQHESIPYVIDPVMLAKSGDSLMDNDTKQNLQHTLLPLADVVTPNLPEAEEITGLTIDSEEKIMQA-G 162
Cdd:PRK12412  83 SVEIIEMVAETIEKHNFKNVVVDPVMVCKGADEALHPETNDCLRDVLVPKALVVTPNLFEAYQLSGVKINSLEDMKEAaK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 163 RIFinEIGSKGVIIKGGHSNDTDIAKDYLFTNEGVQTFENERFKTKHTHGTGCTFSAVITAELAKGRPLFEAVHKAKKFI 242
Cdd:PRK12412 163 KIH--ALGAKYVLIKGGSKLGTETAIDVLYDGETFDLLESEKIDTTNTHGAGCTYSAAITAELAKGKPVKEAVKTAKEFI 240

                        250       260
                 ....*....|....*....|....
gi 582524153 243 SMSIQYTPEIGRGRGPVNHFAYLK 266
Cdd:PRK12412 241 TAAIRYSFKINEYVGPTHHGAYRK 264
PTZ00347 PTZ00347
phosphomethylpyrimidine kinase; Provisional
 2-261 2.54e-60

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240375 [Multi-domain]  Cd Length: 504  Bit Score: 199.03  E-value: 2.54e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153   2 IKPKIALTIAGTDPTGGAGVMADLKSFHSCGVYGMGVVTSIVAQNTLGVQHIHNLNHQWVDEQLDSVFNDTLPHAIKTGM 81
Cdd:PTZ00347 228 MKIPTVLTVSGSDSGGGAGHQADLKTLEALGVYSTSALTSLTAQNTKGVQQIQVVNEDFFAAQIDSVMSDFNISVVKLGL 307

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  82 IATADTMETIRHYLmqhESIPYVIDPVMLAKSGDSLMDNDTKQNL----QHTLLPLADVVTPNLPEAEEITGLTIDSEEK 157
Cdd:PTZ00347 308 VPTARQLEIVIEKL---KNLPMVVDPVLVATSGDDLVAQKNADDVlamyKERIFPMATIITPNIPEAERILGRKEITGVY 384

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 158 IMQAGRIFINEIGSKGVIIKGGHS-NDTDIAKDYLFTNEGVQ--TFENERFKTKHTHGTGCTFSAVITAELAKGRPLFEA 234
Cdd:PTZ00347 385 EARAAAQALAQYGSRYVLVKGGHDlIDPEACRDVLYDREKDRfyEFTANRIATINTHGTGCTLASAISSFLARGYTVPDA 464

                        250       260       270
                 ....*....|....*....|....*....|
gi 582524153 235 VHKAKKFISMSI--QYTPEIGRG-RGPVNH 261
Cdd:PTZ00347 465 VERAIGYVHEAIvrSCGVPLGQGtNRPLVH 494
PRK12616 PRK12616
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
7-263 3.31e-56

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183624  Cd Length: 270  Bit Score: 181.78  E-value: 3.31e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153   7 ALTIAGTDPTGGAGVMADLKSFHSCGVYGMGVVTSIVAQNTLgvqhiHNLNHQ-------WVDEQLDSVFNDTLPHAIKT 79
Cdd:PRK12616   6 ALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPE-----NSWDHQvfpidtdTIRAQLSTIVDGIGVDAMKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  80 GMIATADTMETIRHYLMQHESIPYVIDPVMLAKSGDSLMDNDTKQNLQHTLLPLADVVTPNLPEAEEITGL-TIDSEEKI 158
Cdd:PRK12616  81 GMLPTVDIIELAADTIKEKQLKNVVIDPVMVCKGANEVLYPEHAEALREQLAPLATVITPNLFEAGQLSGMgEIKTVEQM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 159 MQAGRIfINEIGSKGVIIKGGHSNDTDIAKDYLFTNEGVQTFENERFKTKHTHGTGCTFSAVITAELAKGRPLFEAVHKA 238
Cdd:PRK12616 161 KEAAKK-IHELGAQYVVITGGGKLKHEKAVDVLYDGETAEVLESEMIDTPYTHGAGCTFSAAVTAELAKGSEVKEAIYAA 239

                        250       260
                 ....*....|....*....|....*
gi 582524153 239 KKFISMSIQYTPEIGRGRGPVNHFA 263
Cdd:PRK12616 240 KEFITAAIKESFPLNQYVGPTKHSA 264
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
3-253 4.98e-45

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 152.52  E-value: 4.98e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153   3 KPKIALTIAGTDPTGGAGVMADLKSFHSCGVYGMGVVTSIVAQNTLGVQhIHNLNHQWVDEQLDSvFNDTLPHAIKTGMI 82
Cdd:PRK12413   2 KTNYILAISGNDIFSGGGLHADLATYTRNGLHGFVAVTCLTAMTEKGFE-VFPVDKEIFQQQLDS-LKDVPFSAIKIGLL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  83 ATADTMETIRHYLMQHESIPYVIDPVMLAKSGDSLMDNDTKQNLQhTLLPLADVVTPNLPEAEEITGLTIDSEEKiMQAG 162
Cdd:PRK12413  80 PNVEIAEQALDFIKGHPGIPVVLDPVLVCKETHDVEVSELRQELI-QFFPYVTVITPNLVEAELLSGKEIKTLED-MKEA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 163 RIFINEIGSKGVIIKGGHSNDTDIAKDYLFTNEGVQTFENERFKTKHThGTGCTFSAVITAELAKGRPLFEAVHKAKKFI 242
Cdd:PRK12413 158 AKKLYDLGAKAVVIKGGNRLSQKKAIDLFYDGKEFVILESPVLEKNNI-GAGCTFASSIASQLVKGKSPLEAVKNSKDFV 236

                        250
                 ....*....|.
gi 582524153 243 SMSIQYTPEIG 253
Cdd:PRK12413 237 YQAIQQSDQYG 247
COG1992 COG1992
Predicted transcriptional regulator fused phosphomethylpyrimidine kinase (thiamin biosynthesis) ...
 17-268 1.83e-37

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


Pssm-ID: 441595 [Multi-domain]  Cd Length: 432  Bit Score: 136.81  E-value: 1.83e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  17 GGAGVMADLKSFHSCGVYGMGVVTSIVAQNTLGVQHIHNLNHQWVDEQLDSVFNDTLPHAIKTGMIATADTMETIRHYLM 96
Cdd:COG1992    2 GGGGGGADAKTAAALGAGGGGTTTAVTVTATTTVTGVGSDPPPPVEVQQQAVAADDDVDDAKTGMLMTATIVEVVAVVVK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  97 QHESIPYV-IDPVMLAKSGDSLMDNDTKQNLQhtLLPLADVVTPNLPEAEEITGLTIDSEEKIMQAGRIFINEIGSKGVI 175
Cdd:COG1992   82 SRDKPLVVvVVPVAVAAAGLGLLLAEAELAKL--LLPLLATVTPNEPEVEELLLPTIRSLLAEARAARLALQEEGADALG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 176 IKGGHSnDTDIAKDYLFTNEGVQTFENERFKTKHTHGTGCTFSAVITAELAKGRPLFEAVHKAKKFISMSIQYTPEIGRG 255
Cdd:COG1992  160 VKGGHV-SGDAVVDVLEDERDVETFRHPRLVTEATHGSGCTFSAAIAALLAKGLSLEEAVRGAKLFLLHAIRYGLLVGKG 238

                        250
                 ....*....|...
gi 582524153 256 RGPVNHFAYLKKE 268
Cdd:COG1992  239 VGPVNHLADLRLE 251
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 76-253 4.54e-26

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: 103.30  E-value: 4.54e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  76 AIKTGMIATAD----TMETIRHYLMQHESIPYVIDPVMlaksGD-----SLMDNDTKQNLQHtLLPLADVVTPNLPEAEE 146
Cdd:COG2240   77 AVLSGYLGSAEqgdiIADFVARVKAANPDALYLCDPVM----GDngkgyYVFPGIAEFIMRR-LVPLADIITPNLTELAL 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 147 ITGLTIDSEEKIMQAGRIFINeIGSKGVIIKGGHSNDTDIAK--DYLFTNEGVQTFENERFKtKHTHGTGCTFSAVITAE 224
Cdd:COG2240  152 LTGRPYETLEEALAAARALLA-LGPKIVVVTSVPLDDTPADKigNLAVTADGAWLVETPLLP-FSPNGTGDLFAALLLAH 229

                        170       180
                 ....*....|....*....|....*....
gi 582524153 225 LAKGRPLFEAVHKAKKFISMSIQYTPEIG 253
Cdd:COG2240  230 LLRGKSLEEALERAAAFVYEVLERTAAAG 258
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 76-249 2.81e-25

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: 100.74  E-value: 2.81e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  76 AIKTGMIATADTMETIRHYLMQ----HESIPYVIDPVMlaksGDS----LMDNDTKQNLQHTLLPLADVVTPNLPEAEEI 147
Cdd:cd01173   75 AVLTGYLGSAEQVEAVAEIVKRlkekNPNLLYVCDPVM----GDNgklyVVAEEIVPVYRDLLVPLADIITPNQFELELL 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 148 TGLTIDSEEKIMQAGRIFINEiGSKGVIIKGGHSNDTDIAKDYLFTNEGVQTFENERFKTK-HTHGTGCTFSAVITAELA 226
Cdd:cd01173  151 TGKKINDLEDAKAAARALHAK-GPKTVVVTSVELADDDRIEMLGSTATEAWLVQRPKIPFPaYFNGTGDLFAALLLARLL 229

                        170       180
                 ....*....|....*....|...
gi 582524153 227 KGRPLFEAVHKAKKFISMSIQYT 249
Cdd:cd01173  230 KGKSLAEALEKALNFVHEVLEAT 252
PTZ00493 PTZ00493
phosphomethylpyrimidine kinase; Provisional
 4-262 1.72e-24

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240440  Cd Length: 321  Bit Score: 100.07  E-value: 1.72e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153   4 PKIaLTIAGTDPTGGAGVMADLKSFHSCGVYGMGVVTSIVAQNTLGVQHIHNLNHQWVDEQLDSVFNDTLPHAIKTGMIA 83
Cdd:PTZ00493   5 SNI-LSIAGSDSCGGAGMQADIKTAMGLGCHCCTALVVLTAQNTKEVKRIVEIEEKFIVEQLDSIFADVTIDVVKLGVLY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  84 TADTMETIRHYL-----MQHESIPYVIDPVMLAKSGDSLMDN-DTKQNLQHTLLPLADVVTPNLPEAEEI---------- 147
Cdd:PTZ00493  84 SKKIISLVHNYItnmnkKRGKKLLVVFDPVFVSSSGCLLVENlEYIKFALDLICPISCIITPNFYECKVIlealdcqmdl 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 148 ---------------------------TGLTIDSEEKIMQAGRIFINEIGSkgviIKGGHSNDTDIAK-DYLFTnegVQT 199
Cdd:PTZ00493 164 skanmtelcklvteklninaclfkscnVGENSAEENEVYAVDHLCIRNVGS----YPTGEKQQIDAGGvTYLYD---VYK 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 582524153 200 FENERFKTKHTHGTGCTFSAVITAELAKGRPLFEAVHKAKKFISMSIQYTPEIGRGRGPVNHF 262
Cdd:PTZ00493 237 LRSKRKPGKDIHGTGCTLSTAIACYLAKKHNILQSCIESKKYIYNCIRYAYPFGSKSQGLNHL 299
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
76-253 1.66e-14

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 71.61  E-value: 1.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  76 AIKTGMIATADTMETIRHYLM----QHESIPYVIDPVMlaksGD--SLM--DNDTKQNLQHTLLPLADVVTPNLPEAEEI 147
Cdd:PRK08176  91 AVTTGYMGSASQIKILAEWLTalraDHPDLLIMVDPVI----GDidSGIyvKPDLPEAYRQHLLPLAQGLTPNIFELEIL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 148 TGLTIDSEEKIMQAGRIFINEiGSKGVIIKGGHSNDTDIAKDYLF-TNEGVQTFENERFKTKhTHGTGCTFSAVITAELA 226
Cdd:PRK08176 167 TGKPCRTLDSAIAAAKSLLSD-TLKWVVITSAAGNEENQEMQVVVvTADSVNVISHPRVDTD-LKGTGDLFCAELVSGLL 244

                        170       180
                 ....*....|....*....|....*..
gi 582524153 227 KGRPLFEAVHKAKKFISMSIQYTPEIG 253
Cdd:PRK08176 245 KGKALTDAAHRAGLRVLEVMRYTQQAG 271
PRK07105 PRK07105
pyridoxamine kinase; Validated
 75-249 1.26e-13

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 69.17  E-value: 1.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  75 HAIKTGMIATADTMETIRHYL--MQHESIPYVIDPVMlaksGDS--LMDNDTKQNLQH--TLLPLADVVTPNLPEA---- 144
Cdd:PRK07105  77 DAIYSGYLGSPRQIQIVSDFIkyFKKKDLLVVVDPVM----GDNgkLYQGFDQEMVEEmrKLIQKADVITPNLTEAclll 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 145 -EEITGLTIDsEEKIMQAGRIfINEIGSKGVIIKGGHSNDTDIakdylftneGVQTF--ENERFkTKHTH--------GT 213
Cdd:PRK07105 153 dKPYLEKSYS-EEEIKQLLRK-LADLGPKIVIITSVPFEDGKI---------GVAYYdrATDRF-WKVFCkyipahypGT 220

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 582524153 214 GCTFSAVITAELAKGRPLFEAVHKAKKFISMSIQYT 249
Cdd:PRK07105 221 GDIFTSVITGSLLQGDSLPIALDRAVQFIEKGIRAT 256
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 79-226 2.42e-12

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: 64.04  E-value: 2.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  79 TGMIATADTMETIRHYLMQHeSIPYVIDPVMLAKSGDslmdndtKQNLQHtLLPLADVVTPNLPEAEEITGLTIDSEEKI 158
Cdd:cd00287   64 SGLSPAPEAVLDALEEARRR-GVPVVLDPGPRAVRLD-------GEELEK-LLPGVDILTPNEEEAEALTGRRDLEVKEA 134

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 159 MQAGRIfINEIGSKGVIIKGGhsndtdiAKDYLFTNEGVQTFENERF--KTKHTHGTGCTFSAVITAELA 226
Cdd:cd00287  135 AEAAAL-LLSKGPKVVIVTLG-------EKGAIVATRGGTEVHVPAFpvKVVDTTGAGDAFLAALAAGLA 196
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 79-238 2.87e-12

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 65.49  E-value: 2.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  79 TGMIATADTMETIRHYLMQ----HESIPYVIDPVMlaksGDslmDND--TKQNLQHT---LLPLADVVTPNLPEAEEITG 149
Cdd:PTZ00344  83 TGYINSADILREVLATVKEikelRPKLIFLCDPVM----GD---DGKlyVKEEVVDAyreLIPYADVITPNQFEASLLSG 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 150 LTIDSEEKIMQAGRIFiNEIGSKGVIIKGGHSNDTDIAKDYLFTNEGVQTFENERFKTK-------HThGTGCTFSAVIT 222
Cdd:PTZ00344 156 VEVKDLSDALEAIDWF-HEQGIPVVVITSFREDEDPTHLRFLLSCRDKDTKNNKRFTGKvpyiegrYT-GTGDLFAALLL 233

                        170
                 ....*....|....*.
gi 582524153 223 AELAKGrPLFEAVHKA 238
Cdd:PTZ00344 234 AFSHQH-PMDLAVGKA 248
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 128-247 2.86e-11

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: 62.57  E-value: 2.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 128 HTLLPLADVVTPNLPEAEEITGLTIDSEEKIMQAGRIFiNEIGSKGVIIKGGhsndtdiAK-DYLFTNEGVQTFENERFK 206
Cdd:cd01174  170 AELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLL-LAKGVKNVIVTLG-------AKgALLASGGEVEHVPAFKVK 241

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 582524153 207 TKHTHGTGCTFSAVITAELAKGRPLFEAVHKAKKFISMSIQ 247
Cdd:cd01174  242 AVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVT 282
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 106-249 1.45e-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: 60.43  E-value: 1.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  106 DPVMLAKSGDslmdndTKQNLQHtLLPLADVVTPNLPEAEEITGLTIDSEEKIMQAGRIFInEIGSKGVIIKGGhsndtd 185
Cdd:pfam00294 160 DPNLLDPLGA------AREALLE-LLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLL-AKGIKTVIVTLG------ 225

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 582524153  186 iakdylftNEGVQTFENER-------FKTK--HTHGTGCTFSAVITAELAKGRPLFEAVHKAKKFISMSIQYT 249
Cdd:pfam00294 226 --------ADGALVVEGDGevhvpavPKVKvvDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKS 290
PRK11142 PRK11142
ribokinase; Provisional
 81-238 6.99e-08

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 52.56  E-value: 6.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  81 MIATADTMetirhyLMQHES-IPYVIDPVMLAKSgdslmdNDTK--------QNLQHTLLPLADVVTPNLPEAEEITGLT 151
Cdd:PRK11142 129 LIANADAL------LMQLETpLETVLAAAKIAKQ------HGTKvilnpapaRELPDELLALVDIITPNETEAEKLTGIR 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 152 IDSEEKIMQAGRIF--------INEIGSKGViikgghsndtdiakdYLFTNEGVQTFENERFKTKHTHGTGCTFS-AVIT 222
Cdd:PRK11142 197 VEDDDDAAKAAQVLhqkgietvLITLGSRGV---------------WLSENGEGQRVPGFRVQAVDTIAAGDTFNgALVT 261

                        170
                 ....*....|....*....
gi 582524153 223 AELAkGRPLFEAV---HKA 238
Cdd:PRK11142 262 ALLE-GKPLPEAIrfaHAA 279
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
 134-236 7.46e-07

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: 49.48  E-value: 7.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 134 ADVVTPNLPEAEEITGLTIDSEEKIMQAGRIFINEIGSKGVIIKGGhsndtdiaKD--YLFTNEGvqtfENERFKTKHTH 211
Cdd:cd01172  182 ATLLTPNEKEAREALGDEINDDDELEAAGEKLLELLNLEALLVTLG--------EEgmTLFERDG----EVQHIPALAKE 249

                         90       100       110
                 ....*....|....*....|....*....|
gi 582524153 212 -----GTGCTFSAVITAELAKGRPLFEAVH 236
Cdd:cd01172  250 vydvtGAGDTVIATLALALAAGADLEEAAF 279
PRK05756 PRK05756
pyridoxal kinase PdxY;
103-234 1.02e-06

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 49.10  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 103 YVIDPVMlaksGDSL----MDNDTKQNLQHTLLPLADVVTPNLPEAEEITGLTIDSEEKIMQAGRIFInEIGSKGVIIKG 178
Cdd:PRK05756 108 YFCDPVM----GDPEkgciVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETLEDAVAAARALI-ARGPKIVLVTS 182

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 582524153 179 GHSNDTDIAK--DYLFTNEG---VQT----FENERfktkhtHGTGCTFSAVITAELAKGRPLFEA 234
Cdd:PRK05756 183 LARAGYPADRfeMLLVTADGawhISRplvdFMRQP------VGVGDLTSALFLARLLQGGSLEEA 241
PLN02978 PLN02978
pyridoxal kinase
 70-176 1.43e-06

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 48.58  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  70 NDTLPHA-IKTGMIATADTMETIR---HYLMQHES-IPYVIDPVMlAKSGDSLMDNDTKQNLQHTLLPLADVVTPNLPEA 144
Cdd:PLN02978  82 NGLLFYThLLTGYIGSVSFLRTVLrvvKKLRSVNPnLTYVCDPVL-GDEGKLYVPPELVPVYREKVVPLATMLTPNQFEA 160

                         90       100       110
                 ....*....|....*....|....*....|..
gi 582524153 145 EEITGLTIDSEEKIMQAGRIfINEIGSKGVII 176
Cdd:PLN02978 161 EQLTGIRIVTEEDAREACAI-LHAAGPSKVVI 191
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 83-238 5.17e-06

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


Pssm-ID: 440290 [Multi-domain]  Cd Length: 301  Bit Score: 46.80  E-value: 5.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153  83 ATADTMETIRHYL--MQHESIPYVIDPvmlakSGDSLMDNDTKQNLQHtLLPLADVVTPNLPEAEEITGltIDSEEKIMQ 160
Cdd:COG0524  139 ASEPPREALLAALeaARAAGVPVSLDP-----NYRPALWEPARELLRE-LLALVDILFPNEEEAELLTG--ETDPEEAAA 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 161 AgrifINEIGSKGVIIKGGhsndtdiaKD--YLFTNEGVQTFENERFKTKHTHGTGCTFSAVITAELAKGRPLFEAVHKA 238
Cdd:COG0524  211 A----LLARGVKLVVVTLG--------AEgaLLYTGGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFA 278
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
 7-235 2.90e-04

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


Pssm-ID: 396007  Cd Length: 242  Bit Score: 41.20  E-value: 2.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153    7 ALTIAGTDPTGGAGVMADLksfhSCGVYGMGVVTSIVAQNTLGVQHIH--NLNHQWVDEQldSVFNDTLPH----AIKTG 80
Cdd:pfam01256   1 VLVIGGSKDYTGAPLLAAL----AALRSGAGLVSVATDSEAIAVLKSPlpEVMVHPLPET--SSILEKLSRydavVIGPG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153   81 MIATADTMETIRHYLMQHEsiPYVIDpvmlaksGDSLmdNDTKQNLQHTLLPLADVVTPNLPEAEEITGLTIDSEEKIMQ 160
Cdd:pfam01256  75 LGRDEKGKAALEEVLAKDC--PLVID-------ADAL--NLLAINNEKPAREGPTVLTPHPGEFERLCGLAGILGDDRLE 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 582524153  161 AGRIFINEIGSKgVIIKGGHsndtdiakDYLFTNEGvQTFENERFKT-KHTHGTGCTFSAVITAELAKGRPLFEAV 235
Cdd:pfam01256 144 AARELAQKLNGT-ILLKGNV--------TVIAAPGG-EVWINSTGNSaLAKGGSGDVLAGLIGGLLAQNEDPYDAA 209
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 126-235 3.60e-04

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


Pssm-ID: 238916 [Multi-domain]  Cd Length: 288  Bit Score: 41.15  E-value: 3.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 126 LQHTLLPLA--DVVTPNLPEAEEITGLTIDSEEKIMQAGRIFInEIGSKGVIIKGGhsndtdiAKD-YLFTNEGVQTFEN 202
Cdd:cd01941  167 LKKLFYLLHaiDLLTPNRAELEALAGALIENNEDENKAAKILL-LPGIKNVIVTLG-------AKGvLLSSREGGVETKL 238

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 582524153 203 ERFKTKHT----HGTGCTFSAVITAELAKGRPLFEAV 235
Cdd:cd01941  239 FPAPQPETvvnvTGAGDAFVAGLVAGLLEGMSLDDSL 275
PTZ00292 PTZ00292
ribokinase; Provisional
 130-247 7.89e-03

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 37.02  E-value: 7.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582524153 130 LLPLADVVTPNLPEAEEITGLTIDSEEKIMQAGRIFINeIGSKGVIIKGGhsndtdiAKDYLFTNEGVQT--FENERFKT 207
Cdd:PTZ00292 195 FLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQ-LGVENVIITLG-------ANGCLIVEKENEPvhVPGKRVKA 266

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 582524153 208 KHTHGTGCTFSAVITAELAKGRPLFEAVHKAKKFISMSIQ 247
Cdd:PTZ00292 267 VDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVT 306
 
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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