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Conserved domains on  [gi|1478758191|gb|RIQ50085|]
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pyridoxine/pyridoxal/pyridoxamine kinase [Bordetella avium]

Protein Classification

carbohydrate kinase family protein( domain architecture ID 399)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ribokinase_pfkB_like super family cl00192
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 1-282 1.59e-148

ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).


The actual alignment was detected with superfamily member PRK08176:

Pssm-ID: 469648 [Multi-domain]  Cd Length: 281  Bit Score: 417.52  E-value: 1.59e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191   1 MSSGQGYVASGRPLLFDVVSVQSQVVYGHVGNNVAAPALRAHGLHPGIVPTVLLSNTPHYPTLHGGALPLSWFEGYLQDL 80
Cdd:PRK08176    1 MSSLLLFNDKSRALQADIVAVQSQVVYGSVGNSIAVPAIKANGLRVFAVPTVLLSNTPHYPTFYGGAIPDEWFSGYLRAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191  81 QARGALQALRAILVGYLGSAEQARVLGRWIARIREVHPQVLVIVDPVMGDDDHGLYVTEGLAEASRECLVPQAHGLTPNS 160
Cdd:PRK08176   81 QERDALRQLRAVTTGYMGSASQIKILAEWLTALRADHPDLLIMVDPVIGDIDSGIYVKPDLPEAYRQHLLPLAQGLTPNI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 161 FELGLLTGCEVGRVDQAVAAARRLLAQGLRWVVVTSAAQQDcPPGQVQLLAVTASQAHLLRHQRVDTAPKGTGDLFCAEL 240
Cdd:PRK08176  161 FELEILTGKPCRTLDSAIAAAKSLLSDTLKWVVITSAAGNE-ENQEMQVVVVTADSVNVISHPRVDTDLKGTGDLFCAEL 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1478758191 241 TAHLLAGASLERAVEASSRYLVQALACTRLADSAELLMPSRD 282
Cdd:PRK08176  240 VSGLLKGKALTDAAHRAGLRVLEVMRYTQQAGSDELILPPLA 281
 
Name Accession Description Interval E-value
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
1-282 1.59e-148

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 417.52  E-value: 1.59e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191   1 MSSGQGYVASGRPLLFDVVSVQSQVVYGHVGNNVAAPALRAHGLHPGIVPTVLLSNTPHYPTLHGGALPLSWFEGYLQDL 80
Cdd:PRK08176    1 MSSLLLFNDKSRALQADIVAVQSQVVYGSVGNSIAVPAIKANGLRVFAVPTVLLSNTPHYPTFYGGAIPDEWFSGYLRAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191  81 QARGALQALRAILVGYLGSAEQARVLGRWIARIREVHPQVLVIVDPVMGDDDHGLYVTEGLAEASRECLVPQAHGLTPNS 160
Cdd:PRK08176   81 QERDALRQLRAVTTGYMGSASQIKILAEWLTALRADHPDLLIMVDPVIGDIDSGIYVKPDLPEAYRQHLLPLAQGLTPNI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 161 FELGLLTGCEVGRVDQAVAAARRLLAQGLRWVVVTSAAQQDcPPGQVQLLAVTASQAHLLRHQRVDTAPKGTGDLFCAEL 240
Cdd:PRK08176  161 FELEILTGKPCRTLDSAIAAAKSLLSDTLKWVVITSAAGNE-ENQEMQVVVVTADSVNVISHPRVDTDLKGTGDLFCAEL 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1478758191 241 TAHLLAGASLERAVEASSRYLVQALACTRLADSAELLMPSRD 282
Cdd:PRK08176  240 VSGLLKGKALTDAAHRAGLRVLEVMRYTQQAGSDELILPPLA 281
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 27-277 5.08e-94

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: 278.95  E-value: 5.08e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191  27 YGHVGNNVAAPALRAHGLHPGIVPTVLLSNTPHYPTLHGGALPLSWFEGYLQDLQARGALQALRAILVGYLGSAEQARVL 106
Cdd:COG2240    13 YGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLLEFDAVLSGYLGSAEQGDII 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 107 GRWIARIREVHPQVLVIVDPVMGDDDHGLYVTEGLAEASRECLVPQAHGLTPNSFELGLLTGCEVGRVDQAVAAARRLLA 186
Cdd:COG2240    93 ADFVARVKAANPDALYLCDPVMGDNGKGYYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETLEEALAAARALLA 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 187 QGLRWVVVTSAAQQDCPPGQVQLLAVTASQAHLLRHQRVDTAPKGTGDLFCAELTAHLLAGASLERAVEASSRYLVQALA 266
Cdd:COG2240   173 LGPKIVVVTSVPLDDTPADKIGNLAVTADGAWLVETPLLPFSPNGTGDLFAALLLAHLLRGKSLEEALERAAAFVYEVLE 252

                         250
                  ....*....|.
gi 1478758191 267 CTRLADSAELL 277
Cdd:COG2240   253 RTAAAGSDELL 263
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 27-269 1.33e-76

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: 234.02  E-value: 1.33e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191  27 YGHVGNNVAAPALRAHGLHPGIVPTVLLSNTPHYPTLHGGALPLSWFEGYLQDLQARGALQALRAILVGYLGSAEQARVL 106
Cdd:cd01173    11 HGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLLLEYDAVLTGYLGSAEQVEAV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 107 GRWIARIREVHPQVLVIVDPVMGDDDHGLYVTEGLAEASRECLVPQAHGLTPNSFELGLLTGCEVGRVDQAVAAARRLLA 186
Cdd:cd01173    91 AEIVKRLKEKNPNLLYVCDPVMGDNGKLYVVAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLEDAKAAARALHA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 187 QGLRWVVVTSAAQQDcpPGQVQLLAVTASQAHLLRHQRVD--TAPKGTGDLFCAELTAHLLAGASLERAVEASSRYLVQA 264
Cdd:cd01173   171 KGPKTVVVTSVELAD--DDRIEMLGSTATEAWLVQRPKIPfpAYFNGTGDLFAALLLARLLKGKSLAEALEKALNFVHEV 248


                  ....*
gi 1478758191 265 LACTR 269
Cdd:cd01173   249 LEATY 253
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
 27-282 2.42e-38

pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal/pyridoxamine kinase, but mutants lacking PdxK activity retain a specific pyridoxal kinase, PdxY. PdxY acts in the salvage pathway of pyridoxal 5'-phosphate biosynthesis. Mammalian forms of pyridoxal kinase are more similar to PdxY than to PdxK. The PdxK isozyme is omitted from the seed alignment but scores above the trusted cutoff.ThiD and related proteins form an outgroup. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]


Pssm-ID: 273221 [Multi-domain]  Cd Length: 287  Bit Score: 136.50  E-value: 2.42e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191  27 YGHVGNNVAAPALRAHGLHPGIVPTVLLSNTPHYPTLHGGALPLSWFEGYLQDLQARGALQALRAILVGYLGSAEQ-ARV 105
Cdd:TIGR00687  13 YGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAINKLNQCDAVLSGYLGSAEQvAMV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 106 LGRwIARIREVHPQVLVIVDPVMGDDDHGLYVTEGLAEASRECLVPQAHGLTPNSFELGLLTGCEVGRVDQAVAAARRLL 185
Cdd:TIGR00687  93 VGI-VRQVKQANPQALYVCDPVMGDPWKGCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTEEEALAAADALI 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 186 AQGLRWVVVTSAAQQDCPPGQ-VQLLAVTASQAHLLRHQRV--DTAPKGTGDLFCAELTAHLLAGASLERAVEASSRYLV 262
Cdd:TIGR00687 172 AMGPDIVLVTHLIRAGSQRDRsFEGLVATQEGRWHISRPLAvfDPPPVGTGDLIAALLLATLLHGNSLKEALEKTVSAVY 251

                         250       260
                  ....*....|....*....|.
gi 1478758191 263 QALACTRLADSAEL-LMPSRD 282
Cdd:TIGR00687 252 HVLRTTIQLGKYELqPVAAQL 272
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 91-266 1.29e-15

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: 74.44  E-value: 1.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191  91 AILVGYLGSAEQARVLGRWIArirevHPQVLVIVDPVMGDDDHGLYVTEGLAEASRECLVPQAHGLTPNSFELGLLTGCE 170
Cdd:pfam08543  63 AVKTGMLGSAEIIEAVAEKLD-----KYGVPVVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 171 VGRVDQAVAAARRLLAQGLRWVVVTsAAQQDCPPGQVQLLAVTASQAHLLRHQRVDTapK---GTGDLFCAELTAHLLAG 247
Cdd:pfam08543 138 IKTLEDMKEAAKKLLALGAKAVLIK-GGHLEGEEAVVTDVLYDGGGFYTLEAPRIPT--KnthGTGCTLSAAIAANLAKG 214

                         170
                  ....*....|....*....
gi 1478758191 248 ASLERAVEASSRYLVQALA 266
Cdd:pfam08543 215 LSLPEAVREAKEYVTEAIR 233
 
Name Accession Description Interval E-value
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
1-282 1.59e-148

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 417.52  E-value: 1.59e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191   1 MSSGQGYVASGRPLLFDVVSVQSQVVYGHVGNNVAAPALRAHGLHPGIVPTVLLSNTPHYPTLHGGALPLSWFEGYLQDL 80
Cdd:PRK08176    1 MSSLLLFNDKSRALQADIVAVQSQVVYGSVGNSIAVPAIKANGLRVFAVPTVLLSNTPHYPTFYGGAIPDEWFSGYLRAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191  81 QARGALQALRAILVGYLGSAEQARVLGRWIARIREVHPQVLVIVDPVMGDDDHGLYVTEGLAEASRECLVPQAHGLTPNS 160
Cdd:PRK08176   81 QERDALRQLRAVTTGYMGSASQIKILAEWLTALRADHPDLLIMVDPVIGDIDSGIYVKPDLPEAYRQHLLPLAQGLTPNI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 161 FELGLLTGCEVGRVDQAVAAARRLLAQGLRWVVVTSAAQQDcPPGQVQLLAVTASQAHLLRHQRVDTAPKGTGDLFCAEL 240
Cdd:PRK08176  161 FELEILTGKPCRTLDSAIAAAKSLLSDTLKWVVITSAAGNE-ENQEMQVVVVTADSVNVISHPRVDTDLKGTGDLFCAEL 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1478758191 241 TAHLLAGASLERAVEASSRYLVQALACTRLADSAELLMPSRD 282
Cdd:PRK08176  240 VSGLLKGKALTDAAHRAGLRVLEVMRYTQQAGSDELILPPLA 281
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 27-277 5.08e-94

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: 278.95  E-value: 5.08e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191  27 YGHVGNNVAAPALRAHGLHPGIVPTVLLSNTPHYPTLHGGALPLSWFEGYLQDLQARGALQALRAILVGYLGSAEQARVL 106
Cdd:COG2240    13 YGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLLEFDAVLSGYLGSAEQGDII 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 107 GRWIARIREVHPQVLVIVDPVMGDDDHGLYVTEGLAEASRECLVPQAHGLTPNSFELGLLTGCEVGRVDQAVAAARRLLA 186
Cdd:COG2240    93 ADFVARVKAANPDALYLCDPVMGDNGKGYYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETLEEALAAARALLA 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 187 QGLRWVVVTSAAQQDCPPGQVQLLAVTASQAHLLRHQRVDTAPKGTGDLFCAELTAHLLAGASLERAVEASSRYLVQALA 266
Cdd:COG2240   173 LGPKIVVVTSVPLDDTPADKIGNLAVTADGAWLVETPLLPFSPNGTGDLFAALLLAHLLRGKSLEEALERAAAFVYEVLE 252

                         250
                  ....*....|.
gi 1478758191 267 CTRLADSAELL 277
Cdd:COG2240   253 RTAAAGSDELL 263
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 27-269 1.33e-76

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: 234.02  E-value: 1.33e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191  27 YGHVGNNVAAPALRAHGLHPGIVPTVLLSNTPHYPTLHGGALPLSWFEGYLQDLQARGALQALRAILVGYLGSAEQARVL 106
Cdd:cd01173    11 HGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLLLEYDAVLTGYLGSAEQVEAV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 107 GRWIARIREVHPQVLVIVDPVMGDDDHGLYVTEGLAEASRECLVPQAHGLTPNSFELGLLTGCEVGRVDQAVAAARRLLA 186
Cdd:cd01173    91 AEIVKRLKEKNPNLLYVCDPVMGDNGKLYVVAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLEDAKAAARALHA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 187 QGLRWVVVTSAAQQDcpPGQVQLLAVTASQAHLLRHQRVD--TAPKGTGDLFCAELTAHLLAGASLERAVEASSRYLVQA 264
Cdd:cd01173   171 KGPKTVVVTSVELAD--DDRIEMLGSTATEAWLVQRPKIPfpAYFNGTGDLFAALLLARLLKGKSLAEALEKALNFVHEV 248


                  ....*
gi 1478758191 265 LACTR 269
Cdd:cd01173   249 LEATY 253
PRK05756 PRK05756
pyridoxal kinase PdxY;
27-277 4.04e-56

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 182.76  E-value: 4.04e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191  27 YGHVGNNVAAPALRAHGLHPGIVPTVLLSNTPHYPTLHGGALPLSWFEGYLQDLQARGALQALRAILVGYLGSAEQARVL 106
Cdd:PRK05756   13 YGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGECDAVLSGYLGSAEQGEAI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 107 GRWIARIREVHPQVLVIVDPVMGDDDHGLYVTEGLAEASRECLVPQAHGLTPNSFELGLLTGCEVGRVDQAVAAARRLLA 186
Cdd:PRK05756   93 LDAVRRVKAANPQALYFCDPVMGDPEKGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETLEDAVAAARALIA 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 187 QGLRWVVVTSAAQQDCPPGQVQLLAVTASQAHLLRHQRVD--TAPKGTGDLFCAELTAHLLAGASLERAVE--ASSRYLV 262
Cdd:PRK05756  173 RGPKIVLVTSLARAGYPADRFEMLLVTADGAWHISRPLVDfmRQPVGVGDLTSALFLARLLQGGSLEEALEhtTAAVYEV 252

                         250
                  ....*....|....*
gi 1478758191 263 qaLACTRLADSAELL 277
Cdd:PRK05756  253 --MARTKERGSYELQ 265
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
 27-282 2.42e-38

pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal/pyridoxamine kinase, but mutants lacking PdxK activity retain a specific pyridoxal kinase, PdxY. PdxY acts in the salvage pathway of pyridoxal 5'-phosphate biosynthesis. Mammalian forms of pyridoxal kinase are more similar to PdxY than to PdxK. The PdxK isozyme is omitted from the seed alignment but scores above the trusted cutoff.ThiD and related proteins form an outgroup. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]


Pssm-ID: 273221 [Multi-domain]  Cd Length: 287  Bit Score: 136.50  E-value: 2.42e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191  27 YGHVGNNVAAPALRAHGLHPGIVPTVLLSNTPHYPTLHGGALPLSWFEGYLQDLQARGALQALRAILVGYLGSAEQ-ARV 105
Cdd:TIGR00687  13 YGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAINKLNQCDAVLSGYLGSAEQvAMV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 106 LGRwIARIREVHPQVLVIVDPVMGDDDHGLYVTEGLAEASRECLVPQAHGLTPNSFELGLLTGCEVGRVDQAVAAARRLL 185
Cdd:TIGR00687  93 VGI-VRQVKQANPQALYVCDPVMGDPWKGCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTEEEALAAADALI 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 186 AQGLRWVVVTSAAQQDCPPGQ-VQLLAVTASQAHLLRHQRV--DTAPKGTGDLFCAELTAHLLAGASLERAVEASSRYLV 262
Cdd:TIGR00687 172 AMGPDIVLVTHLIRAGSQRDRsFEGLVATQEGRWHISRPLAvfDPPPVGTGDLIAALLLATLLHGNSLKEALEKTVSAVY 251

                         250       260
                  ....*....|....*....|.
gi 1478758191 263 QALACTRLADSAEL-LMPSRD 282
Cdd:TIGR00687 252 HVLRTTIQLGKYELqPVAAQL 272
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 28-242 2.54e-30

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 115.56  E-value: 2.54e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191  28 GHVGNNVAAPALRAHGLHPGIVPTVLLSNTPHYPTLHGGALPLSWFEGYLQDLQARGALQALRAILVGYLGSAEQARVLG 107
Cdd:PTZ00344   17 GYVGNRAATFPLQLLGFDVDFVNTVQLSNHTGYPVIKGHRLDLNELITLMDGLRANNLLSDYTYVLTGYINSADILREVL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 108 RWIARIREVHPQVLVIVDPVMGDDDHgLYVTEGLAEASREcLVPQAHGLTPNSFELGLLTGCEVGRVDQAVAAARRLLAQ 187
Cdd:PTZ00344   97 ATVKEIKELRPKLIFLCDPVMGDDGK-LYVKEEVVDAYRE-LIPYADVITPNQFEASLLSGVEVKDLSDALEAIDWFHEQ 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 188 GLRWVVVTSAAQQDCPPGQVQLLAVTASQA-----HLLRHQRVDTAPKGTGDLFCAELTA 242
Cdd:PTZ00344  175 GIPVVVITSFREDEDPTHLRFLLSCRDKDTknnkrFTGKVPYIEGRYTGTGDLFAALLLA 234
PLN02978 PLN02978
pyridoxal kinase
 28-255 1.80e-23

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 97.50  E-value: 1.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191  28 GHVGNNVAAPALRAHGLHPGIVPTVLLSNTPHYPTLHGGALPLSWFEGYLQDLQARGALQALRaILVGYLGSAEQARVLG 107
Cdd:PLN02978   27 GYVGNKSAVFPLQLLGFDVDPINSVQFSNHTGYPTFKGQVLDGEQLWALIEGLEANGLLFYTH-LLTGYIGSVSFLRTVL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 108 RWIARIREVHPQVLVIVDPVMGDDDHgLYVTEGLAEASRECLVPQAHGLTPNSFELGLLTGCEVGRVDQAVAAARRLLAQ 187
Cdd:PLN02978  106 RVVKKLRSVNPNLTYVCDPVLGDEGK-LYVPPELVPVYREKVVPLATMLTPNQFEAEQLTGIRIVTEEDAREACAILHAA 184

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1478758191 188 GLRWVVVTSAAqqdcPPGQVQLLAVTASQAHLLRHQRVDTAPK------GTGDLFCAELTAHLLAGA-SLERAVE 255
Cdd:PLN02978  185 GPSKVVITSID----IDGKLLLVGSHRKEKGARPEQFKIVIPKipayftGTGDLMAALLLGWSHKYPdNLDKAAE 255
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 90-266 4.80e-22

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: 92.41  E-value: 4.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191  90 RAILVGYLGSAEQARVLGRWIARirevHPQVLVIVDPVM--GDDDHGLyvTEGLAEASRECLVPQAHGLTPNSFELGLLT 167
Cdd:COG0351    68 DAIKIGMLGSAEIIEAVAEILAD----YPLVPVVLDPVMvaKSGDRLL--DEDAVEALRELLLPLATVVTPNLPEAEALL 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 168 GCEVGRVDQAVAAARRLLAQGLRWVVVTSAAQQDcppGQVQLLAVTASQAHLLRHQRVDTAPK-GTGDLFCAELTAHLLA 246
Cdd:COG0351   142 GIEITTLDDMREAAKALLELGAKAVLVKGGHLPG---DEAVDVLYDGDGVREFSAPRIDTGNThGTGCTLSSAIAALLAK 218

                         170       180
                  ....*....|....*....|
gi 1478758191 247 GASLERAVEASSRYLVQALA 266
Cdd:COG0351   219 GLDLEEAVREAKEYVTQAIR 238
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 81-266 3.42e-19

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: 84.48  E-value: 3.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191  81 QARGALQALR--AILVGYLGSAEQARVLGRWIARirevHPQVLVIVDPVM----GDDdhglYVTEGLAEASRECLVPQAH 154
Cdd:cd01169    59 QLDAVLEDIPvdAIKIGMLGSAEIIEAVAEALKD----YPDIPVVLDPVMvaksGDS----LLDDDAIEALRELLLPLAT 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 155 GLTPNSFELGLLTGCEVGRVDQAVAAARRLLAQGLRWVVVTSAAqqdCPPGQVQLLAVTASQAHLLRHQRVDTAPK-GTG 233
Cdd:cd01169   131 LITPNLPEAELLTGLEIATEEDMMKAAKALLALGAKAVLIKGGH---LPGDEAVDVLYDGGGFFEFESPRIDTKNThGTG 207

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1478758191 234 DLFCAELTAHLLAGASLERAVEASSRYLVQALA 266
Cdd:cd01169   208 CTLSSAIAANLAKGLSLEEAVREAKEYVTQAIR 240
PRK07105 PRK07105
pyridoxamine kinase; Validated
 27-268 2.44e-18

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 83.04  E-value: 2.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191  27 YGHVGNNVAAPALRAHGLHPGIVPTVLLSNtphyptlHGGALPLSWFEGYLQDLQA-RGALQALR----AILVGYLGSAE 101
Cdd:PRK07105   16 FGRVALTASIPIMSSMGLQVCPLPTALLSS-------HTGGFQNPSIIDLTDGMQAfLTHWKSLNlkfdAIYSGYLGSPR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 102 QARVLGRWIARIREvhPQVLVIVDPVMGDDdhG-LY--VTEGLAEASREcLVPQAHGLTPNSFELGLLTG-----CEVGR 173
Cdd:PRK07105   89 QIQIVSDFIKYFKK--KDLLVVVDPVMGDN--GkLYqgFDQEMVEEMRK-LIQKADVITPNLTEACLLLDkpyleKSYSE 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 174 vDQAVAAARRLLAQGLRWVVVTSAaqqdcpPGQVQLLAVTASQA-----HLLRHQRVDTAPKGTGDLFCAELTAHLLAGA 248
Cdd:PRK07105  164 -EEIKQLLRKLADLGPKIVIITSV------PFEDGKIGVAYYDRatdrfWKVFCKYIPAHYPGTGDIFTSVITGSLLQGD 236

                         250       260
                  ....*....|....*....|
gi 1478758191 249 SLERAVEASSRYLVQALACT 268
Cdd:PRK07105  237 SLPIALDRAVQFIEKGIRAT 256
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 91-266 1.29e-15

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: 74.44  E-value: 1.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191  91 AILVGYLGSAEQARVLGRWIArirevHPQVLVIVDPVMGDDDHGLYVTEGLAEASRECLVPQAHGLTPNSFELGLLTGCE 170
Cdd:pfam08543  63 AVKTGMLGSAEIIEAVAEKLD-----KYGVPVVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 171 VGRVDQAVAAARRLLAQGLRWVVVTsAAQQDCPPGQVQLLAVTASQAHLLRHQRVDTapK---GTGDLFCAELTAHLLAG 247
Cdd:pfam08543 138 IKTLEDMKEAAKKLLALGAKAVLIK-GGHLEGEEAVVTDVLYDGGGFYTLEAPRIPT--KnthGTGCTLSAAIAANLAKG 214

                         170
                  ....*....|....*....
gi 1478758191 248 ASLERAVEASSRYLVQALA 266
Cdd:pfam08543 215 LSLPEAVREAKEYVTEAIR 233
HMP-P_kinase TIGR00097
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ...
 95-266 2.48e-13

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: 68.47  E-value: 2.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191  95 GYLGSAEQARVLGRwiaRIREVHPQVLViVDPVMGDDDHGLYVTEGLAEASRECLVPQAHGLTPNSFELGLLTGCEVGRV 174
Cdd:TIGR00097  74 GMLASAEIVEAVAR---KLREYPVRPLV-VDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGTKIRTE 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 175 DQAVAAARRLLAQGLRWVVVTSAAQQDCPPGQVqllAVTASQAHLLRHQRVDTA-PKGTGDLFCAELTAHLLAGASLERA 253
Cdd:TIGR00097 150 QDMIKAAKKLRELGPKAVLIKGGHLEGDQAVDV---LFDGGEIHILKAPRIETKnTHGTGCTLSAAIAANLAKGLSLKEA 226

                         170
                  ....*....|...
gi 1478758191 254 VEASSRYLVQALA 266
Cdd:TIGR00097 227 VKEAKEFVTGAIR 239
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 89-266 3.12e-12

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 65.15  E-value: 3.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191  89 LRAILVGYLGSAEQARVlgrwIARIREVHPQVLVIVDPVM--------GDDDHGlyvteglaEASRECLVPQAHGLTPNS 160
Cdd:PRK06427   74 IDAVKIGMLASAEIIET----VAEALKRYPIPPVVLDPVMiaksgdplLADDAV--------AALRERLLPLATLITPNL 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 161 FELGLLTGCEVGR-VDQAVAAARRLLAQGLRWVVVTSAAQQDCPPGqVQLLaVTASQAHLLRHQRVDTAP-KGTGDLFCA 238
Cdd:PRK06427  142 PEAEALTGLPIADtEDEMKAAARALHALGCKAVLIKGGHLLDGEES-VDWL-FDGEGEERFSAPRIPTKNtHGTGCTLSA 219

                         170       180
                  ....*....|....*....|....*...
gi 1478758191 239 ELTAHLLAGASLERAVEASSRYLVQALA 266
Cdd:PRK06427  220 AIAAELAKGASLLDAVQTAKDYVTRAIR 247
PRK12616 PRK12616
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
122-265 9.17e-11

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183624  Cd Length: 270  Bit Score: 61.21  E-value: 9.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 122 VIVDPVM--GDDDHGLYVTEglAEASRECLVPQAHGLTPNSFELGLLTGC-EVGRVDQAVAAARRLLAQGLRWVVVTSAA 198
Cdd:PRK12616  104 VVIDPVMvcKGANEVLYPEH--AEALREQLAPLATVITPNLFEAGQLSGMgEIKTVEQMKEAAKKIHELGAQYVVITGGG 181

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1478758191 199 QQDcPPGQVQLLaVTASQAHLLRHQRVDTA-PKGTGDLFCAELTAHLLAGASLERAVEASSRYLVQAL 265
Cdd:PRK12616  182 KLK-HEKAVDVL-YDGETAEVLESEMIDTPyTHGAGCTFSAAVTAELAKGSEVKEAIYAAKEFITAAI 247
PRK14713 PRK14713
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
88-266 8.22e-10

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 237797 [Multi-domain]  Cd Length: 530  Bit Score: 59.42  E-value: 8.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191  88 ALRAILVGYLGSAEQARVLGRWIARirevHPQVLVIVDPVM----GDDdhglyVTEGLAEASRECLVPQAHGLTPNSFEL 163
Cdd:PRK14713   98 TVDAVKIGMLGDAEVIDAVRTWLAE----HRPPVVVLDPVMvatsGDR-----LLEEDAEAALRELVPRADLITPNLPEL 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 164 GLLTGCEVGRvdqavaAARRLLAQGLRWVVVTSAA---------QQDCPpgqvQLLAVTASQAHLLRHQRVDT-APKGTG 233
Cdd:PRK14713  169 AVLLGEPPAT------TWEEALAQARRLAAETGTTvlvkgghldGQRAP----DALVGPDGAVTEVPGPRVDTrNTHGTG 238

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1478758191 234 DLFCAELTAHLLAGASLERAVEASSRYLVQALA 266
Cdd:PRK14713  239 CSLSSALATRLGRGGDWAAALRWATAWLHGAIA 271
PRK12412 PRK12412
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
51-265 4.08e-09

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183512 [Multi-domain]  Cd Length: 268  Bit Score: 56.13  E-value: 4.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191  51 TVLLSNTPHYPTLHG-GALPLSWFEGYLQDLQARGALQALRAilvGYLGSAEQARVLGRWIarirEVHPQVLVIVDPVMg 129
Cdd:PRK12412   37 TTIVTMDPHNGWAHNvFPIPASTLKPQLETTIEGVGVDALKT---GMLGSVEIIEMVAETI----EKHNFKNVVVDPVM- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 130 dddhglyVTEGLAEA--------SRECLVPQAHGLTPNSFELGLLTGCEVGRVDQAVAAARRLLAQGLRWVVVTSAAQqd 201
Cdd:PRK12412  109 -------VCKGADEAlhpetndcLRDVLVPKALVVTPNLFEAYQLSGVKINSLEDMKEAAKKIHALGAKYVLIKGGSK-- 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1478758191 202 CPPGQVQLLAVTASQAHLLRHQRVDTA-PKGTGDLFCAELTAHLLAGASLERAVEASSRYLVQAL 265
Cdd:PRK12412  180 LGTETAIDVLYDGETFDLLESEKIDTTnTHGAGCTYSAAITAELAKGKPVKEAVKTAKEFITAAI 244
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 156-270 3.41e-08

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: 53.71  E-value: 3.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 156 LTPNSFELGLLTGCEVGRVDQAVAAARRLLAQGLRWVVVTSAAQQD--CPPGQVQLLAVTASQAhllrhqrVDTApkGTG 233
Cdd:cd01174   179 LVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGAllASGGEVEHVPAFKVKA-------VDTT--GAG 249

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1478758191 234 DLFCAELTAHLLAGASLERAVEASSRylVQALACTRL 270
Cdd:cd01174   250 DTFIGALAAALARGLSLEEAIRFANA--AAALSVTRP 284
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 149-269 2.53e-07

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 51.19  E-value: 2.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 149 LVPQAHGLTPNSFELGLLTGCEVGRVDQAVAAARRLLAQGLRWVVVTSAAQqdcppG-----QVQLLAVTASQAHLLrhq 223
Cdd:pfam00294 177 LLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGAD-----GalvveGDGEVHVPAVPKVKV--- 248

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1478758191 224 rVDTApkGTGDLFCAELTAHLLAGASLERAVEASSRylVQALACTR 269
Cdd:pfam00294 249 -VDTT--GAGDSFVGGFLAGLLAGKSLEEALRFANA--AAALVVQK 289
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 95-266 4.08e-06

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 47.84  E-value: 4.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191  95 GYLGSAEQARVLgrwIARIREvHPQVLVIVDPVM----GDDdhglyvtegLAEAS-----RECLVPQAHGLTPNSFELG- 164
Cdd:PLN02898   85 GMLPSAEIVKVL---CQALKE-FPVKALVVDPVMvstsGDV---------LAGPSilsalREELLPLATIVTPNVKEASa 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 165 LLTGCEVGRVDQAVAAARRLLAQGLRWVVVTSAAQqdcpPGQVQLLAV--TASQAHLLRHQRVDT-APKGTGDLFCAELT 241
Cdd:PLN02898  152 LLGGDPLETVADMRSAAKELHKLGPRYVLVKGGHL----PDSLDAVDVlyDGTEFHELRSSRIKTrNTHGTGCTLASCIA 227

                         170       180
                  ....*....|....*....|....*
gi 1478758191 242 AHLLAGASLERAVEASSRYLVQALA 266
Cdd:PLN02898  228 AELAKGSDMLSAVKVAKRYVETALE 252
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
123-266 4.15e-05

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 44.72  E-value: 4.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 123 IVDPVMGDDDHGLYVTEGLAEASRECLVPQAHGLTPNSFELGLLTGCEVGRVDQAVAAARRLLAQ-GLRWVVVTSAAQQD 201
Cdd:PRK08573  101 VVDPVMIAKSGAPLLREDAVDALIKRLLPLATVVTPNRPEAEKLTGMKIRSVEDARKAAKYIVEElGAEAVVVKGGHLEG 180

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1478758191 202 cpPGQVQLLAVTASqAHLLRHQRVDT-APKGTGDLFCAELTAHLLAGASLERAVEASSRYLVQALA 266
Cdd:PRK08573  181 --EEAVDVLYHNGT-FREFRAPRVESgCTHGTGCSFSAAIAAGLAKGLDPEEAIKTAKKFITMAIK 243
PTZ00347 PTZ00347
phosphomethylpyrimidine kinase; Provisional
 89-265 1.93e-04

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240375 [Multi-domain]  Cd Length: 504  Bit Score: 42.64  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191  89 LRAILVGYLGSAEQARVLGRWIARIRevhpqvlVIVDPVM----GDDDHGLYVTEGLAEASRECLVPQAHGLTPNSFELG 164
Cdd:PTZ00347  300 ISVVKLGLVPTARQLEIVIEKLKNLP-------MVVDPVLvatsGDDLVAQKNADDVLAMYKERIFPMATIITPNIPEAE 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 165 LLTG-CEVGRVDQAVAAARRLLAQGLRWVVVTSAAQQDCPPGQVQLL-AVTASQAHLLRHQRVDTA-PKGTGDLFCAELT 241
Cdd:PTZ00347  373 RILGrKEITGVYEARAAAQALAQYGSRYVLVKGGHDLIDPEACRDVLyDREKDRFYEFTANRIATInTHGTGCTLASAIS 452

                         170       180
                  ....*....|....*....|....
gi 1478758191 242 AHLLAGASLERAVEASSRYLVQAL 265
Cdd:PTZ00347  453 SFLARGYTVPDAVERAIGYVHEAI 476
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 85-282 4.35e-04

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: 41.02  E-value: 4.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191  85 ALQALRAILV-GYLGSAEQAR-VLGRWIARIREVHpqVLVIVDPvmgddDHGLYVTEGLAEASREcLVPQAHGLTPNSFE 162
Cdd:COG0524   124 LLAGADILHLgGITLASEPPReALLAALEAARAAG--VPVSLDP-----NYRPALWEPARELLRE-LLALVDILFPNEEE 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 163 LGLLTGcevgrVDQAVAAARRLLAQGLRWVVVTSAAQqdcppGqvqLLAVTASQAHLLRHQRVDTA-PKGTGDLFCAELT 241
Cdd:COG0524   196 AELLTG-----ETDPEEAAAALLARGVKLVVVTLGAE-----G---ALLYTGGEVVHVPAFPVEVVdTTGAGDAFAAGFL 262

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1478758191 242 AHLLAGASLERAVEASSRylVQALACTRLADSAEllMPSRD 282
Cdd:COG0524   263 AGLLEGLDLEEALRFANA--AAALVVTRPGAQPA--LPTRE 299
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
91-265 1.67e-03

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 39.28  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191  91 AILVGYLGSAEQARVLGRWIarirEVHPQVLVIVDPVMG-DDDHGLYVTEgLAEASREcLVPQAHGLTPNSFELGLLTGC 169
Cdd:PRK12413   73 AIKIGLLPNVEIAEQALDFI----KGHPGIPVVLDPVLVcKETHDVEVSE-LRQELIQ-FFPYVTVITPNLVEAELLSGK 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478758191 170 EVGRVDQAVAAARRLLAQGLRWVVVTSAAQQDcppGQVQL-LAVTASQAHLLRHQRVDTAPKGTGDLFCAELTAHLLAGA 248
Cdd:PRK12413  147 EIKTLEDMKEAAKKLYDLGAKAVVIKGGNRLS---QKKAIdLFYDGKEFVILESPVLEKNNIGAGCTFASSIASQLVKGK 223

                         170
                  ....*....|....*..
gi 1478758191 249 SLERAVEASSRYLVQAL 265
Cdd:PRK12413  224 SPLEAVKNSKDFVYQAI 240
 
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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