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Conserved domains on  [gi|499997160|ref|WP_011677878|]
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pyridoxamine kinase [Lactobacillus delbrueckii]

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 ...
 1-261 3.85e-88

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 PRK07105:

Pssm-ID: 469648 [Multi-domain]  Cd Length: 284  Bit Score: 263.70  E-value: 3.85e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160   1 MKSVLISQDLSCVGQVSLAVALPVLGASGLQTAALPTAILSTHTGGFGENTFLDLSASLPDIWAHWDKENISFDAIYLGY 80
Cdd:PRK07105   4 VKRVAAIHDLSGFGRVALTASIPIMSSMGLQVCPLPTALLSSHTGGFQNPSIIDLTDGMQAFLTHWKSLNLKFDAIYSGY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160  81 LGQaaSRVWEKGLE---EYSRQGKLILLDPAMADHGRLYRGFDDSYVVQMQLLARQATILTPNLTEALLLLNEPVDFTEV 157
Cdd:PRK07105  84 LGS--PRQIQIVSDfikYFKKKDLLVVVDPVMGDNGKLYQGFDQEMVEEMRKLIQKADVITPNLTEACLLLDKPYLEKSY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160 158 DSHRACVITQRLAQKFAlSQVVLTGVPLADNRIGVYGLSR-GGRVWERTQDRIPHSYFGTGDLFASSLLAGLLHGLDLEQ 236
Cdd:PRK07105 162 SEEEIKQLLRKLADLGP-KIVIITSVPFEDGKIGVAYYDRaTDRFWKVFCKYIPAHYPGTGDIFTSVITGSLLQGDSLPI 240

                        250       260
                 ....*....|....*....|....*.
gi 499997160 237 AAGVAGDFVAKAILAT-DLDQDQRFG 261
Cdd:PRK07105 241 ALDRAVQFIEKGIRATlGLKYDLREG 266
 
Name Accession Description Interval E-value
PRK07105 PRK07105
pyridoxamine kinase; Validated
 1-261 3.85e-88

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 263.70  E-value: 3.85e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160   1 MKSVLISQDLSCVGQVSLAVALPVLGASGLQTAALPTAILSTHTGGFGENTFLDLSASLPDIWAHWDKENISFDAIYLGY 80
Cdd:PRK07105   4 VKRVAAIHDLSGFGRVALTASIPIMSSMGLQVCPLPTALLSSHTGGFQNPSIIDLTDGMQAFLTHWKSLNLKFDAIYSGY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160  81 LGQaaSRVWEKGLE---EYSRQGKLILLDPAMADHGRLYRGFDDSYVVQMQLLARQATILTPNLTEALLLLNEPVDFTEV 157
Cdd:PRK07105  84 LGS--PRQIQIVSDfikYFKKKDLLVVVDPVMGDNGKLYQGFDQEMVEEMRKLIQKADVITPNLTEACLLLDKPYLEKSY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160 158 DSHRACVITQRLAQKFAlSQVVLTGVPLADNRIGVYGLSR-GGRVWERTQDRIPHSYFGTGDLFASSLLAGLLHGLDLEQ 236
Cdd:PRK07105 162 SEEEIKQLLRKLADLGP-KIVIITSVPFEDGKIGVAYYDRaTDRFWKVFCKYIPAHYPGTGDIFTSVITGSLLQGDSLPI 240

                        250       260
                 ....*....|....*....|....*.
gi 499997160 237 AAGVAGDFVAKAILAT-DLDQDQRFG 261
Cdd:PRK07105 241 ALDRAVQFIEKGIRATlGLKYDLREG 266
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 1-272 9.08e-74

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: 226.57  E-value: 9.08e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160   1 MKSVLISQDLSCVGQVSLAVALPVLGASGLQTAALPTAILSTHTGgFGENTFLDLSAS-LPDIWAHWDKEN--ISFDAIY 77
Cdd:COG2240    1 MKRVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTG-YGTFTGRDLPTDdIADILDGWKELGvlLEFDAVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160  78 LGYLGQAAS-RVWEKGLEEY--SRQGKLILLDPAMADHGRLYRGFDDSYVVQMQLLARQATILTPNLTEALLLLNEPVDf 154
Cdd:COG2240   80 SGYLGSAEQgDIIADFVARVkaANPDALYLCDPVMGDNGKGYYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYE- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160 155 TEVDSHRACvitQRLAQKFAlSQVVLTGVPLAD---NRIGVYGLSRGGrVWERTQDRIPHSYFGTGDLFASSLLAGLLHG 231
Cdd:COG2240  159 TLEEALAAA---RALLALGP-KIVVVTSVPLDDtpaDKIGNLAVTADG-AWLVETPLLPFSPNGTGDLFAALLLAHLLRG 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 499997160 232 LDLEQAAGVAGDFVAKAILAT-DLDQDQrfgPNYAAALPWLL 272
Cdd:COG2240  234 KSLEEALERAAAFVYEVLERTaAAGSDE---LLLEAALDELV 272
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 3-252 1.20e-52

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: 172.00  E-value: 1.20e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160   3 SVLISQDLSCVGQVSLAVALPVLGASGLQTAALPTAILSTHTGGFGENTFLDLSASLPDIWAHWDKEN--ISFDAIYLGY 80
Cdd:cd01173    1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGllLEYDAVLTGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160  81 LGQAAS-RVWEKGLEEYSRQGK--LILLDPAMADHGRLYrGFDDSYVVQM-QLLARQATILTPNLTEALLLLNEPVDfTE 156
Cdd:cd01173   81 LGSAEQvEAVAEIVKRLKEKNPnlLYVCDPVMGDNGKLY-VVAEEIVPVYrDLLVPLADIITPNQFELELLTGKKIN-DL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160 157 VDSHRACvitQRLAQKFAlSQVVLTGVPLA-DNRIGVYGLSRGG--RVWERTQDRIPHsYFGTGDLFASSLLAGLLHGLD 233
Cdd:cd01173  159 EDAKAAA---RALHAKGP-KTVVVTSVELAdDDRIEMLGSTATEawLVQRPKIPFPAY-FNGTGDLFAALLLARLLKGKS 233

                        250
                 ....*....|....*....
gi 499997160 234 LEQAAGVAGDFVAKAILAT 252
Cdd:cd01173  234 LAEALEKALNFVHEVLEAT 252
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 69-249 1.25e-13

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: 68.66  E-value: 1.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160   69 ENISFDAIYLGYLGQAA--SRVWEKgLEEYSRQgklILLDPAM-ADHG-RLYrgfDDSYVVQM-QLLARQATILTPNLTE 143
Cdd:pfam08543  57 EDIPVDAVKTGMLGSAEiiEAVAEK-LDKYGVP---VVLDPVMvAKSGdSLL---DDEAIEALkEELLPLATLITPNLPE 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160  144 ALLLLNEPVDfTEVDSHRACVITQRLAQKFalsqVVLTGVPLADNR-IGVYGLSRGGRVWERTQDRIP-HSYFGTGDLFA 221
Cdd:pfam08543 130 AEALTGRKIK-TLEDMKEAAKKLLALGAKA----VLIKGGHLEGEEaVVTDVLYDGGGFYTLEAPRIPtKNTHGTGCTLS 204

                         170       180
                  ....*....|....*....|....*...
gi 499997160  222 SSLLAGLLHGLDLEQAAGVAGDFVAKAI 249
Cdd:pfam08543 205 AAIAANLAKGLSLPEAVREAKEYVTEAI 232
 
Name Accession Description Interval E-value
PRK07105 PRK07105
pyridoxamine kinase; Validated
 1-261 3.85e-88

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 263.70  E-value: 3.85e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160   1 MKSVLISQDLSCVGQVSLAVALPVLGASGLQTAALPTAILSTHTGGFGENTFLDLSASLPDIWAHWDKENISFDAIYLGY 80
Cdd:PRK07105   4 VKRVAAIHDLSGFGRVALTASIPIMSSMGLQVCPLPTALLSSHTGGFQNPSIIDLTDGMQAFLTHWKSLNLKFDAIYSGY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160  81 LGQaaSRVWEKGLE---EYSRQGKLILLDPAMADHGRLYRGFDDSYVVQMQLLARQATILTPNLTEALLLLNEPVDFTEV 157
Cdd:PRK07105  84 LGS--PRQIQIVSDfikYFKKKDLLVVVDPVMGDNGKLYQGFDQEMVEEMRKLIQKADVITPNLTEACLLLDKPYLEKSY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160 158 DSHRACVITQRLAQKFAlSQVVLTGVPLADNRIGVYGLSR-GGRVWERTQDRIPHSYFGTGDLFASSLLAGLLHGLDLEQ 236
Cdd:PRK07105 162 SEEEIKQLLRKLADLGP-KIVIITSVPFEDGKIGVAYYDRaTDRFWKVFCKYIPAHYPGTGDIFTSVITGSLLQGDSLPI 240

                        250       260
                 ....*....|....*....|....*.
gi 499997160 237 AAGVAGDFVAKAILAT-DLDQDQRFG 261
Cdd:PRK07105 241 ALDRAVQFIEKGIRATlGLKYDLREG 266
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 1-272 9.08e-74

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: 226.57  E-value: 9.08e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160   1 MKSVLISQDLSCVGQVSLAVALPVLGASGLQTAALPTAILSTHTGgFGENTFLDLSAS-LPDIWAHWDKEN--ISFDAIY 77
Cdd:COG2240    1 MKRVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTG-YGTFTGRDLPTDdIADILDGWKELGvlLEFDAVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160  78 LGYLGQAAS-RVWEKGLEEY--SRQGKLILLDPAMADHGRLYRGFDDSYVVQMQLLARQATILTPNLTEALLLLNEPVDf 154
Cdd:COG2240   80 SGYLGSAEQgDIIADFVARVkaANPDALYLCDPVMGDNGKGYYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYE- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160 155 TEVDSHRACvitQRLAQKFAlSQVVLTGVPLAD---NRIGVYGLSRGGrVWERTQDRIPHSYFGTGDLFASSLLAGLLHG 231
Cdd:COG2240  159 TLEEALAAA---RALLALGP-KIVVVTSVPLDDtpaDKIGNLAVTADG-AWLVETPLLPFSPNGTGDLFAALLLAHLLRG 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 499997160 232 LDLEQAAGVAGDFVAKAILAT-DLDQDQrfgPNYAAALPWLL 272
Cdd:COG2240  234 KSLEEALERAAAFVYEVLERTaAAGSDE---LLLEAALDELV 272
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 3-252 1.20e-52

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: 172.00  E-value: 1.20e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160   3 SVLISQDLSCVGQVSLAVALPVLGASGLQTAALPTAILSTHTGGFGENTFLDLSASLPDIWAHWDKEN--ISFDAIYLGY 80
Cdd:cd01173    1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGllLEYDAVLTGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160  81 LGQAAS-RVWEKGLEEYSRQGK--LILLDPAMADHGRLYrGFDDSYVVQM-QLLARQATILTPNLTEALLLLNEPVDfTE 156
Cdd:cd01173   81 LGSAEQvEAVAEIVKRLKEKNPnlLYVCDPVMGDNGKLY-VVAEEIVPVYrDLLVPLADIITPNQFELELLTGKKIN-DL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160 157 VDSHRACvitQRLAQKFAlSQVVLTGVPLA-DNRIGVYGLSRGG--RVWERTQDRIPHsYFGTGDLFASSLLAGLLHGLD 233
Cdd:cd01173  159 EDAKAAA---RALHAKGP-KTVVVTSVELAdDDRIEMLGSTATEawLVQRPKIPFPAY-FNGTGDLFAALLLARLLKGKS 233

                        250
                 ....*....|....*....
gi 499997160 234 LEQAAGVAGDFVAKAILAT 252
Cdd:cd01173  234 LAEALEKALNFVHEVLEAT 252
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 69-251 9.21e-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: 82.94  E-value: 9.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160  69 ENISFDAIYLGYLG--QAASRVWEKgLEEYsrQGKLILLDPAM-ADHGRlyRGFDDSYVVQM-QLLARQATILTPNLTEA 144
Cdd:cd01169   65 EDIPVDAIKIGMLGsaEIIEAVAEA-LKDY--PDIPVVLDPVMvAKSGD--SLLDDDAIEALrELLLPLATLITPNLPEA 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160 145 LLLLNEPVDfTEVDSHRACVITQRLAQKFalsqVVLTGVPLADNRIGVYGLSRGGRVWERTQDRIPHSYFGTGDLFASSL 224
Cdd:cd01169  140 ELLTGLEIA-TEEDMMKAAKALLALGAKA----VLIKGGHLPGDEAVDVLYDGGGFFEFESPRIDTKNTHGTGCTLSSAI 214

                        170       180
                 ....*....|....*....|....*..
gi 499997160 225 LAGLLHGLDLEQAAGVAGDFVAKAILA 251
Cdd:cd01169  215 AANLAKGLSLEEAVREAKEYVTQAIRN 241
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 69-251 7.62e-16

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: 75.07  E-value: 7.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160  69 ENISFDAIYLGYLGQAA--SRVWEKgLEEYsrQGKLILLDPAM-ADHGrlYRGFDDSYVVQM-QLLARQATILTPNLTEA 144
Cdd:COG0351   63 EDIPVDAIKIGMLGSAEiiEAVAEI-LADY--PLVPVVLDPVMvAKSG--DRLLDEDAVEALrELLLPLATVVTPNLPEA 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160 145 LLLLNEPVDfTEVDSHRACvitQRLAQKFALSqVVLTGVPLADNRIGVYgLSRGGRVWERTQDRIPHSYF-GTGDLFASS 223
Cdd:COG0351  138 EALLGIEIT-TLDDMREAA---KALLELGAKA-VLVKGGHLPGDEAVDV-LYDGDGVREFSAPRIDTGNThGTGCTLSSA 211

                        170       180
                 ....*....|....*....|....*...
gi 499997160 224 LLAGLLHGLDLEQAAGVAGDFVAKAILA 251
Cdd:COG0351  212 IAALLAKGLDLEEAVREAKEYVTQAIRA 239
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
14-252 2.70e-15

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 73.92  E-value: 2.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160  14 GQVSLAVALPVLGASGLQTAALPTAILS------THTGGfgentfldlsaSLPDIW-AHWDKENISFD------AIYLGY 80
Cdd:PRK08176  28 GSVGNSIAVPAIKANGLRVFAVPTVLLSntphypTFYGG-----------AIPDEWfSGYLRALQERDalrqlrAVTTGY 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160  81 LGQAASRV----WEKGLEEySRQGKLILLDPAMADHGR-LYRGFDDSYVVQMQLLArQATILTPNLTEALLLLNEPVDFT 155
Cdd:PRK08176  97 MGSASQIKilaeWLTALRA-DHPDLLIMVDPVIGDIDSgIYVKPDLPEAYRQHLLP-LAQGLTPNIFELEILTGKPCRTL 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160 156 E--VDSHRAcVITQRlaqkfaLSQVVLTGVP--LADNRIGVYGLSRGGRVwERTQDRIPHSYFGTGDLFASSLLAGLLHG 231
Cdd:PRK08176 175 DsaIAAAKS-LLSDT------LKWVVITSAAgnEENQEMQVVVVTADSVN-VISHPRVDTDLKGTGDLFCAELVSGLLKG 246

                        250       260
                 ....*....|....*....|.
gi 499997160 232 LDLEQAAGVAGDFVAKAILAT 252
Cdd:PRK08176 247 KALTDAAHRAGLRVLEVMRYT 267
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 69-249 1.25e-13

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: 68.66  E-value: 1.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160   69 ENISFDAIYLGYLGQAA--SRVWEKgLEEYSRQgklILLDPAM-ADHG-RLYrgfDDSYVVQM-QLLARQATILTPNLTE 143
Cdd:pfam08543  57 EDIPVDAVKTGMLGSAEiiEAVAEK-LDKYGVP---VVLDPVMvAKSGdSLL---DDEAIEALkEELLPLATLITPNLPE 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160  144 ALLLLNEPVDfTEVDSHRACVITQRLAQKFalsqVVLTGVPLADNR-IGVYGLSRGGRVWERTQDRIP-HSYFGTGDLFA 221
Cdd:pfam08543 130 AEALTGRKIK-TLEDMKEAAKKLLALGAKA----VLIKGGHLEGEEaVVTDVLYDGGGFYTLEAPRIPtKNTHGTGCTLS 204

                         170       180
                  ....*....|....*....|....*...
gi 499997160  222 SSLLAGLLHGLDLEQAAGVAGDFVAKAI 249
Cdd:pfam08543 205 AAIAANLAKGLSLPEAVREAKEYVTEAI 232
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 74-262 5.48e-10

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 58.60  E-value: 5.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160  74 DAIYLGYLGQAA--SRVWEKgLEEYsrQGKLILLDPAM-ADHGRlyRGFDDS--YVVQMQLLArQATILTPNLTEALLLL 148
Cdd:PRK06427  75 DAVKIGMLASAEiiETVAEA-LKRY--PIPPVVLDPVMiAKSGD--PLLADDavAALRERLLP-LATLITPNLPEAEALT 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160 149 NEPVDFTEVDSHRAcvitQRLAQKFALSQVVLTGVPLADNRIGVYGLSRGGRVWERTQDRIP-HSYFGTGDLFASSLLAG 227
Cdd:PRK06427 149 GLPIADTEDEMKAA----ARALHALGCKAVLIKGGHLLDGEESVDWLFDGEGEERFSAPRIPtKNTHGTGCTLSAAIAAE 224

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 499997160 228 LLHGLDLEQAAGVAGDFVAKAILATdLDQDQRFGP 262
Cdd:PRK06427 225 LAKGASLLDAVQTAKDYVTRAIRHA-LEIGQGHGP 258
PLN02978 PLN02978
pyridoxal kinase
 106-241 2.01e-09

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 57.06  E-value: 2.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160 106 DPAMADHGRLYRGFDDSYVVQMQLLARqATILTPNLTEALLLLNEPVDfTEVDSHRACVITQRLAQkfalSQVVLTGVPL 185
Cdd:PLN02978 123 DPVLGDEGKLYVPPELVPVYREKVVPL-ATMLTPNQFEAEQLTGIRIV-TEEDAREACAILHAAGP----SKVVITSIDI 196

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499997160 186 ADN--RIGVYGLSRGGRVwERTQDRIP--HSYF-GTGDLFASSLLAGLLHGLD-LEQAAGVA 241
Cdd:PLN02978 197 DGKllLVGSHRKEKGARP-EQFKIVIPkiPAYFtGTGDLMAALLLGWSHKYPDnLDKAAELA 257
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 2-253 1.61e-08

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 54.32  E-value: 1.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160   2 KSVLISQDLSCVGQVSLAVALPVLGASGLQTAALPTAILSTHTG-------GFGENTFLDLSASLPDiwAHWDKeniSFD 74
Cdd:PTZ00344   5 KKVLSIQSHVTHGYVGNRAATFPLQLLGFDVDFVNTVQLSNHTGypvikghRLDLNELITLMDGLRA--NNLLS---DYT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160  75 AIYLGYLGQA------ASRVweKGLEEySRQGKLILLDPAMADHGRLYrgFDDSYVVQMQLLARQATILTPNLTEALLLL 148
Cdd:PTZ00344  80 YVLTGYINSAdilrevLATV--KEIKE-LRPKLIFLCDPVMGDDGKLY--VKEEVVDAYRELIPYADVITPNQFEASLLS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160 149 NEPVDfTEVDSHRACvitqRLAQKFALSQVVLTGVPLADN--RIGVYGLSRGGRVWERTQ-----DRIPHSYFGTGDLFA 221
Cdd:PTZ00344 155 GVEVK-DLSDALEAI----DWFHEQGIPVVVITSFREDEDptHLRFLLSCRDKDTKNNKRftgkvPYIEGRYTGTGDLFA 229

                        250       260       270
                 ....*....|....*....|....*....|..
gi 499997160 222 SSLLAgLLHGLDLEQAAGVAGDFVAKAILATD 253
Cdd:PTZ00344 230 ALLLA-FSHQHPMDLAVGKAMGVLQDIIKATR 260
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 31-238 7.10e-08

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: 52.58  E-value: 7.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160  31 QTAALPTAILSTHTGGFGENTFldlsASLPDIWAHWDKENI------SFDAIYLGYLGQA---ASRVWEKGLEEYSRQGK 101
Cdd:COG0524   84 RDPGAPTGLAFILVDPDGERTI----VFYRGANAELTPEDLdeallaGADILHLGGITLAsepPREALLAALEAARAAGV 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160 102 LILLDPAmadhgrLYRGFDDSYVVQMQLLARQATILTPNLTEALLLLNEPvDFTEvdshracvITQRLAQKFAlSQVVLT 181
Cdd:COG0524  160 PVSLDPN------YRPALWEPARELLRELLALVDILFPNEEEAELLTGET-DPEE--------AAAALLARGV-KLVVVT 223

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499997160 182 gvplaDNRIGVYGLSRGGRVWERTQ-----DRIphsyfGTGDLFASSLLAGLLHGLDLEQAA 238
Cdd:COG0524  224 -----LGAEGALLYTGGEVVHVPAFpvevvDTT-----GAGDAFAAGFLAGLLEGLDLEEAL 275
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 70-249 2.62e-06

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 48.23  E-value: 2.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160  70 NISFDAIYLGYLGQAAS-RVWEKGLEEYSRQGklILLDPAM-ADHGRLYRGFDDSYVVQMQLLArQATILTPNLTEALLL 147
Cdd:PLN02898  76 DMPVDVVKTGMLPSAEIvKVLCQALKEFPVKA--LVVDPVMvSTSGDVLAGPSILSALREELLP-LATIVTPNVKEASAL 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160 148 LN-EPVDFTeVDSHRACVITQRLAQKFalsqVVLTGVPLADNRIGVYGLSRGGRVWERTQDRIP-HSYFGTGDLFASSLL 225
Cdd:PLN02898 153 LGgDPLETV-ADMRSAAKELHKLGPRY----VLVKGGHLPDSLDAVDVLYDGTEFHELRSSRIKtRNTHGTGCTLASCIA 227

                        170       180
                 ....*....|....*....|....
gi 499997160 226 AGLLHGLDLEQAAGVAGDFVAKAI 249
Cdd:PLN02898 228 AELAKGSDMLSAVKVAKRYVETAL 251
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 36-238 4.15e-06

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 47.34  E-value: 4.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160   36 PTAILSTHTGGFGENTFL----DLSASLPDIWAHWDKENISFDAIYLGYLGQAASRV-WEKGLEEYSRQGK---LILLDP 107
Cdd:pfam00294  87 RTGTALIEVDGDGERTIVfnrgAAADLTPEELEENEDLLENADLLYISGSLPLGLPEaTLEELIEAAKNGGtfdPNLLDP 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160  108 AMadhgrlyrgfddSYVVQMQLLARQATILTPNLTEALLLLNEPVDFTEVDSHRACVITQRLAQKFALSQVVLtgvplad 187
Cdd:pfam00294 167 LG------------AAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGAD------- 227

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 499997160  188 nriGVYGLSRGGRV-WERTQDRIPHSYFGTGDLFASSLLAGLLHGLDLEQAA 238
Cdd:pfam00294 228 ---GALVVEGDGEVhVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEAL 276
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 25-238 8.17e-05

Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway.


Pssm-ID: 238573 [Multi-domain]  Cd Length: 312  Bit Score: 43.37  E-value: 8.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160  25 LGASGLQTAALPTAILSTHT-----GGFGE---NTFLDLSASLPDIWAHWDK-ENISFdaIYL-GYLGQAASRVWEKGLE 94
Cdd:cd01168   91 LRAAGVDTRYQVQPDGPTGTcavlvTPDAErtmCTYLGAANELSPDDLDWSLlAKAKY--LYLeGYLLTVPPEAILLAAE 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160  95 EYSRQGKLILLDpamadhgrlyrgFDDSYVVQ-----MQLLARQATILTPNLTEALlllnepvDFTEVDSHRACVITQRL 169
Cdd:cd01168  169 HAKENGVKIALN------------LSAPFIVQrfkeaLLELLPYVDILFGNEEEAE-------ALAEAETTDDLEAALKL 229

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499997160 170 AQKFAlSQVVLTgvplaDNRIGVYGLSRGGRVW--ERTQDRIPHSYfGTGDLFASSLLAGLLHGLDLEQAA 238
Cdd:cd01168  230 LALRC-RIVVIT-----QGAKGAVVVEGGEVYPvpAIPVEKIVDTN-GAGDAFAGGFLYGLVQGEPLEECI 293
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
62-249 5.22e-04

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 41.25  E-value: 5.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160  62 IWAHWdkENISFDAIYLGYLGQAasRVWEKGLEEYSRQGKLILLDPAM-ADHG-RLYRgfDDSYVVQMQLLARQATILTP 139
Cdd:PRK08573  63 IEAVW--EDMGIDAAKTGMLSNR--EIIEAVAKTVSKYGFPLVVDPVMiAKSGaPLLR--EDAVDALIKRLLPLATVVTP 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160 140 NLTEALLLLNEPVDFTEvDSHRACVItqrLAQKFALSQVVLTGVPL-ADNRIGVygLSRGGRVWE----RTQDRIPHsyf 214
Cdd:PRK08573 137 NRPEAEKLTGMKIRSVE-DARKAAKY---IVEELGAEAVVVKGGHLeGEEAVDV--LYHNGTFREfrapRVESGCTH--- 207

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 499997160 215 GTGDLFASSLLAGLLHGLDLEQAAGVAGDFVAKAI 249
Cdd:PRK08573 208 GTGCSFSAAIAAGLAKGLDPEEAIKTAKKFITMAI 242
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 70-229 6.30e-04

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: 39.77  E-value: 6.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160  70 NISFDAIYLGYLGQAASRVwEKGLEEYSRQGKLILLDPAmadhgrlYRGFDDSYVVQMQLLaRQATILTPNLTEALLLln 149
Cdd:cd00287   55 LVGADAVVISGLSPAPEAV-LDALEEARRRGVPVVLDPG-------PRAVRLDGEELEKLL-PGVDILTPNEEEAEAL-- 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160 150 epvdfTEVDSHRACVITQRLAQKFALSQ--VVLTGvpladNRIGVYGLSRGGRVwERTQDRIPHSY--FGTGDLFASSLL 225
Cdd:cd00287  124 -----TGRRDLEVKEAAEAAALLLSKGPkvVIVTL-----GEKGAIVATRGGTE-VHVPAFPVKVVdtTGAGDAFLAALA 192


                 ....
gi 499997160 226 AGLL 229
Cdd:cd00287  193 AGLA 196
Guanosine_kinase_like cd01947
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ...
 169-238 8.35e-04

Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like group is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238922 [Multi-domain]  Cd Length: 265  Bit Score: 40.09  E-value: 8.35e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160 169 LAQKFALSQVVLTGVPLADNRIGVYGLSRGGRVwERTQDRIPHSYfGTGDLFASSLLAGLLHGLDLEQAA 238
Cdd:cd01947  181 VAEKIAGPFPRYLIVTEGELGAILYPGGRYNHV-PAKKAKVPDST-GAGDSFAAGFIYGLLKGWSIEEAL 248
PRK05756 PRK05756
pyridoxal kinase PdxY;
34-237 9.89e-04

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 39.85  E-value: 9.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160  34 ALPTAILSTHTgGFGENTFLDLSAS-LPDIWAhwDKENI----SFDAIYLGYLGQAAsrvwekgleeysrQGKLIL---- 104
Cdd:PRK05756  34 PLNTVQFSNHT-GYGKWTGCVMPPShLTEIVQ--GIADIgwlgECDAVLSGYLGSAE-------------QGEAILdavr 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160 105 ------------LDPAMADHGrlyRGFddsYV---VQMQLLAR---QATILTPNLTEALLLLNEPVDFTEvdshrACVIT 166
Cdd:PRK05756  98 rvkaanpqalyfCDPVMGDPE---KGC---IVapgVAEFLRDRalpAADIITPNLFELEWLSGRPVETLE-----DAVAA 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499997160 167 QRLAQKFALSQVVLTGVPLADNRIGVYG--LSRGGRVWERTQDRIP--HSYFGTGDLFASSLLAGLLHGLDLEQA 237
Cdd:PRK05756 167 ARALIARGPKIVLVTSLARAGYPADRFEmlLVTADGAWHISRPLVDfmRQPVGVGDLTSALFLARLLQGGSLEEA 241
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 135-241 2.51e-03

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: 38.45  E-value: 2.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160 135 TILTPNLTEALLLLNEPVDftEVDSHRACVITQRLAqkfALSQVVLTgvpLADNriGVYGLSRGGRVWERT----QDRIP 210
Cdd:cd01941  178 DLLTPNRAELEALAGALIE--NNEDENKAAKILLLP---GIKNVIVT---LGAK--GVLLSSREGGVETKLfpapQPETV 247

                         90       100       110
                 ....*....|....*....|....*....|.
gi 499997160 211 HSYFGTGDLFASSLLAGLLHGLDLEQAAGVA 241
Cdd:cd01941  248 VNVTGAGDAFVAGLVAGLLEGMSLDDSLRFA 278
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
 99-241 3.12e-03

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: 38.31  E-value: 3.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160  99 QGKLILLDPAMADHGRlYRGfddsyvvqmqllarqATILTPNLTEALLLLNEPVDFTEVDSHRAcvitQRLAQKFALSQV 178
Cdd:cd01172  163 LGIPVLVDPKGRDYSK-YRG---------------ATLLTPNEKEAREALGDEINDDDELEAAG----EKLLELLNLEAL 222

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499997160 179 VLTgvpLADNriGVYGLSRGGRVWertqdRIP-HS-----YFGTGDLFASSLLAGLLHGLDLEQAAGVA 241
Cdd:cd01172  223 LVT---LGEE--GMTLFERDGEVQ-----HIPaLAkevydVTGAGDTVIATLALALAAGADLEEAAFLA 281
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
 64-238 4.81e-03

2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.


Pssm-ID: 238571 [Multi-domain]  Cd Length: 294  Bit Score: 37.94  E-value: 4.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160  64 AHWDKENI-SFDAIYLG----YLGQAASRVWEKGLEEYSRQGKLILLD----PAMADHGRLyrgfddsyVVQMQLLARQA 134
Cdd:cd01166  115 EDLDEAALaGADHLHLSgitlALSESAREALLEALEAAKARGVTVSFDlnyrPKLWSAEEA--------REALEELLPYV 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160 135 TILTPNLTEALLLLNEPVDftevdshrACVITQRLAQKFALSQVVLTGVPLadnriGVYGLSRGGRVW---ERTQ--DRI 209
Cdd:cd01166  187 DIVLPSEEEAEALLGDEDP--------TDAAERALALALGVKAVVVKLGAE-----GALVYTGGGRVFvpaYPVEvvDTT 253

                        170       180
                 ....*....|....*....|....*....
gi 499997160 210 phsyfGTGDLFASSLLAGLLHGLDLEQAA 238
Cdd:cd01166  254 -----GAGDAFAAGFLAGLLEGWDLEEAL 277
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
 130-277 7.58e-03

NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport and metabolism];


Pssm-ID: 439833  Cd Length: 280  Bit Score: 37.02  E-value: 7.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160 130 LARQATILTPNLTEALLLLNEPVDftEVDSHRAcVITQRLAQKFALSqVVLTG----VPLADNRIGVY-----GLSRGgr 200
Cdd:COG0063  143 ALPAPTVLTPHPGEFARLLGCSVA--EIQADRL-EAAREAAKRYGAV-VVLKGagtvIAAPDGRVYINptgnpGLATA-- 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499997160 201 vwertqdriphsyfGTGDLFAsSLLAGLL-HGLDLEQAA-------GVAGDFVAK----AILATDLdqdqrfgpnyAAAL 268
Cdd:COG0063  217 --------------GSGDVLA-GIIAGLLaQGLDPFEAAaagvylhGLAGDLAAEergrGLLASDL----------IEAL 271


                 ....*....
gi 499997160 269 PWLLQQLHN 277
Cdd:COG0063  272 PAALRELLE 280
 
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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