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Conserved domains on  [gi|2034426951|gb|QUX26301|]
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AGE family epimerase/isomerase [Nocardiopsis changdeensis]

Protein Classification

carbohydrate kinase( domain architecture ID 10100215)

carbohydrate kinase similar to fructokinase and aminoimidazole riboside kinase, which catalyze the phosphorylation of fructose and aminoimidazole ribotide, respectively

CATH:  3.40.1190.20
EC:  2.7.1.-
Gene Ontology:  GO:0016301|GO:0005975
SCOP:  4000759

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
bac_FRK cd01167
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ...
 90-376 1.46e-72

Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.


:

Pssm-ID: 238572 [Multi-domain]  Cd Length: 295  Bit Score: 229.06  E-value: 1.46e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951  90 VVVGENVMDLLPVPGG-PGLLRAAPGGGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGLDPDGLLA-AEEPS 167
Cdd:cd01167     3 VCFGEALIDFIPEGSGaPETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFdPAAPT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 168 ALALARLGADGSAVYDFRMDDAADWRWRSGELPEELEpGVRALHAASLALFREPGAGAVEALLRREHGRGrVTVSVDPNI 247
Cdd:cd01167    83 TLAFVTLDADGERSFEFYRGPAADLLLDTELNPDLLS-EADILHFGSIALASEPSRSALLELLEAAKKAG-VLISFDPNL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 248 RPGVIGDPDTARALALRNAAQAHLVKASDEDLAFLYPDQDVEKAAAALAALGPSLVVVTRGARGALALAHGARAEVAAPR 327
Cdd:cd01167   161 RPPLWRDEEEARERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRGADGALLYTKGGVGEVPGIP 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2034426951 328 VEVVDTVGAGDTFMGALLAWLDGRDRLGEDprarlagltERDLEEMLSF 376
Cdd:cd01167   241 VEVVDTTGAGDAFVAGLLAQLLSRGLLALD---------EDELAEALRF 280
AGE super family cl23840
AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate ...
 2-73 1.57e-17

AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate epimerization during biosynthesis of N-acetylneuraminic acid. Catalytic mechanism is believed to be via nucleotide elimination and readdition and is ATP modulated. AGE is structurally and mechanistically distinct from the other four types of epimerases. The AGE domain monomer is composed of an alpha(6)/alpha(6)-barrel, the structure of which is also found in glucoamylase and cellulase. The active form is a homodimer. The alignment also contains subtype III mannose 6-phosphate isomerases.


The actual alignment was detected with superfamily member COG2942:

Pssm-ID: 474077  Cd Length: 380  Bit Score: 83.39  E-value: 1.57e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2034426951   2 AAWALALHTGDRTLLEYYEQWWDYAERHHLDFEHGSWHHELDPRNRPA--ATVWAGKPDvYHAYQATLLPQLPL 73
Cdd:COG2942   308 AALLLYQLTGDERYLDWYRRLWDYIWAHFIDHEYGEWFGELDRDGEPLtdLKGGPWKGD-YHNPRALLEVLRRL 380
 
Name Accession Description Interval E-value
bac_FRK cd01167
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ...
 90-376 1.46e-72

Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.


Pssm-ID: 238572 [Multi-domain]  Cd Length: 295  Bit Score: 229.06  E-value: 1.46e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951  90 VVVGENVMDLLPVPGG-PGLLRAAPGGGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGLDPDGLLA-AEEPS 167
Cdd:cd01167     3 VCFGEALIDFIPEGSGaPETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFdPAAPT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 168 ALALARLGADGSAVYDFRMDDAADWRWRSGELPEELEpGVRALHAASLALFREPGAGAVEALLRREHGRGrVTVSVDPNI 247
Cdd:cd01167    83 TLAFVTLDADGERSFEFYRGPAADLLLDTELNPDLLS-EADILHFGSIALASEPSRSALLELLEAAKKAG-VLISFDPNL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 248 RPGVIGDPDTARALALRNAAQAHLVKASDEDLAFLYPDQDVEKAAAALAALGPSLVVVTRGARGALALAHGARAEVAAPR 327
Cdd:cd01167   161 RPPLWRDEEEARERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRGADGALLYTKGGVGEVPGIP 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2034426951 328 VEVVDTVGAGDTFMGALLAWLDGRDRLGEDprarlagltERDLEEMLSF 376
Cdd:cd01167   241 VEVVDTTGAGDAFVAGLLAQLLSRGLLALD---------EDELAEALRF 280
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 88-352 5.07e-58

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: 191.64  E-value: 5.07e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951  88 HLVVVGENVMDLLP-VPGGP--------GLLRAAPGGGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGLDPD 158
Cdd:COG0524     1 DVLVIGEALVDLVArVDRLPkggetvlaGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 159 GLL-AAEEPSALALARLGADGSAVYDFRMddAADWRWRSGELPEELEPGVRALHAASLALFREPGAGAVEALLRREHGRG 237
Cdd:COG0524    81 GVRrDPGAPTGLAFILVDPDGERTIVFYR--GANAELTPEDLDEALLAGADILHLGGITLASEPPREALLAALEAARAAG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 238 rVTVSVDPNIRPGVIgdpDTARALALRNAAQAHLVKASDEDLAFLYPDQDVEKAAAALAALGPSLVVVTRGARGALALAH 317
Cdd:COG0524   159 -VPVSLDPNYRPALW---EPARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVTLGAEGALLYTG 234

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2034426951 318 GARAEVAAPRVEVVDTVGAGDTFMGALLA-WLDGRD 352
Cdd:COG0524   235 GEVVHVPAFPVEVVDTTGAGDAFAAGFLAgLLEGLD 270
PRK09434 PRK09434
aminoimidazole riboside kinase; Provisional
 91-354 1.09e-35

aminoimidazole riboside kinase; Provisional


Pssm-ID: 236514 [Multi-domain]  Cd Length: 304  Bit Score: 132.75  E-value: 1.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951  91 VVGENVMDLlpVPGGPGLLRAAPGGGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGLDPDGL-LAAEEPSAL 169
Cdd:PRK09434    7 VLGDAVVDL--IPEGENRYLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLrLDPAHRTST 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 170 ALARLGADGSAVYDFRMDDAADWRWRSGELPEeLEPGvRALHAASLALFREPGAG-AVEALLRREHGRGRVtvSVDPNIR 248
Cdd:PRK09434   85 VVVDLDDQGERSFTFMVRPSADLFLQPQDLPP-FRQG-EWLHLCSIALSAEPSRStTFEAMRRIKAAGGFV--SFDPNLR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 249 PGVIGDPDTARALALRNAAQAHLVKASDEDLAFLYPDQDVEKAAAA-LAALGPSLVVVTRGARGALALAHGARAEVAAPR 327
Cdd:PRK09434  161 EDLWQDEAELRECLRQALALADVVKLSEEELCFLSGTSQLEDAIYAlADRYPIALLLVTLGAEGVLVHTRGQVQHFPAPS 240

                         250       260
                  ....*....|....*....|....*..
gi 2034426951 328 VEVVDTVGAGDTFMGALLAWLDGRDRL 354
Cdd:PRK09434  241 VDPVDTTGAGDAFVAGLLAGLSQAGLW 267
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 88-348 2.40e-31

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 120.91  E-value: 2.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951  88 HLVVVGENVMDLLPVPGG--PGLLRAA-----PGGGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGLDPDGL 160
Cdd:pfam00294   1 KVVVIGEANIDLIGNVEGlpGELVRVStvekgPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 161 LA-AEEPSALALARLGADG--SAVYDFRmdDAADWRWRSGELPEELEPGVRALHAASLALFREPGAGAVEALLRREHGRG 237
Cdd:pfam00294  81 VIdEDTRTGTALIEVDGDGerTIVFNRG--AAADLTPEELEENEDLLENADLLYISGSLPLGLPEATLEELIEAAKNGGT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 238 RVTVSVDPNIRPgvigdpdtaRALALRNAAQAHLVKASDEDLAFLY--PDQDVE---KAAAALAALGPSLVVVTRGARGA 312
Cdd:pfam00294 159 FDPNLLDPLGAA---------REALLELLPLADLLKPNEEELEALTgaKLDDIEealAALHKLLAKGIKTVIVTLGADGA 229

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2034426951 313 LALAHGARAEV-AAPRVEVVDTVGAGDTFMGALLAWL 348
Cdd:pfam00294 230 LVVEGDGEVHVpAVPKVKVVDTTGAGDSFVGGFLAGL 266
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
 93-344 4.38e-18

ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose catabolism. The rbsK gene encoding ribokinase typically is found with ribose transport genes. Ribokinase belongs to the carbohydrate kinase pfkB family (pfam00294). In the wide gulf between the current trusted (360 bit) and noise (100 bit) cutoffs are a number of sequences, few of which are clustered with predicted ribose transport genes but many of which are currently annotated as if having ribokinase activity. Most likely some have this function and others do not. [Energy metabolism, Sugars]


Pssm-ID: 274000 [Multi-domain]  Cd Length: 293  Bit Score: 83.80  E-value: 4.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951  93 GENVMDL------LPVPG----GPGLlRAAPGGGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGLDPDGL-L 161
Cdd:TIGR02152   1 GSINMDLvlrtdrLPKPGetvhGHSF-QIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVgT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 162 AAEEPSALALARLGADGS--------AVYDFRMDDAADWRWR---------SGELPEELepgvrALHAASLAlfrepgag 224
Cdd:TIGR02152  80 VKDTPTGTAFITVDDTGEnrivvvagANAELTPEDIDAAEALiaesdivllQLEIPLET-----VLEAAKIA-------- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 225 aveallrREHGrgrVTVSVDPniRPGVIGDPDTaralalrnaaqahLVKASD------EDLAFLYPD-----QDVEKAAA 293
Cdd:TIGR02152 147 -------KKHG---VKVILNP--APAIKDLDDE-------------LLSLVDiitpneTEAEILTGIevtdeEDAEKAAE 201

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2034426951 294 ALAALGPSLVVVTRGARGALALAHGARAEVAAPRVEVVDTVGAGDTFMGAL 344
Cdd:TIGR02152 202 KLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAVDTTAAGDTFNGAF 252
YihS COG2942
Mannose or cellobiose epimerase, N-acyl-D-glucosamine 2-epimerase family [Carbohydrate ...
 2-73 1.57e-17

Mannose or cellobiose epimerase, N-acyl-D-glucosamine 2-epimerase family [Carbohydrate transport and metabolism];


Pssm-ID: 442185  Cd Length: 380  Bit Score: 83.39  E-value: 1.57e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2034426951   2 AAWALALHTGDRTLLEYYEQWWDYAERHHLDFEHGSWHHELDPRNRPA--ATVWAGKPDvYHAYQATLLPQLPL 73
Cdd:COG2942   308 AALLLYQLTGDERYLDWYRRLWDYIWAHFIDHEYGEWFGELDRDGEPLtdLKGGPWKGD-YHNPRALLEVLRRL 380
GlcNAc_2-epim pfam07221
N-acylglucosamine 2-epimerase (GlcNAc 2-epimerase); This family contains a number of ...
 2-65 2.05e-16

N-acylglucosamine 2-epimerase (GlcNAc 2-epimerase); This family contains a number of eukaryotic and bacterial N-acylglucosamine 2-epimerase (GlcNAc 2-epimerase) enzymes (EC:5.1.3.8) approximately 500 residues long. This converts N-acyl-D-glucosamine to N-acyl-D-mannosamine.


Pssm-ID: 399891  Cd Length: 347  Bit Score: 79.75  E-value: 2.05e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2034426951   2 AAWALALHTGDRTLLEYYEQWWDYAERHHLDFEHGSWHHELDPRNRPAATVWAGKPDVYHAYQA 65
Cdd:pfam07221 284 AAAALAQRTGEARYWDWYRRAWDYLWRHFIDPEYGSWFDELDADGEVALPLPAGKSDFYHALGA 347
AGE cd00249
AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate ...
 2-74 4.56e-11

AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate epimerization during biosynthesis of N-acetylneuraminic acid. Catalytic mechanism is believed to be via nucleotide elimination and readdition and is ATP modulated. AGE is structurally and mechanistically distinct from the other four types of epimerases. The AGE domain monomer is composed of an alpha(6)/alpha(6)-barrel, the structure of which is also found in glucoamylase and cellulase. The active form is a homodimer. The alignment also contains subtype III mannose 6-phosphate isomerases.


Pssm-ID: 238153  Cd Length: 384  Bit Score: 63.92  E-value: 4.56e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2034426951   2 AAWALALHTGDRTLLEYYEQWWDYAERHHLDFEHGSWHHELDPRNRPAATVWAGKPDVYHAYQATLLPQLPLS 74
Cdd:cd00249   310 AALALAGITGDERYWQWYQRAWAYLWRHFIDPEYGLWFGYLDADGKVLLTPKGPAKTFYHVVRALYEALDVLA 382
 
Name Accession Description Interval E-value
bac_FRK cd01167
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ...
 90-376 1.46e-72

Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.


Pssm-ID: 238572 [Multi-domain]  Cd Length: 295  Bit Score: 229.06  E-value: 1.46e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951  90 VVVGENVMDLLPVPGG-PGLLRAAPGGGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGLDPDGLLA-AEEPS 167
Cdd:cd01167     3 VCFGEALIDFIPEGSGaPETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFdPAAPT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 168 ALALARLGADGSAVYDFRMDDAADWRWRSGELPEELEpGVRALHAASLALFREPGAGAVEALLRREHGRGrVTVSVDPNI 247
Cdd:cd01167    83 TLAFVTLDADGERSFEFYRGPAADLLLDTELNPDLLS-EADILHFGSIALASEPSRSALLELLEAAKKAG-VLISFDPNL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 248 RPGVIGDPDTARALALRNAAQAHLVKASDEDLAFLYPDQDVEKAAAALAALGPSLVVVTRGARGALALAHGARAEVAAPR 327
Cdd:cd01167   161 RPPLWRDEEEARERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRGADGALLYTKGGVGEVPGIP 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2034426951 328 VEVVDTVGAGDTFMGALLAWLDGRDRLGEDprarlagltERDLEEMLSF 376
Cdd:cd01167   241 VEVVDTTGAGDAFVAGLLAQLLSRGLLALD---------EDELAEALRF 280
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 88-352 5.07e-58

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: 191.64  E-value: 5.07e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951  88 HLVVVGENVMDLLP-VPGGP--------GLLRAAPGGGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGLDPD 158
Cdd:COG0524     1 DVLVIGEALVDLVArVDRLPkggetvlaGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 159 GLL-AAEEPSALALARLGADGSAVYDFRMddAADWRWRSGELPEELEPGVRALHAASLALFREPGAGAVEALLRREHGRG 237
Cdd:COG0524    81 GVRrDPGAPTGLAFILVDPDGERTIVFYR--GANAELTPEDLDEALLAGADILHLGGITLASEPPREALLAALEAARAAG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 238 rVTVSVDPNIRPGVIgdpDTARALALRNAAQAHLVKASDEDLAFLYPDQDVEKAAAALAALGPSLVVVTRGARGALALAH 317
Cdd:COG0524   159 -VPVSLDPNYRPALW---EPARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVTLGAEGALLYTG 234

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2034426951 318 GARAEVAAPRVEVVDTVGAGDTFMGALLA-WLDGRD 352
Cdd:COG0524   235 GEVVHVPAFPVEVVDTTGAGDAFAAGFLAgLLEGLD 270
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
 89-352 7.79e-45

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: 156.97  E-value: 7.79e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951  89 LVVVGENVMDLLPVPGGP----GLLRAAPGGGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGLDPDGLLA-A 163
Cdd:cd01166     2 VVTIGEVMVDLSPPGGGRleqaDSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRVdP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 164 EEPSALALARLGADGSAVYDFRMDDAADWRWRSGELPEELEPGVRALHAA--SLALFREPGAGAVEAL-LRREHGrgrVT 240
Cdd:cd01166    82 GRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEAALAGADHLHLSgiTLALSESAREALLEALeAAKARG---VT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 241 VSVDPNIRPgVIGDPDTARALALRNAAQAHLVKASDEDLAFLYPDQDVEKA--AAALAALGPSLVVVTRGARGALALAHG 318
Cdd:cd01166   159 VSFDLNYRP-KLWSAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAaeRALALALGVKAVVVKLGAEGALVYTGG 237

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2034426951 319 ARAEVAAPRVEVVDTVGAGDTFMGALLA-WLDGRD 352
Cdd:cd01166   238 GRVFVPAYPVEVVDTTGAGDAFAAGFLAgLLEGWD 272
PRK09434 PRK09434
aminoimidazole riboside kinase; Provisional
 91-354 1.09e-35

aminoimidazole riboside kinase; Provisional


Pssm-ID: 236514 [Multi-domain]  Cd Length: 304  Bit Score: 132.75  E-value: 1.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951  91 VVGENVMDLlpVPGGPGLLRAAPGGGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGLDPDGL-LAAEEPSAL 169
Cdd:PRK09434    7 VLGDAVVDL--IPEGENRYLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLrLDPAHRTST 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 170 ALARLGADGSAVYDFRMDDAADWRWRSGELPEeLEPGvRALHAASLALFREPGAG-AVEALLRREHGRGRVtvSVDPNIR 248
Cdd:PRK09434   85 VVVDLDDQGERSFTFMVRPSADLFLQPQDLPP-FRQG-EWLHLCSIALSAEPSRStTFEAMRRIKAAGGFV--SFDPNLR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 249 PGVIGDPDTARALALRNAAQAHLVKASDEDLAFLYPDQDVEKAAAA-LAALGPSLVVVTRGARGALALAHGARAEVAAPR 327
Cdd:PRK09434  161 EDLWQDEAELRECLRQALALADVVKLSEEELCFLSGTSQLEDAIYAlADRYPIALLLVTLGAEGVLVHTRGQVQHFPAPS 240

                         250       260
                  ....*....|....*....|....*..
gi 2034426951 328 VEVVDTVGAGDTFMGALLAWLDGRDRL 354
Cdd:PRK09434  241 VDPVDTTGAGDAFVAGLLAGLSQAGLW 267
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 88-348 2.40e-31

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 120.91  E-value: 2.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951  88 HLVVVGENVMDLLPVPGG--PGLLRAA-----PGGGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGLDPDGL 160
Cdd:pfam00294   1 KVVVIGEANIDLIGNVEGlpGELVRVStvekgPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 161 LA-AEEPSALALARLGADG--SAVYDFRmdDAADWRWRSGELPEELEPGVRALHAASLALFREPGAGAVEALLRREHGRG 237
Cdd:pfam00294  81 VIdEDTRTGTALIEVDGDGerTIVFNRG--AAADLTPEELEENEDLLENADLLYISGSLPLGLPEATLEELIEAAKNGGT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 238 RVTVSVDPNIRPgvigdpdtaRALALRNAAQAHLVKASDEDLAFLY--PDQDVE---KAAAALAALGPSLVVVTRGARGA 312
Cdd:pfam00294 159 FDPNLLDPLGAA---------REALLELLPLADLLKPNEEELEALTgaKLDDIEealAALHKLLAKGIKTVIVTLGADGA 229

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2034426951 313 LALAHGARAEV-AAPRVEVVDTVGAGDTFMGALLAWL 348
Cdd:pfam00294 230 LVVEGDGEVHVpAVPKVKVVDTTGAGDSFVGGFLAGL 266
PLN02323 PLN02323
probable fructokinase
 87-376 1.96e-25

probable fructokinase


Pssm-ID: 215183 [Multi-domain]  Cd Length: 330  Bit Score: 105.47  E-value: 1.96e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951  87 PHLVVVGENVMDLLPVPGG------PGLLRAaPGGGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGLDPDGL 160
Cdd:PLN02323   11 SLVVCFGEMLIDFVPTVSGvslaeaPAFKKA-PGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 161 L-AAEEPSALALARLGADGSAVYDFRMDDAADWRWRSGELPEELEPGVRALHAASLALFREPGAGAVEALLR--REHGrg 237
Cdd:PLN02323   90 RfDPGARTALAFVTLRSDGEREFMFYRNPSADMLLRESELDLDLIRKAKIFHYGSISLITEPCRSAHLAAMKiaKEAG-- 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 238 rVTVSVDPNIRPGVIGDPDTARALALRNAAQAHLVKASDEDLAFLYPDQDV-EKAAAALAALGPSLVVVTRGARGALALA 316
Cdd:PLN02323  168 -ALLSYDPNLRLPLWPSAEAAREGIMSIWDEADIIKVSDEEVEFLTGGDDPdDDTVVKLWHPNLKLLLVTEGEEGCRYYT 246

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 317 HGARAEVAAPRVEVVDTVGAGDTFMGALLAWLDGRDRLGEDprarlagltERDLEEMLSF 376
Cdd:PLN02323  247 KDFKGRVEGFKVKAVDTTGAGDAFVGGLLSQLAKDLSLLED---------EERLREALRF 297
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 90-366 3.74e-23

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: 98.39  E-value: 3.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951  90 VVVGENVMDL------LPVPG----GPGLlRAAPGGGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGLDPDG 159
Cdd:cd01174     3 VVVGSINVDLvtrvdrLPKPGetvlGSSF-ETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 160 L-LAAEEPSALALARLGADGS---AVY---DFRMDdaadwrwrsgelPEELEPGVRALHAASLALF-REPGAGAVEALLR 231
Cdd:cd01174    82 VeVVVGAPTGTAVITVDESGEnriVVVpgaNGELT------------PADVDAALELIAAADVLLLqLEIPLETVLAALR 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 232 REHGRGrVTVSVDP----NIRPGVIGDPDtaralalrnaaqaHLVKASDEdLAFLYPD-----QDVEKAAAALAALGPSL 302
Cdd:cd01174   150 AARRAG-VTVILNPaparPLPAELLALVD-------------ILVPNETE-AALLTGIevtdeEDAEKAARLLLAKGVKN 214

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2034426951 303 VVVTRGARGALALAHGARAEVAAPRVEVVDTVGAGDTFMGALLAWLDGRDRLGEDPR--ARLAGLT 366
Cdd:cd01174   215 VIVTLGAKGALLASGGEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRfaNAAAALS 280
Fructoselysine_kinase_like cd01940
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ...
 89-354 4.66e-22

Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a non-enzymatic reaction of glucose with a primary amine followed by an Amadori rearrangement, resulting in a protein that is modified at the amino terminus and at the lysine side chains. Fructoseamines are typically metabolized by fructoseamine-3-kinase, especially in higher eukaryotes. In E. coli, fructoselysine kinase has been shown in vitro to catalyze the phosphorylation of fructoselysine. It is proposed that fructoselysine is released from glycated proteins during human digestion and is partly metabolized by bacteria in the hind gut using a protein such as fructoselysine kinase. This family is found only in bacterial sequences, and its oligomeric state is currently unknown.


Pssm-ID: 238915 [Multi-domain]  Cd Length: 264  Bit Score: 94.73  E-value: 4.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951  89 LVVVGENVMDLLPVPGgpgllRAAPGGGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGLDPDGLLAAEEPSA 168
Cdd:cd01940     2 LAAIGDNVVDKYLHLG-----KMYPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGENA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 169 LALARL-------GADGSAVYDFRMDDAADWRWRSG---------ELPEELEPGVRALHAASLAL---FRepgagaveal 229
Cdd:cd01940    77 VADVELvdgdrifGLSNKGGVAREHPFEADLEYLSQfdlvhtgiySHEGHLEKALQALVGAGALIsfdFS---------- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 230 lrrehgrGRVTVSVDPNIRPGVigdpdtaralalrnaaqahlvkasdeDLAFL-YPDQD---VEKAAAALAALGPSLVVV 305
Cdd:cd01940   147 -------DRWDDDYLQLVCPYV--------------------------DFAFFsASDLSdeeVKAKLKEAVSRGAKLVIV 193

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2034426951 306 TRGARGALALAHGARAEVAAPRVEVVDTVGAGDTFM-GALLAWLDGRDRL 354
Cdd:cd01940   194 TRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIaGFLLSLLAGGTAI 243
ribokinase_group_A cd01942
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ...
 89-352 9.02e-20

Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238917 [Multi-domain]  Cd Length: 279  Bit Score: 88.52  E-value: 9.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951  89 LVVVGENVMD-LLPVPGGPGL--------LRAAPGGGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGLDPDG 159
Cdd:cd01942     2 VAVVGHLNYDiILKVESFPGPfesvlvkdLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 160 L-LAAEEPSALALARLGADGSAVYDFRMDDAADWRwrsGELPEELEPGVRALHaaslalfrePGAGAVEALLRREHGRGR 238
Cdd:cd01942    82 VrVVDEDSTGVAFILTDGDDNQIAYFYPGAMDELE---PNDEADPDGLADIVH---------LSSGPGLIELARELAAGG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 239 VTVSVDPNIRpgvigDPDTARALALRNAAQAHLVKASDEDLaflypDQDVEK--AAAALAALGPSLVVVTRGARGALALA 316
Cdd:cd01942   150 ITVSFDPGQE-----LPRLSGEELEEILERADILFVNDYEA-----ELLKERtgLSEAELASGVRVVVVTLGPKGAIVFE 219

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2034426951 317 HGARAEV-AAPRVEVVDTVGAGDTFMGALL-AWLDGRD 352
Cdd:cd01942   220 DGEEVEVpAVPAVKVVDTTGAGDAFRAGFLyGLLRGYD 257
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
 93-344 4.38e-18

ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose catabolism. The rbsK gene encoding ribokinase typically is found with ribose transport genes. Ribokinase belongs to the carbohydrate kinase pfkB family (pfam00294). In the wide gulf between the current trusted (360 bit) and noise (100 bit) cutoffs are a number of sequences, few of which are clustered with predicted ribose transport genes but many of which are currently annotated as if having ribokinase activity. Most likely some have this function and others do not. [Energy metabolism, Sugars]


Pssm-ID: 274000 [Multi-domain]  Cd Length: 293  Bit Score: 83.80  E-value: 4.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951  93 GENVMDL------LPVPG----GPGLlRAAPGGGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGLDPDGL-L 161
Cdd:TIGR02152   1 GSINMDLvlrtdrLPKPGetvhGHSF-QIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVgT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 162 AAEEPSALALARLGADGS--------AVYDFRMDDAADWRWR---------SGELPEELepgvrALHAASLAlfrepgag 224
Cdd:TIGR02152  80 VKDTPTGTAFITVDDTGEnrivvvagANAELTPEDIDAAEALiaesdivllQLEIPLET-----VLEAAKIA-------- 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 225 aveallrREHGrgrVTVSVDPniRPGVIGDPDTaralalrnaaqahLVKASD------EDLAFLYPD-----QDVEKAAA 293
Cdd:TIGR02152 147 -------KKHG---VKVILNP--APAIKDLDDE-------------LLSLVDiitpneTEAEILTGIevtdeEDAEKAAE 201

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2034426951 294 ALAALGPSLVVVTRGARGALALAHGARAEVAAPRVEVVDTVGAGDTFMGAL 344
Cdd:TIGR02152 202 KLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVKAVDTTAAGDTFNGAF 252
PRK11142 PRK11142
ribokinase; Provisional
 86-351 1.17e-17

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 83.00  E-value: 1.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951  86 APHLVVVG----ENVMDL--LPVPG----GPGLlRAAPGGGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGL 155
Cdd:PRK11142    2 MGKLVVLGsinaDHVLNLesFPRPGetltGRHY-QVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 156 DPDGL-LAAEEPSALALARLGADG------SAVYDFRMDdaadwrwrsgelPEELEPGvRALHAASLALFRE---PGAGA 225
Cdd:PRK11142   81 DTAPVsVIKGESTGVALIFVNDEGensigiHAGANAALT------------PALVEAH-RELIANADALLMQletPLETV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 226 VEAL-LRREHGrgrVTVSVDPnirpgvigdpdtaralalrnaaqAHLVKASDEDLAFL------------------YPDQ 286
Cdd:PRK11142  148 LAAAkIAKQHG---TKVILNP-----------------------APARELPDELLALVdiitpneteaekltgirvEDDD 201

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2034426951 287 DVEKAAAALAALGPSLVVVTRGARGALALAHGARAEVAAPRVEVVDTVGAGDTFMGALL-AWLDGR 351
Cdd:PRK11142  202 DAAKAAQVLHQKGIETVLITLGSRGVWLSENGEGQRVPGFRVQAVDTIAAGDTFNGALVtALLEGK 267
YihS COG2942
Mannose or cellobiose epimerase, N-acyl-D-glucosamine 2-epimerase family [Carbohydrate ...
 2-73 1.57e-17

Mannose or cellobiose epimerase, N-acyl-D-glucosamine 2-epimerase family [Carbohydrate transport and metabolism];


Pssm-ID: 442185  Cd Length: 380  Bit Score: 83.39  E-value: 1.57e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2034426951   2 AAWALALHTGDRTLLEYYEQWWDYAERHHLDFEHGSWHHELDPRNRPA--ATVWAGKPDvYHAYQATLLPQLPL 73
Cdd:COG2942   308 AALLLYQLTGDERYLDWYRRLWDYIWAHFIDHEYGEWFGELDRDGEPLtdLKGGPWKGD-YHNPRALLEVLRRL 380
ribokinase_group_B cd01945
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ...
 92-345 8.16e-17

Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time. .


Pssm-ID: 238920 [Multi-domain]  Cd Length: 284  Bit Score: 80.03  E-value: 8.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951  92 VGENVMDLL----PVPGGPGLLRAAP----GGGPA-NTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGLDPDGLL- 161
Cdd:cd01945     5 VGLAVLDLIylvaSFPGGDGKIVATDyaviGGGNAaNAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVv 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 162 AAEEPSALALARLGADGSAVYDFRMDDAADWRwrsGELPEELEPGVRALHAASlalfREPGAGAVeaLLRREHGRGrvtv 241
Cdd:cd01945    85 APGARSPISSITDITGDRATISITAIDTQAAP---DSLPDAILGGADAVLVDG----RQPEAALH--LAQEARARG---- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 242 svdpnIRPGVIGDPDTARALALRNAAQAHLVkASDEDLAFLYPDQDvEKAAAALAALGPSLVVVTRGARGALAL-AHGAR 320
Cdd:cd01945   152 -----IPIPLDLDGGGLRVLEELLPLADHAI-CSENFLRPNTGSAD-DEALELLASLGIPFVAVTLGEAGCLWLeRDGEL 224

                         250       260
                  ....*....|....*....|....*
gi 2034426951 321 AEVAAPRVEVVDTVGAGDTFMGALL 345
Cdd:cd01945   225 FHVPAFPVEVVDTTGAGDVFHGAFA 249
GlcNAc_2-epim pfam07221
N-acylglucosamine 2-epimerase (GlcNAc 2-epimerase); This family contains a number of ...
 2-65 2.05e-16

N-acylglucosamine 2-epimerase (GlcNAc 2-epimerase); This family contains a number of eukaryotic and bacterial N-acylglucosamine 2-epimerase (GlcNAc 2-epimerase) enzymes (EC:5.1.3.8) approximately 500 residues long. This converts N-acyl-D-glucosamine to N-acyl-D-mannosamine.


Pssm-ID: 399891  Cd Length: 347  Bit Score: 79.75  E-value: 2.05e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2034426951   2 AAWALALHTGDRTLLEYYEQWWDYAERHHLDFEHGSWHHELDPRNRPAATVWAGKPDVYHAYQA 65
Cdd:pfam07221 284 AAAALAQRTGEARYWDWYRRAWDYLWRHFIDPEYGSWFDELDADGEVALPLPAGKSDFYHALGA 347
PRK09813 PRK09813
fructoselysine 6-kinase; Provisional
 89-352 2.41e-16

fructoselysine 6-kinase; Provisional


Pssm-ID: 182090 [Multi-domain]  Cd Length: 260  Bit Score: 78.24  E-value: 2.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951  89 LVVVGENVMDLLPVPGgpgllRAAPGGGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGLDPDGLLAAEEPSA 168
Cdd:PRK09813    3 LATIGDNCVDIYPQLG-----KAFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGVTA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 169 LALARLgADGSAVY---------DFRMDDAaDWRWRSGElpeelepgvRALHAASLalfrepgaGAVEALLRREHGRGrV 239
Cdd:PRK09813   78 QTQVEL-HDNDRVFgdytegvmaDFALSEE-DYAWLAQY---------DIVHAAIW--------GHAEDAFPQLHAAG-K 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 240 TVSVDPNIRPGvigDPdtaralalrnaaqahLVKASDE--DLAFLYPDQD---VEKAAAALAALGPSLVVVTRGARGALA 314
Cdd:PRK09813  138 LTAFDFSDKWD---SP---------------LWQTLVPhlDYAFASAPQEdefLRLKMKAIVARGAGVVIVTLGENGSIA 199

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2034426951 315 LaHGARAEVAAP-RVEVVDTVGAGDTFM-GALLAWLDGRD 352
Cdd:PRK09813  200 W-DGAQFWRQAPePVTVVDTMGAGDSFIaGFLCGWLAGMT 238
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 89-353 1.56e-12

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: 67.34  E-value: 1.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951  89 LVVVGENVMDL------LPVPGG--PGLLRAAPGGGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGLDPDGL 160
Cdd:cd01941     2 IVVIGAANIDLrgkvsgSLVPGTsnPGHVKQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 161 LAAEEPSALALARLGADG---SAVYDfrMDdaadwrwRSGELPEELEPGVR-ALHAASLALFR-EPGAGAVEAL--LRRE 233
Cdd:cd01941    82 VFEGRSTASYTAILDKDGdlvVALAD--MD-------IYELLTPDFLRKIReALKEAKPIVVDaNLPEEALEYLlaLAAK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 234 HGRgRVTVSVD--PNIRP--GVIGDPDTARALALRNaaqAHLVKASDEDLAFLYPDQDVekaaaaLAALGPSLVVVTRGA 309
Cdd:cd01941   153 HGV-PVAFEPTsaPKLKKlfYLLHAIDLLTPNRAEL---EALAGALIENNEDENKAAKI------LLLPGIKNVIVTLGA 222

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2034426951 310 RGALA----LAHGARAEVAAPRVEVVDTVGAGDTFMGALLA-WLDGRDR 353
Cdd:cd01941   223 KGVLLssreGGVETKLFPAPQPETVVNVTGAGDAFVAGLVAgLLEGMSL 271
AGE cd00249
AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate ...
 2-74 4.56e-11

AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate epimerization during biosynthesis of N-acetylneuraminic acid. Catalytic mechanism is believed to be via nucleotide elimination and readdition and is ATP modulated. AGE is structurally and mechanistically distinct from the other four types of epimerases. The AGE domain monomer is composed of an alpha(6)/alpha(6)-barrel, the structure of which is also found in glucoamylase and cellulase. The active form is a homodimer. The alignment also contains subtype III mannose 6-phosphate isomerases.


Pssm-ID: 238153  Cd Length: 384  Bit Score: 63.92  E-value: 4.56e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2034426951   2 AAWALALHTGDRTLLEYYEQWWDYAERHHLDFEHGSWHHELDPRNRPAATVWAGKPDVYHAYQATLLPQLPLS 74
Cdd:cd00249   310 AALALAGITGDERYWQWYQRAWAYLWRHFIDPEYGLWFGYLDADGKVLLTPKGPAKTFYHVVRALYEALDVLA 382
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 206-348 1.42e-10

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: 60.19  E-value: 1.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 206 GVRALHAASLALFREPGAGAVEALLRRehgrgRVTVSVDPNIRPGvigdpDTARALALRNAAQAHLVKASDEDLAFLYPD 285
Cdd:cd00287    57 GADAVVISGLSPAPEAVLDALEEARRR-----GVPVVLDPGPRAV-----RLDGEELEKLLPGVDILTPNEEEAEALTGR 126

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2034426951 286 QDVEKAAAALAAL-----GPSLVVVTRGARGA-LALAHGARAEVAAPRVEVVDTVGAGDTFMGALLAWL 348
Cdd:cd00287   127 RDLEVKEAAEAAAlllskGPKVVIVTLGEKGAiVATRGGTEVHVPAFPVKVVDTTGAGDAFLAALAAGL 195
YegV_kinase_like cd01944
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ...
 89-348 2.19e-09

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


Pssm-ID: 238919 [Multi-domain]  Cd Length: 289  Bit Score: 58.20  E-value: 2.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951  89 LVVVGENVMDL------LPVPGG--PGLLRAAPGGGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGLDPDGL 160
Cdd:cd01944     2 VLVIGAAVVDIvldvdkLPASGGdiEAKSKSYVIGGGFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEILLP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 161 LAAEEPSALALARLGADGS----AVYDFRMDDAADWRWRSGELPEELepgvraLHAASLALFREpgaGAVEALLRREHGR 236
Cdd:cd01944    82 PRGGDDGGCLVALVEPDGErsfiSISGAEQDWSTEWFATLTVAPYDY------VYLSGYTLASE---NASKVILLEWLEA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 237 --GRVTVSVDPNIRPGVIGDPdtaraLALRNAAQAHLVKASDEDLAFLYPDQDVEKAAAALAALGP--SLVVVTRGARGA 312
Cdd:cd01944   153 lpAGTTLVFDPGPRISDIPDT-----ILQALMAKRPIWSCNREEAAIFAERGDPAAEASALRIYAKtaAPVVVRLGSNGA 227

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2034426951 313 -LALAHGARAEVAAPRVEVVDTVGAGDTFMGALLAWL 348
Cdd:cd01944   228 wIRLPDGNTHIIPGFKVKAVDTIGAGDTHAGGMLAGL 264
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
 268-352 2.85e-09

1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.


Pssm-ID: 238570 [Multi-domain]  Cd Length: 289  Bit Score: 57.54  E-value: 2.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 268 QAHLVKASDEDLA-----FLYPDQDVEKAAAALAALGPSLVVVTRGARGALaLAHGARAEVA-APRVEVVDTVGAGDTFM 341
Cdd:cd01164   177 KPFLIKPNREELEelfgrPLGDEEDVIAAARKLIERGAENVLVSLGADGAL-LVTKDGVYRAsPPKVKVVSTVGAGDSMV 255

                          90
                  ....*....|..
gi 2034426951 342 GALL-AWLDGRD 352
Cdd:cd01164   256 AGFVaGLAQGLS 267
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
299-352 1.07e-08

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 55.91  E-value: 1.07e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2034426951 299 GPSLVVVTRGARGALALAHGARAEVAAPRVEVVDTVGAGDTFMGALL-AWLDGRD 352
Cdd:COG1105   213 GAENVVVSLGADGALLVTEDGVYRAKPPKVEVVSTVGAGDSMVAGFLaGLARGLD 267
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 109-352 1.40e-08

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: 55.70  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 109 LRAAPGGGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGLDPDGLLAAEEPSALALARLGAD---------GS 179
Cdd:cd01168    50 VKYIAGGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTPDaertmctylGA 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 180 AVY------DFRMDDAADWRWRSGELpeeLEPGVRA-LHAASLAlfrepgagaveallrREHGRgRVTVS-VDPNIrpgv 251
Cdd:cd01168   130 ANElspddlDWSLLAKAKYLYLEGYL---LTVPPEAiLLAAEHA---------------KENGV-KIALNlSAPFI---- 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 252 igdpdtaraLALRNAAQAHLVKASD---------EDLAFLYPDQDVEkAAAALAALGPSLVVVTRGARGALALAHGARAE 322
Cdd:cd01168   187 ---------VQRFKEALLELLPYVDilfgneeeaEALAEAETTDDLE-AALKLLALRCRIVVITQGAKGAVVVEGGEVYP 256

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2034426951 323 VAA-PRVEVVDTVGAGDTFMGALL-AWLDGRD 352
Cdd:cd01168   257 VPAiPVEKIVDTNGAGDAFAGGFLyGLVQGEP 288
RfaE COG2870
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ...
 113-348 1.47e-08

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


Pssm-ID: 442117 [Multi-domain]  Cd Length: 321  Bit Score: 55.59  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 113 PGGGpANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGLDPDGLLAAEEPSALALARLGADGSAVydFRMDDaadw 192
Cdd:COG2870    55 PGGA-ANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPTTTKTRVIAGGQQL--LRLDF---- 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 193 rwrsgelpEELEPGVRALHAASLALFRE--PGAGAV-----------EALLRREHGRGR---VTVSVDPNIRpgvigdpd 256
Cdd:COG2870   128 --------EDRFPLSAELEARLLAALEAalPEVDAVilsdygkgvltPELIQALIALARaagKPVLVDPKGR-------- 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 257 taralALRNAAQAHLVK--------------ASDEDLaflypdqdVEKAAAALAALGPSLVVVTRGARG-ALALAHGARA 321
Cdd:COG2870   192 -----DFSRYRGATLLTpnlkeaeaavgipiADEEEL--------VAAAAELLERLGLEALLVTRGEEGmTLFDADGPPH 258

                         250       260
                  ....*....|....*....|....*..
gi 2034426951 322 EVAAPRVEVVDTVGAGDTFMGALLAWL 348
Cdd:COG2870   259 HLPAQAREVFDVTGAGDTVIATLALAL 285
PTZ00292 PTZ00292
ribokinase; Provisional
 85-344 2.79e-08

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 55.13  E-value: 2.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951  85 AAPHLVVVGENVMDL------LPVPGGPGL---LRAAPGGGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGL 155
Cdd:PTZ00292   14 AEPDVVVVGSSNTDLigyvdrMPQVGETLHgtsFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 156 DPDGLLAAEE-PSALALARL-------------GADGSAVYDFRMDDAADWRWRSGELPEELE-PGVRALHAaslalfre 220
Cdd:PTZ00292   94 NTSFVSRTENsSTGLAMIFVdtktgnneiviipGANNALTPQMVDAQTDNIQNICKYLICQNEiPLETTLDA-------- 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 221 pgagavealLRREHGRGRVTVSvdpNIRPGVigDPDTARALALRNAAQAHLVKASDEdLAFLY-----PDQDVEKAAAAL 295
Cdd:PTZ00292  166 ---------LKEAKERGCYTVF---NPAPAP--KLAEVEIIKPFLKYVSLFCVNEVE-AALITgmevtDTESAFKASKEL 230

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2034426951 296 AALGPSLVVVTRGARGALALAHG-ARAEVAAPRVEVVDTVGAGDTFMGAL 344
Cdd:PTZ00292  231 QQLGVENVIITLGANGCLIVEKEnEPVHVPGKRVKAVDTTGAGDCFVGSM 280
ribokinase_group_D cd01937
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ...
 89-346 2.81e-08

Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238912 [Multi-domain]  Cd Length: 254  Bit Score: 54.33  E-value: 2.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951  89 LVVVGENVMDLLPVPGGPgllRAAPGGGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGL--DPDG------L 160
Cdd:cd01937     2 IVIIGHVTIDEIVTNGSG---VVKPGGPATYASLTLSRLGLTVKLVTKVGRDYPDKWSDLFDNGIEVisLLSTetttfeL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 161 LAAEEPSALALARLGADGSavydfrmDDAADWRWRSGE------LPEELEPGvralhaaslaLFREPGagaveallrreh 234
Cdd:cd01937    79 NYTNEGRTRTLLAKCAAIP-------DTESPLSTITAEivilgpVPEEISPS----------LFRKFA------------ 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 235 grgrvTVSVDPNirpGVIGDPDTARALALRNAAQAHLVKASDEDLAFLypdQDVEKAAAALAALGPSLVVVTRGARGALA 314
Cdd:cd01937   130 -----FISLDAQ---GFLRRANQEKLIKCVILKLHDVLKLSRVEAEVI---STPTELARLIKETGVKEIIVTDGEEGGYI 198

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2034426951 315 LAHGARAEVAAPRVEVVDTVGAGDTFMGALLA 346
Cdd:cd01937   199 FDGNGKYTIPASKKDVVDPTGAGDVFLAAFLY 230
Guanosine_kinase_like cd01947
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ...
 98-348 3.86e-08

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: 53.96  E-value: 3.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951  98 DLLPVPGGP---GLLRAAPGGGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAvEGLDPDGLLAAEEPSALALARL 174
Cdd:cd01947    17 DAPPQPGGIshsSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELE-SGGDKHTVAWRDKPTRKTLSFI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 175 GADGSavydfrmddaadwrwrsgelPEELEPGVR---ALHAASL----ALFREPGAGAVEAllrREHGRGRVTVSVDPNI 247
Cdd:cd01947    96 DPNGE--------------------RTITVPGERledDLKWPILdegdGVFITAAAVDKEA---IRKCRETKLVILQVTP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 248 RPGVIGDPDTARalalrnaaQAHLVKASDEDLAFLYPDQDvekaaaaLAALGPSLVVVTRGARGALALAHGARAEVAAPR 327
Cdd:cd01947   153 RVRVDELNQALI--------PLDILIGSRLDPGELVVAEK-------IAGPFPRYLIVTEGELGAILYPGGRYNHVPAKK 217

                         250       260
                  ....*....|....*....|.
gi 2034426951 328 VEVVDTVGAGDTFMGALLAWL 348
Cdd:cd01947   218 AKVPDSTGAGDSFAAGFIYGL 238
1-PFK TIGR03168
hexose kinase, 1-phosphofructokinase family; This family consists largely of ...
 270-350 6.26e-08

hexose kinase, 1-phosphofructokinase family; This family consists largely of 1-phosphofructokinases, but also includes tagatose-6-kinases and 6-phosphofructokinases.


Pssm-ID: 274464 [Multi-domain]  Cd Length: 303  Bit Score: 53.73  E-value: 6.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 270 HLVKASDEDLAFL-----YPDQDVEKAAAALAALGPSLVVVTRGARGALALAHGARAEVAAPRVEVVDTVGAGDTFMGAL 344
Cdd:TIGR03168 178 FLIKPNHEELEELfgrelKTLEEIIEAARELLDRGAENVLVSLGADGALLVTKEGALKATPPKVEVVNTVGAGDSMVAGF 257


                  ....*..
gi 2034426951 345 L-AWLDG 350
Cdd:TIGR03168 258 LaGLARG 264
PLN02341 PLN02341
pfkB-type carbohydrate kinase family protein
 115-344 1.62e-07

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215195 [Multi-domain]  Cd Length: 470  Bit Score: 53.30  E-value: 1.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 115 GGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGLDPDGLL----AAEEPSALA---LARLGADG------SAV 181
Cdd:PLN02341  120 GGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGISVVGLIegtdAGDSSSASYetlLCWVLVDPlqrhgfCSR 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 182 YDFRMDDAADWrwrSGELPEElepgVRALHAASLALF------REPGAGAVEALLRREHGRGRVtVSVDPNIRPG--VIG 253
Cdd:PLN02341  200 ADFGPEPAFSW---ISKLSAE----AKMAIRQSKALFcngyvfDELSPSAIASAVDYAIDVGTA-VFFDPGPRGKslLVG 271

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 254 DPDTARALalrnaaqAHLVKASD------EDLAFLYPDQDVEKAAAALAALG--PSLVVVTRGARGALALAHGARAEVAA 325
Cdd:PLN02341  272 TPDERRAL-------EHLLRMSDvllltsEEAEALTGIRNPILAGQELLRPGirTKWVVVKMGSKGSILVTRSSVSCAPA 344

                         250
                  ....*....|....*....
gi 2034426951 326 PRVEVVDTVGAGDTFMGAL 344
Cdd:PLN02341  345 FKVNVVDTVGCGDSFAAAI 363
Ketohexokinase cd01939
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ...
 114-364 1.64e-07

Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.


Pssm-ID: 238914 [Multi-domain]  Cd Length: 290  Bit Score: 52.41  E-value: 1.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 114 GGGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVEGLDPDGL--LAAEEPSALALARLGADGSAVY--------- 182
Cdd:cd01939    36 GGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDISHCyrKDIDEPASSYIIRSRAGGRTTIvndnnlpev 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 183 ---DFR--MDDAADWRWRSGELPEELEPGVRAlhaaslalfrepgagaVEALLRREhGRGRVTVSVDpNIRPGvigdpdt 257
Cdd:cd01939   116 tydDFSkiDLTQYGWIHFEGRNPDETLRMMQH----------------IEEHNNRR-PEIRITISVE-VEKPR------- 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 258 arALALRNAAQAHLVKASdEDLAFLYPDQDVEKAAAALAALG--PSLVVVTRGARGALAL-AHGARAEV-AAPRVEVVDT 333
Cdd:cd01939   171 --EELLELAAYCDVVFVS-KDWAQSRGYKSPEECLRGEGPRAkkAALLVCTWGDQGAGALgPDGEYVHSpAHKPIRVVDT 247

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2034426951 334 VGAGDTFMGALL-AWLDGRDRLGE--DPRARLAG 364
Cdd:cd01939   248 LGAGDTFNAAVIyALNKGPDDLSEalDFGNRVAS 281
pfkB TIGR03828
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ...
 268-350 5.91e-07

1-phosphofructokinase; This enzyme acts in concert with the fructose-specific phosphotransferase system (PTS) which imports fructose as fructose-1-phosphate. The action of 1-phosphofructokinase results in beta-D-fructose-1,6-bisphosphate and is an entry point into glycolysis (GenProp0688).


Pssm-ID: 274804 [Multi-domain]  Cd Length: 304  Bit Score: 50.67  E-value: 5.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 268 QAHLVKASDEDLAFLY-----PDQDVEKAAAALAALGPSLVVVTRGARGALALAHGARAEVAAPRVEVVDTVGAGDTFMG 342
Cdd:TIGR03828 176 KPFLIKPNDEELEELFgrelkTLEEIIEAARELLDLGAENVLISLGADGALLVTKEGALFAQPPKGEVVSTVGAGDSMVA 255


                  ....*....
gi 2034426951 343 ALL-AWLDG 350
Cdd:TIGR03828 256 GFLaGLESG 264
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
 301-344 2.14e-04

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: 42.93  E-value: 2.14e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2034426951 301 SLVVVTRGARGALAL-AHGARAEVAAPRVEVVDTVGAGDTFMGAL 344
Cdd:cd01172   220 EALLVTLGEEGMTLFeRDGEVQHIPALAKEVYDVTGAGDTVIATL 264
fruK PRK09513
1-phosphofructokinase; Provisional
 303-345 6.83e-04

1-phosphofructokinase; Provisional


Pssm-ID: 181923 [Multi-domain]  Cd Length: 312  Bit Score: 41.22  E-value: 6.83e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2034426951 303 VVVTRGARGALALahGARAEVAA--PRVEVVDTVGAGDTFMGALL 345
Cdd:PRK09513  220 VVISLGAEGALWV--NASGEWIAkpPACDVVSTVGAGDSMVGGLI 262
PLN02543 PLN02543
pfkB-type carbohydrate kinase family protein
 112-153 2.01e-03

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215299  Cd Length: 496  Bit Score: 40.28  E-value: 2.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2034426951 112 APGGGPANTAVAARRLGVPTRFLARIGSDGFGRTIRHRLAVE 153
Cdd:PLN02543  170 APGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKE 211
ribokinase_group_C cd01946
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ...
 299-348 2.21e-03

Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238921 [Multi-domain]  Cd Length: 277  Bit Score: 39.76  E-value: 2.21e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2034426951 299 GPSLVVVTRGARGALALAH-GARAEVAAPRVEVVDTVGAGDTFMGALLAWL 348
Cdd:cd01946   194 GPKALIIKRGEYGALLFTDdGYFAAPAYPLESVFDPTGAGDTFAGGFIGYL 244
PRK10294 PRK10294
6-phosphofructokinase 2; Provisional
 271-344 2.71e-03

6-phosphofructokinase 2; Provisional


Pssm-ID: 182361 [Multi-domain]  Cd Length: 309  Bit Score: 39.38  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2034426951 271 LVKASDEDLAFLY------PDqDVEKAAAALAALGPS-LVVVTRGARGALALAHGARAEVAAPRVEVVDTVGAGDTFMGA 343
Cdd:PRK10294  183 LVKPNQKELSALVnrdltqPD-DVRKAAQELVNSGKAkRVVVSLGPQGALGVDSENCIQVVPPPVKSQSTVGAGDSMVGA 261


                  .
gi 2034426951 344 L 344
Cdd:PRK10294  262 M 262
 
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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