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Conserved domains on  [gi|493369371|ref|WP_006325708|]
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5-dehydro-2-deoxygluconokinase [Mesorhizobium sp. STM 4661]

Protein Classification

5-dehydro-2-deoxygluconokinase( domain architecture ID 10800799)

5-dehydro-2-deoxygluconokinase catalyzes the phosphorylation of 5-dehydro-2-deoxy-D-gluconate (2-deoxy-5-keto-D-gluconate or DKG) to 6-phospho-5-dehydro-2-deoxy-D-gluconate (DKGP); contains a C-terminal DUF2090 domain

CATH:  3.40.1190.20
EC:  2.7.1.92
PubMed:  18310071|8382990
SCOP:  4000759

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
IolC COG3892
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism];
7-644 0e+00

Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism];


:

Pssm-ID: 443099 [Multi-domain]  Cd Length: 640  Bit Score: 1037.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371   7 AKHAPLDIITIGRASVDLYGQQIGSRLEDITSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVC 86
Cdd:COG3892    1 ARMKTLDVICIGRVSVDLYGQQIGGRLEDMSSFAKYLGGSSGNIAYGTARLGLKSAMLTRVGDEHMGRFLREELEREGVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  87 VDGLKTDPDRLTALVLLSVEEEGVSPMIFYRTDCADMALSEDDIDEAFIASARAIVVTGTHFSRPNSDAAQRKAIRIMKA 166
Cdd:COG3892   81 TSGVVTDPERLTALVLLGIRDDETFPLIFYRENCADMALTEDDIDEAFIASARALLITGTHLSHPRTRAAVLKALRYARA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 167 RGGKVVFDIDYRPNLWGLAGHAEGFERYVKSDRVSAQLKTVLPHCDLIVGTEEEIMIASGADDCLSALKTIRSLSSATIV 246
Cdd:COG3892  161 HGGKVVLDIDYRPVLWGLTGHGDGETRFVASDAVTAHLQEVLPLFDLIVGTEEEFHIAGGSTDTLAALRAVRRVSTATLV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 247 LKRGAMGCIVYDGPISDDLEDGVVGKGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSRLLCAPEY 326
Cdd:COG3892  241 CKRGALGCVVFEGAIPDDLDDGITGPGFPVEVFNVLGAGDAFMSGFLRGWLRGESWETACAYANACGALVVSRHGCAPAM 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 327 PTFEELRFFLKNGSKHMALRKDEAINHIHWATTRRRDIPALMALACDHRVQLEDVAAKAGADVSRIPAFKVLTVKAAARV 406
Cdd:COG3892  321 PTWEELDYFLARGSRVPRPDKDAELNHLHRVTTRRRQWDELCVFAFDHRSQFEDMAREAGADEARIPALKRLLLEAAAQV 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 407 AAGRAG---YGMLLDEKYGRDAMFEFARHPFtWLGRPVELPGSRPLRFEFSQDIGSQLVEWPVDHCIKCLCFYHPDDPAA 483
Cdd:COG3892  401 AAGAGLrggIGVLIDDRYGQDALNAATGRGW-WIGRPVELPGSRPLRFEHGRDIGSQLVEWPQEHVVKCLVFYHPDDPAE 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 484 LKEEQQQKLRGLFEAARKVGRELLVEIIAGKHGKLDDTTIPRALEELYALGIKPDWWKLEPQaSANAWARIEAVILKHDP 563
Cdd:COG3892  480 LRLEQEAQLRRLYDACRRSGHELLLEVIPPKDGPVDDDTVARAIQRFYNLGIKPDWWKLEPM-SAAAWQAIDALIAERDP 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 564 WCRGVVLLGLEAPQDELEAAFAATAKAPIVRGFAVGRTIFINAAEQWLAGRMSDDEAVADMASRFEKLTDAWLAARDRKA 643
Cdd:COG3892  559 YCRGVVLLGLDAPEEELAAGFAAAAGSPLVKGFAVGRTIFAEPARAWLAGEIDDEEAVAEVADNYARLIDLWRAARQAAA 638

                 .
gi 493369371 644 A 644
Cdd:COG3892  639 A 639
 
Name Accession Description Interval E-value
IolC COG3892
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism];
7-644 0e+00

Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism];


Pssm-ID: 443099 [Multi-domain]  Cd Length: 640  Bit Score: 1037.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371   7 AKHAPLDIITIGRASVDLYGQQIGSRLEDITSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVC 86
Cdd:COG3892    1 ARMKTLDVICIGRVSVDLYGQQIGGRLEDMSSFAKYLGGSSGNIAYGTARLGLKSAMLTRVGDEHMGRFLREELEREGVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  87 VDGLKTDPDRLTALVLLSVEEEGVSPMIFYRTDCADMALSEDDIDEAFIASARAIVVTGTHFSRPNSDAAQRKAIRIMKA 166
Cdd:COG3892   81 TSGVVTDPERLTALVLLGIRDDETFPLIFYRENCADMALTEDDIDEAFIASARALLITGTHLSHPRTRAAVLKALRYARA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 167 RGGKVVFDIDYRPNLWGLAGHAEGFERYVKSDRVSAQLKTVLPHCDLIVGTEEEIMIASGADDCLSALKTIRSLSSATIV 246
Cdd:COG3892  161 HGGKVVLDIDYRPVLWGLTGHGDGETRFVASDAVTAHLQEVLPLFDLIVGTEEEFHIAGGSTDTLAALRAVRRVSTATLV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 247 LKRGAMGCIVYDGPISDDLEDGVVGKGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSRLLCAPEY 326
Cdd:COG3892  241 CKRGALGCVVFEGAIPDDLDDGITGPGFPVEVFNVLGAGDAFMSGFLRGWLRGESWETACAYANACGALVVSRHGCAPAM 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 327 PTFEELRFFLKNGSKHMALRKDEAINHIHWATTRRRDIPALMALACDHRVQLEDVAAKAGADVSRIPAFKVLTVKAAARV 406
Cdd:COG3892  321 PTWEELDYFLARGSRVPRPDKDAELNHLHRVTTRRRQWDELCVFAFDHRSQFEDMAREAGADEARIPALKRLLLEAAAQV 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 407 AAGRAG---YGMLLDEKYGRDAMFEFARHPFtWLGRPVELPGSRPLRFEFSQDIGSQLVEWPVDHCIKCLCFYHPDDPAA 483
Cdd:COG3892  401 AAGAGLrggIGVLIDDRYGQDALNAATGRGW-WIGRPVELPGSRPLRFEHGRDIGSQLVEWPQEHVVKCLVFYHPDDPAE 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 484 LKEEQQQKLRGLFEAARKVGRELLVEIIAGKHGKLDDTTIPRALEELYALGIKPDWWKLEPQaSANAWARIEAVILKHDP 563
Cdd:COG3892  480 LRLEQEAQLRRLYDACRRSGHELLLEVIPPKDGPVDDDTVARAIQRFYNLGIKPDWWKLEPM-SAAAWQAIDALIAERDP 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 564 WCRGVVLLGLEAPQDELEAAFAATAKAPIVRGFAVGRTIFINAAEQWLAGRMSDDEAVADMASRFEKLTDAWLAARDRKA 643
Cdd:COG3892  559 YCRGVVLLGLDAPEEELAAGFAAAAGSPLVKGFAVGRTIFAEPARAWLAGEIDDEEAVAEVADNYARLIDLWRAARQAAA 638

                 .
gi 493369371 644 A 644
Cdd:COG3892  639 A 639
myo_inos_iolC_N TIGR04382
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ...
11-336 1.65e-147

5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are translated from the iolC gene of known or putative inositol catabolism operons. Members with characterized function are 5-dehydro-2-deoxygluconokinase, the enzyme catalyzing the fifth step in degradation from myo-inositol or closely related compounds. Note that many members of this family are fusion proteins with an additional C-terminal domain, of unknown function, described by pfam09863. [Energy metabolism, Sugars]


Pssm-ID: 275175 [Multi-domain]  Cd Length: 309  Bit Score: 429.71  E-value: 1.65e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371   11 PLDIITIGRASVDLYGQQIGSRLEDITSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGL 90
Cdd:TIGR04382   1 KLDVITIGRVGVDLYPQQIGVPLEDVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371   91 KTDPDRLTALVLLSVEEEGVSPMIFYRTDCADMALSEDDIDEAFIASARAIVVTGTHFSRPNSDAAQRKAIRIMKARGGK 170
Cdd:TIGR04382  81 VTDPGRRTSLVFLEIKPPDEFPLLFYRENAADLALTPDDVDEDYIASARALLVSGTALSQEPSREAVLKALEYARAAGVR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  171 VVFDIDYRPNLWGlaghaegferyvKSDRVSAQLKTVLPHCDLIVGTEEEIMIASGADDCLSALKTIRSLSSATIVLKRG 250
Cdd:TIGR04382 161 VVLDIDYRPYLWK------------SPEEAGIYLRLVLPLVDVIIGTREEFDIAGGEGDDEAAARALLDAGVEILVVKRG 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  251 AMGCIVYDGPisddlEDGVVGKGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSRLLCAPEYPTFE 330
Cdd:TIGR04382 229 PEGSLVYTGD-----GEGVEVPGFPVEVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCSPAMPTLE 303

                  ....*.
gi 493369371  331 ELRFFL 336
Cdd:TIGR04382 304 ELEAFL 309
DUF2090 pfam09863
Uncharacterized protein conserved in bacteria (DUF2090); This domain, found in various ...
331-639 8.11e-147

Uncharacterized protein conserved in bacteria (DUF2090); This domain, found in various prokaryotic carbohydrate kinases, has no known function.


Pssm-ID: 430888  Cd Length: 310  Bit Score: 427.85  E-value: 8.11e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  331 ELRFFLKNGSKHMALRKDEAINHIHWATTRRRDIPALMALACDHRVQLEDVAAKAGADVSRIPAFKVLTVKAAARVAAGR 410
Cdd:pfam09863   1 ELDYFLSRGERVPRPDKDAELEHLHRVTTRRRQWDELCVLAFDHRSQLEELAREAGADLARIPALKRLLLRAAEEVAQEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  411 ---AGYGMLLDEKYGRDAMFEFARHPFtWLGRPVELPGSRPLRFEFSQDIGSQLVEWPVDHCIKCLCFYHPDDPAALKEE 487
Cdd:pfam09863  81 glqGGAGVLIDGRYGQDALNAATGRGW-WIGRPIELPGSRPLRFEHGRSIGSQLIEWPLEHVVKCLVFYHPDDDAALRAE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  488 QQQKLRGLFEAARKVGRELLVEIIAGKHGKLDDTTIPRALEELYALGIKPDWWKLEPQASAnAWARIEAVILKHDPWCRG 567
Cdd:pfam09863 160 QEAQLRELYDACRKSGHELLLEVIPPKDGPVDDETYARAIRRFYNLGVKPDWWKLPPLSAA-AWEQIDALIEERDPYCRG 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493369371  568 VVLLGLEAPQDELEAAFAATAKAPIVRGFAVGRTIFINAAEQWLAGRMSDDEAVADMASRFEKLTDAWLAAR 639
Cdd:pfam09863 239 VVILGLDAPEEELAAGFAAAAGFPLVKGFAVGRTIFADPARAWLAGEIDDEELIAEVAANYARLIDLWRQRR 310
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
13-320 1.46e-85

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: 269.83  E-value: 1.46e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  13 DIITIGRASVDLYGQQIGsRLEDITSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKT 92
Cdd:cd01166    1 DVVTIGEVMVDLSPPGGG-RLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  93 DPDRLTALVLLSVEEEGVSPMIFYRTDCADMALSEDDIDEAFIASARAIVVTGTHFSR-PNSDAAQRKAIRIMKARGGKV 171
Cdd:cd01166   80 DPGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEAALAGADHLHLSGITLALsESAREALLEALEAAKARGVTV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 172 VFDIDYRPNLWGLaghaegferyvksDRVSAQLKTVLPHCDLIVGTEEEIMIASGADDCLSALKTIRS--LSSATIVLKR 249
Cdd:cd01166  160 SFDLNYRPKLWSA-------------EEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALAlaLGVKAVVVKL 226
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493369371 250 GAMGCIVYDGpisddlEDGVVGKGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSRL 320
Cdd:cd01166  227 GAEGALVYTG------GGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRP 291
PRK09434 PRK09434
aminoimidazole riboside kinase; Provisional
17-318 1.29e-31

aminoimidazole riboside kinase; Provisional


Pssm-ID: 236514 [Multi-domain]  Cd Length: 304  Bit Score: 125.05  E-value: 1.29e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  17 IGRASVDLYGqqigsrlEDITSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKTDPDR 96
Cdd:PRK09434   8 LGDAVVDLIP-------EGENRYLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  97 LTALVLLSVEEEGVSPMIFYRTDCADMALSEDDI-----DEAFIASARAIVvtgthfSRPNSDAAqRKAIRIMKARGGKV 171
Cdd:PRK09434  81 RTSTVVVDLDDQGERSFTFMVRPSADLFLQPQDLppfrqGEWLHLCSIALS------AEPSRSTT-FEAMRRIKAAGGFV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 172 VFDIDYRPNLWglaghaegferyvksdRVSAQLKTVLPH----CDLIVGTEEEIMIASGADDCLSALKTIRSLSSATIVL 247
Cdd:PRK09434 154 SFDPNLREDLW----------------QDEAELRECLRQalalADVVKLSEEELCFLSGTSQLEDAIYALADRYPIALLL 217
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493369371 248 -KRGAMGCIVYDGPISDDledgVVGKgfPIEVYNVLGAGDAFMSGFLRG------WLGGESFATAATWANACGAFAVS 318
Cdd:PRK09434 218 vTLGAEGVLVHTRGQVQH----FPAP--SVDPVDTTGAGDAFVAGLLAGlsqaglWTDEAELAEIIAQAQACGALATT 289
 
Name Accession Description Interval E-value
IolC COG3892
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism];
7-644 0e+00

Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism];


Pssm-ID: 443099 [Multi-domain]  Cd Length: 640  Bit Score: 1037.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371   7 AKHAPLDIITIGRASVDLYGQQIGSRLEDITSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVC 86
Cdd:COG3892    1 ARMKTLDVICIGRVSVDLYGQQIGGRLEDMSSFAKYLGGSSGNIAYGTARLGLKSAMLTRVGDEHMGRFLREELEREGVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  87 VDGLKTDPDRLTALVLLSVEEEGVSPMIFYRTDCADMALSEDDIDEAFIASARAIVVTGTHFSRPNSDAAQRKAIRIMKA 166
Cdd:COG3892   81 TSGVVTDPERLTALVLLGIRDDETFPLIFYRENCADMALTEDDIDEAFIASARALLITGTHLSHPRTRAAVLKALRYARA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 167 RGGKVVFDIDYRPNLWGLAGHAEGFERYVKSDRVSAQLKTVLPHCDLIVGTEEEIMIASGADDCLSALKTIRSLSSATIV 246
Cdd:COG3892  161 HGGKVVLDIDYRPVLWGLTGHGDGETRFVASDAVTAHLQEVLPLFDLIVGTEEEFHIAGGSTDTLAALRAVRRVSTATLV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 247 LKRGAMGCIVYDGPISDDLEDGVVGKGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSRLLCAPEY 326
Cdd:COG3892  241 CKRGALGCVVFEGAIPDDLDDGITGPGFPVEVFNVLGAGDAFMSGFLRGWLRGESWETACAYANACGALVVSRHGCAPAM 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 327 PTFEELRFFLKNGSKHMALRKDEAINHIHWATTRRRDIPALMALACDHRVQLEDVAAKAGADVSRIPAFKVLTVKAAARV 406
Cdd:COG3892  321 PTWEELDYFLARGSRVPRPDKDAELNHLHRVTTRRRQWDELCVFAFDHRSQFEDMAREAGADEARIPALKRLLLEAAAQV 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 407 AAGRAG---YGMLLDEKYGRDAMFEFARHPFtWLGRPVELPGSRPLRFEFSQDIGSQLVEWPVDHCIKCLCFYHPDDPAA 483
Cdd:COG3892  401 AAGAGLrggIGVLIDDRYGQDALNAATGRGW-WIGRPVELPGSRPLRFEHGRDIGSQLVEWPQEHVVKCLVFYHPDDPAE 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 484 LKEEQQQKLRGLFEAARKVGRELLVEIIAGKHGKLDDTTIPRALEELYALGIKPDWWKLEPQaSANAWARIEAVILKHDP 563
Cdd:COG3892  480 LRLEQEAQLRRLYDACRRSGHELLLEVIPPKDGPVDDDTVARAIQRFYNLGIKPDWWKLEPM-SAAAWQAIDALIAERDP 558
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 564 WCRGVVLLGLEAPQDELEAAFAATAKAPIVRGFAVGRTIFINAAEQWLAGRMSDDEAVADMASRFEKLTDAWLAARDRKA 643
Cdd:COG3892  559 YCRGVVLLGLDAPEEELAAGFAAAAGSPLVKGFAVGRTIFAEPARAWLAGEIDDEEAVAEVADNYARLIDLWRAARQAAA 638

                 .
gi 493369371 644 A 644
Cdd:COG3892  639 A 639
myo_inos_iolC_N TIGR04382
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ...
11-336 1.65e-147

5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are translated from the iolC gene of known or putative inositol catabolism operons. Members with characterized function are 5-dehydro-2-deoxygluconokinase, the enzyme catalyzing the fifth step in degradation from myo-inositol or closely related compounds. Note that many members of this family are fusion proteins with an additional C-terminal domain, of unknown function, described by pfam09863. [Energy metabolism, Sugars]


Pssm-ID: 275175 [Multi-domain]  Cd Length: 309  Bit Score: 429.71  E-value: 1.65e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371   11 PLDIITIGRASVDLYGQQIGSRLEDITSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGL 90
Cdd:TIGR04382   1 KLDVITIGRVGVDLYPQQIGVPLEDVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371   91 KTDPDRLTALVLLSVEEEGVSPMIFYRTDCADMALSEDDIDEAFIASARAIVVTGTHFSRPNSDAAQRKAIRIMKARGGK 170
Cdd:TIGR04382  81 VTDPGRRTSLVFLEIKPPDEFPLLFYRENAADLALTPDDVDEDYIASARALLVSGTALSQEPSREAVLKALEYARAAGVR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  171 VVFDIDYRPNLWGlaghaegferyvKSDRVSAQLKTVLPHCDLIVGTEEEIMIASGADDCLSALKTIRSLSSATIVLKRG 250
Cdd:TIGR04382 161 VVLDIDYRPYLWK------------SPEEAGIYLRLVLPLVDVIIGTREEFDIAGGEGDDEAAARALLDAGVEILVVKRG 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  251 AMGCIVYDGPisddlEDGVVGKGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSRLLCAPEYPTFE 330
Cdd:TIGR04382 229 PEGSLVYTGD-----GEGVEVPGFPVEVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCSPAMPTLE 303

                  ....*.
gi 493369371  331 ELRFFL 336
Cdd:TIGR04382 304 ELEAFL 309
DUF2090 pfam09863
Uncharacterized protein conserved in bacteria (DUF2090); This domain, found in various ...
331-639 8.11e-147

Uncharacterized protein conserved in bacteria (DUF2090); This domain, found in various prokaryotic carbohydrate kinases, has no known function.


Pssm-ID: 430888  Cd Length: 310  Bit Score: 427.85  E-value: 8.11e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  331 ELRFFLKNGSKHMALRKDEAINHIHWATTRRRDIPALMALACDHRVQLEDVAAKAGADVSRIPAFKVLTVKAAARVAAGR 410
Cdd:pfam09863   1 ELDYFLSRGERVPRPDKDAELEHLHRVTTRRRQWDELCVLAFDHRSQLEELAREAGADLARIPALKRLLLRAAEEVAQEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  411 ---AGYGMLLDEKYGRDAMFEFARHPFtWLGRPVELPGSRPLRFEFSQDIGSQLVEWPVDHCIKCLCFYHPDDPAALKEE 487
Cdd:pfam09863  81 glqGGAGVLIDGRYGQDALNAATGRGW-WIGRPIELPGSRPLRFEHGRSIGSQLIEWPLEHVVKCLVFYHPDDDAALRAE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  488 QQQKLRGLFEAARKVGRELLVEIIAGKHGKLDDTTIPRALEELYALGIKPDWWKLEPQASAnAWARIEAVILKHDPWCRG 567
Cdd:pfam09863 160 QEAQLRELYDACRKSGHELLLEVIPPKDGPVDDETYARAIRRFYNLGVKPDWWKLPPLSAA-AWEQIDALIEERDPYCRG 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493369371  568 VVLLGLEAPQDELEAAFAATAKAPIVRGFAVGRTIFINAAEQWLAGRMSDDEAVADMASRFEKLTDAWLAAR 639
Cdd:pfam09863 239 VVILGLDAPEEELAAGFAAAAGFPLVKGFAVGRTIFADPARAWLAGEIDDEELIAEVAANYARLIDLWRQRR 310
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
13-320 1.46e-85

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: 269.83  E-value: 1.46e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  13 DIITIGRASVDLYGQQIGsRLEDITSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKT 92
Cdd:cd01166    1 DVVTIGEVMVDLSPPGGG-RLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  93 DPDRLTALVLLSVEEEGVSPMIFYRTDCADMALSEDDIDEAFIASARAIVVTGTHFSR-PNSDAAQRKAIRIMKARGGKV 171
Cdd:cd01166   80 DPGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEAALAGADHLHLSGITLALsESAREALLEALEAAKARGVTV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 172 VFDIDYRPNLWGLaghaegferyvksDRVSAQLKTVLPHCDLIVGTEEEIMIASGADDCLSALKTIRS--LSSATIVLKR 249
Cdd:cd01166  160 SFDLNYRPKLWSA-------------EEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALAlaLGVKAVVVKL 226
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493369371 250 GAMGCIVYDGpisddlEDGVVGKGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSRL 320
Cdd:cd01166  227 GAEGALVYTG------GGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRP 291
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
13-332 9.90e-84

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: 265.21  E-value: 9.90e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  13 DIITIGRASVDLYGQ----QIGSRLEDITSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVD 88
Cdd:COG0524    1 DVLVIGEALVDLVARvdrlPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  89 GLKTDPDRLTALVLLSVEEEGVSPMIFYRtdCADMALSEDDIDEAFIASARAIVVTGTHFSRPNSDAAQRKAIRIMKARG 168
Cdd:COG0524   81 GVRRDPGAPTGLAFILVDPDGERTIVFYR--GANAELTPEDLDEALLAGADILHLGGITLASEPPREALLAALEAARAAG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 169 GKVVFDIDYRPNLWglaghaegferyvksDRVSAQLKTVLPHCDLIVGTEEEIMIASGADDCLSALKTIRSLSSATIVLK 248
Cdd:COG0524  159 VPVSLDPNYRPALW---------------EPARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVT 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 249 RGAMGCIVYDGpisddlEDGVVGKGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSRLLCAPEYPT 328
Cdd:COG0524  224 LGAEGALLYTG------GEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPT 297

                 ....
gi 493369371 329 FEEL 332
Cdd:COG0524  298 REEV 301
bac_FRK cd01167
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ...
14-319 1.46e-47

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: 168.97  E-value: 1.46e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  14 IITIGRASVDLYGQQIGSRLEditsFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKTD 93
Cdd:cd01167    2 VVCFGEALIDFIPEGSGAPET----FTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  94 PDRLTALVLLSVEEEGVSPMIFYRTDCADMALsEDDIDEAFIASARaIVVTGTH-FSRPNSDAAQRKAIRIMKARGGKVV 172
Cdd:cd01167   78 PAAPTTLAFVTLDADGERSFEFYRGPAADLLL-DTELNPDLLSEAD-ILHFGSIaLASEPSRSALLELLEAAKKAGVLIS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 173 FDIDYRPNLWGlaghaegferyvKSDRVSAQLKTVLPHCDLIVGTEEEIMIASGADDCLSALKTIRSLSSATIVLKRGAM 252
Cdd:cd01167  156 FDPNLRPPLWR------------DEEEARERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRGAD 223
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493369371 253 GCIVYDGpisddledGVVG--KGFPIEVYNVLGAGDAFMSGFLRG-WLGGESFATAATW------ANACGAFAVSR 319
Cdd:cd01167  224 GALLYTK--------GGVGevPGIPVEVVDTTGAGDAFVAGLLAQlLSRGLLALDEDELaealrfANAVGALTCTK 291
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
13-319 5.11e-46

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 164.82  E-value: 5.11e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371   13 DIITIGRASVDLYGQQIGSRLEDIT--SFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGL 90
Cdd:pfam00294   1 KVVVIGEANIDLIGNVEGLPGELVRvsTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371   91 KTDPDRLTALVLLSVEEEGVSPMIFYRTDCADMALSEDDIDEAFIASARAIVVTGThFSRPNSDAAQRKAIRIMKARGgk 170
Cdd:pfam00294  81 VIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLYISGS-LPLGLPEATLEELIEAAKNGG-- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  171 vVFDIDYRPNLWGLAGhaegferyvksdrvsaQLKTVLPHCDLIVGTEEEIMIASGA-----DDCLSALKTIRSLSSATI 245
Cdd:pfam00294 158 -TFDPNLLDPLGAARE----------------ALLELLPLADLLKPNEEELEALTGAklddiEEALAALHKLLAKGIKTV 220
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493369371  246 VLKRGAMGCIVYDGpisddleDGVVG--KGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSR 319
Cdd:pfam00294 221 IVTLGADGALVVEG-------DGEVHvpAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQK 289
PRK09434 PRK09434
aminoimidazole riboside kinase; Provisional
17-318 1.29e-31

aminoimidazole riboside kinase; Provisional


Pssm-ID: 236514 [Multi-domain]  Cd Length: 304  Bit Score: 125.05  E-value: 1.29e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  17 IGRASVDLYGqqigsrlEDITSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKTDPDR 96
Cdd:PRK09434   8 LGDAVVDLIP-------EGENRYLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  97 LTALVLLSVEEEGVSPMIFYRTDCADMALSEDDI-----DEAFIASARAIVvtgthfSRPNSDAAqRKAIRIMKARGGKV 171
Cdd:PRK09434  81 RTSTVVVDLDDQGERSFTFMVRPSADLFLQPQDLppfrqGEWLHLCSIALS------AEPSRSTT-FEAMRRIKAAGGFV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 172 VFDIDYRPNLWglaghaegferyvksdRVSAQLKTVLPH----CDLIVGTEEEIMIASGADDCLSALKTIRSLSSATIVL 247
Cdd:PRK09434 154 SFDPNLREDLW----------------QDEAELRECLRQalalADVVKLSEEELCFLSGTSQLEDAIYALADRYPIALLL 217
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493369371 248 -KRGAMGCIVYDGPISDDledgVVGKgfPIEVYNVLGAGDAFMSGFLRG------WLGGESFATAATWANACGAFAVS 318
Cdd:PRK09434 218 vTLGAEGVLVHTRGQVQH----FPAP--SVDPVDTTGAGDAFVAGLLAGlsqaglWTDEAELAEIIAQAQACGALATT 289
PLN02323 PLN02323
probable fructokinase
30-341 1.09e-28

probable fructokinase


Pssm-ID: 215183 [Multi-domain]  Cd Length: 330  Bit Score: 117.03  E-value: 1.09e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  30 GSRLEDITSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKTDPDRLTALVLLSVEEEG 109
Cdd:PLN02323  29 GVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDG 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 110 VSPMIFYRTDCADMALSEDDIDEAFIASARAIvvtgtHF------SRPnSDAAQRKAIRIMKARGGKVVFDIDYRPNLWG 183
Cdd:PLN02323 109 EREFMFYRNPSADMLLRESELDLDLIRKAKIF-----HYgsisliTEP-CRSAHLAAMKIAKEAGALLSYDPNLRLPLWP 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 184 LAGHAEgferyvksdrvsAQLKTVLPHCDLIVGTEEEIMIASGADDCL--SALKTIRSLSSATIVLKrGAMGCIVYDGPI 261
Cdd:PLN02323 183 SAEAAR------------EGIMSIWDEADIIKVSDEEVEFLTGGDDPDddTVVKLWHPNLKLLLVTE-GEEGCRYYTKDF 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 262 SddledGVVGkGFPIEVYNVLGAGDAFMSGFL------RGWLGGES-FATAATWANACGAFAVSRLLCAPEYPTFEELRF 334
Cdd:PLN02323 250 K-----GRVE-GFKVKAVDTTGAGDAFVGGLLsqlakdLSLLEDEErLREALRFANACGAITTTERGAIPALPTKEAVLK 323

                 ....*..
gi 493369371 335 FLKNGSK 341
Cdd:PLN02323 324 LLKKAVA 330
ribokinase_group_A cd01942
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ...
41-319 4.21e-27

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: 111.25  E-value: 4.21e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  41 KSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKTDPDRLTALVLLSVEEEGVSPMIFYRtdc 120
Cdd:cd01942   33 REFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSHVRVVDEDSTGVAFILTDGDDNQIAYFYP--- 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 121 ADMALSEDDIDEAFIASARAIvvtgtHFSrpNSDAAQRKAiRIMKARGGKVVFDidyrPnlwglaGHAEgferyvkSDRV 200
Cdd:cd01942  110 GAMDELEPNDEADPDGLADIV-----HLS--SGPGLIELA-RELAAGGITVSFD----P------GQEL-------PRLS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 201 SAQLKTVLPHCDLIVGTEEEIMIASGaddcLSALKT-IRSLSSATIVLKRGAMGCIVYDGpisddlEDGVVGKGFP-IEV 278
Cdd:cd01942  165 GEELEEILERADILFVNDYEAELLKE----RTGLSEaELASGVRVVVVTLGPKGAIVFED------GEEVEVPAVPaVKV 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 493369371 279 YNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSR 319
Cdd:cd01942  235 VDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVER 275
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
13-328 2.46e-26

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: 109.18  E-value: 2.46e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  13 DIITIGRASVDLYgqqigSRLEDI---------TSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKRE 83
Cdd:cd01174    1 KVVVVGSINVDLV-----TRVDRLpkpgetvlgSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  84 GVCVDGLKTDPDRLTALVLLSVEEEG-----VSPMifyrtdcADMALSEDDIDEA--FIASARAIVV---TgthfsrpnS 153
Cdd:cd01174   76 GIDVSYVEVVVGAPTGTAVITVDESGenrivVVPG-------ANGELTPADVDAAleLIAAADVLLLqleI--------P 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 154 DAAQRKAIRIMKARGGKVVFDidyrpnlwgLAGhaegferyvksdrVSAQLKTVLPHCDLIVGTEEEIMIASGA-----D 228
Cdd:cd01174  141 LETVLAALRAARRAGVTVILN---------PAP-------------ARPLPAELLALVDILVPNETEAALLTGIevtdeE 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 229 DCLSALKTIRSLSSATIVLKRGAMGCIVYDGPISDDLEdgvvgkGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATW 308
Cdd:cd01174  199 DAEKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVP------AFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRF 272
                        330       340
                 ....*....|....*....|
gi 493369371 309 ANACGAFAVSRLLCAPEYPT 328
Cdd:cd01174  273 ANAAAALSVTRPGAQPSIPT 292
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
11-320 3.48e-22

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: 97.68  E-value: 3.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  11 PLDIITIGRASVDL-----------YGQQIGS-------RLEDITSFAKSV---GGCPANISVGTARLGLRSALLTRVGD 69
Cdd:cd01168    1 RYDVLGLGNALVDIlaqvddaflekLGLKKGDmiladmeEQEELLAKLPVKyiaGGSAANTIRGAAALGGSAAFIGRVGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  70 EQMGRFIREQLKREGVCVDgLKTDPDRLTA--LVLLSVEEEgvspmifyRTDCADMA----LSEDDIDEAFIASARAIVV 143
Cdd:cd01168   81 DKLGDFLLKDLRAAGVDTR-YQVQPDGPTGtcAVLVTPDAE--------RTMCTYLGaaneLSPDDLDWSLLAKAKYLYL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 144 TGTHFsRPNSDAAQrKAIRIMKARGGKVVFDIdyrpnlwglaghAEGFEryvkSDRVSAQLKTVLPHCDLIVGTEEEIMI 223
Cdd:cd01168  152 EGYLL-TVPPEAIL-LAAEHAKENGVKIALNL------------SAPFI----VQRFKEALLELLPYVDILFGNEEEAEA 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 224 ASGADDCLS---ALKTIRSLSSaTIVLKRGAMGCIVYDGpisddledgvvGKGFPIEVYNV------LGAGDAFMSGFLR 294
Cdd:cd01168  214 LAEAETTDDleaALKLLALRCR-IVVITQGAKGAVVVEG-----------GEVYPVPAIPVekivdtNGAGDAFAGGFLY 281
                        330       340
                 ....*....|....*....|....*.
gi 493369371 295 GWLGGESFATAATWANACGAFAVSRL 320
Cdd:cd01168  282 GLVQGEPLEECIRLGSYAAAEVIQQL 307
PRK09813 PRK09813
fructoselysine 6-kinase; Provisional
16-318 6.32e-18

fructoselysine 6-kinase; Provisional


Pssm-ID: 182090 [Multi-domain]  Cd Length: 260  Bit Score: 84.02  E-value: 6.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  16 TIGRASVDLYgQQIGSRLEditsfaksvGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKTDPD 95
Cdd:PRK09813   5 TIGDNCVDIY-PQLGKAFS---------GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  96 RlTALVLLSVE---------EEGVspmifyrtdCADMALSEDDIDeaFIASaRAIVVTGThFSRPNSDAAQrkairiMKA 166
Cdd:PRK09813  75 V-TAQTQVELHdndrvfgdyTEGV---------MADFALSEEDYA--WLAQ-YDIVHAAI-WGHAEDAFPQ------LHA 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 167 RGGKVVFDIDYRPN--LWglaghaegferyvksdrvsaqlKTVLPHCDLIVGTeeeimiASGADDCL-SALKTIRSLSSA 243
Cdd:PRK09813 135 AGKLTAFDFSDKWDspLW----------------------QTLVPHLDYAFAS------APQEDEFLrLKMKAIVARGAG 186
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493369371 244 TIVLKRGAMGCIVYDGpisDDLEDGVVgkgFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVS 318
Cdd:PRK09813 187 VVIVTLGENGSIAWDG---AQFWRQAP---EPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQ 255
Fructoselysine_kinase_like cd01940
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ...
14-315 7.70e-18

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: 83.94  E-value: 7.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  14 IITIGRASVDLYGQQIGSRleditsfaksVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKTD 93
Cdd:cd01940    2 LAAIGDNVVDKYLHLGKMY----------PGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVK 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  94 P-DRLTALVLLS-------VEEEGVspmifyrtdCADMALSEDDIdeAFIASARaIVVTGTHfSRPNSdaaQRKAIRIMK 165
Cdd:cd01940   72 EgENAVADVELVdgdrifgLSNKGG---------VAREHPFEADL--EYLSQFD-LVHTGIY-SHEGH---LEKALQALV 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 166 ARGGKVVFDIDYRpnlwglaghaegferyvksdRVSAQLKTVLPHCDlivgteeeIMIASGADD----CLSALKTIRSLS 241
Cdd:cd01940  136 GAGALISFDFSDR--------------------WDDDYLQLVCPYVD--------FAFFSASDLsdeeVKAKLKEAVSRG 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 242 SATIVLKRGAMGCIVYDGpiSDDLEDGVVgkgfPIEVYNVLGAGDAFMSGFLRGWL-GGESFATAA-----TWANAC--- 312
Cdd:cd01940  188 AKLVIVTRGEDGAIAYDG--AVFYSVAPR----PVEVVDTLGAGDSFIAGFLLSLLaGGTAIAEAMrqgaqFAAKTCghe 261

                 ...
gi 493369371 313 GAF 315
Cdd:cd01940  262 GAF 264
PTZ00292 PTZ00292
ribokinase; Provisional
13-332 4.84e-16

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 79.78  E-value: 4.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  13 DIITIGRASVDLYG-----QQIGSRLEDiTSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCV 87
Cdd:PTZ00292  17 DVVVVGSSNTDLIGyvdrmPQVGETLHG-TSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNT 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  88 DGLKTDPDRLTALVLLSVEEE-GVSPMIFyrTDCADMALSEDDIDEAF--IASARAIVVTGTHFSRPNSDAaqrkAIRIM 164
Cdd:PTZ00292  96 SFVSRTENSSTGLAMIFVDTKtGNNEIVI--IPGANNALTPQMVDAQTdnIQNICKYLICQNEIPLETTLD----ALKEA 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 165 KARGGKVVFDIDYRPNLWGLaghaegferyvksdrvsAQLKTVLPHCDLIVGTEEEIMIASGAD--DCLSALKTIRS--- 239
Cdd:PTZ00292 170 KERGCYTVFNPAPAPKLAEV-----------------EIIKPFLKYVSLFCVNEVEAALITGMEvtDTESAFKASKElqq 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 240 LSSATIVLKRGAMGC-IVYDGpisddlEDGVVGKGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVS 318
Cdd:PTZ00292 233 LGVENVIITLGANGClIVEKE------NEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVT 306
                        330
                 ....*....|....
gi 493369371 319 RLLCAPEYPTFEEL 332
Cdd:PTZ00292 307 RHGTQSSYPHPSEL 320
ribokinase_group_B cd01945
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ...
37-320 2.77e-15

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: 76.56  E-value: 2.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  37 TSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKTDPDRLTALVLLSVEEEGVSPMIFY 116
Cdd:cd01945   29 TDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSPISSITDITGDRATISIT 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 117 rtdCADMALSEDDIDEAFIASARAIVVTGTHfsrpnSDAAQrKAIRIMKARGGKVVFDIDyrpnlwglAGHAEGFERyvk 196
Cdd:cd01945  109 ---AIDTQAAPDSLPDAILGGADAVLVDGRQ-----PEAAL-HLAQEARARGIPIPLDLD--------GGGLRVLEE--- 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 197 sdrvsaqlktVLPHCDLIVGTEEEIMIASGADDcLSALKTIRSLSSATIVLKRGAMGCIVYDgpisddlEDGVVGKG--F 274
Cdd:cd01945  169 ----------LLPLADHAICSENFLRPNTGSAD-DEALELLASLGIPFVAVTLGEAGCLWLE-------RDGELFHVpaF 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 493369371 275 PIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSRL 320
Cdd:cd01945  231 PVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGL 276
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
14-318 5.05e-13

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: 70.04  E-value: 5.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  14 IITIGRASVDLYGQqIGSRLEDITSFA----KSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDG 89
Cdd:cd01941    2 IVVIGAANIDLRGK-VSGSLVPGTSNPghvkQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  90 LKtDPDRLTALVLLSVEEEGVSPMIFyrtdcADMA----LSEDDIDEA--FIASARAIVVTGthfsrpN--SDAAQRkai 161
Cdd:cd01941   81 IV-FEGRSTASYTAILDKDGDLVVAL-----ADMDiyelLTPDFLRKIreALKEAKPIVVDA------NlpEEALEY--- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 162 rIMKARGGKVVfdidyrpnlwglaghAEGFERyVKSDRVSAqLKTVLPHCDLIVGTEEEI-----MIASGADDCLSALKT 236
Cdd:cd01941  146 -LLALAAKHGV---------------PVAFEP-TSAPKLKK-LFYLLHAIDLLTPNRAELealagALIENNEDENKAAKI 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 237 IRSLSSATIVLKRGAMGCIVYDGpisddlEDGVVGKGFPI----EVYNVLGAGDAFMSGFLRGWLGGESFATAATWANAC 312
Cdd:cd01941  208 LLLPGIKNVIVTLGAKGVLLSSR------EGGVETKLFPApqpeTVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAA 281

                 ....*.
gi 493369371 313 GAFAVS 318
Cdd:cd01941  282 AALTLE 287
Guanosine_kinase_like cd01947
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ...
14-319 1.51e-12

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: 68.21  E-value: 1.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  14 IITIGRASVDLYGQ-----QIGSRLEdITSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVC-V 87
Cdd:cd01947    2 IAVVGHVEWDIFLSldappQPGGISH-SSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKhT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  88 DGLKTDPDRLTALVLLSVEEEGVSpmIFYRTDCADMALSE-DDIDEAFIASARAivvtgthfsrpnsDAAQRKAIRIMKA 166
Cdd:cd01947   81 VAWRDKPTRKTLSFIDPNGERTIT--VPGERLEDDLKWPIlDEGDGVFITAAAV-------------DKEAIRKCRETKL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 167 RggkvvfdidyrpnLWGLAGHAEgferyvksdrvSAQLKTVLPHCDLIVGTEEEIMIASGADDclSALKTIRslssaTIV 246
Cdd:cd01947  146 V-------------ILQVTPRVR-----------VDELNQALIPLDILIGSRLDPGELVVAEK--IAGPFPR-----YLI 194
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493369371 247 LKRGAMGCIVYDGpisddLEDGVVgKGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSR 319
Cdd:cd01947  195 VTEGELGAILYPG-----GRYNHV-PAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSH 261
PLN02967 PLN02967
kinase
7-182 8.24e-12

kinase


Pssm-ID: 215521 [Multi-domain]  Cd Length: 581  Bit Score: 68.15  E-value: 8.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371   7 AKHApldIITIGRASVDLYGQQIGSRLEDI----TSFAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKR 82
Cdd:PLN02967 205 AQHA---FVPSGRPANRLLDYEIHERMKDAfwapEKFVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNV 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  83 EGVCVDGLKTDPDRLTALVLLSVEEEGVSPMIFYRTdCADMALSEDDIDEAFIASARAIVVTGTHFSRPNSDAAQRKAIR 162
Cdd:PLN02967 282 NKVQTRSVCIDGKRATAVSTMKIAKRGRLKTTCVKP-CAEDSLSKSEINIDVLKEAKMFYFNTHSLLDPTMRSTTLRAIK 360
                        170       180
                 ....*....|....*....|
gi 493369371 163 IMKARGGKVVFDIDYRPNLW 182
Cdd:PLN02967 361 ISKKLGGVIFYDLNLPLPLW 380
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
49-325 1.24e-11

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 65.93  E-value: 1.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  49 NISVGTARLGLRSALLTRVGDEQmGRFIREQLKREGVCVDGLKTDPD-RLTalVLLSVEEEGVSPMIFYRTdcadMALSE 127
Cdd:COG1105   40 NVARVLKALGVDVTALGFLGGFT-GEFIEELLDEEGIPTDFVPIEGEtRIN--IKIVDPSDGTETEINEPG----PEISE 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 128 DDIDEAF------IASARAIVVTGthfSRPN--SDAAQRKAIRIMKARGGKVVFDIDyrpnlwglaGHAegferyvksdr 199
Cdd:COG1105  113 EELEALLerleelLKEGDWVVLSG---SLPPgvPPDFYAELIRLARARGAKVVLDTS---------GEA----------- 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 200 vsaqLKTVLPHC-DLIVGTEEEIMIASG-----ADDCLSALKTIRSLSSATIVLKRGAMGCIVYDgpisddlEDGVV-GK 272
Cdd:COG1105  170 ----LKAALEAGpDLIKPNLEELEELLGrpletLEDIIAAARELLERGAENVVVSLGADGALLVT-------EDGVYrAK 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 493369371 273 GFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSRL---LCAPE 325
Cdd:COG1105  239 PPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPgtgLPDRE 294
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
14-333 2.39e-11

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: 65.27  E-value: 2.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  14 IITIGRASVD--LYGQQIGSRLE------DITSFAKSVGGCpANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGV 85
Cdd:cd01172    2 VLVVGDVILDeyLYGDVERISPEapvpvvKVEREEIRLGGA-ANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  86 CVDGLkTDPDRLT---------ALVLLSVEEEGVSPMifyrtdcadMALSEDDIDEAF---IASARAIVVT----GThFS 149
Cdd:cd01172   81 DTDGI-VDEGRPTttktrviarNQQLLRVDREDDSPL---------SAEEEQRLIERIaerLPEADVVILSdygkGV-LT 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 150 RPNSDAAQRKAirimKARGGKVVFDidyrpnlwgLAGHaeGFERYvksdrvsaqlktvlPHCDLIVGTEEEIMIASGADD 229
Cdd:cd01172  150 PRVIEALIAAA----RELGIPVLVD---------PKGR--DYSKY--------------RGATLLTPNEKEAREALGDEI 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 230 C-----LSALKTIRSLSSATIVL-KRGAMGCIVYDGpisddlEDGVVGkgFP---IEVYNVLGAGDAFMSGFLRGWLGGE 300
Cdd:cd01172  201 NdddelEAAGEKLLELLNLEALLvTLGEEGMTLFER------DGEVQH--IPalaKEVYDVTGAGDTVIATLALALAAGA 272
                        330       340       350
                 ....*....|....*....|....*....|...
gi 493369371 301 SFATAATWANACGAFAVSRLLCAPeyPTFEELR 333
Cdd:cd01172  273 DLEEAAFLANAAAGVVVGKVGTAP--VTPKELL 303
1-PFK TIGR03168
hexose kinase, 1-phosphofructokinase family; This family consists largely of ...
49-319 7.83e-11

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: 63.75  E-value: 7.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371   49 NISVGTARLGLRSALLTRVGDEQmGRFIREQLKREGVCVDGLKTDPD-RL-TALVLLSVEEegvspmifYRTDCADMALS 126
Cdd:TIGR03168  40 NVARVLARLGAEVVATGFLGGFT-GEFIEALLAEEGIKNDFVEVKGEtRInVKIKESSGEE--------TELNEPGPEIS 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  127 EDDIDE------AFIASARAIVVTGthfSRPN--SDAAQRKAIRIMKARGGKVVFD---------IDYRPNLwglaghae 189
Cdd:TIGR03168 111 EEELEQlleklrELLASGDIVVISG---SLPPgvPPDFYAQLIAIARKKGAKVILDtsgealreaLAAKPFL-------- 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  190 gferyVKSDRvsAQLKTvlpHCDLIVGTEEEImiasgaddcLSALKTIRSLSSATIVLKRGAMGCIVYDGpisddlEDGV 269
Cdd:TIGR03168 180 -----IKPNH--EELEE---LFGRELKTLEEI---------IEAARELLDRGAENVLVSLGADGALLVTK------EGAL 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 493369371  270 VGKGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSR 319
Cdd:TIGR03168 235 KATPPKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFS 284
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
130-297 8.04e-11

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: 61.73  E-value: 8.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 130 IDEAFIASARAIVVTGTHFSRpnsdAAQRKAIRIMKARGGKVVFDIDYRPNLWglaghaegferyvksdrVSAQLKTVLP 209
Cdd:cd00287   50 GVSVTLVGADAVVISGLSPAP----EAVLDALEEARRRGVPVVLDPGPRAVRL-----------------DGEELEKLLP 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 210 HCDLIVGTEEEIMIASGADD-----CLSALKTIRSLSSATIVLKRGAMGCIVYDGPisddlEDGVVGKGFPIEVYNVLGA 284
Cdd:cd00287  109 GVDILTPNEEEAEALTGRRDlevkeAAEAAALLLSKGPKVVIVTLGEKGAIVATRG-----GTEVHVPAFPVKVVDTTGA 183
                        170
                 ....*....|...
gi 493369371 285 GDAFMSGFLRGWL 297
Cdd:cd00287  184 GDAFLAALAAGLA 196
RfaE COG2870
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ...
48-333 8.51e-11

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


Pssm-ID: 442117 [Multi-domain]  Cd Length: 321  Bit Score: 63.68  E-value: 8.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  48 ANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKTDPDRLTAL---------VLLSVEEEGVSPmifyrt 118
Cdd:COG2870   59 ANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPTTTktrviaggqQLLRLDFEDRFP------ 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 119 dcadmaLSEDDID------EAFIASARAIVV--------TGTHFsrpnsdaaqRKAIRIMKARGGKVVFD------IDYR 178
Cdd:COG2870  133 ------LSAELEArllaalEAALPEVDAVILsdygkgvlTPELI---------QALIALARAAGKPVLVDpkgrdfSRYR 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 179 ------PNLwglaghAEgFERYVKSDRVsaqlktvlphcdlivgTEEEIMIAsgaddclsALKTIRSLSSATIVLKRGAM 252
Cdd:COG2870  198 gatlltPNL------KE-AEAAVGIPIA----------------DEEELVAA--------AAELLERLGLEALLVTRGEE 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 253 GCIVYDgpisddlEDGVVgKGFPI---EVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSRLLCAPeyPTF 329
Cdd:COG2870  247 GMTLFD-------ADGPP-HHLPAqarEVFDVTGAGDTVIATLALALAAGASLEEAAELANLAAGIVVGKLGTAT--VSP 316

                 ....
gi 493369371 330 EELR 333
Cdd:COG2870  317 EELL 320
PLN02341 PLN02341
pfkB-type carbohydrate kinase family protein
44-314 5.39e-10

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215195 [Multi-domain]  Cd Length: 470  Bit Score: 62.16  E-value: 5.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  44 GGCpaNISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKTDPD-----RLTALVLLS-VEEEGVSPMIF-Y 116
Cdd:PLN02341 121 GNC--NFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGISVVGLIEGTDagdssSASYETLLCwVLVDPLQRHGFcS 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 117 RTD-CADMALS-----EDDIDEAfIASARAIVVTGTHFSRPNSDAAQrKAIRIMKARGGKVVFDIDYRpnlwglaghaeG 190
Cdd:PLN02341 199 RADfGPEPAFSwisklSAEAKMA-IRQSKALFCNGYVFDELSPSAIA-SAVDYAIDVGTAVFFDPGPR-----------G 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 191 FERYVKSDRVSAQLKTVLPHCDLIVGTEEEIMIASGADDCLSALKTIRSLSSAT--IVLKRGAMGCIVYDgpisddlEDG 268
Cdd:PLN02341 266 KSLLVGTPDERRALEHLLRMSDVLLLTSEEAEALTGIRNPILAGQELLRPGIRTkwVVVKMGSKGSILVT-------RSS 338
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 493369371 269 VVGKG-FPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGA 314
Cdd:PLN02341 339 VSCAPaFKVNVVDTVGCGDSFAAAIALGYIHNLPLVNTLTLANAVGA 385
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
44-320 7.62e-10

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: 60.24  E-value: 7.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  44 GGCPANISVGTARLGLRSALLTRVGDEqMGRFIREQLKREGVCVDGLKTDPDRLTALVLlsVEEEGVSpmifYRTDCADM 123
Cdd:cd01164   36 GGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVEVAGETRINVKI--KEEDGTE----TEINEPGP 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 124 ALSEDDIdEAFIASARAIVVTGTHF----SRPNS--DAAQRKAIRIMKARGGKVVFDIDYRPNLWGLAGHAegferyvks 197
Cdd:cd01164  109 EISEEEL-EALLEKLKALLKKGDIVvlsgSLPPGvpADFYAELVRLAREKGARVILDTSGEALLAALAAKP--------- 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 198 drvsaqlktvlphcDLIVGTEEEIMIASGA-----DDCLSALKTIRSLSSATIVLKRGAMGCIVYDGpisddlEDGVVGK 272
Cdd:cd01164  179 --------------FLIKPNREELEELFGRplgdeEDVIAAARKLIERGAENVLVSLGADGALLVTK------DGVYRAS 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 493369371 273 GFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSRL 320
Cdd:cd01164  239 PPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSP 286
PRK09850 PRK09850
pseudouridine kinase; Provisional
14-332 1.60e-09

pseudouridine kinase; Provisional


Pssm-ID: 182111 [Multi-domain]  Cd Length: 313  Bit Score: 59.62  E-value: 1.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  14 IITIGRASVDLYGQQIGSrlediTSFAKS--------VGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGV 85
Cdd:PRK09850   7 VVIIGSANIDVAGYSHES-----LNYADSnpgkikftPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  86 CVDGLKTDPDRLTALVLLSVEEEGvsPMIfyrTDCADMALSeDDIDEAFIASARAIVvtgthfsrpnsdaaqrkairimk 165
Cdd:PRK09850  82 YVDKCLIVPGENTSSYLSLLDNTG--EML---VAINDMNIS-NAITAEYLAQHREFI----------------------- 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 166 aRGGKVVF---DIDYRPNLWGL--AGHAEGFERYVKS-------DRVSaQLKTVLPHcDLIVGTEEEIMIaSGADDCLSA 233
Cdd:PRK09850 133 -QRAKVIVadcNISEEALAWILdnAANVPVFVDPVSAwkcvkvrDRLN-QIHTLKPN-RLEAETLSGIAL-SGREDVAKV 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 234 LKTIRSLSSATIVLKRGAMGciVYDGPISddledGVVGKGFPIE--VYNVLGAGDAFMSGFLRGWLGGESFATAATWANA 311
Cdd:PRK09850 209 AAWFHQHGLNRLVLSMGGDG--VYYSDIS-----GESGWSAPIKtnVINVTGAGDAMMAGLASCWVDGMPFAESVRFAQG 281
                        330       340
                 ....*....|....*....|.
gi 493369371 312 CGAFAVsrllcAPEYPTFEEL 332
Cdd:PRK09850 282 CSSMAL-----SCEYTNNPDL 297
PLN02543 PLN02543
pfkB-type carbohydrate kinase family protein
39-182 3.45e-09

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215299  Cd Length: 496  Bit Score: 59.54  E-value: 3.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  39 FAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKTDPDRLTALVLLSVE-EEGVSPMIFYR 117
Cdd:PLN02543 167 FARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACSRMKIKfRDGGKMVAETV 246
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493369371 118 TDCADMALSEDDIDEAFIASARAIVVTGTHFSRPNSDAAQRKAIRIMKARGGKVVFDIDYRPNLW 182
Cdd:PLN02543 247 KEAAEDSLLASELNLAVLKEARMFHFNSEVLTSPSMQSTLFRAIELSKKFGGLIFFDLNLPLPLW 311
PRK11142 PRK11142
ribokinase; Provisional
44-336 5.13e-09

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 57.96  E-value: 5.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  44 GGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKTDPDRLTALVLLSVEEEG-----VSPMifyrt 118
Cdd:PRK11142  39 GGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEGensigIHAG----- 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 119 dcADMALSEDDID--EAFIASARAIVVtgtHFSRPNSDAAqrKAIRIMKARGGKVVFDidyrPnlwglAGHAEgferyvk 196
Cdd:PRK11142 114 --ANAALTPALVEahRELIANADALLM---QLETPLETVL--AAAKIAKQHGTKVILN----P-----APARE------- 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 197 sdrVSAQLktvLPHCDLIVGTEEEIMIASG-----ADDCLSALKTIRSLSSATIVLKRGAMGciVYdgpISDDLEDGVVg 271
Cdd:PRK11142 171 ---LPDEL---LALVDIITPNETEAEKLTGirvedDDDAAKAAQVLHQKGIETVLITLGSRG--VW---LSENGEGQRV- 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493369371 272 KGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSRLLCAPEYPTFEELRFFL 336
Cdd:PRK11142 239 PGFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFL 303
PLN02813 PLN02813
pfkB-type carbohydrate kinase family protein
13-301 6.15e-09

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215434 [Multi-domain]  Cd Length: 426  Bit Score: 58.67  E-value: 6.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  13 DIITIGRASVDLYG----------------------QQIGSRLE--DITSFAKSVGGCPANISVGTARLGLRS------- 61
Cdd:PLN02813  71 DVLGLGQAMVDFSGmvddeflerlglekgtrkvinhEERGKVLRalDGCSYKASAGGSLSNTLVALARLGSQSaagpaln 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  62 -ALLTRVGDEQMGRFIREQLKREGVCVDGlKTDPDRLTALVLLSVEEEGVSPMIFYRTDCADMALSEdDIDEAfIASARA 140
Cdd:PLN02813 151 vAMAGSVGSDPLGDFYRTKLRRANVHFLS-QPVKDGTTGTVIVLTTPDAQRTMLSYQGTSSTVNYDS-CLASA-ISKSRV 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 141 IVVTGTHFSRPNSDAAQRKAIRIMKARGGKVVF---DID----YRPNLWGLAGHAEGFeRYVKSDRVSAQlktvlphCDL 213
Cdd:PLN02813 228 LVVEGYLWELPQTIEAIAQACEEAHRAGALVAVtasDVScierHRDDFWDVMGNYADI-LFANSDEARAL-------CGL 299
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 214 ivGTEEEIMIASGADDCLSALKTIRSLSSATIVlkrGAMGCIVYDGPisddledgvvgkgFPIEVYNVLGAGDAFMSGFL 293
Cdd:PLN02813 300 --GSEESPESATRYLSHFCPLVSVTDGARGSYI---GVKGEAVYIPP-------------SPCVPVDTCGAGDAYAAGIL 361

                 ....*...
gi 493369371 294 RGWLGGES 301
Cdd:PLN02813 362 YGLLRGVS 369
YegV_kinase_like cd01944
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ...
37-319 6.72e-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: 57.43  E-value: 6.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  37 TSFAKSVGGCpANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDGLKTDPDRLTALVLLSveeEGVSPMIFY 116
Cdd:cd01944   29 KSKSYVIGGG-FNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEILLPPRGGDDGGCLVALV---EPDGERSFI 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 117 RTDCADMALSEDDIDEAFIASARAIVVTGTHFSRPN-SDAAQRKAIRIMKARggkVVFDIDYRPNLWGLAGHaegferyv 195
Cdd:cd01944  105 SISGAEQDWSTEWFATLTVAPYDYVYLSGYTLASENaSKVILLEWLEALPAG---TTLVFDPGPRISDIPDT-------- 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 196 ksdrvsaQLKTVLPHCDLIVGTEEEIMIASGADDcLSALKTIRSLSS---ATIVLKRGAMGCIVYDGpisdDLEDGVVgK 272
Cdd:cd01944  174 -------ILQALMAKRPIWSCNREEAAIFAERGD-PAAEASALRIYAktaAPVVVRLGSNGAWIRLP----DGNTHII-P 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 493369371 273 GFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSR 319
Cdd:cd01944  241 GFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTR 287
pfkB TIGR03828
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ...
161-319 2.16e-08

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: 56.06  E-value: 2.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  161 IRIMKARGGKVVFD---------IDYRPNLwglaghaegferyVKSDRvsAQLKTvlpHCDLIVGTEEEImiasgaddcL 231
Cdd:TIGR03828 150 IALAREKGAKVILDtsgealrdgLKAKPFL-------------IKPND--EELEE---LFGRELKTLEEI---------I 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  232 SALKTIRSLSSATIVLKRGAMGCIVYDGpisddlEDGVVGKGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANA 311
Cdd:TIGR03828 203 EAARELLDLGAENVLISLGADGALLVTK------EGALFAQPPKGEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVA 276

                  ....*...
gi 493369371  312 CGAFAVSR 319
Cdd:TIGR03828 277 AGSAAAFS 284
ribokinase_group_D cd01937
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ...
14-317 5.81e-06

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: 48.17  E-value: 5.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  14 IITIGRASVDLYgQQIGSRleditsfAKSVGGCPANISVGTARLGLRSALLTRVGDEQMGRFIREQLKREGVCVDG---- 89
Cdd:cd01937    2 IVIIGHVTIDEI-VTNGSG-------VVKPGGPATYASLTLSRLGLTVKLVTKVGRDYPDKWSDLFDNGIEVISLLstet 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371  90 ------LKTDPDRLTALVLLSVEEEGVSPMIFYRTDCADMALSEDDIDEAFIASARAIVVTgthfsrpnsdaaqrkairi 163
Cdd:cd01937   74 ttfelnYTNEGRTRTLLAKCAAIPDTESPLSTITAEIVILGPVPEEISPSLFRKFAFISLD------------------- 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 164 mkarggkvvfdidyrpnlwglaghAEGFERYVKSDRVSAQlkTVLPHCDLIVGTEEEIMIASgadDCLSALKTIRSLSSA 243
Cdd:cd01937  135 ------------------------AQGFLRRANQEKLIKC--VILKLHDVLKLSRVEAEVIS---TPTELARLIKETGVK 185
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493369371 244 TIVLKRGAMGCIVYDGpisddlEDGVVGKGFPIEVYNVLGAGDAFMSGFLRGWLGGESFATAATWANACGAFAV 317
Cdd:cd01937  186 EIIVTDGEEGGYIFDG------NGKYTIPASKKDVVDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAKFI 253
ribokinase_group_C cd01946
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ...
204-297 7.38e-06

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: 48.23  E-value: 7.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 204 LKTVLPHCDLIVGTEEEIMIASGADDCLSALKTIRSLSSATIVLKRGAMGCIVYDgpisddlEDGV-VGKGFPIE-VYNV 281
Cdd:cd01946  157 LKKVLAKVDVVIINDGEARQLTGAANLVKAARLILAMGPKALIIKRGEYGALLFT-------DDGYfAAPAYPLEsVFDP 229
                         90
                 ....*....|....*.
gi 493369371 282 LGAGDAFMSGFLrGWL 297
Cdd:cd01946  230 TGAGDTFAGGFI-GYL 244
PTZ00247 PTZ00247
adenosine kinase; Provisional
201-329 7.43e-04

adenosine kinase; Provisional


Pssm-ID: 240328 [Multi-domain]  Cd Length: 345  Bit Score: 42.32  E-value: 7.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493369371 201 SAQLKTVLPHCDLIVGTEEEIMIASGADDC-LSALKTIrSLSSATIVLKRGAMGCIVYdgpISDDLEDGVVGKGFPIEVY 279
Cdd:PTZ00247 205 FERLLQVLPYVDILFGNEEEAKTFAKAMKWdTEDLKEI-AARIAMLPKYSGTRPRLVV---FTQGPEPTLIATKDGVTSV 280
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493369371 280 NVL-----------GAGDAFMSGFLRGWLGGESFATAATWANACGAFAVSRLLCA-PEYPTF 329
Cdd:PTZ00247 281 PVPpldqekivdtnGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGCTyPEKPPF 342
 
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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