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Conserved domains on  [gi|1720410217|ref|XP_030109733|]
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FGGY carbohydrate kinase domain-containing protein isoform X25 [Mus musculus]

Protein Classification

FGGY-family carbohydrate kinase( domain architecture ID 10167359)

FGGY-family carbohydrate kinase catalyzes the ATP-dependent phosphorylation of a carbohydrate substrate to produce phosphorylated sugar and ADP; similar to Homo sapiens FGGY carbohydrate kinase domain-containing protein and Saccharomyces cerevisiae D-ribulokinase YDR109C

CATH:  3.30.420.40
EC:  2.7.1.-
Gene Ontology:  GO:0016310|GO:0019200|GO:0005524
PubMed:  22215998|8800467|7781919
SCOP:  3000092

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASKHA_NBD_FGGY_D-RBK cd07782
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ...
 2-336 0e+00

nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily includes vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein) and similar proteins, such as Saccharomyces cerevisiae D-ribulokinase YDR109C, Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.


:

Pssm-ID: 466800 [Multi-domain]  Cd Length: 540  Bit Score: 614.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217   2 IGLEDLIDDNYSKIGNLVLLPGAALGIGLTPEAARELGLPSGIAVAASLIDAHAGGLGVIGADVrgHGLTCEGQPVTSRL 81
Cdd:cd07782   205 IGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAKELGLPEGTPVGVSLIDAHAGGLGTLGADV--GGLPCEADPLTRRL 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  82 AVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNSH 161
Cdd:cd07782   283 ALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGLWLNEGGQSATGALLDHIIETHPAYPELKEEAKAAGKSIYEYLNER 362

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 162 LDLIKKAQ--PVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEAAGH 239
Cdd:cd07782   363 LEQLAEEKglPLAYLTRDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALLYLATLQALAYGTRHIIEAMNAAGH 442

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 240 SLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFPEHADKKYY 319
Cdd:cd07782   443 KIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWDAMAAMSGPGKVVEPNEELKKYH 522

                         330
                  ....*....|....*..
gi 1720410217 320 DKKYQVFLRMVEHQKEY 336
Cdd:cd07782   523 DRKYEVFLKMYEDQREY 539
 
Name Accession Description Interval E-value
ASKHA_NBD_FGGY_D-RBK cd07782
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ...
 2-336 0e+00

nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily includes vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein) and similar proteins, such as Saccharomyces cerevisiae D-ribulokinase YDR109C, Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.


Pssm-ID: 466800 [Multi-domain]  Cd Length: 540  Bit Score: 614.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217   2 IGLEDLIDDNYSKIGNLVLLPGAALGIGLTPEAARELGLPSGIAVAASLIDAHAGGLGVIGADVrgHGLTCEGQPVTSRL 81
Cdd:cd07782   205 IGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAKELGLPEGTPVGVSLIDAHAGGLGTLGADV--GGLPCEADPLTRRL 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  82 AVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNSH 161
Cdd:cd07782   283 ALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGLWLNEGGQSATGALLDHIIETHPAYPELKEEAKAAGKSIYEYLNER 362

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 162 LDLIKKAQ--PVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEAAGH 239
Cdd:cd07782   363 LEQLAEEKglPLAYLTRDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALLYLATLQALAYGTRHIIEAMNAAGH 442

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 240 SLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFPEHADKKYY 319
Cdd:cd07782   443 KIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWDAMAAMSGPGKVVEPNEELKKYH 522

                         330
                  ....*....|....*..
gi 1720410217 320 DKKYQVFLRMVEHQKEY 336
Cdd:cd07782   523 DRKYEVFLKMYEDQREY 539
5C_CHO_kinase TIGR01315
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of ...
 2-336 8.29e-140

FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of carbohydrate kinases. This subfamily is closely related to a set of ribulose kinases, and many members are designated ribitol kinase. However, the member from Klebsiella pneumoniae, from a ribitol catabolism operon, accepts D-ribulose and to a lesser extent D-arabinitol and ribitol (and JW Lengeler, personal communication); its annotation in GenBank as ribitol kinase is imprecise and may have affected public annotation of related proteins.


Pssm-ID: 273552 [Multi-domain]  Cd Length: 541  Bit Score: 406.97  E-value: 8.29e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217   2 IGLEDLIDDNYSKIGNLVLLPGAALGIGLTPEAARELGLPSGIAVAASLIDAHAGGLGVIGADVRGHGltcEGQPVTSRL 81
Cdd:TIGR01315 205 IGLGELVTDNFIRMGGSWMSPGELVGGGLTAEAAQELGLPAGTAVGSGLIDAHAGWIGTVGAKVAENG---DVSQAFTRL 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  82 AVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNSH 161
Cdd:TIGR01315 282 AAVAGTSTCHMAMTKGPVFVPGVWGPYRDALIPGYWLAEGGQSAAGELMDHMLETHVAYDETVKEAEAAGKNIYDYLNEH 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 162 LdLIKKAQP----VGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEAA 237
Cdd:TIGR01315 362 L-KEMAAKTnapsISYLVRHFHVYPDLWGNRSPIADPNMRGVIIGLSMDRSKDGLALLYYATMEFIAYGTRQIVEAMNTA 440

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 238 GHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFP-EHADK 316
Cdd:TIGR01315 441 GHTIKSIFMSGGQCQNPLLMQLIADACDMPVLIPYVNEAVLHGAAMLGAKAAGTTESLWDAMDRMSKPGKTVWPrGDPAK 520

                         330       340
                  ....*....|....*....|
gi 1720410217 317 KYYDKKYQVFLRMVEHQKEY 336
Cdd:TIGR01315 521 KLHDRKYEIFLQLARTQQEY 540
AraB COG1069
Ribulose kinase [Carbohydrate transport and metabolism];
3-338 7.02e-124

Ribulose kinase [Carbohydrate transport and metabolism];


Pssm-ID: 440687 [Multi-domain]  Cd Length: 532  Bit Score: 365.98  E-value: 7.02e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217   3 GLEDLIDdnysKIGNLVLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAGGLGVIGAdvrghgltCEGQpvtsrLA 82
Cdd:COG1069   222 LLDGLAD----RLGTEIYPLGEPAG-TLTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGGV--------EPGT-----LV 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  83 VICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNshl 162
Cdd:COG1069   284 KVMGTSTCHMLVSPEERFVPGICGQVDGSIVPGMWGYEAGQSAVGDIFAWFVRLLVPPLEYEKEAEERGISLHPLLT--- 360

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 163 dliKKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDlaiLYLATVQAIAFGTRFIIETMEAAGHSLS 242
Cdd:COG1069   361 ---EEAAKLPPGESGLHALDWFNGNRSPLADQRLKGVILGLTLGTDAED---IYRALVEATAFGTRAIIERFEEEGVPID 434

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 243 TLFLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKV-GKVVFPEHADKKYYD 320
Cdd:COG1069   435 EIIACGGIAtKNPLVMQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEEAMAAMGSGfDKVYTPDPENVAVYD 514

                         330
                  ....*....|....*...
gi 1720410217 321 KKYQVFLRMVEHQKEYSA 338
Cdd:COG1069   515 ALYAEYLQLHDYFGRGRN 532
FGGY_C pfam02782
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ...
 81-288 5.04e-60

FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.


Pssm-ID: 426979 [Multi-domain]  Cd Length: 197  Bit Score: 191.38  E-value: 5.04e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  81 LAVICGTSSCHMGISKDPV-FVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAkaTARCQSIYAYLN 159
Cdd:pfam02782   1 LAISAGTSSFVLVETPEPVlSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELRD--AGNVESLAELAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 160 SHLDLikkaqpvgfLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLddlAILYLATVQAIAFGTRFIIETMEA-AG 238
Cdd:pfam02782  79 LAAVA---------PAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTL---AHLYRAILESLALQLRQILEALTKqEG 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720410217 239 HSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACA 288
Cdd:pfam02782 147 HPIDTIHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
PRK04123 PRK04123
ribulokinase; Provisional
 29-340 1.48e-59

ribulokinase; Provisional


Pssm-ID: 235221 [Multi-domain]  Cd Length: 548  Bit Score: 200.46  E-value: 1.48e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  29 GLTPEAARELGLPSGIAVAASLIDAHAGglgVIGADVRGHGLTcegqpvtsrlAVIcGTSSCHMGISKDPVFVPGVWGPY 108
Cdd:PRK04123  251 TLTAEWAQRLGLPEGVAVSVGAFDAHMG---AVGAGAEPGTLV----------KVM-GTSTCDILLADKQRAVPGICGQV 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 109 YSAMVPGFWLNEGGQSVTGKL----IDHMVQghpafPELQAKATARCQSIYAYLNshldliKKA--QPVG---FLTVDlh 179
Cdd:PRK04123  317 DGSIVPGLIGYEAGQSAVGDIfawfARLLVP-----PEYKDEAEARGKQLLELLT------EAAakQPPGehgLVALD-- 383

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 180 vWpdFHGNRSPLADLTLKGMVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLS-KNPLFVQ 258
Cdd:PRK04123  384 -W--FNGRRTPLADQRLKGVITGLTLGTDAPDI---YRALIEATAFGTRAIMECFEDQGVPVEEVIAAGGIArKNPVLMQ 457

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 259 MHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARM-SKVGKVVFPEHADKKYYDKKYQVFLRMVE-HQKEY 336
Cdd:PRK04123  458 IYADVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDIPEAQQAMaSPVEKTYQPDPENVARYEQLYQEYKQLHDyFGRGG 537


                  ....
gi 1720410217 337 SAIM 340
Cdd:PRK04123  538 NAVM 541
 
Name Accession Description Interval E-value
ASKHA_NBD_FGGY_D-RBK cd07782
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ...
 2-336 0e+00

nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily includes vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein) and similar proteins, such as Saccharomyces cerevisiae D-ribulokinase YDR109C, Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.


Pssm-ID: 466800 [Multi-domain]  Cd Length: 540  Bit Score: 614.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217   2 IGLEDLIDDNYSKIGNLVLLPGAALGIGLTPEAARELGLPSGIAVAASLIDAHAGGLGVIGADVrgHGLTCEGQPVTSRL 81
Cdd:cd07782   205 IGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAKELGLPEGTPVGVSLIDAHAGGLGTLGADV--GGLPCEADPLTRRL 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  82 AVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNSH 161
Cdd:cd07782   283 ALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGLWLNEGGQSATGALLDHIIETHPAYPELKEEAKAAGKSIYEYLNER 362

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 162 LDLIKKAQ--PVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEAAGH 239
Cdd:cd07782   363 LEQLAEEKglPLAYLTRDLHVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALLYLATLQALAYGTRHIIEAMNAAGH 442

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 240 SLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFPEHADKKYY 319
Cdd:cd07782   443 KIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWDAMAAMSGPGKVVEPNEELKKYH 522

                         330
                  ....*....|....*..
gi 1720410217 320 DKKYQVFLRMVEHQKEY 336
Cdd:cd07782   523 DRKYEVFLKMYEDQREY 539
5C_CHO_kinase TIGR01315
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of ...
 2-336 8.29e-140

FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of carbohydrate kinases. This subfamily is closely related to a set of ribulose kinases, and many members are designated ribitol kinase. However, the member from Klebsiella pneumoniae, from a ribitol catabolism operon, accepts D-ribulose and to a lesser extent D-arabinitol and ribitol (and JW Lengeler, personal communication); its annotation in GenBank as ribitol kinase is imprecise and may have affected public annotation of related proteins.


Pssm-ID: 273552 [Multi-domain]  Cd Length: 541  Bit Score: 406.97  E-value: 8.29e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217   2 IGLEDLIDDNYSKIGNLVLLPGAALGIGLTPEAARELGLPSGIAVAASLIDAHAGGLGVIGADVRGHGltcEGQPVTSRL 81
Cdd:TIGR01315 205 IGLGELVTDNFIRMGGSWMSPGELVGGGLTAEAAQELGLPAGTAVGSGLIDAHAGWIGTVGAKVAENG---DVSQAFTRL 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  82 AVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNSH 161
Cdd:TIGR01315 282 AAVAGTSTCHMAMTKGPVFVPGVWGPYRDALIPGYWLAEGGQSAAGELMDHMLETHVAYDETVKEAEAAGKNIYDYLNEH 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 162 LdLIKKAQP----VGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEAA 237
Cdd:TIGR01315 362 L-KEMAAKTnapsISYLVRHFHVYPDLWGNRSPIADPNMRGVIIGLSMDRSKDGLALLYYATMEFIAYGTRQIVEAMNTA 440

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 238 GHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFP-EHADK 316
Cdd:TIGR01315 441 GHTIKSIFMSGGQCQNPLLMQLIADACDMPVLIPYVNEAVLHGAAMLGAKAAGTTESLWDAMDRMSKPGKTVWPrGDPAK 520

                         330       340
                  ....*....|....*....|
gi 1720410217 317 KYYDKKYQVFLRMVEHQKEY 336
Cdd:TIGR01315 521 KLHDRKYEIFLQLARTQQEY 540
AraB COG1069
Ribulose kinase [Carbohydrate transport and metabolism];
3-338 7.02e-124

Ribulose kinase [Carbohydrate transport and metabolism];


Pssm-ID: 440687 [Multi-domain]  Cd Length: 532  Bit Score: 365.98  E-value: 7.02e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217   3 GLEDLIDdnysKIGNLVLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAGGLGVIGAdvrghgltCEGQpvtsrLA 82
Cdd:COG1069   222 LLDGLAD----RLGTEIYPLGEPAG-TLTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGGV--------EPGT-----LV 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  83 VICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNshl 162
Cdd:COG1069   284 KVMGTSTCHMLVSPEERFVPGICGQVDGSIVPGMWGYEAGQSAVGDIFAWFVRLLVPPLEYEKEAEERGISLHPLLT--- 360

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 163 dliKKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDlaiLYLATVQAIAFGTRFIIETMEAAGHSLS 242
Cdd:COG1069   361 ---EEAAKLPPGESGLHALDWFNGNRSPLADQRLKGVILGLTLGTDAED---IYRALVEATAFGTRAIIERFEEEGVPID 434

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 243 TLFLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKV-GKVVFPEHADKKYYD 320
Cdd:COG1069   435 EIIACGGIAtKNPLVMQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEEAMAAMGSGfDKVYTPDPENVAVYD 514

                         330
                  ....*....|....*...
gi 1720410217 321 KKYQVFLRMVEHQKEYSA 338
Cdd:COG1069   515 ALYAEYLQLHDYFGRGRN 532
ASKHA_NBD_FGGY_RBK-like cd07768
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ...
 2-326 1.91e-84

nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family includes bacterial RBK, vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein), Saccharomyces cerevisiae D-ribulokinase YDR109C, and Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466788 [Multi-domain]  Cd Length: 522  Bit Score: 264.49  E-value: 1.91e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217   2 IGLEDLiDDNYSKIGNLVLLPGAALGIGLtPEAARELGLPSGIAVAASLIDAHAGGLGVIGADVRGhgltcegqpvtsRL 81
Cdd:cd07768   205 IDPRLE-HLTTTKNLPSNVPIGTTSGVAL-PEMAEKMGLHPGTAVVVSCIDAHASWFAVASPHLET------------SL 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  82 AVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQaKATARCQSIYAYLNsh 161
Cdd:cd07768   271 FMIAGTSSCHMYGTTISDRIPGVWGPFDTIIDPDYSVYEAGQSATGKLIEHLFESHPCARKFD-EALKKGADIYQVLE-- 347

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 162 lDLIKKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEAAGHSL 241
Cdd:cd07768   348 -QTIRQIEKNNGLSIHILTLDMFFGNRSEFADPRLKGSFIGESLDTSMLNLTYKYIAILEALAFGTRLIIDTFQNEGIHI 426

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 242 STLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFT---SVQEAMARMSKVGKVVFPE-HADKK 317
Cdd:cd07768   427 KELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGILGAAVLAKVAAGKKQladSITEADISNDRKSETFEPLaYRLGA 506


                  ....*....
gi 1720410217 318 YYDKKYQVF 326
Cdd:cd07768   507 DYILLYKLL 515
ASKHA_NBD_FGGY_L-RBK cd07781
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ...
 2-329 2.10e-84

nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466799 [Multi-domain]  Cd Length: 504  Bit Score: 264.01  E-value: 2.10e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217   2 IGLEDLidDNYSKIGNLVLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAGglgVIGADVRGHGltcegqpvtsRL 81
Cdd:cd07781   201 LDPGLL--KLREKLPGEVVPVGEPAG-TLTAEAAERLGLPAGIPVAQGGIDAHMG---AIGAGVVEPG----------TL 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  82 AVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDhmvqghpAFPELQAKATA-RCQSIYAYLNs 160
Cdd:cd07781   265 ALIMGTSTCHLMVSPKPVDIPGICGPVPDAVVPGLYGLEAGQSAVGDIFA-------WFVRLFVPPAEeRGDSIYALLS- 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 161 hlDLIKKAQPV--GFLTVDlhvWpdFHGNRSPLADLTLKGMVTGLTLSQDLddlAILYLATVQAIAFGTRFIIETMEAAG 238
Cdd:cd07781   337 --EEAAKLPPGesGLVALD---W--FNGNRTPLVDPRLRGAIVGLTLGTTP---AHIYRALLEATAFGTRAIIERFEEAG 406

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 239 HSLSTLFLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFPEHADKK 317
Cdd:cd07781   407 VPVNRVVACGGIAeKNPLWMQIYADVLGRPIKVPKSDQAPALGAAILAAVAAGVYADIEEAADAMVRVDRVYEPDPENHA 486

                         330
                  ....*....|..
gi 1720410217 318 YYDKKYQVFLRM 329
Cdd:cd07781   487 VYEELYALYKEL 498
FGGY_C pfam02782
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ...
 81-288 5.04e-60

FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.


Pssm-ID: 426979 [Multi-domain]  Cd Length: 197  Bit Score: 191.38  E-value: 5.04e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  81 LAVICGTSSCHMGISKDPV-FVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAkaTARCQSIYAYLN 159
Cdd:pfam02782   1 LAISAGTSSFVLVETPEPVlSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELRD--AGNVESLAELAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 160 SHLDLikkaqpvgfLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLddlAILYLATVQAIAFGTRFIIETMEA-AG 238
Cdd:pfam02782  79 LAAVA---------PAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTL---AHLYRAILESLALQLRQILEALTKqEG 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720410217 239 HSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACA 288
Cdd:pfam02782 147 HPIDTIHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
PRK04123 PRK04123
ribulokinase; Provisional
 29-340 1.48e-59

ribulokinase; Provisional


Pssm-ID: 235221 [Multi-domain]  Cd Length: 548  Bit Score: 200.46  E-value: 1.48e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  29 GLTPEAARELGLPSGIAVAASLIDAHAGglgVIGADVRGHGLTcegqpvtsrlAVIcGTSSCHMGISKDPVFVPGVWGPY 108
Cdd:PRK04123  251 TLTAEWAQRLGLPEGVAVSVGAFDAHMG---AVGAGAEPGTLV----------KVM-GTSTCDILLADKQRAVPGICGQV 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 109 YSAMVPGFWLNEGGQSVTGKL----IDHMVQghpafPELQAKATARCQSIYAYLNshldliKKA--QPVG---FLTVDlh 179
Cdd:PRK04123  317 DGSIVPGLIGYEAGQSAVGDIfawfARLLVP-----PEYKDEAEARGKQLLELLT------EAAakQPPGehgLVALD-- 383

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 180 vWpdFHGNRSPLADLTLKGMVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLS-KNPLFVQ 258
Cdd:PRK04123  384 -W--FNGRRTPLADQRLKGVITGLTLGTDAPDI---YRALIEATAFGTRAIMECFEDQGVPVEEVIAAGGIArKNPVLMQ 457

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 259 MHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARM-SKVGKVVFPEHADKKYYDKKYQVFLRMVE-HQKEY 336
Cdd:PRK04123  458 IYADVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDIPEAQQAMaSPVEKTYQPDPENVARYEQLYQEYKQLHDyFGRGG 537


                  ....
gi 1720410217 337 SAIM 340
Cdd:PRK04123  538 NAVM 541
XylB COG1070
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ...
 19-335 1.23e-53

Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440688 [Multi-domain]  Cd Length: 494  Bit Score: 183.50  E-value: 1.23e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  19 VLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDP 98
Cdd:COG1070   207 LVPPGEVAG-TLTAEAAAETGLPAGTPVVAGAGDNAAAALGA--------GAVEPGD-----AAVSLGTSGVVFVVSDKP 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  99 VFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQghpafpELQAKAtarcQSIYAYLNshlDLIKKAQP----VGFL 174
Cdd:COG1070   273 LPDPEGRVHTFCHAVPGRWLPMGATNNGGSALRWFRD------LFADGE----LDDYEELN---ALAAEVPPgadgLLFL 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 175 tvdlhvwPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNP 254
Cdd:COG1070   340 -------PYLSGERTPHWDPNARGAFFGLTLSHTRAHL---ARAVLEGVAFALRDGLEALEEAGVKIDRIRATGGGARSP 409

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 255 LFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFPEHADKKYYDKKYQVFLRMVEHQK 334
Cdd:COG1070   410 LWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMVRVGETIEPDPENVAAYDELYERYRELYPALK 489


                  .
gi 1720410217 335 E 335
Cdd:COG1070   490 P 490
ASKHA_NBD_FGGY_YgcE-like cd07779
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ...
 22-319 2.67e-51

nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli sugar kinase YgcE. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466798 [Multi-domain]  Cd Length: 433  Bit Score: 175.78  E-value: 2.67e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  22 PGAALGiGLTPEAARELGLPSGIAVAASlidAHAGGLGVIGAdvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFV 101
Cdd:cd07779   162 PGTVIG-TLTKEAAEETGLPEGTPVVAG---GGDQQCAALGA-----GVLEPGT-----ASLSLGTAAVVIAVSDKPVED 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 102 PGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQghpAFPELQAKATARCQSIYAYLNSHLDLIkkaqPVGFLtvDLHVW 181
Cdd:cd07779   228 PERRIPCNPSAVPGKWVLEGSINTGGSAVRWFRD---EFGQDEVAEKELGVSPYELLNEEAAKS----PPGSD--GLLFL 298

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 182 PDFHGNRSPLADLTLKGMVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHA 261
Cdd:cd07779   299 PYLAGAGTPYWNPEARGAFIGLTLSHTRAHL---ARAILEGIAFELRDNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIA 375

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720410217 262 DITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFPEHADKKYY 319
Cdd:cd07779   376 DVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKAMVRVTDTFEPDPENVAIY 433
L-ribulokinase TIGR01234
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely ...
 30-336 2.49e-47

ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely related protein subfamily outside the scope of this model includes ribitol kinase from E. coli. [Energy metabolism, Sugars]


Pssm-ID: 130301 [Multi-domain]  Cd Length: 536  Bit Score: 167.41  E-value: 2.49e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  30 LTPEAARELGLPSGIAVAASLIDAHaggLGVIGADVrghgltceGQPvtSRLAVICGTSSCHMGISKDPVFVPGVWGPYY 109
Cdd:TIGR01234 248 LTPEWAQRTGLPEGVVVAVGNFDAH---VGAVAAGI--------AQP--GALVKIMGTSTCHVLIGDKQRAVPGMCGVVD 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 110 SAMVPGFWLNEGGQSVTGKLIDHMVQgHPAFPELQAKATARCQSiyayLNSHLDLIKKAQPV---GFLTVDlhvWpdFHG 186
Cdd:TIGR01234 315 GGIVPGFIGYEAGQSAVGDIFAWFGK-VCVPPELKTEANASQKQ----LHEALSEAAAKQPSgehGLVALD---W--FNG 384

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 187 NRSPLADLTLKGMVTGLTLSQDLDDlaiLYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLS-KNPLFVQMHADITG 265
Cdd:TIGR01234 385 NRSPLVDQRLKGVITGLTLATDAPL---LYRALIEATAFGTRMIMETFTDSGVPVEELMAAGGIArKNPVIMQIYADVTN 461

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720410217 266 MPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVF---PEHADKkyYDKKYQVFLRMVEHQKEY 336
Cdd:TIGR01234 462 RPLQIVASDQAPALGAAIFAAVAAGVYADIPSAQAKMGSAVEKTLtpcSENAQR--YEQLYARYQELAMSFGQY 533
ASKHA_NBD_FGGY cd00366
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ...
 19-285 2.00e-40

nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466787 [Multi-domain]  Cd Length: 392  Bit Score: 146.17  E-value: 2.00e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  19 VLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQPVtsrlaVICGTSSCHMGISKDP 98
Cdd:cd00366   158 IVESGEVVG-RVTPEAAEETGLPAGTPVVAGGGDTAAAALGA--------GVVEPGDAV-----DSTGTSSVLSVCTDEP 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  99 VFVPGVWGPYYSAmVPGFWLNEGGQSVTGKLIDHMvqghpafpelqAKATARCQSIYAYLNSHLDLIKKAQP----VGFL 174
Cdd:cd00366   224 VPPDPRLLNRCHV-VPGLWLLEGAINTGGASLRWF-----------RDEFGEEEDSDAEYEGLDELAAEVPPgsdgLIFL 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 175 tvdlhvwPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNP 254
Cdd:cd00366   292 -------PYLSGERSPIWDPAARGVFFGLTLSHTRAHL---IRAVLEGVAYALRDNLEILEELGVKIKEIRVTGGGAKSR 361

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1720410217 255 LFVQMHADITGMPVVLSQEVESVLVGAAILG 285
Cdd:cd00366   362 LWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
ASKHA_NBD_FGGY_MPA43-like cd07778
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ...
 2-327 1.02e-38

nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Saccharomyces cerevisiae protein MPA43. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466797 [Multi-domain]  Cd Length: 544  Bit Score: 144.08  E-value: 1.02e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217   2 IGLEDLIDDNYSKIGNLVLLPGAALGIG-LTPEAARELGLPSGIAVAASLIDAHAGGLGVIgadvrghgltCEGQPVTSR 80
Cdd:cd07778   214 LKISTKVCNVGNTFKEAPPLPYAGIPIGkVNVILASYLGIDKSTVVGHGCIDCYAGWFSTF----------AAAKTLDTT 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  81 LAVICGTSSCHMGISKDPV--FVPGVWGPYySAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAKATarcqSIYAYL 158
Cdd:cd07778   284 LFMVAGTSTCFLYATSSSQvgPIPGIWGPF-DQLLKNYSVYEGGQSATGKLIEKLFNSHPAIIELLKSDA----NFFETV 358

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 159 NSHLDLI--KKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEA 236
Cdd:cd07778   359 EEKIDKYerLLGQSIHYLTRHMFFYGDYLGNRTPYNDPNMSGSFIGESTDSSLTDLVLKYILILEFLAFQTKLIIDNFQK 438

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 237 AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVV---LSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFPEH 313
Cdd:cd07778   439 EKIIIQKVVISGSQAKNARLLQLLSTVLSKIHIivpLSDSKYAVVKGAALLGKAAFLHNQSIEERLISLKNEDQISICAS 518

                         330       340
                  ....*....|....*....|....*
gi 1720410217 314 ADK-----------KYYDKKYQVFL 327
Cdd:cd07778   519 ASIvklvsdetklaIILRAKYQIMN 543
ASKHA_NBD_FGGY_EcXK-like cd07808
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ...
 30-329 4.99e-38

nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466808 [Multi-domain]  Cd Length: 482  Bit Score: 141.52  E-value: 4.99e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  30 LTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQPV----TSrlAVICGTSSCHMGISKDPVF----- 100
Cdd:cd07808   215 LTPEAAEELGLPEGTPVVAGAGDNAAAALGA--------GVVEPGDALislgTS--GVVFAPTDKPVPDPKGRLHtfpha 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 101 VPGVWgpYYSAMVPGF-----WLNE--GGQSVTGKLIDHMVQGHPAfpelqakatarcqsiyaylnshldlikKAQPVGF 173
Cdd:cd07808   285 VPGKW--YAMGVTLSAglslrWLRDlfGPDRESFDELDAEAAKVPP---------------------------GSEGLLF 335

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 174 LtvdlhvwPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKN 253
Cdd:cd07808   336 L-------PYLSGERTPYWDPNARGSFFGLSLSHTRAHLA---RAVLEGVAFSLRDSLEVLKELGIKVKEIRLIGGGAKS 405

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720410217 254 PLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFPEHADKKYYDKKYQVFLRM 329
Cdd:cd07808   406 PLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAACIKIEKTIEPDPERHEAYDELYARYREL 481
ASKHA_NBD_FGGY_CvXK-like cd07805
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ...
 29-327 1.34e-34

nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Chromobacterium violaceum xylulose kinase (CvXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466807 [Multi-domain]  Cd Length: 485  Bit Score: 131.87  E-value: 1.34e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  29 GLTPEAARELGLPSGIAVAASLIDAHAGGLGViGADVRGHgltcegqpvtsrlAVIC-GTSSCHMGISKDPVFVPGvwGP 107
Cdd:cd07805   216 ELTPEAAAELGLPAGTPVVGGGGDAAAAALGA-GAVEEGD-------------AHIYlGTSGWVAAHVPKPKTDPD--HG 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 108 YYS--AMVPGFWLNEGGQSVTGKLIDHMVqghpafpELQAKATARCQSIYAYLNshlDLIKKAQP----VGFLtvdlhvw 181
Cdd:cd07805   280 IFTlaSADPGRYLLAAEQETAGGALEWAR-------DNLGGDEDLGADDYELLD---ELAAEAPPgsngLLFL------- 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 182 PDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHA 261
Cdd:cd07805   343 PWLNGERSPVEDPNARGAFIGLSLEHTRADLA---RAVLEGVAFNLRWLLEALEKLTRKIDELRLVGGGARSDLWCQILA 419

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720410217 262 DITGMPV-VLSQEVESVLVGAAILGACASGDFTSVQEAmARMSKVGKVVFPEHADKKYYDKKYQVFL 327
Cdd:cd07805   420 DVLGRPVeVPENPQEAGALGAALLAAVGLGLLKSFDEA-KALVKVEKVFEPDPENRARYDRLYEVFK 485
ASKHA_NBD_FGGY_FK cd07773
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ...
 19-290 4.10e-31

nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466793 [Multi-domain]  Cd Length: 443  Bit Score: 121.93  E-value: 4.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  19 VLLPGAALGIgLTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDP 98
Cdd:cd07773   204 LVPSGTVIGT-VTPEAAEELGLPAGTPVVVGGHDHLCAALGA--------GVIEPGD-----VLDSTGTAEALLAVVDEP 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  99 VFVPGVWGPYYS---AMVPGFWLNEGGQSvTGKLIDHMVQghpafpELQAKATARCQSIYAYLNShldlIKKAQPVGFLt 175
Cdd:cd07773   270 PLDEMLAEGGLSyghHVPGGYYYLAGSLP-GGALLEWFRD------LFGGDESDLAAADELAEAA----PPGPTGLLFL- 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 176 vdlhvwPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPL 255
Cdd:cd07773   338 ------PHLSGSGTPDFDPDARGAFLGLTLGTTRADL---LRAILEGLAFELRLNLEALEKAGIPIDEIRAVGGGARSPL 408

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1720410217 256 FVQMHADITGMPVVLSQEVESVLVGAAILGACASG 290
Cdd:cd07773   409 WLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
ASKHA_NBD_FGGY_RrXK-like cd07804
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ...
 30-290 1.87e-29

nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Rhodospirillum rubrum xylulose kinase (RrXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466806 [Multi-domain]  Cd Length: 451  Bit Score: 117.24  E-value: 1.87e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  30 LTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGPYY 109
Cdd:cd07804   217 VTKEAAEETGLAEGTPVVAGTVDAAASALSA--------GVVEPGD-----LLLMLGTAGDIGVVTDKLPTDPRLWLDYH 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 110 SamVPGFWLNEGGQSVTGKLIDHMVQGhpAFPELQAKATARCQSIYAYLNshldliKKAQPVGFLTVDLHVWPDFHGNRS 189
Cdd:cd07804   284 D--IPGTYVLNGGMATSGSLLRWFRDE--FAGEEVEAEKSGGDSAYDLLD------EEAEKIPPGSDGLIVLPYFMGERT 353

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 190 PLADLTLKGMVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVV 269
Cdd:cd07804   354 PIWDPDARGVIFGLTLSHTRAHL---YRALLEGVAYGLRHHLEVIREAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQE 430

                         250       260
                  ....*....|....*....|.
gi 1720410217 270 LSQEVESVLVGAAILGACASG 290
Cdd:cd07804   431 YVKDTVGASLGDAFLAGVGVG 451
ASKHA_NBD_FGGY_EcLyxK-like cd07802
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ...
 1-290 1.89e-28

nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK; EC 2.7.1.-/EC 2.7.1.53), Pasteurella multocida L-xylulose kinase (PmLyX, also known as L-xylulokinase; EC 2.7.1.53), and Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). EcLyxK catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. It is involved in L-lyxose utilization via xylulose and may also be involved in the utilization of 2,3-diketo-L-gulonate. PmLyX catalyzes the phosphorylation of L-xylulose only. BaEryA catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466805 [Multi-domain]  Cd Length: 444  Bit Score: 114.57  E-value: 1.89e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217   1 MIGLEDLIDdnysKIGNLVllPGAALGIGLTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsr 80
Cdd:cd07802   194 LLGIEELKD----KLPPLV--PSTEIAGRVTAEAAALTGLPEGTPVAAGAFDVVASALGA--------GAVDEGQ----- 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  81 LAVICGTSSCHMGISKDPVFVPGVWGpYYSAMVPGFWLNEGGQSVTGKLIDHMVQghpafpELQAKATARCQSIYAYLNs 160
Cdd:cd07802   255 LCVILGTWSINEVVTDEPVVPDSVGS-NSLHADPGLYLIVEASPTSASNLDWFLD------TLLGEEKEAGGSDYDELD- 326

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 161 hlDLIKKAQPVG----FLtvdlhvwPDFHGNRsplADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEA 236
Cdd:cd07802   327 --ELIAAVPPGSsgviFL-------PYLYGSG---ANPNARGGFFGLTAWHTRAHLL---RAVYEGIAFSHRDHLERLLV 391

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720410217 237 AGHsLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASG 290
Cdd:cd07802   392 ARK-PETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
ASKHA_NBD_FGGY_SePSK_AtXK1-like cd07783
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ...
 19-286 1.17e-27

nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466801 [Multi-domain]  Cd Length: 429  Bit Score: 111.93  E-value: 1.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  19 VLLPGAALGIgLTPEAARELGLPSGIAVAASLIDAHAGGLGViGADVRGHGLTcegqpvtsrlavICGTSSCHMGISKDP 98
Cdd:cd07783   202 VVAPGTVIGT-LTAEAAEELGLPAGTPVVAGTTDSIAAFLAS-GAVRPGDAVT------------SLGTTLVLKLLSDKR 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  99 VFVPGvwGPYYSAMVP-GFWLNEGGQSVTGKLIDHMVQGHPaFPELQAKATARCQSiyaylnshldlikkaqpvgfltvD 177
Cdd:cd07783   268 VPDPG--GGVYSHRHGdGYWLVGGASNTGGAVLRWFFSDDE-LAELSAQADPPGPS-----------------------G 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 178 LHVWP-DFHGNRSPLADLTLKGMVTGLTlsqdlDDLAILYLATVQAIAFGTRFIIETMEAAGHS-LSTLFLCGGLSKNPL 255
Cdd:cd07783   322 LIYYPlPLRGERFPFWDPDARGFLLPRP-----HDRAEFLRALLEGIAFIERLGYERLEELGAPpVEEVRTAGGGARNDL 396

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1720410217 256 FVQMHADITGMPVVLSQEVESVLvGAAILGA 286
Cdd:cd07783   397 WNQIRADVLGVPVVIAEEEEAAL-GAALLAA 426
ASKHA_NBD_FGGY_GntK cd07770
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ...
 29-330 1.79e-27

nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7.1.12), also known as gluconokinase, catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, Members of this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466790 [Multi-domain]  Cd Length: 478  Bit Score: 112.26  E-value: 1.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  29 GLTPEAARELGLPSGIAVAASLIDAHAGGLGViGADVRGhgltcegqpvtsRLAVICGTSschmG----ISKDPVFVP-- 102
Cdd:cd07770   213 GLKPEFAERLGLLAGTPVVLGASDGALANLGS-GALDPG------------RAALTVGTS----GairvVSDRPVLDPpg 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 103 GVWgPYYSAmvPGFWL-----NEGGqSVTGKLIDHMVQGHPAFPELQAKATArcqsiyAYLNSHlDLIkkaqpvgFLtvd 177
Cdd:cd07770   276 RLW-CYRLD--ENRWLvggaiNNGG-NVLDWLRDTLLLSGDDYEELDKLAEA------VPPGSH-GLI-------FL--- 334

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 178 lhvwPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFV 257
Cdd:cd07770   335 ----PYLAGERAPGWNPDARGAFFGLTLNHTRADI---LRAVLEGVAFNLKSIYEALEELAGPVKEIRASGGFLRSPLWL 407

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720410217 258 QMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEamARMSKVGKVVFPEHADKKYYDKKYQVFLRMV 330
Cdd:cd07770   408 QILADVLGRPVLVPEEEEASALGAALLALEALGLISSLEA--DELVKIGKVVEPDPENHAIYAELYERFKKLY 478
ASKHA_NBD_FGGY_YoaC-like cd07798
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ...
 19-290 2.63e-23

nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to Bacillus subtilis sugar kinase YoaC. It is part of the yoaDCB operon and induced by sulfate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466804 [Multi-domain]  Cd Length: 448  Bit Score: 99.99  E-value: 2.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  19 VLLPGAALGIgLTPEAARELGLPSGIAVAASLIDAHAGGLGViGADVRGHgltcegqpvtsrLAVICGTSSCHMGISKDP 98
Cdd:cd07798   206 IVPSGTVLGT-VSEEAARELGLPEGTPVVVGGADTQCALLGS-GAIEPGD------------IGIVAGTTTPVQMVTDEP 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  99 VFVP--GVW-GPYysaMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQakatarcqsiYAYLNSHLDLIKKAQP--VGF 173
Cdd:cd07798   272 IIDPerRLWtGCH---LVPGKWVLESNAGVTGLNYQWLKELLYGDPEDS----------YEVLEEEASEIPPGANgvLAF 338

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 174 LTVDLhvwpdFHGNRSPLADLTLKGMVTGLTLSQDLDDLAIlylATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSK 252
Cdd:cd07798   339 LGPQI-----FDARLSGLKNGGFLFPTPLSASELTRGDFAR---AILENIAFAIRANLEQLEEvSGREIPYIILCGGGSR 410

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1720410217 253 NPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASG 290
Cdd:cd07798   411 SALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
ASKHA_NBD_FGGY_BaXK-like cd07809
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ...
 19-290 2.09e-19

nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466809 [Multi-domain]  Cd Length: 443  Bit Score: 88.38  E-value: 2.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  19 VLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAG--GLGVIGadvrghgltcEGQPVTSrlaviCGTSSCHMGISK 96
Cdd:cd07809   209 VLPAGEVAG-RLTPEGAEELGLPAGIPVAPGEGDNMTGalGTGVVN----------PGTVAVS-----LGTSGTAYGVSD 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  97 DPVFVPgvwgpyySAMVPGF--------WLNEG---GQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYlnshldli 165
Cdd:cd07809   273 KPVSDP-------HGRVATFcdstggmlPLINTtncLTAWTELFRELLGVSYEELDELAAQAPPGAGGLLLL-------- 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 166 kkaqpvgfltvdlhvwPDFHGNRSP-LADLTlkGMVTGLTLSQDldDLAILYLATVQAIAFGTRFIIETMEAAGHSLSTL 244
Cdd:cd07809   338 ----------------PFLNGERTPnLPHGR--ASLVGLTLSNF--TRANLARAALEGATFGLRYGLDILRELGVEIDEI 397

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1720410217 245 FLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASG 290
Cdd:cd07809   398 RLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
ASKHA_NBD_FGGY_GK cd07769
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ...
 182-331 4.48e-17

nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), also called ATP:glycerol 3-phosphotransferase, or glycerokinase, is a key enzyme in the regulation of glycerol uptake and metabolism. It catalyzes the Mg-ATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. The subfamily includes GKs and GK-like proteins from all three kingdoms of living organisms. Metazoan GKs, coded by X chromosome-linked GK genes, and GK-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse) are closely related to the bacterial GKs. The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Under different conditions, GKs from different species may exist in different oligomeric states. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466789 [Multi-domain]  Cd Length: 486  Bit Score: 81.74  E-value: 4.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 182 PDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFVQMH 260
Cdd:cd07769   341 PAFSGLGAPYWDPDARGAIVGLTRGTTKAHIV---RAALESIAYQTRDVLEAMEKdSGIKLKELRVDGGATANNFLMQFQ 417

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720410217 261 ADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEaMARMSKVGKVVFPEhADKKYYDKKYQVFLRMVE 331
Cdd:cd07769   418 ADILGVPVVRPKVAETTALGAAYLAGLAVGFWKDLDE-LASLWQVDKRFEPS-MDEEERERLYRGWKKAVE 486
ASKHA_NBD_FGGY_GK1-3-like cd07792
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ...
 218-331 1.84e-16

nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466802 [Multi-domain]  Cd Length: 499  Bit Score: 79.88  E-value: 1.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 218 ATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQ 296
Cdd:cd07792   384 AALEAVCFQTREILDAMNKdSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLD 463

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1720410217 297 EaMARMSKVGKVVFPEHADKKYYDKKYQVFLRMVE 331
Cdd:cd07792   464 E-LKSLNEGGRTVFEPQISEEERERRYKRWKKAVE 497
ASKHA_NBD_FGGY_BaEryA-like cd24121
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ...
 20-290 2.21e-16

nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). It catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466971 [Multi-domain]  Cd Length: 452  Bit Score: 79.59  E-value: 2.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  20 LLPGAALGIG----LTPEAARELGLPSGIAVAASLIDAHAGGLGViGADVRGHGLTcegqpvtsrlavICGTSSCHMGIS 95
Cdd:cd24121   203 LLPPIRPGTEvigpLTPEAAAATGLPAGTPVVLGPFDVVATALGS-GAIEPGDACS------------ILGTTGVHEVVV 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  96 KDPVFvpgvwGPYYSAM-----VPGFWLNEGGqSVTGKL-IDHMVQghPAFPELQAKATARCQSIYAYLNSHLdlikKAQ 169
Cdd:cd24121   270 DEPDL-----EPEGVGYticlgVPGRWLRAMA-NMAGTPnLDWFLR--ELGEVLKEGAEPAGSDLFQDLEELA----ASS 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 170 PVGFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRfiiETMEAAGHSLSTLFLCGG 249
Cdd:cd24121   338 PPGAEGVLYHPYLSPAGERAPFVNPNARAQFTGLSLEHTRADLL---RAVYEGVALAMR---DCYEHMGEDPGELRLSGG 411

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1720410217 250 LSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASG 290
Cdd:cd24121   412 GARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
GlpK COG0554
Glycerol kinase [Energy production and conversion];
197-331 4.06e-16

Glycerol kinase [Energy production and conversion];


Pssm-ID: 440320 [Multi-domain]  Cd Length: 496  Bit Score: 78.95  E-value: 4.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 197 KGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVE 275
Cdd:COG0554   359 RGAIFGLTRGTTRAHIA---RAALESIAYQTRDVLDAMEAdSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTE 435

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720410217 276 SVLVGAAILGACASGDFTSVQEaMARMSKVGKVVFPEhADKKYYDKKYQVFLRMVE 331
Cdd:COG0554   436 TTALGAAYLAGLAVGFWKSLEE-LAALWKVDRRFEPQ-MDEEERERLYAGWKKAVE 489
PTZ00294 PTZ00294
glycerol kinase-like protein; Provisional
 182-323 1.05e-15

glycerol kinase-like protein; Provisional


Pssm-ID: 240348 [Multi-domain]  Cd Length: 504  Bit Score: 77.71  E-value: 1.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 182 PDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETME-AAGHSLSTLFLCGGLSKNPLFVQMH 260
Cdd:PTZ00294  350 PAFSGLFAPYWRPDARGTIVGMTLKTTRAHIV---RAALEAIALQTNDVIESMEkDAGIELNSLRVDGGLTKNKLLMQFQ 426

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720410217 261 ADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFPeHADKKYYDKKY 323
Cdd:PTZ00294  427 ADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEVKKLIRRSNSTFSP-QMSAEERKAIY 488
FGGY_EcGK_like cd07786
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ...
 197-331 3.51e-15

Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate kinases; This subgroup is composed of mostly bacterial and archaeal glycerol kinases (GK), including the well characterized proteins from Escherichia coli (EcGK), Thermococcus kodakaraensis (TkGK), and Enterococcus casseliflavus (EnGK). GKs contain two large domains separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The high affinity ATP binding site of EcGK is created only by a substrate-induced conformational change, which is initiated by protein-protein interactions through complex formation with enzyme IIAGlc (also known as IIIGlc), the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS). EcGK exists in a dimer-tetramer equilibrium. IIAGlc binds to both EcGK dimer and tetramer, and inhibits the uptake and subsequent metabolism of glycerol and maltose. Another well-known allosteric regulator of EcGK is fructose 1,6-bisphosphate (FBP), which binds to the EcGK tetramer and plays an essential role in the stabilization of the inactive tetrameric form. EcGK requires Mg2+ for its enzymatic activity. Members in this subgroup belong to the FGGY family of carbohydrate kinases


Pssm-ID: 198361 [Multi-domain]  Cd Length: 486  Bit Score: 75.99  E-value: 3.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 197 KGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVE 275
Cdd:cd07786   356 RGAIFGLTRGTTRAHIA---RAALESIAYQTRDLLEAMEAdSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTE 432

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720410217 276 SVLVGAAILGACASGDFTSVQEAmARMSKVGKVVFPEhADKKYYDKKYQVFLRMVE 331
Cdd:cd07786   433 TTALGAAYLAGLAVGLWKSLDEL-AKLWQVDRRFEPS-MSEEEREALYAGWKKAVK 486
ASKHA_NBD_FGGY_GK5-like cd07793
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ...
 182-331 1.85e-14

nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The subfamily corresponds to a group of metazoan putative glycerol kinases (GK), which may be coded by the GK-like gene, GK5. Sequence comparison shows members of this group are homologs of bacterial GKs, and they retain all functionally important residues. However, GK-like proteins in this family do not have detectable GK activity. The reason remains unclear. It has been suggested that the conserved catalytic residues might facilitate them performing a distinct function. GK5 is a skin-specific kinase expressed predominantly in sebaceous glands. It can form a complex with the sterol regulatory element-binding proteins (SREBPs) through their C-terminal regulatory domains, inhibiting SREBP processing and activation. GK5 also promotes gefitinib resistance by inhibiting apoptosis and cell cycle arrest. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466803 [Multi-domain]  Cd Length: 501  Bit Score: 74.14  E-value: 1.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 182 PDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAIlylATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFVQMH 260
Cdd:cd07793   356 PAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVR---AILESIAFRVKQLLETMEKeTSIKISSIRVDGGVSNNDFILQLI 432

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720410217 261 ADITGMPVVLSQEVESVLVGAAILGACASGDFTSVqEAMARMSKVGKVVFPEhADKKYYDKKYQVFLRMVE 331
Cdd:cd07793   433 ADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSK-EELKKLRKIEKIFEPK-MDNEKREELYKNWKKAVK 501
ASKHA_NBD_FGGY_AI-2K cd07775
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ...
 28-324 1.26e-13

nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466794 [Multi-domain]  Cd Length: 492  Bit Score: 71.59  E-value: 1.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  28 IG-LTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrlAVICGTSSCHMGI-SKDPVFVPGVW 105
Cdd:cd07775   215 IGkVTKEAAEETGLKEGTPVVVGGGDVQLGCLGL--------GVVRPGQ------TAVLGGSFWQQEVnTAAPVTDPAMN 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 106 GPYYSAMVPGFWLNEGGQSVTGKLIDHMVQghpAF-PELQAKATARCQSIYAYLNshldliKKAQ--PVGF-----LTVD 177
Cdd:cd07775   281 IRVNCHVIPDMWQAEGISFFPGLVMRWFRD---AFcAEEKEIAERLGIDAYDLLE------EMAKdvPPGSygimpIFSD 351

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 178 L-------HVWPDFhgnrspladltlkgmvTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEAA-GHSLSTLFLCGG 249
Cdd:cd07775   352 VmnyknwrHAAPSF----------------LNLDIDPEKCNKATFFRAIMENAAIVSAGNLERIAEFsGIFPDSLVFAGG 415

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720410217 250 LSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFPEHADKKYYDKKYQ 324
Cdd:cd07775   416 ASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGAGIYSSLEEAVESLVKWEREYLPNPENHEVYQDLYE 490
glpK PRK00047
glycerol kinase GlpK;
179-332 1.16e-12

glycerol kinase GlpK;


Pssm-ID: 234594 [Multi-domain]  Cd Length: 498  Bit Score: 68.70  E-value: 1.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 179 HVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFV 257
Cdd:PRK00047  344 YVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHII---RATLESIAYQTRDVLDAMQAdSGIRLKELRVDGGAVANNFLM 420

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720410217 258 QMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEaMARMSKVGKVVFPEHADKKyYDKKYQVFLRMVEH 332
Cdd:PRK00047  421 QFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDE-LKEQWKIDRRFEPQMDEEE-REKLYAGWKKAVKR 493
PRK10331 PRK10331
L-fuculokinase; Provisional
 28-311 1.06e-10

L-fuculokinase; Provisional


Pssm-ID: 182383 [Multi-domain]  Cd Length: 470  Bit Score: 62.35  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  28 IG-LTPEAARELGLPSGIAVAASlidAHAGGLGVIGAdvrGHGLtceGQPV-----------------TSRLAVICGtSS 89
Cdd:PRK10331  215 IGtLQPSAAALLGLPVGIPVISA---GHDTQFALFGS---GAGQ---NQPVlssgtweilmvrsaqvdTSLLSQYAG-ST 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217  90 CHMGiSKDPVFVPGVWgpyysamvpgfWLNEGGQSVTGKLIdhmvqghpaFPELQAKATarcqsiyaylnshldLIKKAQ 169
Cdd:PRK10331  285 CELD-SQSGLYNPGMQ-----------WLASGVLEWVRKLF---------WTAETPYQT---------------MIEEAR 328

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 170 PVGFLTVDLHVWPDFHGNRspladltlKGMVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGH-SLSTLFLCG 248
Cdd:PRK10331  329 AIPPGADGVKMQCDLLACQ--------NAGWQGVTLNTTRGHF---YRAALEGLTAQLKRNLQVLEKIGHfKASELLLVG 397

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720410217 249 GLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFP 311
Cdd:PRK10331  398 GGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQARAQMKYQYRYFYP 460
PLN02295 PLN02295
glycerol kinase
 157-318 3.87e-09

glycerol kinase


Pssm-ID: 215166 [Multi-domain]  Cd Length: 512  Bit Score: 57.79  E-value: 3.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 157 YLNSHLDLIKKAQPVGFL--TVD----LHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFI 230
Cdd:PLN02295  320 WLRDNLGIIKSASEIEALaaTVDdtggVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIA---RAVLESMCFQVKDV 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 231 IETM------EAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSK 304
Cdd:PLN02295  397 LDAMrkdageEKSHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTEEEIFASEKWK 476

                         170
                  ....*....|....*...
gi 1720410217 305 VGKVVFP----EHADKKY 318
Cdd:PLN02295  477 NTTTFRPkldeEERAKRY 494
ASKHA_NBD_FGGY_RhaB-like cd07771
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ...
 223-298 1.17e-07

nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase (EC 2.7.1.5), also known as L-rhamnulose kinase, ATP:L-rhamnulose phosphotransferase, L-rhamnulose 1-kinase, or rhamnulose kinase, is an enzyme involved in the second step in rhamnose catabolism. It catalyzes the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Rhamnulokinase exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. The subfamily also includes Streptococcus pneumoniae L-fuculose k fuculose Kinase inase (FcsK) that uses ATP to phosphorylate fuculose creating fuculose-1-phosphate, and Alkalihalobacillus clausii bifunctional enzyme RhaA/RhaB. Members of this subfamily belong to the FGGY family of carbohydrate kinases.


Pssm-ID: 466791 [Multi-domain]  Cd Length: 460  Bit Score: 52.92  E-value: 1.17e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720410217 223 IAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSqEVESVLVGAAILGACASGDFTSVQEA 298
Cdd:cd07771   378 LALKYAKTIEELEElTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIAG-PVEATAIGNLLVQLIALGEIKSLEEG 453
ASKHA_NBD_FGGY_SHK cd07777
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ...
 152-284 2.05e-07

nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466796 [Multi-domain]  Cd Length: 436  Bit Score: 52.22  E-value: 2.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 152 QSIYAYLNShLDLIKKAQPvgfLTVDlhvwPDFHGNRSplaDLTLKGMVTGLTLsqdlDDLAI--LYLATVQAIAFGTRF 229
Cdd:cd07777   315 DEIWEKLDE-LAESEESSD---LSVD----PTFFGERH---DPEGRGSITNIGE----SNFTLgnLFRALCRGIAENLHE 379

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720410217 230 IIETMEAAGHSLSTLFLCGG-LSKNPLFVQMHADITGMPVVLSQEVESVLVGAAIL 284
Cdd:cd07777   380 MLPRLDLDLSGIERIVGSGGaLRKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALL 435
PRK10939 PRK10939
autoinducer-2 (AI-2) kinase; Provisional
 237-333 4.65e-06

autoinducer-2 (AI-2) kinase; Provisional


Pssm-ID: 182853 [Multi-domain]  Cd Length: 520  Bit Score: 48.08  E-value: 4.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 237 AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKVGKVVFPEHADK 316
Cdd:PRK10939  406 SGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEATALGCAIAAGVGAGIYSSLAETGERLVRWERTFEPNPENH 485

                          90
                  ....*....|....*..
gi 1720410217 317 KYYDKKYQVFLRMVEHQ 333
Cdd:PRK10939  486 ELYQEAKEKWQAVYADQ 502
ASKHA_NBD_FGGY_SpXK-like cd07776
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ...
 238-321 4.96e-04

nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. The subfamily includes XKs mainly from eukaryote. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466795 [Multi-domain]  Cd Length: 514  Bit Score: 41.77  E-value: 4.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 238 GHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQEAMARMSKV----GKVVFPEH 313
Cdd:cd07776   423 DIPPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAGSGDFSPEFVVFSaeepKLVAEPDP 502


                  ....*...
gi 1720410217 314 ADKKYYDK 321
Cdd:cd07776   503 EAAEVYDK 510
ASKHA_NBD_FGGY_NaCK-like cd07772
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ...
 180-284 2.57e-03

nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.


Pssm-ID: 466792 [Multi-domain]  Cd Length: 424  Bit Score: 39.55  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410217 180 VWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAILYLATVQAIAfgtrfiietMEAAGHSLSTLFLCGGLSKNPLFVQM 259
Cdd:cd07772   327 ALPSFAPGGGPFPGSGGRGVLSAFPSAEEAYALAILYLALMTDYA---------LDLLGSGVGRIIVEGGFAKNPVFLRL 397

                          90       100
                  ....*....|....*....|....*.
gi 1720410217 260 HADI-TGMPVVLSQEVESVLVGAAIL 284
Cdd:cd07772   398 LAALrPDQPVYLSDDSEGTALGAALL 423
 
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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