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Conserved domains on  [gi|1034559850|ref|XP_016857167|]
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FGGY carbohydrate kinase domain-containing protein isoform X11 [Homo sapiens]

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 ...
 2-360 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: 603.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850   2 IGLEDFVADNYSKIGNQVLPPGASLGNGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIGADVrgHGLICEGQPVTSRL 81
Cdd:cd07782   205 IGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAKELGLPEGTPVGVSLIDAHAGGLGTLGADV--GGLPCEADPLTRRL 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  82 AVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYLNSH 161
Cdd:cd07782   283 ALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGLWLNEGGQSATGALLDHIIETHPAYPELKEEAKAAGKSIYEYLNER 362

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 162 LDLIKKAQ--PVGFLTVDLHVWPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLAIL 239
Cdd:cd07782   363 LEQLAEEKglPLAYLTRDLHVLPDFHGNRSPLADPTLRGM------------------------ISGLTLDTSLDDLALL 418

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 240 YLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASV 319
Cdd:cd07782   419 YLATLQALAYGTRHIIEAMNAAGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSL 498

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1034559850 320 QEAMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKLVEHQKEY 360
Cdd:cd07782   499 WDAMAAMSGPGKVVEPNEELKKYHDRKYEVFLKMYEDQREY 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 ...
 2-360 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: 603.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850   2 IGLEDFVADNYSKIGNQVLPPGASLGNGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIGADVrgHGLICEGQPVTSRL 81
Cdd:cd07782   205 IGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAKELGLPEGTPVGVSLIDAHAGGLGTLGADV--GGLPCEADPLTRRL 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  82 AVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYLNSH 161
Cdd:cd07782   283 ALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGLWLNEGGQSATGALLDHIIETHPAYPELKEEAKAAGKSIYEYLNER 362

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 162 LDLIKKAQ--PVGFLTVDLHVWPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLAIL 239
Cdd:cd07782   363 LEQLAEEKglPLAYLTRDLHVLPDFHGNRSPLADPTLRGM------------------------ISGLTLDTSLDDLALL 418

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 240 YLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASV 319
Cdd:cd07782   419 YLATLQALAYGTRHIIEAMNAAGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSL 498

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1034559850 320 QEAMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKLVEHQKEY 360
Cdd:cd07782   499 WDAMAAMSGPGKVVEPNEELKKYHDRKYEVFLKMYEDQREY 539
5C_CHO_kinase TIGR01315
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of ...
 2-360 1.46e-134

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: 394.64  E-value: 1.46e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850   2 IGLEDFVADNYSKIGNQVLPPGASLGNGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIGADVRGHGLICEGQpvtSRL 81
Cdd:TIGR01315 205 IGLGELVTDNFIRMGGSWMSPGELVGGGLTAEAAQELGLPAGTAVGSGLIDAHAGWIGTVGAKVAENGDVSQAF---TRL 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  82 AVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYLNSH 161
Cdd:TIGR01315 282 AAVAGTSTCHMAMTKGPVFVPGVWGPYRDALIPGYWLAEGGQSAAGELMDHMLETHVAYDETVKEAEAAGKNIYDYLNEH 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 162 LdLIKKAQP----VGFLTVDLHVWPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLA 237
Cdd:TIGR01315 362 L-KEMAAKTnapsISYLVRHFHVYPDLWGNRSPIADPNMRGV------------------------IIGLSMDRSKDGLA 416

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 238 ILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFA 317
Cdd:TIGR01315 417 LLYYATMEFIAYGTRQIVEAMNTAGHTIKSIFMSGGQCQNPLLMQLIADACDMPVLIPYVNEAVLHGAAMLGAKAAGTTE 496

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1034559850 318 SVQEAMAKMSKVGKVVFPRLQ-DKKYYDKKYQVFLKLVEHQKEY 360
Cdd:TIGR01315 497 SLWDAMDRMSKPGKTVWPRGDpAKKLHDRKYEIFLQLARTQQEY 540
AraB COG1069
Ribulose kinase [Carbohydrate transport and metabolism];
6-360 1.59e-118

Ribulose kinase [Carbohydrate transport and metabolism];


Pssm-ID: 440687 [Multi-domain]  Cd Length: 532  Bit Score: 353.27  E-value: 1.59e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850   6 DFVADnysKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIGadvrghglICEGQpvtsrLAVIC 85
Cdd:COG1069   224 DGLAD---RLGTEIYPLGEPAGT-LTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGG--------VEPGT-----LVKVM 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  86 GTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYLNshldli 165
Cdd:COG1069   287 GTSTCHMLVSPEERFVPGICGQVDGSIVPGMWGYEAGQSAVGDIFAWFVRLLVPPLEYEKEAEERGISLHPLLT------ 360

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 166 KKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDlaiLYLATVQ 245
Cdd:COG1069   361 EEAAKLPPGESGLHALDWFNGNRSPLADQRLKGV------------------------ILGLTLGTDAED---IYRALVE 413

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 246 AIALGTRFIIEAMEAAGHSISTLFLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMA 324
Cdd:COG1069   414 ATAFGTRAIIERFEEEGVPIDEIIACGGIAtKNPLVMQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEEAMA 493

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1034559850 325 KMSKV-GKVVFPRLQDKKYYDKKYQVFLKLVEHQKEY 360
Cdd:COG1069   494 AMGSGfDKVYTPDPENVAVYDALYAEYLQLHDYFGRG 530
FGGY_C pfam02782
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ...
 81-312 1.53e-54

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: 177.90  E-value: 1.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  81 LAVICGTSSCHMGISKDP-IFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQvkATARCQSIYAYLN 159
Cdd:pfam02782   1 LAISAGTSSFVLVETPEPvLSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELR--DAGNVESLAELAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 160 SHLDLikkaqpvgfLTVDLHVWPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLddlAIL 239
Cdd:pfam02782  79 LAAVA---------PAGGLLFYPDFSGNRAPGADPGARGS------------------------ITGLSSPTTL---AHL 122

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034559850 240 YLATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACA 312
Cdd:pfam02782 123 YRAILESLALQLRQILEALTKqEGHPIDTIHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
PRK04123 PRK04123
ribulokinase; Provisional
 3-364 3.54e-54

ribulokinase; Provisional


Pssm-ID: 235221 [Multi-domain]  Cd Length: 548  Bit Score: 186.98  E-value: 3.54e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850   3 GLEDFVADnysKIGNQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGglgVIGADVRGHGLicegqpvtsrLA 82
Cdd:PRK04123  229 LLARGLRD---KLFTETWTAGEPAG-TLTAEWAQRLGLPEGVAVSVGAFDAHMG---AVGAGAEPGTL----------VK 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  83 VIcGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQgHAAFPELQVKATARCQSIYAYLNshl 162
Cdd:PRK04123  292 VM-GTSTCDILLADKQRAVPGICGQVDGSIVPGLIGYEAGQSAVGDIFAWFAR-LLVPPEYKDEAEARGKQLLELLT--- 366

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 163 dliKKA--QPVG---FLTVDlhvWpdFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLa 237
Cdd:PRK04123  367 ---EAAakQPPGehgLVALD---W--FNGRRTPLADQRLKGV------------------------ITGLTLGTDAPDI- 413

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 238 ilYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDF 316
Cdd:PRK04123  414 --YRALIEATAFGTRAIMECFEDQGVPVEEVIAAGGIArKNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAAVAAGAY 491

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034559850 317 ASVQEAMAKM-SKVGKVVFPRLQDKKYYDKKYQVFLKLVE-HQKEYLAIM 364
Cdd:PRK04123  492 PDIPEAQQAMaSPVEKTYQPDPENVARYEQLYQEYKQLHDyFGRGGNAVM 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 ...
 2-360 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: 603.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850   2 IGLEDFVADNYSKIGNQVLPPGASLGNGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIGADVrgHGLICEGQPVTSRL 81
Cdd:cd07782   205 IGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAKELGLPEGTPVGVSLIDAHAGGLGTLGADV--GGLPCEADPLTRRL 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  82 AVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYLNSH 161
Cdd:cd07782   283 ALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGLWLNEGGQSATGALLDHIIETHPAYPELKEEAKAAGKSIYEYLNER 362

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 162 LDLIKKAQ--PVGFLTVDLHVWPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLAIL 239
Cdd:cd07782   363 LEQLAEEKglPLAYLTRDLHVLPDFHGNRSPLADPTLRGM------------------------ISGLTLDTSLDDLALL 418

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 240 YLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASV 319
Cdd:cd07782   419 YLATLQALAYGTRHIIEAMNAAGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSL 498

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1034559850 320 QEAMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKLVEHQKEY 360
Cdd:cd07782   499 WDAMAAMSGPGKVVEPNEELKKYHDRKYEVFLKMYEDQREY 539
5C_CHO_kinase TIGR01315
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of ...
 2-360 1.46e-134

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: 394.64  E-value: 1.46e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850   2 IGLEDFVADNYSKIGNQVLPPGASLGNGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIGADVRGHGLICEGQpvtSRL 81
Cdd:TIGR01315 205 IGLGELVTDNFIRMGGSWMSPGELVGGGLTAEAAQELGLPAGTAVGSGLIDAHAGWIGTVGAKVAENGDVSQAF---TRL 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  82 AVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYLNSH 161
Cdd:TIGR01315 282 AAVAGTSTCHMAMTKGPVFVPGVWGPYRDALIPGYWLAEGGQSAAGELMDHMLETHVAYDETVKEAEAAGKNIYDYLNEH 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 162 LdLIKKAQP----VGFLTVDLHVWPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLA 237
Cdd:TIGR01315 362 L-KEMAAKTnapsISYLVRHFHVYPDLWGNRSPIADPNMRGV------------------------IIGLSMDRSKDGLA 416

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 238 ILYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFA 317
Cdd:TIGR01315 417 LLYYATMEFIAYGTRQIVEAMNTAGHTIKSIFMSGGQCQNPLLMQLIADACDMPVLIPYVNEAVLHGAAMLGAKAAGTTE 496

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1034559850 318 SVQEAMAKMSKVGKVVFPRLQ-DKKYYDKKYQVFLKLVEHQKEY 360
Cdd:TIGR01315 497 SLWDAMDRMSKPGKTVWPRGDpAKKLHDRKYEIFLQLARTQQEY 540
AraB COG1069
Ribulose kinase [Carbohydrate transport and metabolism];
6-360 1.59e-118

Ribulose kinase [Carbohydrate transport and metabolism];


Pssm-ID: 440687 [Multi-domain]  Cd Length: 532  Bit Score: 353.27  E-value: 1.59e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850   6 DFVADnysKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIGadvrghglICEGQpvtsrLAVIC 85
Cdd:COG1069   224 DGLAD---RLGTEIYPLGEPAGT-LTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGG--------VEPGT-----LVKVM 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  86 GTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQVKATARCQSIYAYLNshldli 165
Cdd:COG1069   287 GTSTCHMLVSPEERFVPGICGQVDGSIVPGMWGYEAGQSAVGDIFAWFVRLLVPPLEYEKEAEERGISLHPLLT------ 360

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 166 KKAQPVGFLTVDLHVWPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDlaiLYLATVQ 245
Cdd:COG1069   361 EEAAKLPPGESGLHALDWFNGNRSPLADQRLKGV------------------------ILGLTLGTDAED---IYRALVE 413

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 246 AIALGTRFIIEAMEAAGHSISTLFLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMA 324
Cdd:COG1069   414 ATAFGTRAIIERFEEEGVPIDEIIACGGIAtKNPLVMQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEEAMA 493

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1034559850 325 KMSKV-GKVVFPRLQDKKYYDKKYQVFLKLVEHQKEY 360
Cdd:COG1069   494 AMGSGfDKVYTPDPENVAVYDALYAEYLQLHDYFGRG 530
ASKHA_NBD_FGGY_RBK-like cd07768
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ...
 11-350 1.12e-79

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: 253.32  E-value: 1.12e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  11 NYSKIGNQVLPPGASLGNGLtPEAARDLGLLPGIAVAASLIDAHAGGLGVIGADVRGhglicegqpvtsRLAVICGTSSC 90
Cdd:cd07768   213 TTTKNLPSNVPIGTTSGVAL-PEMAEKMGLHPGTAVVVSCIDAHASWFAVASPHLET------------SLFMIAGTSSC 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  91 HMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELqVKATARCQSIYAYLNshlDLIKKAQP 170
Cdd:cd07768   280 HMYGTTISDRIPGVWGPFDTIIDPDYSVYEAGQSATGKLIEHLFESHPCARKF-DEALKKGADIYQVLE---QTIRQIEK 355

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 171 VGFLTVDLHVWPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLAILYLATVQAIALG 250
Cdd:cd07768   356 NNGLSIHILTLDMFFGNRSEFADPRLKGS------------------------FIGESLDTSMLNLTYKYIAILEALAFG 411

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 251 TRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFA---SVQEAMAKMS 327
Cdd:cd07768   412 TRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGILGAAVLAKVAAGKKQladSITEADISND 491

                         330       340
                  ....*....|....*....|....
gi 1034559850 328 KVGKVVFPRLQD-KKYYDKKYQVF 350
Cdd:cd07768   492 RKSETFEPLAYRlGADYILLYKLL 515
ASKHA_NBD_FGGY_L-RBK cd07781
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ...
 2-353 1.26e-79

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: 252.46  E-value: 1.26e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850   2 IGLEDfvADNYSKIGNQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrL 81
Cdd:cd07781   201 LDPGL--LKLREKLPGEVVPVGEPAG-TLTAEAAERLGLPAGIPVAQGGIDAHMGAIGA--------GVVEPGT-----L 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  82 AVICGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIdhmvqghAAFPELQVKATA-RCQSIYAYLNs 160
Cdd:cd07781   265 ALIMGTSTCHLMVSPKPVDIPGICGPVPDAVVPGLYGLEAGQSAVGDIF-------AWFVRLFVPPAEeRGDSIYALLS- 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 161 hlDLIKKAQPV--GFLTVDlhvWpdFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLddlAI 238
Cdd:cd07781   337 --EEAAKLPPGesGLVALD---W--FNGNRTPLVDPRLRGA------------------------IVGLTLGTTP---AH 382

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 239 LYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFA 317
Cdd:cd07781   383 IYRALLEATAFGTRAIIERFEEAGVPVNRVVACGGIAeKNPLWMQIYADVLGRPIKVPKSDQAPALGAAILAAVAAGVYA 462

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1034559850 318 SVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKL 353
Cdd:cd07781   463 DIEEAADAMVRVDRVYEPDPENHAVYEELYALYKEL 498
FGGY_C pfam02782
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ...
 81-312 1.53e-54

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: 177.90  E-value: 1.53e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  81 LAVICGTSSCHMGISKDP-IFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQvkATARCQSIYAYLN 159
Cdd:pfam02782   1 LAISAGTSSFVLVETPEPvLSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELR--DAGNVESLAELAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 160 SHLDLikkaqpvgfLTVDLHVWPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLddlAIL 239
Cdd:pfam02782  79 LAAVA---------PAGGLLFYPDFSGNRAPGADPGARGS------------------------ITGLSSPTTL---AHL 122

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034559850 240 YLATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACA 312
Cdd:pfam02782 123 YRAILESLALQLRQILEALTKqEGHPIDTIHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
PRK04123 PRK04123
ribulokinase; Provisional
 3-364 3.54e-54

ribulokinase; Provisional


Pssm-ID: 235221 [Multi-domain]  Cd Length: 548  Bit Score: 186.98  E-value: 3.54e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850   3 GLEDFVADnysKIGNQVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGglgVIGADVRGHGLicegqpvtsrLA 82
Cdd:PRK04123  229 LLARGLRD---KLFTETWTAGEPAG-TLTAEWAQRLGLPEGVAVSVGAFDAHMG---AVGAGAEPGTL----------VK 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  83 VIcGTSSCHMGISKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQgHAAFPELQVKATARCQSIYAYLNshl 162
Cdd:PRK04123  292 VM-GTSTCDILLADKQRAVPGICGQVDGSIVPGLIGYEAGQSAVGDIFAWFAR-LLVPPEYKDEAEARGKQLLELLT--- 366

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 163 dliKKA--QPVG---FLTVDlhvWpdFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLa 237
Cdd:PRK04123  367 ---EAAakQPPGehgLVALD---W--FNGRRTPLADQRLKGV------------------------ITGLTLGTDAPDI- 413

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 238 ilYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDF 316
Cdd:PRK04123  414 --YRALIEATAFGTRAIMECFEDQGVPVEEVIAAGGIArKNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAAVAAGAY 491

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034559850 317 ASVQEAMAKM-SKVGKVVFPRLQDKKYYDKKYQVFLKLVE-HQKEYLAIM 364
Cdd:PRK04123  492 PDIPEAQQAMaSPVEKTYQPDPENVARYEQLYQEYKQLHDyFGRGGNAVM 541
XylB COG1070
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ...
 18-359 8.42e-49

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: 171.17  E-value: 8.42e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  18 QVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKD 97
Cdd:COG1070   206 ELVPPGEVAG-TLTAEAAAETGLPAGTPVVAGAGDNAAAALGA--------GAVEPGD-----AAVSLGTSGVVFVVSDK 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  98 PIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQghaafpelqvKATARCQSIYAYLNshlDLIKKAqPVG----- 172
Cdd:COG1070   272 PLPDPEGRVHTFCHAVPGRWLPMGATNNGGSALRWFRD----------LFADGELDDYEELN---ALAAEV-PPGadgll 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 173 FLtvdlhvwPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLailYLATVQAIALGTR 252
Cdd:COG1070   338 FL-------PYLSGERTPHWDPNARGA------------------------FFGLTLSHTRAHL---ARAVLEGVAFALR 383

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 253 FIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKV 332
Cdd:COG1070   384 DGLEALEEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMVRVGET 463

                         330       340
                  ....*....|....*....|....*..
gi 1034559850 333 VFPRLQDKKYYDKKYQVFLKLVEHQKE 359
Cdd:COG1070   464 IEPDPENVAAYDELYERYRELYPALKP 490
ASKHA_NBD_FGGY_YgcE-like cd07779
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ...
 18-343 2.28e-44

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: 158.07  E-value: 2.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  18 QVLPPGASLGNgLTPEAARDLGLLPGIAVAASlidAHAGGLGVIGADVRGHGLICegqpvtsrlaVICGTSSCHMGISKD 97
Cdd:cd07779   158 ELVPPGTVIGT-LTKEAAEETGLPEGTPVVAG---GGDQQCAALGAGVLEPGTAS----------LSLGTAAVVIAVSDK 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  98 PIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQghaAFPELQVKATARCQSIYAYLNSHLDLIkkaqPVGFLtvD 177
Cdd:cd07779   224 PVEDPERRIPCNPSAVPGKWVLEGSINTGGSAVRWFRD---EFGQDEVAEKELGVSPYELLNEEAAKS----PPGSD--G 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 178 LHVWPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLailYLATVQAIALGTRFIIEA 257
Cdd:cd07779   295 LLFLPYLAGAGTPYWNPEARGA------------------------FIGLTLSHTRAHL---ARAILEGIAFELRDNLEA 347

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 258 MEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRL 337
Cdd:cd07779   348 MEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKAMVRVTDTFEPDP 427


                  ....*.
gi 1034559850 338 QDKKYY 343
Cdd:cd07779   428 ENVAIY 433
L-ribulokinase TIGR01234
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely ...
 30-361 2.66e-41

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: 152.00  E-value: 2.66e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  30 LTPEAARDLGLLPGIAVAASLIDAHaggLGVIGADVrghgliceGQPvtSRLAVICGTSSCHMGISKDPIFVPGVWGPYF 109
Cdd:TIGR01234 248 LTPEWAQRTGLPEGVVVAVGNFDAH---VGAVAAGI--------AQP--GALVKIMGTSTCHVLIGDKQRAVPGMCGVVD 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 110 SAMVPGFWLNEGGQSVTGKLIDHMVQgHAAFPELQVKATARCQSiyayLNSHLDLIKKAQPV---GFLTVDlhvWpdFHG 186
Cdd:TIGR01234 315 GGIVPGFIGYEAGQSAVGDIFAWFGK-VCVPPELKTEANASQKQ----LHEALSEAAAKQPSgehGLVALD---W--FNG 384

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 187 NRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDlaiLYLATVQAIALGTRFIIEAMEAAGHSIS 266
Cdd:TIGR01234 385 NRSPLVDQRLKGV------------------------ITGLTLATDAPL---LYRALIEATAFGTRMIMETFTDSGVPVE 437

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 267 TLFLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVF-PRLQDKKYYD 344
Cdd:TIGR01234 438 ELMAAGGIArKNPVIMQIYADVTNRPLQIVASDQAPALGAAIFAAVAAGVYADIPSAQAKMGSAVEKTLtPCSENAQRYE 517

                         330
                  ....*....|....*..
gi 1034559850 345 KKYQVFLKLVEHQKEYL 361
Cdd:TIGR01234 518 QLYARYQELAMSFGQYN 534
ASKHA_NBD_FGGY_MPA43-like cd07778
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ...
 11-313 2.39e-32

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: 127.14  E-value: 2.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  11 NYSKIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVIgadvrghgliCEGQPVTSRLAVICGTSSC 90
Cdd:cd07778   225 NTFKEAPPLPYAGIPIGK-VNVILASYLGIDKSTVVGHGCIDCYAGWFSTF----------AAAKTLDTTLFMVAGTSTC 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  91 HMGISKDPI--FVPGVWGPyFSAMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQVKATarcqSIYAYLNSHLDLI--K 166
Cdd:cd07778   294 FLYATSSSQvgPIPGIWGP-FDQLLKNYSVYEGGQSATGKLIEKLFNSHPAIIELLKSDA----NFFETVEEKIDKYerL 368

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 167 KAQPVGFLTVDLHVWPDFHGNRSPLADltlkgmrttgylyipalaalhspssllsPQVTG--LKLSQD--LDDLAILYLA 242
Cdd:cd07778   369 LGQSIHYLTRHMFFYGDYLGNRTPYND----------------------------PNMSGsfIGESTDssLTDLVLKYIL 420

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034559850 243 TVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVV---LSQEVESVLVGAAVLGACAS 313
Cdd:cd07778   421 ILEFLAFQTKLIIDNFQKEKIIIQKVVISGSQAKNARLLQLLSTVLSKIHIivpLSDSKYAVVKGAALLGKAAF 494
ASKHA_NBD_FGGY cd00366
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ...
 19-309 1.40e-31

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: 122.67  E-value: 1.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  19 VLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPVtsrlaVICGTSSCHMGISKDP 98
Cdd:cd00366   158 IVESGEVVG-RVTPEAAEETGLPAGTPVVAGGGDTAAAALGA--------GVVEPGDAV-----DSTGTSSVLSVCTDEP 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  99 IFVPGVWGPYFSAmVPGFWLNEGGQSVTGKLIDHMVQghaafpelqvkATARCQSIYAYLNSHLDLIKKAQP----VGFL 174
Cdd:cd00366   224 VPPDPRLLNRCHV-VPGLWLLEGAINTGGASLRWFRD-----------EFGEEEDSDAEYEGLDELAAEVPPgsdgLIFL 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 175 tvdlhvwPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLailYLATVQAIALGTRFI 254
Cdd:cd00366   292 -------PYLSGERSPIWDPAARGV------------------------FFGLTLSHTRAHL---IRAVLEGVAYALRDN 337

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034559850 255 IEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLG 309
Cdd:cd00366   338 LEILEELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
ASKHA_NBD_FGGY_EcXK-like cd07808
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ...
 19-353 2.84e-30

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: 120.72  E-value: 2.84e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  19 VLPP---GASLGNGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPV----TSrlAVICGTSSCH 91
Cdd:cd07808   201 ILPPiveSTEIVGTLTPEAAEELGLPEGTPVVAGAGDNAAAALGA--------GVVEPGDALislgTS--GVVFAPTDKP 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  92 MGISKDPIF-----VPGVW---GPYFSAmvpGF---WLNE--GGQSVTGKLIDHMVQGHAAfpelqvkatarcqsiyayl 158
Cdd:cd07808   271 VPDPKGRLHtfphaVPGKWyamGVTLSA---GLslrWLRDlfGPDRESFDELDAEAAKVPP------------------- 328

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 159 nshldlikKAQPVGFLtvdlhvwPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLAi 238
Cdd:cd07808   329 --------GSEGLLFL-------PYLSGERTPYWDPNARGS------------------------FFGLSLSHTRAHLA- 368

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 239 lyLATVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFAS 318
Cdd:cd07808   369 --RAVLEGVAFSLRDSLEVLKELGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDD 446

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1034559850 319 VQEAMAKMSKVGKVVFPRLQDKKYYDKKYQVFLKL 353
Cdd:cd07808   447 LEEAAAACIKIEKTIEPDPERHEAYDELYARYREL 481
ASKHA_NBD_FGGY_CvXK-like cd07805
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ...
 19-351 7.62e-30

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: 119.55  E-value: 7.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  19 VLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGViGADVRGHGLICegqpvtsrlaviCGTSS---CHmgiS 95
Cdd:cd07805   207 LVPSTEVVG-ELTPEAAAELGLPAGTPVVGGGGDAAAAALGA-GAVEEGDAHIY------------LGTSGwvaAH---V 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  96 KDPIFVPGvwGPYFS--AMVPGFWLNEGGQSVTGKLIDHMVQgHAAFPELQVKatarcqSIYAYLNshlDLIKKAQP--- 170
Cdd:cd07805   270 PKPKTDPD--HGIFTlaSADPGRYLLAAEQETAGGALEWARD-NLGGDEDLGA------DDYELLD---ELAAEAPPgsn 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 171 -VGFLtvdlhvwPDFHGNRSPLADLTLKGMrttgylYIpalaalhspssllspqvtGLKLSQDLDDLAilyLATVQAIAL 249
Cdd:cd07805   338 gLLFL-------PWLNGERSPVEDPNARGA------FI------------------GLSLEHTRADLA---RAVLEGVAF 383

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 250 GTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPV-VLSQEVESVLVGAAVLGACASGDFASVQEAmAKMSK 328
Cdd:cd07805   384 NLRWLLEALEKLTRKIDELRLVGGGARSDLWCQILADVLGRPVeVPENPQEAGALGAALLAAVGLGLLKSFDEA-KALVK 462

                         330       340
                  ....*....|....*....|...
gi 1034559850 329 VGKVVFPRLQDKKYYDKKYQVFL 351
Cdd:cd07805   463 VEKVFEPDPENRARYDRLYEVFK 485
ASKHA_NBD_FGGY_FK cd07773
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ...
 18-314 1.97e-25

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: 106.52  E-value: 1.97e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  18 QVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKD 97
Cdd:cd07773   203 ELVPSGTVIGT-VTPEAAEELGLPAGTPVVVGGHDHLCAALGA--------GVIEPGD-----VLDSTGTAEALLAVVDE 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  98 PIFVPGVWGPYFS---AMVPGFWLNEGGQSvTGKLIDHMVQGHAAFPELQVKATARCQSIYAylnshldlikKAQPVGFL 174
Cdd:cd07773   269 PPLDEMLAEGGLSyghHVPGGYYYLAGSLP-GGALLEWFRDLFGGDESDLAAADELAEAAPP----------GPTGLLFL 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 175 tvdlhvwPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLailYLATVQAIALGTRFI 254
Cdd:cd07773   338 -------PHLSGSGTPDFDPDARGA------------------------FLGLTLGTTRADL---LRAILEGLAFELRLN 383

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 255 IEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 314
Cdd:cd07773   384 LEALEKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
ASKHA_NBD_FGGY_EcLyxK-like cd07802
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ...
 19-314 4.11e-23

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: 99.93  E-value: 4.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  19 VLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKDP 98
Cdd:cd07802   207 LVPSTEIAG-RVTAEAAALTGLPEGTPVAAGAFDVVASALGA--------GAVDEGQ-----LCVILGTWSINEVVTDEP 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  99 IFVPGVWGpYFSAMVPGFWLNEGGQSVTGKLIDHMVQghaafpELQVKATARCQSIYAYLNshlDLIKKAQPVgfltvdl 178
Cdd:cd07802   273 VVPDSVGS-NSLHADPGLYLIVEASPTSASNLDWFLD------TLLGEEKEAGGSDYDELD---ELIAAVPPG------- 335

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 179 hvwpdfhgnrspladltlkgmrTTGYLYIPALAAlhspsSLLSPQVT----GLKLSQDLDDLAilyLATVQAIALGTRFI 254
Cdd:cd07802   336 ----------------------SSGVIFLPYLYG-----SGANPNARggffGLTAWHTRAHLL---RAVYEGIAFSHRDH 385

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 255 IEAMEAAGHsISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 314
Cdd:cd07802   386 LERLLVARK-PETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
ASKHA_NBD_FGGY_RrXK-like cd07804
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ...
 18-314 1.02e-22

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: 98.75  E-value: 1.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  18 QVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKD 97
Cdd:cd07804   206 ELVPSTEIVG-EVTKEAAEETGLAEGTPVVAGTVDAAASALSA--------GVVEPGD-----LLLMLGTAGDIGVVTDK 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  98 PIFVPGVWGPYFSamVPGFWLNEGGQSVTGKLIDHMVQGHAafPELQVKATARCQSIYAYLNshldliKKAQPVGFLTVD 177
Cdd:cd07804   272 LPTDPRLWLDYHD--IPGTYVLNGGMATSGSLLRWFRDEFA--GEEVEAEKSGGDSAYDLLD------EEAEKIPPGSDG 341

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 178 LHVWPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLailYLATVQAIALGTRFIIEA 257
Cdd:cd07804   342 LIVLPYFMGERTPIWDPDARGV------------------------IFGLTLSHTRAHL---YRALLEGVAYGLRHHLEV 394

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034559850 258 MEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 314
Cdd:cd07804   395 IREAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
ASKHA_NBD_FGGY_GntK cd07770
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ...
 18-354 1.76e-22

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: 98.40  E-value: 1.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  18 QVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDahaGGLGVIGAdvrghGLICEGqpvtsRLAVICGTSschmG---- 93
Cdd:cd07770   203 ELVDPTEVLP-GLKPEFAERLGLLAGTPVVLGASD---GALANLGS-----GALDPG-----RAALTVGTS----Gairv 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  94 ISKDPIFVP--GVWgPYFSAmvPGFWL-----NEGGqSVTGKLIDHMVQGHAAFPELQVKATArcqsiyAYLNSHlDLIk 166
Cdd:cd07770   265 VSDRPVLDPpgRLW-CYRLD--ENRWLvggaiNNGG-NVLDWLRDTLLLSGDDYEELDKLAEA------VPPGSH-GLI- 332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 167 kaqpvgFLtvdlhvwPDFHGNRSPLADLTLKGMrttgylyipalaalhspssllspqVTGLKLSQDLDDLailYLATVQA 246
Cdd:cd07770   333 ------FL-------PYLAGERAPGWNPDARGA------------------------FFGLTLNHTRADI---LRAVLEG 372

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 247 IALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEamAKM 326
Cdd:cd07770   373 VAFNLKSIYEALEELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSLEA--DEL 450

                         330       340
                  ....*....|....*....|....*...
gi 1034559850 327 SKVGKVVFPRLQDKKYYDKKYQVFLKLV 354
Cdd:cd07770   451 VKIGKVVEPDPENHAIYAELYERFKKLY 478
ASKHA_NBD_FGGY_SePSK_AtXK1-like cd07783
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ...
 19-310 2.47e-22

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: 97.29  E-value: 2.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  19 VLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPVTSrlaviCGTSSCHMGISKDP 98
Cdd:cd07783   202 VVAPGTVIGT-LTAEAAEELGLPAGTPVVAGTTDSIAAFLAS--------GAVRPGDAVTS-----LGTTLVLKLLSDKR 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  99 IFVPGVwGPYFSAMVPGFWLNEGGQSVTGKLIDHmvqghaAFPELQVKAtarcqsiyaylnshldLIKKAQPVGflTVDL 178
Cdd:cd07783   268 VPDPGG-GVYSHRHGDGYWLVGGASNTGGAVLRW------FFSDDELAE----------------LSAQADPPG--PSGL 322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 179 HVWP-DFHGNRSPLADltlkgmrttgylyipalaalhspssllsPQVTGLKLSQDLDDlAILYLATVQAIALGTRFIIEA 257
Cdd:cd07783   323 IYYPlPLRGERFPFWD----------------------------PDARGFLLPRPHDR-AEFLRALLEGIAFIERLGYER 373

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034559850 258 MEAAGHS-ISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLvGAAVLGA 310
Cdd:cd07783   374 LEELGAPpVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEAAL-GAALLAA 426
ASKHA_NBD_FGGY_YoaC-like cd07798
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ...
 18-314 5.56e-20

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: 90.75  E-value: 5.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  18 QVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsrLAVICGTSSCHMGISKD 97
Cdd:cd07798   205 EIVPSGTVLGT-VSEEAARELGLPEGTPVVVGGADTQCALLGS--------GAIEPGD-----IGIVAGTTTPVQMVTDE 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  98 PIFVP--GVW-GPYfsaMVPGFWLNEGGQSVTGKLIDHMVQGHAAFPELQvkatarcqsiYAYLNSHLDLIKKAQP--VG 172
Cdd:cd07798   271 PIIDPerRLWtGCH---LVPGKWVLESNAGVTGLNYQWLKELLYGDPEDS----------YEVLEEEASEIPPGANgvLA 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 173 FLTvdlhvwpdfhgnrSPLADLTLKGMRTTGYLYipalaalhspSSLLSPQVTGLKlsqdldDLAIlylATVQAIALGTR 252
Cdd:cd07798   338 FLG-------------PQIFDARLSGLKNGGFLF----------PTPLSASELTRG------DFAR---AILENIAFAIR 385

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034559850 253 FIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 314
Cdd:cd07798   386 ANLEQLEEvSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
ASKHA_NBD_FGGY_GK cd07769
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ...
 242-355 4.73e-16

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: 79.05  E-value: 4.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 242 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGdFASVQ 320
Cdd:cd07769   374 AALESIAYQTRDVLEAMEKdSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVG-FWKDL 452

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1034559850 321 EAMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVE 355
Cdd:cd07769   453 DELASLWQVDKRFEPSMDEEE-RERLYRGWKKAVE 486
ASKHA_NBD_FGGY_GK1-3-like cd07792
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ...
 242-355 7.27e-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: 78.72  E-value: 7.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 242 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 320
Cdd:cd07792   384 AALEAVCFQTREILDAMNKdSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLD 463

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1034559850 321 EAMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVE 355
Cdd:cd07792   464 ELKSLNEGGRTVFEPQISEEE-RERRYKRWKKAVE 497
GlpK COG0554
Glycerol kinase [Energy production and conversion];
242-355 8.41e-16

Glycerol kinase [Energy production and conversion];


Pssm-ID: 440320 [Multi-domain]  Cd Length: 496  Bit Score: 78.57  E-value: 8.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 242 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 320
Cdd:COG0554   377 AALESIAYQTRDVLDAMEAdSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKSLE 456

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1034559850 321 EaMAKMSKVGKVVFPRLqDKKYYDKKYQVFLKLVE 355
Cdd:COG0554   457 E-LAALWKVDRRFEPQM-DEEERERLYAGWKKAVE 489
ASKHA_NBD_FGGY_BaXK-like cd07809
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ...
 18-314 1.56e-15

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: 77.59  E-value: 1.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  18 QVLPPGASLGnGLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQPVTSrlaviCGTSSCHMGISKD 97
Cdd:cd07809   208 EVLPAGEVAG-RLTPEGAEELGLPAGIPVAPGEGDNMTGALGT--------GVVNPGTVAVS-----LGTSGTAYGVSDK 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  98 PIFVPgvwgpyfSAMVPGF--------WLNEG---GQSVTGKLIDHMVQGHAAFPELQVKATARCQSI--YAYLNshldl 164
Cdd:cd07809   274 PVSDP-------HGRVATFcdstggmlPLINTtncLTAWTELFRELLGVSYEELDELAAQAPPGAGGLllLPFLN----- 341

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 165 ikkaqpvgfltvdlhvwpdfhgnrspladltlkGMRTTGYlyipalaalhspssllsPQVTGLKLSQDLDD--LAILYLA 242
Cdd:cd07809   342 ---------------------------------GERTPNL-----------------PHGRASLVGLTLSNftRANLARA 371

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034559850 243 TVQAIALGTRFIIEAMEAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 314
Cdd:cd07809   372 ALEGATFGLRYGLDILRELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
FGGY_EcGK_like cd07786
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ...
 242-355 5.63e-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: 5.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 242 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 320
Cdd:cd07786   374 AALESIAYQTRDLLEAMEAdSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLD 453

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1034559850 321 EAmAKMSKVGKVVFPRLqDKKYYDKKYQVFLKLVE 355
Cdd:cd07786   454 EL-AKLWQVDRRFEPSM-SEEEREALYAGWKKAVK 486
PTZ00294 PTZ00294
glycerol kinase-like protein; Provisional
 242-342 6.74e-15

glycerol kinase-like protein; Provisional


Pssm-ID: 240348 [Multi-domain]  Cd Length: 504  Bit Score: 75.78  E-value: 6.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 242 ATVQAIALGTRFIIEAME-AAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 320
Cdd:PTZ00294  383 AALEAIALQTNDVIESMEkDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLE 462

                          90       100
                  ....*....|....*....|..
gi 1034559850 321 EAMAKMSKVGKVVFPRLQDKKY 342
Cdd:PTZ00294  463 EVKKLIRRSNSTFSPQMSAEER 484
ASKHA_NBD_FGGY_AI-2K cd07775
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ...
 1-348 5.39e-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: 69.67  E-value: 5.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850   1 MIGLEDFvadnyskIGNQVLPPGASLGNgLTPEAARDLGLLPGIAVAASLIDAHAGGLGVigadvrghGLICEGQpvtsr 80
Cdd:cd07775   197 MAGLKAD-------ILPPVVESGTVIGK-VTKEAAEETGLKEGTPVVVGGGDVQLGCLGL--------GVVRPGQ----- 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  81 lAVICGTSSCHMGI-SKDPIFVPGVWGPYFSAMVPGFWLNEGGQSVTGKLIDHMVQghAAFPELQVKATARCQSIYAYLN 159
Cdd:cd07775   256 -TAVLGGSFWQQEVnTAAPVTDPAMNIRVNCHVIPDMWQAEGISFFPGLVMRWFRD--AFCAEEKEIAERLGIDAYDLLE 332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 160 shldliKKAQ--PVGFltvdlhvwpdfHGNRSPLADLtlkgMRTTGYlYIPAlaalhspssllsPQVTGLKLSQDLDDLA 237
Cdd:cd07775   333 ------EMAKdvPPGS-----------YGIMPIFSDV----MNYKNW-RHAA------------PSFLNLDIDPEKCNKA 378

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 238 ILYLATVQAIALGTRFIIEAMEAA-GHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDF 316
Cdd:cd07775   379 TFFRAIMENAAIVSAGNLERIAEFsGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGAGIY 458

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1034559850 317 ASVQEAMAKMSKVGKVVFPRLQDKKYYDKKYQ 348
Cdd:cd07775   459 SSLEEAVESLVKWEREYLPNPENHEVYQDLYE 490
glpK PRK00047
glycerol kinase GlpK;
242-356 2.04e-12

glycerol kinase GlpK;


Pssm-ID: 234594 [Multi-domain]  Cd Length: 498  Bit Score: 67.93  E-value: 2.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 242 ATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQ 320
Cdd:PRK00047  380 ATLESIAYQTRDVLDAMQAdSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLD 459

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034559850 321 EaMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVEH 356
Cdd:PRK00047  460 E-LKEQWKIDRRFEPQMDEEE-REKLYAGWKKAVKR 493
ASKHA_NBD_FGGY_GK5-like cd07793
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ...
 201-355 2.47e-11

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: 64.89  E-value: 2.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 201 TTGYLYIPALAALHSP--SSLLSPQVTGLKLSQDLDDLAIlylATVQAIALGTRFIIEAMEA-AGHSISTLFLCGGLSKN 277
Cdd:cd07793   349 TNGVYFVPAFSGLQAPynDPTACAGFIGLTPSTTKAHLVR---AILESIAFRVKQLLETMEKeTSIKISSIRVDGGVSNN 425

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034559850 278 PLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVqEAMAKMSKVGKVVFPRlQDKKYYDKKYQVFLKLVE 355
Cdd:cd07793   426 DFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSK-EELKKLRKIEKIFEPK-MDNEKREELYKNWKKAVK 501
ASKHA_NBD_FGGY_BaEryA-like cd24121
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ...
 30-314 1.72e-10

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: 61.87  E-value: 1.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850  30 LTPEAARDLGLLPGIAVAASLIDAHAGGLGViGADVRGHGLicegqpvtsrlaVICGTSSCHMGISKDPIFVPGVWGPYF 109
Cdd:cd24121   217 LTPEAAAATGLPAGTPVVLGPFDVVATALGS-GAIEPGDAC------------SILGTTGVHEVVVDEPDLEPEGVGYTI 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 110 SAMVPGFWLneggqsvtgklidHMVQGHAAFPELQvkatarcqsiYAylnshLDLIKKAQPVGFLTVDLHVWPDFHG--N 187
Cdd:cd24121   284 CLGVPGRWL-------------RAMANMAGTPNLD----------WF-----LRELGEVLKEGAEPAGSDLFQDLEElaA 335

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 188 RSPLAdltlkgmrTTGYLYIPALaalhSPSSLLSP--------QVTGLKLSQDLDDLAilyLATVQAIALGTRFIIEAMe 259
Cdd:cd24121   336 SSPPG--------AEGVLYHPYL----SPAGERAPfvnpnaraQFTGLSLEHTRADLL---RAVYEGVALAMRDCYEHM- 399

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034559850 260 aaGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASG 314
Cdd:cd24121   400 --GEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
PRK10331 PRK10331
L-fuculokinase; Provisional
 239-342 1.64e-08

L-fuculokinase; Provisional


Pssm-ID: 182383 [Multi-domain]  Cd Length: 470  Bit Score: 55.80  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 239 LYLATVQAIALGTRFIIEAMEAAGH-SISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFA 317
Cdd:PRK10331  363 FYRAALEGLTAQLKRNLQVLEKIGHfKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFS 442

                          90       100
                  ....*....|....*....|....*
gi 1034559850 318 SVQEAMAKMSKVGKVVFPRLQDKKY 342
Cdd:PRK10331  443 SPEQARAQMKYQYRYFYPQTEPEFI 467
ASKHA_NBD_FGGY_RhaB-like cd07771
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ...
 247-322 1.88e-08

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: 55.61  E-value: 1.88e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034559850 247 IALGTRFIIEAMEA-AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSqEVESVLVGAAVLGACASGDFASVQEA 322
Cdd:cd07771   378 LALKYAKTIEELEElTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIAG-PVEATAIGNLLVQLIALGEIKSLEEG 453
PLN02295 PLN02295
glycerol kinase
 242-355 9.74e-08

glycerol kinase


Pssm-ID: 215166 [Multi-domain]  Cd Length: 512  Bit Score: 53.55  E-value: 9.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 242 ATVQAIALGTRFIIEAM------EAAGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGD 315
Cdd:PLN02295  384 AVLESMCFQVKDVLDAMrkdageEKSHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGL 463

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034559850 316 FASVQEAMAKMSKVGKVVFPRLQDKKyYDKKYQVFLKLVE 355
Cdd:PLN02295  464 WTEEEIFASEKWKNTTTFRPKLDEEE-RAKRYASWCKAVE 502
PRK10939 PRK10939
autoinducer-2 (AI-2) kinase; Provisional
 261-356 1.26e-05

autoinducer-2 (AI-2) kinase; Provisional


Pssm-ID: 182853 [Multi-domain]  Cd Length: 520  Bit Score: 46.92  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 261 AGHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKVGKVVFPRLQDK 340
Cdd:PRK10939  406 SGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEATALGCAIAAGVGAGIYSSLAETGERLVRWERTFEPNPENH 485

                          90       100
                  ....*....|....*....|...
gi 1034559850 341 KYYDKK-------YQVFLKLVEH 356
Cdd:PRK10939  486 ELYQEAkekwqavYADQLGLVDH 508
ASKHA_NBD_FGGY_SHK cd07777
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ...
 239-306 1.07e-04

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: 43.75  E-value: 1.07e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034559850 239 LYLATVQAIALGTRFIIEAMEAAGHSISTLFLCGG-LSKNPLFVQMHADITGMPVVLSQEVESVLVGAA 306
Cdd:cd07777   365 LFRALCRGIAENLHEMLPRLDLDLSGIERIVGSGGaLRKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAA 433
ASKHA_NBD_FGGY_NaCK-like cd07772
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ...
 203-308 7.55e-04

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: 41.09  E-value: 7.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 203 GYLYIPALAALHSPSSLLSPQVTGLKLS--QDLDDLAILYLATVQAIALgtrfiieamEAAGHSISTLFLCGGLSKNPLF 280
Cdd:cd07772   324 GTFALPSFAPGGGPFPGSGGRGVLSAFPsaEEAYALAILYLALMTDYAL---------DLLGSGVGRIIVEGGFAKNPVF 394

                          90       100
                  ....*....|....*....|....*....
gi 1034559850 281 VQMHADI-TGMPVVLSQEVESVLVGAAVL 308
Cdd:cd07772   395 LRLLAALrPDQPVYLSDDSEGTALGAALL 423
ASKHA_NBD_FGGY_SpXK-like cd07776
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ...
 262-345 1.25e-03

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: 40.62  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034559850 262 GHSISTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAVLGACASGDFASVQEAMAKMSKV----GKVVFPRL 337
Cdd:cd07776   423 DIPPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAGSGDFSPEFVVFSaeepKLVAEPDP 502


                  ....*...
gi 1034559850 338 QDKKYYDK 345
Cdd:cd07776   503 EAAEVYDK 510
 
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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