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Conserved domains on  [gi|755508662|ref|XP_011238938|]
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FGGY carbohydrate kinase domain-containing protein isoform X4 [Mus musculus]

Protein Classification

FGGY-family carbohydrate kinase( domain architecture ID 10167359)

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

CATH:  3.30.420.40
EC:  2.7.1.-
Gene Ontology:  GO:0016310|GO:0019200|GO:0005524
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 ...
20-513 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: 920.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDATCS 97
Cdd:cd07782    1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEgaGVDPEQVKGIGFDATCS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  98 LVVLDKEFHPLPVNHEGDSSRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREiCWDKAGHF 177
Cdd:cd07782   81 LVVLDAEGKPVSVSPSGDDERNVILWMDHRAVEEAERINATGHEVLKYVGGKISPEMEPPKLLWLKENLPE-TWAKAGHF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 178 FDLPDFLSWKATGVTARSLCSLVCKWTYSA----EKGWDDSFWKMIGLEDLIDDNYSKIGNLVLLPGAALGIGLTPEAAR 253
Cdd:cd07782  160 FDLPDFLTWKATGSLTRSLCSLVCKWTYLAhegsEGGWDDDFFKEIGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 254 ELGLPSGIAVAASLIDAHAGGLGVIGADVrgHGLTCEGQPVTSRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGF 333
Cdd:cd07782  240 ELGLPEGTPVGVSLIDAHAGGLGTLGADV--GGLPCEADPLTRRLALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGL 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 334 WLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNSHLDLIKKAQ--PVGFLTVDLHVWPDFHGNRSPLADL 411
Cdd:cd07782  318 WLNEGGQSATGALLDHIIETHPAYPELKEEAKAAGKSIYEYLNERLEQLAEEKglPLAYLTRDLHVLPDFHGNRSPLADP 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 412 TLKGMVTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEV 491
Cdd:cd07782  398 TLRGMISGLTLDTSLDDLALLYLATLQALAYGTRHIIEAMNAAGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEP 477
                        490       500
                 ....*....|....*....|..
gi 755508662 492 ESVLVGAAILGACASGDFTSVQ 513
Cdd:cd07782  478 EAVLLGAAILGAVASGDFPSLW 499
 
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 ...
20-513 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: 920.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDATCS 97
Cdd:cd07782    1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEgaGVDPEQVKGIGFDATCS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  98 LVVLDKEFHPLPVNHEGDSSRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREiCWDKAGHF 177
Cdd:cd07782   81 LVVLDAEGKPVSVSPSGDDERNVILWMDHRAVEEAERINATGHEVLKYVGGKISPEMEPPKLLWLKENLPE-TWAKAGHF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 178 FDLPDFLSWKATGVTARSLCSLVCKWTYSA----EKGWDDSFWKMIGLEDLIDDNYSKIGNLVLLPGAALGIGLTPEAAR 253
Cdd:cd07782  160 FDLPDFLTWKATGSLTRSLCSLVCKWTYLAhegsEGGWDDDFFKEIGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 254 ELGLPSGIAVAASLIDAHAGGLGVIGADVrgHGLTCEGQPVTSRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGF 333
Cdd:cd07782  240 ELGLPEGTPVGVSLIDAHAGGLGTLGADV--GGLPCEADPLTRRLALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGL 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 334 WLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNSHLDLIKKAQ--PVGFLTVDLHVWPDFHGNRSPLADL 411
Cdd:cd07782  318 WLNEGGQSATGALLDHIIETHPAYPELKEEAKAAGKSIYEYLNERLEQLAEEKglPLAYLTRDLHVLPDFHGNRSPLADP 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 412 TLKGMVTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEV 491
Cdd:cd07782  398 TLRGMISGLTLDTSLDDLALLYLATLQALAYGTRHIIEAMNAAGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEP 477
                        490       500
                 ....*....|....*....|..
gi 755508662 492 ESVLVGAAILGACASGDFTSVQ 513
Cdd:cd07782  478 EAVLLGAAILGAVASGDFPSLW 499
5C_CHO_kinase TIGR01315
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of ...
20-522 0e+00

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: 631.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662   20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVV--QGIDAHRIRGLGFDATCS 97
Cdd:TIGR01315   1 HYIGVDVGTGSARACIIDSTGDILALAAQNIKTWTPSSGLEGQSSVYIWQAICNCVKQVLaeSKVDPNSVKGIGFDATCS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662   98 LVVLDKEFHPLPVNHEGDSSRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHF 177
Cdd:TIGR01315  81 LVVLTHDGEPLPVSKNGGADQNIILWMDHRALAEAEKINATNHNLLRYVGGKMSVEMEIPKVLWLKNNMPPE-LFARCKF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  178 FDLPDFLSWKATGVTARSLCSLVCKWTY----SAEKGWDDSFWKMIGLEDLIDDNYSKIGNLVLLPGAALGIGLTPEAAR 253
Cdd:TIGR01315 160 FDLTDFLTWRATGKEIRSFCSVVCKWGFvpvdGSNKGWQEDFYETIGLGELVTDNFIRMGGSWMSPGELVGGGLTAEAAQ 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  254 ELGLPSGIAVAASLIDAHAGGLGVIGADVRGHGltcEGQPVTSRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGF 333
Cdd:TIGR01315 240 ELGLPAGTAVGSGLIDAHAGWIGTVGAKVAENG---DVSQAFTRLAAVAGTSTCHMAMTKGPVFVPGVWGPYRDALIPGY 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  334 WLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNSHLdLIKKAQP----VGFLTVDLHVWPDFHGNRSPLA 409
Cdd:TIGR01315 317 WLAEGGQSAAGELMDHMLETHVAYDETVKEAEAAGKNIYDYLNEHL-KEMAAKTnapsISYLVRHFHVYPDLWGNRSPIA 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  410 DLTLKGMVTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQ 489
Cdd:TIGR01315 396 DPNMRGVIIGLSMDRSKDGLALLYYATMEFIAYGTRQIVEAMNTAGHTIKSIFMSGGQCQNPLLMQLIADACDMPVLIPY 475
                         490       500       510
                  ....*....|....*....|....*....|...
gi 755508662  490 EVESVLVGAAILGACASGDFTSVQIAVPREHGP 522
Cdd:TIGR01315 476 VNEAVLHGAAMLGAKAAGTTESLWDAMDRMSKP 508
AraB COG1069
Ribulose kinase [Carbohydrate transport and metabolism];
18-515 0e+00

Ribulose kinase [Carbohydrate transport and metabolism];


Pssm-ID: 440687 [Multi-domain]  Cd Length: 532  Bit Score: 547.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  18 SRYYVGIDVGTGSVRAALVDQR-GLLLAFAEQPIKKWEP---------QFnhhEQSSEDIWAACCLVTKEVVQ--GIDAH 85
Cdd:COG1069    1 EKYVIGVDFGTDSVRAVVVDAAdGEELASAVHPYPRWVIglylppppdQA---RQHPLDYLEALEAAVREALAqaGVDPA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  86 RIRGLGFDAT-CSLVVLDKEFHPLPVNHE--GDSSRNVIMWLDHRAVSQVHRINE----TKHRVLQYVGGVMSVEMQAPK 158
Cdd:COG1069   78 DVVGIGVDATgCTPVPVDADGTPLALLPEfaENPHAMVILWKDHTAQEEAERINElakaRGEDYLRYVGGIISSEWFWPK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 159 LLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA-EKGW-DDSFWKMIG--LEDLIDdnysKIGN 234
Cdd:COG1069  158 ILHLLREDPEV-YEAADSFVELCDWITWQLTGSLKRSRCTAGHKALWHAhEGGYpSEEFFAALDplLDGLAD----RLGT 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 235 LVLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAGGLGVIGAdvrghgltCEGQpvtsrLAVICGTSSCHMGISKD 314
Cdd:COG1069  233 EIYPLGEPAG-TLTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGGV--------EPGT-----LVKVMGTSTCHMLVSPE 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 315 PVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNshldliKKAQPVGFLTVD 394
Cdd:COG1069  299 ERFVPGICGQVDGSIVPGMWGYEAGQSAVGDIFAWFVRLLVPPLEYEKEAEERGISLHPLLT------EEAAKLPPGESG 372
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 395 LHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDlaiLYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLS-KNPLF 473
Cdd:COG1069  373 LHALDWFNGNRSPLADQRLKGVILGLTLGTDAED---IYRALVEATAFGTRAIIERFEEEGVPIDEIIACGGIAtKNPLV 449
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 755508662 474 VQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQIA 515
Cdd:COG1069  450 MQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEEA 491
PRK04123 PRK04123
ribulokinase; Provisional
20-515 3.53e-80

ribulokinase; Provisional


Pssm-ID: 235221 [Multi-domain]  Cd Length: 548  Bit Score: 260.93  E-value: 3.53e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  20 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKW---------EPQFNHHEQSSEDIWAAcclVTKEVVQ--GIDAHRI 87
Cdd:PRK04123   4 YVIGLDFGTDSVRALLVDcATGEELATAVVEYPHWvkgryldlpPNQALQHPLDYIESLEA---AIPAVLKeaGVDPAAV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  88 RGLGFDAT-CSLVVLDKEFHPLPVNHEGDSSRN--VIMWLDHRAVSQVHRINETKHR-----VLQYVGGVMSVEMQAPKL 159
Cdd:PRK04123  81 VGIGVDFTgSTPAPVDADGTPLALLPEFAENPHamVKLWKDHTAQEEAEEINRLAHErgeadLSRYIGGIYSSEWFWAKI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 160 LWLKENLREIcWDKAGHFFDLPDFLSWKATGVTA-----RSLCSLVCKWTYSAEKG--WDDSFWKMI--GLEDLIDDnys 230
Cdd:PRK04123 161 LHVLREDPAV-YEAAASWVEACDWVVALLTGTTDpqdivRSRCAAGHKALWHESWGglPSADFFDALdpLLARGLRD--- 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 231 KIGNLVLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAgglGVIGADVRGHGLTcegqpvtsrlAVIcGTSSCHMG 310
Cdd:PRK04123 237 KLFTETWTAGEPAG-TLTAEWAQRLGLPEGVAVSVGAFDAHM---GAVGAGAEPGTLV----------KVM-GTSTCDIL 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 311 ISKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKL----IDHMVQghpafPELQAKATARCQSIYAYLNshldliKKA- 385
Cdd:PRK04123 302 LADKQRAVPGICGQVDGSIVPGLIGYEAGQSAVGDIfawfARLLVP-----PEYKDEAEARGKQLLELLT------EAAa 370
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 386 -QPV---GFLTVDlhvWpdFHGNRSPLADLTLKGMVTGLTLSQDLDDlaiLYLATVQAIAFGTRFIIETMEAAGHSLSTL 461
Cdd:PRK04123 371 kQPPgehGLVALD---W--FNGRRTPLADQRLKGVITGLTLGTDAPD---IYRALIEATAFGTRAIMECFEDQGVPVEEV 442
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755508662 462 FLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQIA 515
Cdd:PRK04123 443 IAAGGIArKNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDIPEA 497
FGGY_C pfam02782
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ...
298-505 1.70e-59

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: 195.24  E-value: 1.70e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  298 LAVICGTSSCHMGISKDPV-FVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAkaTARCQSIYAYLN 376
Cdd:pfam02782   1 LAISAGTSSFVLVETPEPVlSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELRD--AGNVESLAELAA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  377 SHLDLikkaqpvgfLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLddlAILYLATVQAIAFGTRFIIETMEA-AG 455
Cdd:pfam02782  79 LAAVA---------PAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTL---AHLYRAILESLALQLRQILEALTKqEG 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 755508662  456 HSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACA 505
Cdd:pfam02782 147 HPIDTIHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
 
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 ...
20-513 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: 920.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDATCS 97
Cdd:cd07782    1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEgaGVDPEQVKGIGFDATCS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  98 LVVLDKEFHPLPVNHEGDSSRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREiCWDKAGHF 177
Cdd:cd07782   81 LVVLDAEGKPVSVSPSGDDERNVILWMDHRAVEEAERINATGHEVLKYVGGKISPEMEPPKLLWLKENLPE-TWAKAGHF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 178 FDLPDFLSWKATGVTARSLCSLVCKWTYSA----EKGWDDSFWKMIGLEDLIDDNYSKIGNLVLLPGAALGIGLTPEAAR 253
Cdd:cd07782  160 FDLPDFLTWKATGSLTRSLCSLVCKWTYLAhegsEGGWDDDFFKEIGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 254 ELGLPSGIAVAASLIDAHAGGLGVIGADVrgHGLTCEGQPVTSRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGF 333
Cdd:cd07782  240 ELGLPEGTPVGVSLIDAHAGGLGTLGADV--GGLPCEADPLTRRLALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGL 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 334 WLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNSHLDLIKKAQ--PVGFLTVDLHVWPDFHGNRSPLADL 411
Cdd:cd07782  318 WLNEGGQSATGALLDHIIETHPAYPELKEEAKAAGKSIYEYLNERLEQLAEEKglPLAYLTRDLHVLPDFHGNRSPLADP 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 412 TLKGMVTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEV 491
Cdd:cd07782  398 TLRGMISGLTLDTSLDDLALLYLATLQALAYGTRHIIEAMNAAGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEP 477
                        490       500
                 ....*....|....*....|..
gi 755508662 492 ESVLVGAAILGACASGDFTSVQ 513
Cdd:cd07782  478 EAVLLGAAILGAVASGDFPSLW 499
5C_CHO_kinase TIGR01315
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of ...
20-522 0e+00

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: 631.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662   20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVV--QGIDAHRIRGLGFDATCS 97
Cdd:TIGR01315   1 HYIGVDVGTGSARACIIDSTGDILALAAQNIKTWTPSSGLEGQSSVYIWQAICNCVKQVLaeSKVDPNSVKGIGFDATCS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662   98 LVVLDKEFHPLPVNHEGDSSRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHF 177
Cdd:TIGR01315  81 LVVLTHDGEPLPVSKNGGADQNIILWMDHRALAEAEKINATNHNLLRYVGGKMSVEMEIPKVLWLKNNMPPE-LFARCKF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  178 FDLPDFLSWKATGVTARSLCSLVCKWTY----SAEKGWDDSFWKMIGLEDLIDDNYSKIGNLVLLPGAALGIGLTPEAAR 253
Cdd:TIGR01315 160 FDLTDFLTWRATGKEIRSFCSVVCKWGFvpvdGSNKGWQEDFYETIGLGELVTDNFIRMGGSWMSPGELVGGGLTAEAAQ 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  254 ELGLPSGIAVAASLIDAHAGGLGVIGADVRGHGltcEGQPVTSRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGF 333
Cdd:TIGR01315 240 ELGLPAGTAVGSGLIDAHAGWIGTVGAKVAENG---DVSQAFTRLAAVAGTSTCHMAMTKGPVFVPGVWGPYRDALIPGY 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  334 WLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNSHLdLIKKAQP----VGFLTVDLHVWPDFHGNRSPLA 409
Cdd:TIGR01315 317 WLAEGGQSAAGELMDHMLETHVAYDETVKEAEAAGKNIYDYLNEHL-KEMAAKTnapsISYLVRHFHVYPDLWGNRSPIA 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  410 DLTLKGMVTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQ 489
Cdd:TIGR01315 396 DPNMRGVIIGLSMDRSKDGLALLYYATMEFIAYGTRQIVEAMNTAGHTIKSIFMSGGQCQNPLLMQLIADACDMPVLIPY 475
                         490       500       510
                  ....*....|....*....|....*....|...
gi 755508662  490 EVESVLVGAAILGACASGDFTSVQIAVPREHGP 522
Cdd:TIGR01315 476 VNEAVLHGAAMLGAKAAGTTESLWDAMDRMSKP 508
AraB COG1069
Ribulose kinase [Carbohydrate transport and metabolism];
18-515 0e+00

Ribulose kinase [Carbohydrate transport and metabolism];


Pssm-ID: 440687 [Multi-domain]  Cd Length: 532  Bit Score: 547.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  18 SRYYVGIDVGTGSVRAALVDQR-GLLLAFAEQPIKKWEP---------QFnhhEQSSEDIWAACCLVTKEVVQ--GIDAH 85
Cdd:COG1069    1 EKYVIGVDFGTDSVRAVVVDAAdGEELASAVHPYPRWVIglylppppdQA---RQHPLDYLEALEAAVREALAqaGVDPA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  86 RIRGLGFDAT-CSLVVLDKEFHPLPVNHE--GDSSRNVIMWLDHRAVSQVHRINE----TKHRVLQYVGGVMSVEMQAPK 158
Cdd:COG1069   78 DVVGIGVDATgCTPVPVDADGTPLALLPEfaENPHAMVILWKDHTAQEEAERINElakaRGEDYLRYVGGIISSEWFWPK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 159 LLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA-EKGW-DDSFWKMIG--LEDLIDdnysKIGN 234
Cdd:COG1069  158 ILHLLREDPEV-YEAADSFVELCDWITWQLTGSLKRSRCTAGHKALWHAhEGGYpSEEFFAALDplLDGLAD----RLGT 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 235 LVLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAGGLGVIGAdvrghgltCEGQpvtsrLAVICGTSSCHMGISKD 314
Cdd:COG1069  233 EIYPLGEPAG-TLTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGGV--------EPGT-----LVKVMGTSTCHMLVSPE 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 315 PVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYLNshldliKKAQPVGFLTVD 394
Cdd:COG1069  299 ERFVPGICGQVDGSIVPGMWGYEAGQSAVGDIFAWFVRLLVPPLEYEKEAEERGISLHPLLT------EEAAKLPPGESG 372
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 395 LHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDlaiLYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLS-KNPLF 473
Cdd:COG1069  373 LHALDWFNGNRSPLADQRLKGVILGLTLGTDAED---IYRALVEATAFGTRAIIERFEEEGVPIDEIIACGGIAtKNPLV 449
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 755508662 474 VQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQIA 515
Cdd:COG1069  450 MQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEEA 491
ASKHA_NBD_FGGY_RBK-like cd07768
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ...
20-509 2.39e-147

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: 433.20  E-value: 2.39e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  20 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKWE-PQFNHHEQSSEDIWAACCLVTKEVV--QGIDAHRIRGLGFDAT 95
Cdd:cd07768    1 YGIGVDVGTSSARAGVYDlYAGLEMAQEPVPYYQDSsKKSWKFWQKSTEIIKALQKCVQKLNirEGVDAYEVKGCGVDAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  96 CSLVVLDKEFHPLPVNHEGDSSRNVIMWLDHRAVSQVHRINETKHRVLQ-YVGGVMSVEMQAPKLLWLKENLREIcWDKA 174
Cdd:cd07768   81 CSLAIFDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWINMQCPQQLLdYLGGKISPEMGVPKLKYFLDEYSHL-RDKH 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 175 GHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA-EKGWDDSFWKMIGLEDLiDDNYSKIGNLVLLPGAALGIGLtPEAAR 253
Cdd:cd07768  160 FHIFDLHDYIAYELTRLYEWNICGLLGKENLDGeESGWSSSFFKNIDPRLE-HLTTTKNLPSNVPIGTTSGVAL-PEMAE 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 254 ELGLPSGIAVAASLIDAHAGGLGVIGADVRGhgltcegqpvtsRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGF 333
Cdd:cd07768  238 KMGLHPGTAVVVSCIDAHASWFAVASPHLET------------SLFMIAGTSSCHMYGTTISDRIPGVWGPFDTIIDPDY 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 334 WLNEGGQSVTGKLIDHMVQGHPAFPELQaKATARCQSIYAYLNshlDLIKKAQPVGFLTVDLHVWPDFHGNRSPLADLTL 413
Cdd:cd07768  306 SVYEAGQSATGKLIEHLFESHPCARKFD-EALKKGADIYQVLE---QTIRQIEKNNGLSIHILTLDMFFGNRSEFADPRL 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 414 KGMVTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVES 493
Cdd:cd07768  382 KGSFIGESLDTSMLNLTYKYIAILEALAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMM 461
                        490
                 ....*....|....*.
gi 755508662 494 VLVGAAILGACASGDF 509
Cdd:cd07768  462 GILGAAVLAKVAAGKK 477
ASKHA_NBD_FGGY_L-RBK cd07781
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ...
20-516 1.22e-140

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: 415.40  E-value: 1.22e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  20 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKWE--PQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDA 94
Cdd:cd07781    1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAeaGVDPEDVVGIGVDT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  95 TCS-LVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINETKHRV----LQYVGGVMSVEMQAPKLLWLKENLREI 169
Cdd:cd07781   81 TSStVVPVDEDGNPL---------APAILWMDHRAQEEAAEINETAHPAleyyLAYYGGVYSSEWMWPKALWLKRNAPEV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 170 cWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEDLidDNYSKIGNLVLLPGAALGiGLT 248
Cdd:cd07781  152 -YDAAYTIVEACDWINARLTGRWVRSRCAAGHKWMYNEWGGgPPREFLAALDPGLL--KLREKLPGEVVPVGEPAG-TLT 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 249 PEAARELGLPSGIAVAASLIDAHAGglgVIGADVRGHGltcegqpvtsRLAVICGTSSCHMGISKDPVFVPGVWGPYYSA 328
Cdd:cd07781  228 AEAAERLGLPAGIPVAQGGIDAHMG---AIGAGVVEPG----------TLALIMGTSTCHLMVSPKPVDIPGICGPVPDA 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 329 MVPGFWLNEGGQSVTGKLIDhmvqghpAFPELQAKATA-RCQSIYAYLNshlDLIKKAQPV--GFLTVDlhvWpdFHGNR 405
Cdd:cd07781  295 VVPGLYGLEAGQSAVGDIFA-------WFVRLFVPPAEeRGDSIYALLS---EEAAKLPPGesGLVALD---W--FNGNR 359
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 406 SPLADLTLKGMVTGLTLSQdldDLAILYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLS-KNPLFVQMHADITGMP 484
Cdd:cd07781  360 TPLVDPRLRGAIVGLTLGT---TPAHIYRALLEATAFGTRAIIERFEEAGVPVNRVVACGGIAeKNPLWMQIYADVLGRP 436
                        490       500       510
                 ....*....|....*....|....*....|..
gi 755508662 485 VVLSQEVESVLVGAAILGACASGDFTSVQIAV 516
Cdd:cd07781  437 IKVPKSDQAPALGAAILAAVAAGVYADIEEAA 468
XylB COG1070
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ...
19-518 5.31e-90

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: 284.80  E-value: 5.31e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  19 RYYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDAT- 95
Cdd:COG1070    1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAkaGVDPEEIAAIGVSGQm 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  96 CSLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINET--KHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDK 173
Cdd:COG1070   81 HGLVLLDADGEPL---------RPAILWNDTRAAAEAAELREElgEEALYEITGNPLHPGFTAPKLLWLKENEPEI-FAR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 174 AGHFFDLPDFLSWKATG--VTARSLCSlvckWT--YSAEKG-WDDSFWKMIGLEDLIddnyskignL--VLLPGAALGiG 246
Cdd:COG1070  151 IAKVLLPKDYLRYRLTGefVTDYSDAS----GTglLDVRTRdWSDELLEALGIDREL---------LpeLVPPGEVAG-T 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 247 LTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGPYY 326
Cdd:COG1070  217 LTAEAAAETGLPAGTPVVAGAGDNAAAALGA--------GAVEPGD-----AAVSLGTSGVVFVVSDKPLPDPEGRVHTF 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 327 SAMVPGFWLNEGGQSVTGKLIDHMVQghpafpELQAKAtarcQSIYAYLNshlDLIKKAqPVG-----FLtvdlhvwPDF 401
Cdd:COG1070  284 CHAVPGRWLPMGATNNGGSALRWFRD------LFADGE----LDDYEELN---ALAAEV-PPGadgllFL-------PYL 342
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 402 HGNRSPLADLTLKGMVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADIT 481
Cdd:COG1070  343 SGERTPHWDPNARGAFFGLTLSHTRAHL---ARAVLEGVAFALRDGLEALEEAGVKIDRIRATGGGARSPLWRQILADVL 419
                        490       500       510
                 ....*....|....*....|....*....|....*..
gi 755508662 482 GMPVVLSQEVESVLVGAAILGACASGDFTSVQIAVPR 518
Cdd:COG1070  420 GRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAA 456
ASKHA_NBD_FGGY_MPA43-like cd07778
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ...
21-518 1.16e-88

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: 282.76  E-value: 1.16e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  21 YVGIDVGTGSVRAALVDQRGLLLAFAEQPI--KKWEPQFNHHEQSSEDIWAACCLVTKEVVQGIDAHRIRGLGFDATCSL 98
Cdd:cd07778    2 GIGIDVGSTSVRIGIFDYHGTLLATSERPIsyKQDPKDLWFVTQSSTEIWKAIKTALKELIEELSDYIVSGIGVSATCSM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  99 VVLDKE-----FHPLPVNHE-GDSSRNVIMWLDHRAVSQVHRINE-TKHRVLQYVGGVMSVEMQAPKLLWLKENLREICW 171
Cdd:cd07778   82 VVMQRDsdtsyLVPYNVIHEkSNPDQDIIFWMDHRASEETQWLNNiLPDDILDYLGGGFIPEMAIPKLKYLIDLIKEDTF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 172 DKAgHFFDLPDFLSWKatgvtarsLCSLVCKW--TYSAE------------KGWDDSFWKMIGLEDLIDDNYSKIGNLVL 237
Cdd:cd07778  162 KKL-EVFDLHDWISYM--------LATNLGHSniVPVNAppsigigidgslKGWSKDFYSKLKISTKVCNVGNTFKEAPP 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 238 LPGAALGIG-LTPEAARELGLPSGIAVAASLIDAHAGGLGVIgadvrghgltCEGQPVTSRLAVICGTSSCHMGISKDPV 316
Cdd:cd07778  233 LPYAGIPIGkVNVILASYLGIDKSTVVGHGCIDCYAGWFSTF----------AAAKTLDTTLFMVAGTSTCFLYATSSSQ 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 317 --FVPGVWGPYySAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAKATarcqSIYAYLNSHLDLI--KKAQPVGFLT 392
Cdd:cd07778  303 vgPIPGIWGPF-DQLLKNYSVYEGGQSATGKLIEKLFNSHPAIIELLKSDA----NFFETVEEKIDKYerLLGQSIHYLT 377
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 393 VDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPL 472
Cdd:cd07778  378 RHMFFYGDYLGNRTPYNDPNMSGSFIGESTDSSLTDLVLKYILILEFLAFQTKLIIDNFQKEKIIIQKVVISGSQAKNAR 457
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 755508662 473 FVQMHADITGMPVV---LSQEVESVLVGAAILGACASGDFTSVQIAVPR 518
Cdd:cd07778  458 LLQLLSTVLSKIHIivpLSDSKYAVVKGAALLGKAAFLHNQSIEERLIS 506
PRK04123 PRK04123
ribulokinase; Provisional
20-515 3.53e-80

ribulokinase; Provisional


Pssm-ID: 235221 [Multi-domain]  Cd Length: 548  Bit Score: 260.93  E-value: 3.53e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  20 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKW---------EPQFNHHEQSSEDIWAAcclVTKEVVQ--GIDAHRI 87
Cdd:PRK04123   4 YVIGLDFGTDSVRALLVDcATGEELATAVVEYPHWvkgryldlpPNQALQHPLDYIESLEA---AIPAVLKeaGVDPAAV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  88 RGLGFDAT-CSLVVLDKEFHPLPVNHEGDSSRN--VIMWLDHRAVSQVHRINETKHR-----VLQYVGGVMSVEMQAPKL 159
Cdd:PRK04123  81 VGIGVDFTgSTPAPVDADGTPLALLPEFAENPHamVKLWKDHTAQEEAEEINRLAHErgeadLSRYIGGIYSSEWFWAKI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 160 LWLKENLREIcWDKAGHFFDLPDFLSWKATGVTA-----RSLCSLVCKWTYSAEKG--WDDSFWKMI--GLEDLIDDnys 230
Cdd:PRK04123 161 LHVLREDPAV-YEAAASWVEACDWVVALLTGTTDpqdivRSRCAAGHKALWHESWGglPSADFFDALdpLLARGLRD--- 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 231 KIGNLVLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAgglGVIGADVRGHGLTcegqpvtsrlAVIcGTSSCHMG 310
Cdd:PRK04123 237 KLFTETWTAGEPAG-TLTAEWAQRLGLPEGVAVSVGAFDAHM---GAVGAGAEPGTLV----------KVM-GTSTCDIL 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 311 ISKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKL----IDHMVQghpafPELQAKATARCQSIYAYLNshldliKKA- 385
Cdd:PRK04123 302 LADKQRAVPGICGQVDGSIVPGLIGYEAGQSAVGDIfawfARLLVP-----PEYKDEAEARGKQLLELLT------EAAa 370
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 386 -QPV---GFLTVDlhvWpdFHGNRSPLADLTLKGMVTGLTLSQDLDDlaiLYLATVQAIAFGTRFIIETMEAAGHSLSTL 461
Cdd:PRK04123 371 kQPPgehGLVALD---W--FNGRRTPLADQRLKGVITGLTLGTDAPD---IYRALIEATAFGTRAIMECFEDQGVPVEEV 442
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755508662 462 FLCGGLS-KNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQIA 515
Cdd:PRK04123 443 IAAGGIArKNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDIPEA 497
ASKHA_NBD_FGGY_CvXK-like cd07805
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ...
20-511 1.22e-71

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: 236.65  E-value: 1.22e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDAT-C 96
Cdd:cd07805    1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEksGIDPSDIAAIAFSGQmQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  97 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINETKHRVLQY---VGGVMSVEMQAPKLLWLKENLREIcWDK 173
Cdd:cd07805   81 GVVPVDKDGNPL---------RNAIIWSDTRAAEEAEEIAGGLGGIEGYrlgGGNPPSGKDPLAKILWLKENEPEI-YAK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 174 AGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLE-DLIDDnyskignlvLLPGAALgIG-LTPE 250
Cdd:cd07805  151 THKFLDAKDYLNFRLTGRAATDPSTASTTGLMDLRKRrWSEELLRAAGIDpDKLPE---------LVPSTEV-VGeLTPE 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 251 AARELGLPSGIAVAASLIDAHAGGLGViGADVRGHgltcegqpvtsrlAVIC-GTSS---CHmgiSKDPVFVPGvwGPYY 326
Cdd:cd07805  221 AAAELGLPAGTPVVGGGGDAAAAALGA-GAVEEGD-------------AHIYlGTSGwvaAH---VPKPKTDPD--HGIF 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 327 S--AMVPGFWLNEGGQSVTGKLIDHMVqghpafpELQAKATARCQSIYAYLNshlDLIKKAQP----VGFLtvdlhvwPD 400
Cdd:cd07805  282 TlaSADPGRYLLAAEQETAGGALEWAR-------DNLGGDEDLGADDYELLD---ELAAEAPPgsngLLFL-------PW 344
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 401 FHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADI 480
Cdd:cd07805  345 LNGERSPVEDPNARGAFIGLSLEHTRADLA---RAVLEGVAFNLRWLLEALEKLTRKIDELRLVGGGARSDLWCQILADV 421
                        490       500       510
                 ....*....|....*....|....*....|..
gi 755508662 481 TGMPV-VLSQEVESVLVGAAILGACASGDFTS 511
Cdd:cd07805  422 LGRPVeVPENPQEAGALGAALLAAVGLGLLKS 453
ASKHA_NBD_FGGY_YgcE-like cd07779
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ...
20-516 7.33e-69

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: 227.79  E-value: 7.33e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDAT-C 96
Cdd:cd07779    1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAkaGVDPEDIAAIGLTSQrS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  97 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVsqvhrinetkhrvlqyvggvmsvemqapkllwlkenlreicwdkagH 176
Cdd:cd07779   81 TFVPVDEDGRPL---------RPAISWQDKRTA----------------------------------------------K 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 177 FFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEDliddnySKIGNLVLlPGAALGiGLTPEAAREL 255
Cdd:cd07779  106 FLTVQDYLLYRLTGEFVTDTTSASRTGLPDIRTRdWSDDLLDAFGIDR------DKLPELVP-PGTVIG-TLTKEAAEET 177
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 256 GLPSGIAVAASlidAHAGGLGVIGAdvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGFWL 335
Cdd:cd07779  178 GLPEGTPVVAG---GGDQQCAALGA-----GVLEPGT-----ASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPGKWV 244
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 336 NEGGQSVTGKLIDHMVQghpAFPELQAKATARCQSIYAYLNSHLDLIkkaqPVGFLtvDLHVWPDFHGNRSPLADLTLKG 415
Cdd:cd07779  245 LEGSINTGGSAVRWFRD---EFGQDEVAEKELGVSPYELLNEEAAKS----PPGSD--GLLFLPYLAGAGTPYWNPEARG 315
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 416 MVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVL 495
Cdd:cd07779  316 AFIGLTLSHTRAHL---ARAILEGIAFELRDNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATA 392
                        490       500
                 ....*....|....*....|.
gi 755508662 496 VGAAILGACASGDFTSVQIAV 516
Cdd:cd07779  393 LGAAILAAVGAGIYPDFEEAV 413
ASKHA_NBD_FGGY_EcXK-like cd07808
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ...
20-518 5.12e-68

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: 227.04  E-value: 5.12e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVV--QGIDAHRIRGLGFDA-TC 96
Cdd:cd07808    1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLakAGISPSDIAAIGLTGqMH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  97 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINET-KHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAG 175
Cdd:cd07808   81 GLVLLDKNGRPL---------RPAILWNDQRSAAECEELEARlGDEILIITGNPPLPGFTLPKLLWLKENEPEI-FARIR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 176 HFFdLP-DFLSWKATGVTAR-------SLCslvckwtYSAEKG-WDDSFWKMIGLEdliddnyskIGNL--VLLPGAALG 244
Cdd:cd07808  151 KIL-LPkDYLRYRLTGELATdpsdasgTLL-------FDVEKReWSEELLEALGLD---------PSILppIVESTEIVG 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 245 iGLTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQPV----TSrlAVICGTSSCHMGISKDPVF--- 317
Cdd:cd07808  214 -TLTPEAAEELGLPEGTPVVAGAGDNAAAALGA--------GVVEPGDALislgTS--GVVFAPTDKPVPDPKGRLHtfp 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 318 --VPGVWgpYYSAMVPGF-----WLNE--GGQSVTGKLIDHMVQGHPAfpelqakatarcqsiyaylnshldlikKAQPV 388
Cdd:cd07808  283 haVPGKW--YAMGVTLSAglslrWLRDlfGPDRESFDELDAEAAKVPP---------------------------GSEGL 333
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 389 GFLtvdlhvwPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLS 468
Cdd:cd07808  334 LFL-------PYLSGERTPYWDPNARGSFFGLSLSHTRAHLA---RAVLEGVAFSLRDSLEVLKELGIKVKEIRLIGGGA 403
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 755508662 469 KNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQIAVPR 518
Cdd:cd07808  404 KSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAA 453
ASKHA_NBD_FGGY cd00366
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ...
20-502 9.54e-68

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: 223.60  E-value: 9.54e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDAT-C 96
Cdd:cd00366    1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAkaGIDPSDIAAIGISGQmP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  97 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAvsqvhrinetkhrvlqyvggvmsvemqapkllwlkenlreicwdkagH 176
Cdd:cd00366   81 GVVLVDADGNPL---------RPAIIWLDRRA-----------------------------------------------K 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 177 FFDLPDFLSWKATGVTA--RSLCSLVCKWTYsAEKGWDDSFWKMIGLEDliddnySKIGNLVLlPGAALGiGLTPEAARE 254
Cdd:cd00366  105 FLQPNDYIVFRLTGEFAidYSNASGTGLYDI-KTGDWSEELLDALGIPR------EKLPPIVE-SGEVVG-RVTPEAAEE 175
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 255 LGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQPVtsrlaVICGTSSCHMGISKDPVFVPGVWGPYYSAmVPGFW 334
Cdd:cd00366  176 TGLPAGTPVVAGGGDTAAAALGA--------GVVEPGDAV-----DSTGTSSVLSVCTDEPVPPDPRLLNRCHV-VPGLW 241
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 335 LNEGGQSVTGKLIDHMvqghpafpelqAKATARCQSIYAYLNSHLDLIKKAQP----VGFLtvdlhvwPDFHGNRSPLAD 410
Cdd:cd00366  242 LLEGAINTGGASLRWF-----------RDEFGEEEDSDAEYEGLDELAAEVPPgsdgLIFL-------PYLSGERSPIWD 303
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 411 LTLKGMVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQE 490
Cdd:cd00366  304 PAARGVFFGLTLSHTRAHL---IRAVLEGVAYALRDNLEILEELGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEV 380
                        490
                 ....*....|..
gi 755508662 491 VESVLVGAAILG 502
Cdd:cd00366  381 AEGAALGAAILA 392
ASKHA_NBD_FGGY_SePSK_AtXK1-like cd07783
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ...
20-503 3.07e-67

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: 223.25  E-value: 3.07e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQGIDAHRIRGLGFDATC-SL 98
Cdd:cd07783    1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRPRRVVAIAVDGTSgTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  99 VVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFF 178
Cdd:cd07783   81 VLVDREGEPL---------RPAIMYNDARAVAEAEELAEAAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEV-LAKTAKFL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 179 DLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGL-EDLIddnyskigNLVLLPGAALGIgLTPEAARELG 256
Cdd:cd07783  151 HQADWLAGRLTGDRGVTDYNNALKLGYDPETGrWPSWLLALLGIpPDLL--------PRVVAPGTVIGT-LTAEAAEELG 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 257 LPSGIAVAASLIDAHAGGLGViGADVRGHGLTcegqpvtsrlavICGTSSCHMGISKDPVFVPGvwGPYYSAMVP-GFWL 335
Cdd:cd07783  222 LPAGTPVVAGTTDSIAAFLAS-GAVRPGDAVT------------SLGTTLVLKLLSDKRVPDPG--GGVYSHRHGdGYWL 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 336 NEGGQSVTGKLIDHMVQGHPaFPELQAKATARCQSiyaylnshldlikkaqpvgfltvDLHVWP-DFHGNRSPLADLTLK 414
Cdd:cd07783  287 VGGASNTGGAVLRWFFSDDE-LAELSAQADPPGPS-----------------------GLIYYPlPLRGERFPFWDPDAR 342
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 415 GMVTGLTlsqdlDDLAILYLATVQAIAFGTRFIIETMEAAGHS-LSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVES 493
Cdd:cd07783  343 GFLLPRP-----HDRAEFLRALLEGIAFIERLGYERLEELGAPpVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEA 417
                        490
                 ....*....|
gi 755508662 494 VLvGAAILGA 503
Cdd:cd07783  418 AL-GAALLAA 426
ASKHA_NBD_FGGY_FK cd07773
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ...
20-507 2.42e-64

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: 216.30  E-value: 2.42e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQGIDAHRIRGLGFdAT--CS 97
Cdd:cd07773    1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGPDPIAAISV-SSqgES 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  98 LVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINE--TKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAG 175
Cdd:cd07773   80 GVPVDRDGEPL---------GPAIVWFDPRGKEEAEELAEriGAEELYRITGLPPSPMYSLAKLLWLREHEPEI-FAKAA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 176 HFFDLPDFLSWKATGVTARSLcSLVCKWTY--SAEKGWDDSfwkmigLEDLIDDNYSKIGNLVlLPGAALGIgLTPEAAR 253
Cdd:cd07773  150 KWLSVADYIAYRLTGEPVTDY-SLASRTMLfdIRKRTWSEE------LLEAAGIDASLLPELV-PSGTVIGT-VTPEAAE 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 254 ELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGPYYS---AMV 330
Cdd:cd07773  221 ELGLPAGTPVVVGGHDHLCAALGA--------GVIEPGD-----VLDSTGTAEALLAVVDEPPLDEMLAEGGLSyghHVP 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 331 PGFWLNEGGQSvTGKLIDHMVQghpafpELQAKATARCQSIYAYLNShldlIKKAQPVGFLtvdlhvwPDFHGNRSPLAD 410
Cdd:cd07773  288 GGYYYLAGSLP-GGALLEWFRD------LFGGDESDLAAADELAEAA----PPGPTGLLFL-------PHLSGSGTPDFD 349
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 411 LTLKGMVTGLTLSQDLDDlaiLYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQE 490
Cdd:cd07773  350 PDARGAFLGLTLGTTRAD---LLRAILEGLAFELRLNLEALEKAGIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEV 426
                        490
                 ....*....|....*..
gi 755508662 491 VESVLVGAAILGACASG 507
Cdd:cd07773  427 PEATALGAALLAGVGAG 443
ASKHA_NBD_FGGY_EcLyxK-like cd07802
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ...
20-507 6.36e-62

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: 209.71  E-value: 6.36e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDAT-C 96
Cdd:cd07802    1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEksGVDPSDIAGVGVTGHgN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  97 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINE--TKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKA 174
Cdd:cd07802   81 GLYLVDKDGKPV---------RNAILSNDSRAADIVDRWEEdgTLEKVYPLTGQPLWPGQPVALLRWLKENEPER-YDRI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 175 GHFFDLPDFLSWKATGVtarslcsLVCKWT-YSA------EKGWDDSFWKMIGLEDLIDdnysKIGNLVllPGAALGIGL 247
Cdd:cd07802  151 RTVLFCKDWIRYRLTGE-------ISTDYTdAGSslldldTGEYDDELLDLLGIEELKD----KLPPLV--PSTEIAGRV 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 248 TPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGpYYS 327
Cdd:cd07802  218 TAEAAALTGLPEGTPVAAGAFDVVASALGA--------GAVDEGQ-----LCVILGTWSINEVVTDEPVVPDSVGS-NSL 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 328 AMVPGFWLNEGGQSVTGKLIDHMVQghpafpELQAKATARCQSIYAYLNshlDLIKKAQPVG----FLtvdlhvwPDFHG 403
Cdd:cd07802  284 HADPGLYLIVEASPTSASNLDWFLD------TLLGEEKEAGGSDYDELD---ELIAAVPPGSsgviFL-------PYLYG 347
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 404 NRsplADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEAAGHsLSTLFLCGGLSKNPLFVQMHADITGM 483
Cdd:cd07802  348 SG---ANPNARGGFFGLTAWHTRAHLL---RAVYEGIAFSHRDHLERLLVARK-PETIRLTGGGARSPVWAQIFADVLGL 420
                        490       500
                 ....*....|....*....|....
gi 755508662 484 PVVLSQEVESVLVGAAILGACASG 507
Cdd:cd07802  421 PVEVPDGEELGALGAAICAAVAAG 444
ASKHA_NBD_FGGY_RrXK-like cd07804
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ...
20-507 1.14e-61

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: 209.30  E-value: 1.14e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  20 YYVGIDVGTGSVRAALVDQRGLLLAFA--EQPIKKwePQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDA- 94
Cdd:cd07804    1 YLLGIDIGTTGTKGVLVDEDGKVLASAsiEHDLLT--PKPGWAEHDPEVWWGAVCEIIRELLAkaGISPKEIAAIGVSGl 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  95 TCSLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINET--KHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWD 172
Cdd:cd07804   79 VPALVPVDENGKPL---------RPAILYGDRRATEEIEWLNENigEDRIFEITGNPLDSQSVGPKLLWIKRNEPEV-FK 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 173 KAGHFFDLPDFLSWKATG--VTARSLCSLvckwtYS-----AEKGWDDSFWKMIGL-EDLIDDNYSkignlvllPGAALG 244
Cdd:cd07804  149 KTRKFLGAYDYIVYKLTGeyVIDYSSAGN-----EGglfdiRKRTWDEELLEALGIdPDLLPELVP--------STEIVG 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 245 iGLTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGP 324
Cdd:cd07804  216 -EVTKEAAEETGLAEGTPVVAGTVDAAASALSA--------GVVEPGD-----LLLMLGTAGDIGVVTDKLPTDPRLWLD 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 325 YYSamVPGFWLNEGGQSVTGKLIDHMVQGhpAFPELQAKATARCQSIYAYLNshldliKKAQPVGFLTVDLHVWPDFHGN 404
Cdd:cd07804  282 YHD--IPGTYVLNGGMATSGSLLRWFRDE--FAGEEVEAEKSGGDSAYDLLD------EEAEKIPPGSDGLIVLPYFMGE 351
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 405 RSPLADLTLKGMVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGMP 484
Cdd:cd07804  352 RTPIWDPDARGVIFGLTLSHTRAHL---YRALLEGVAYGLRHHLEVIREAGLPIKRLVAVGGGAKSPLWRQIVADVTGVP 428
                        490       500
                 ....*....|....*....|...
gi 755508662 485 VVLSQEVESVLVGAAILGACASG 507
Cdd:cd07804  429 QEYVKDTVGASLGDAFLAGVGVG 451
L-ribulokinase TIGR01234
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely ...
20-518 2.41e-60

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: 207.85  E-value: 2.41e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662   20 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKWE--------------PQFNHHEQSSEDIWAAcclVTKEVVQ--GI 82
Cdd:TIGR01234   2 YAIGVDFGTLSGRALAVDvATGEEIATAVEWYRHWVkgqflpktgaklpnDQALQHPADYIEVLEA---AIPTVLAelGV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662   83 DAHRIRGLGFDAT-CSLVVLDKEFHPLPVNHEGDSSRN--VIMWLDHRAVSQVHRINETKHR----VLQYVGGVMSVEMQ 155
Cdd:TIGR01234  79 DPADVVGIGVDFTaCTPAPIDSDGNPLCLLPEFAENPHayFKLWKHHAAQEEADRINRLAHApgevDLSRYGGIISSEWF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  156 APKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKGW-DDSFWKMI--GLEDLIDDNYSK- 231
Cdd:TIGR01234 159 WAKILQITEEDPAI-YQAADRWIELADWIVAQLSGDIRRGRCTAGYKALWHESWGYpSASFFDELnpILNRHLPDKLFTd 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  232 IGNLvllpGAALGiGLTPEAARELGLPSGIAVAASLIDAHaggLGVIGADVrghgltceGQPvtSRLAVICGTSSCHMGI 311
Cdd:TIGR01234 238 IWTA----GEPAG-TLTPEWAQRTGLPEGVVVAVGNFDAH---VGAVAAGI--------AQP--GALVKIMGTSTCHVLI 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  312 SKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQgHPAFPELQAKATARCQSiyayLNSHLDLIKKAQPV--- 388
Cdd:TIGR01234 300 GDKQRAVPGMCGVVDGGIVPGFIGYEAGQSAVGDIFAWFGK-VCVPPELKTEANASQKQ----LHEALSEAAAKQPSgeh 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  389 GFLTVDlhvWpdFHGNRSPLADLTLKGMVTGLTLSQDLDDlaiLYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLS 468
Cdd:TIGR01234 375 GLVALD---W--FNGNRSPLVDQRLKGVITGLTLATDAPL---LYRALIEATAFGTRMIMETFTDSGVPVEELMAAGGIA 446
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755508662  469 -KNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQIAVPR 518
Cdd:TIGR01234 447 rKNPVIMQIYADVTNRPLQIVASDQAPALGAAIFAAVAAGVYADIPSAQAK 497
FGGY_C pfam02782
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ...
298-505 1.70e-59

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: 195.24  E-value: 1.70e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  298 LAVICGTSSCHMGISKDPV-FVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAkaTARCQSIYAYLN 376
Cdd:pfam02782   1 LAISAGTSSFVLVETPEPVlSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELRD--AGNVESLAELAA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  377 SHLDLikkaqpvgfLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLddlAILYLATVQAIAFGTRFIIETMEA-AG 455
Cdd:pfam02782  79 LAAVA---------PAGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTL---AHLYRAILESLALQLRQILEALTKqEG 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 755508662  456 HSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACA 505
Cdd:pfam02782 147 HPIDTIHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
ASKHA_NBD_FGGY_GntK cd07770
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ...
20-526 5.27e-55

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: 192.39  E-value: 5.27e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQGIDAHRIRGLGFDATC-SL 98
Cdd:cd07770    1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGGEVDAIGFSSAMhSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  99 VVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRI--NETKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGH 176
Cdd:cd07770   81 LGVDEDGEPL---------TPVITWADTRAAEEAERLrkEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPEL-FAKAAK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 177 FFDLPDFLSWKATG--VTARSLCSlvckWT---YSAEKGWDDSFWKMIGLEDlidDNYSKignlvLLPGAALGIGLTPEA 251
Cdd:cd07770  151 FVSIKEYLLYRLTGelVTDYSTAS----GTgllNIHTLDWDEEALELLGIDE---EQLPE-----LVDPTEVLPGLKPEF 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 252 ARELGLPSGIAVAASLIDAHAGGLGViGADVRGhgltcegqpvtsRLAVICGTSschmG----ISKDPVFVP--GVWgPY 325
Cdd:cd07770  219 AERLGLLAGTPVVLGASDGALANLGS-GALDPG------------RAALTVGTS----GairvVSDRPVLDPpgRLW-CY 280
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 326 YSAmvPGFWL-----NEGGqSVTGKLIDHMVQGHPAFPELQAKATArcqsiyAYLNSHlDLIkkaqpvgFLtvdlhvwPD 400
Cdd:cd07770  281 RLD--ENRWLvggaiNNGG-NVLDWLRDTLLLSGDDYEELDKLAEA------VPPGSH-GLI-------FL-------PY 336
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 401 FHGNRSPLADLTLKGMVTGLTLSQDLDDLailYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADI 480
Cdd:cd07770  337 LAGERAPGWNPDARGAFFGLTLNHTRADI---LRAVLEGVAFNLKSIYEALEELAGPVKEIRASGGFLRSPLWLQILADV 413
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*.
gi 755508662 481 TGMPVVLSQEVESVLVGAAILGACASGDFTSVQIAVPREHGPLLHP 526
Cdd:cd07770  414 LGRPVLVPEEEEASALGAALLALEALGLISSLEADELVKIGKVVEP 459
ASKHA_NBD_FGGY_YoaC-like cd07798
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ...
20-507 1.60e-43

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: 160.47  E-value: 1.60e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHH--EQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLgfdAT 95
Cdd:cd07798    1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYPDakEFDPEELWEKICEAIREALKkaGISPEDISAV---SS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  96 CS----LVVLDKEFHPL---PvNHegdssrnvimwlDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAP-KLLWLKENLR 167
Cdd:cd07798   78 TSqregIVFLDKDGRELyagP-NI------------DARGVEEAAEIDDEFGEEIYTTTGHWPTELFPAaRLLWFKENRP 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 168 EIcWDKAGHFFDLPDFLSWKATGVtarslcsLVCKWTYSAEKG--------WDDSFWKMIGLEDLIddnyskignL--VL 237
Cdd:cd07798  145 EI-FERIATVLSISDWIGYRLTGE-------LVSEPSQASETQlfdikkreWSQELLEALGLPPEI---------LpeIV 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 238 LPGAALGIgLTPEAARELGLPSGIAVAASLIDAHAGGLGViGADVRGHgltcegqpvtsrLAVICGTSSCHMGISKDPVF 317
Cdd:cd07798  208 PSGTVLGT-VSEEAARELGLPEGTPVVVGGADTQCALLGS-GAIEPGD------------IGIVAGTTTPVQMVTDEPII 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 318 VP--GVW-GPYysaMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQakatarcqsiYAYLNSHLDLIKKAQP--VGFLT 392
Cdd:cd07798  274 DPerRLWtGCH---LVPGKWVLESNAGVTGLNYQWLKELLYGDPEDS----------YEVLEEEASEIPPGANgvLAFLG 340
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 393 VDLhvwpdFHGNRSPLADLTLKGMVTGLTLSQDLDDLAIlylATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNP 471
Cdd:cd07798  341 PQI-----FDARLSGLKNGGFLFPTPLSASELTRGDFAR---AILENIAFAIRANLEQLEEvSGREIPYIILCGGGSRSA 412
                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 755508662 472 LFVQMHADITGMPVVLSQEVESVLVGAAILGACASG 507
Cdd:cd07798  413 LLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
ASKHA_NBD_FGGY_BaXK-like cd07809
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ...
20-507 5.17e-42

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: 156.17  E-value: 5.17e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  20 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPikkWEPQFNHH---EQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFD 93
Cdd:cd07809    1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAP---HENILIDPgwaEQDPEDWWDALQAAFAQLLKdaGAELRDVAAIGIS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  94 ATC-SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINET-KHRVLQYVGGVMSVEMQAPKLLWLKENLREIcW 171
Cdd:cd07809   78 GQMhGLVALDADGKVL---------RPAKLWCDTRTAPEAEELTEAlGGKKCLLVGLNIPARFTASKLLWLKENEPEH-Y 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 172 DKAgHFFDLP-DFLSWKATG--VTARSLCSLVckwtysaekGWDDSF-----WKMIGLEDLIDDNYSKIGNlVLLPGAAL 243
Cdd:cd07809  148 ARI-AKILLPhDYLNWKLTGekVTGLGDASGT---------FPIDPRtrdydAELLAAIDPSRDLRDLLPE-VLPAGEVA 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 244 GiGLTPEAARELGLPSGIAVAASLIDAHAG--GLGVIGadvrghgltcEGQPVTSrlaviCGTSSCHMGISKDPVFVPgv 321
Cdd:cd07809  217 G-RLTPEGAEELGLPAGIPVAPGEGDNMTGalGTGVVN----------PGTVAVS-----LGTSGTAYGVSDKPVSDP-- 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 322 wgpyySAMVPGF--------WLNEG---GQSVTGKLIDHMVQGHPAFPELQAKATARCQSIYAYlnshldlikkaqpvgf 390
Cdd:cd07809  279 -----HGRVATFcdstggmlPLINTtncLTAWTELFRELLGVSYEELDELAAQAPPGAGGLLLL---------------- 337
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 391 ltvdlhvwPDFHGNRSP-LADLTlkGMVTGLTLSQdlDDLAILYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSK 469
Cdd:cd07809  338 --------PFLNGERTPnLPHGR--ASLVGLTLSN--FTRANLARAALEGATFGLRYGLDILRELGVEIDEIRLIGGGSK 405
                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 755508662 470 NPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASG 507
Cdd:cd07809  406 SPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
ASKHA_NBD_FGGY_BaEryA-like cd24121
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ...
20-507 3.41e-40

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: 151.24  E-value: 3.41e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQGID--AHRIRGLGFDAT-- 95
Cdd:cd24121    1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDvlPDRVAAIGVTGQgd 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  96 -CSLVvlDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINE--TKHRVLQYVGGVMSVEMQAPKLLWLKENLREICwD 172
Cdd:cd24121   81 gTWLV--DEDGRPV---------RDAILWLDGRAADIVERWQAdgIAEAVFEITGTGLFPGSQAAQLAWLKENEPERL-E 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 173 KAGHFFDLPDFLSWKATGVTA--RSLCSLVCkwtYSAEKG-WDDSFWKMIGLEDLIDdnyskignlvLLPGAALGIG--- 246
Cdd:cd24121  149 RARTALHCKDWLFYKLTGEIAtdPSDASLTF---LDFRTRqYDDEVLDLLGLEELRH----------LLPPIRPGTEvig 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 247 -LTPEAARELGLPSGIAVAASLIDAHAGGLGViGADVRGHGLTcegqpvtsrlavICGTSSCHMGISKDPVFvpgvwGPY 325
Cdd:cd24121  216 pLTPEAAAATGLPAGTPVVLGPFDVVATALGS-GAIEPGDACS------------ILGTTGVHEVVVDEPDL-----EPE 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 326 YSAM-----VPGFWLNEGGqSVTGKL-IDHMVQghPAFPELQAKATARCQSIYAYLNSHLdlikKAQPVGFLTVDLHVWP 399
Cdd:cd24121  278 GVGYticlgVPGRWLRAMA-NMAGTPnLDWFLR--ELGEVLKEGAEPAGSDLFQDLEELA----ASSPPGAEGVLYHPYL 350
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 400 DFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRfiiETMEAAGHSLSTLFLCGGLSKNPLFVQMHAD 479
Cdd:cd24121  351 SPAGERAPFVNPNARAQFTGLSLEHTRADLL---RAVYEGVALAMR---DCYEHMGEDPGELRLSGGGARSDTWCQILAD 424
                        490       500
                 ....*....|....*....|....*...
gi 755508662 480 ITGMPVVLSQEVESVLVGAAILGACASG 507
Cdd:cd24121  425 ALGVPVRVPAGEEFGARGAAMNAAVALG 452
FGGY_N pfam00370
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ...
20-276 6.15e-26

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


Pssm-ID: 395295 [Multi-domain]  Cd Length: 245  Bit Score: 106.27  E-value: 6.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662   20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDATC- 96
Cdd:pfam00370   1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSqlGISLKQIKGIGISNQGh 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662   97 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINE--TKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKA 174
Cdd:pfam00370  81 GTVLLDKNDKPL---------YNAILWKDRRTAEIVENLKEegNNQKLYEITGLPIWPGFTLSKLRWIKENEPEV-FEKI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  175 GHFFDLPDFLSWKATGVtarslcsLVCKWTYSAEKG--------WDDSFWKMIGLEdliDDNYSKignlvLLPGAALGIG 246
Cdd:pfam00370 151 HKFLTIHDYLRWRLTGV-------FVTDHTNASRSMmfnihkldWDPELLAALGIP---RDHLPP-----LVESSEIYGE 215
                         250       260       270
                  ....*....|....*....|....*....|
gi 755508662  247 LTPEAARELGLPSGIAVAASLIDAHAGGLG 276
Cdd:pfam00370 216 LNPELAAMWGLDEGVPVVGGGGDQQAAAFG 245
ASKHA_NBD_FGGY_AI-2K cd07775
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ...
20-516 7.01e-24

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: 104.72  E-value: 7.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  20 YYVGIDVGTGSVRAALVDQRGLLLAFAEqpiKKWEPQFNHHEQSSEDI-----WAACCLVTKEVVQ--GIDAHRIRGLgf 92
Cdd:cd07775    1 YLLALDAGTGSGRAVIFDLEGNQIAVAQ---REWRHKEVPDVPGSMDFdteknWKLICECIREALKkaGIAPKSIAAI-- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  93 dATCS----LVVLDKEFHPLPVNHegdssrNVimwlDHRAVSQVHRINETKH---RVLQYVGGVMSVEMQAPKLLWLKEN 165
Cdd:cd07775   76 -STTSmregIVLYDNEGEEIWACA------NV----DARAAEEVSELKELYNtleEEVYRISGQTFALGAIPRLLWLKNN 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 166 LREIcWDKAGHFFDLPDFLSWKATGVTAR--SLCSLVCKWTySAEKGWDDSFWKMIGLEDLIDDNyskignlVLLPGAAL 243
Cdd:cd07775  145 RPEI-YRKAAKITMLSDWIAYKLSGELAVepSNGSTTGLFD-LKTRDWDPEILEMAGLKADILPP-------VVESGTVI 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 244 GIgLTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrlAVICGTSSCHMGI-SKDPVFVPGVW 322
Cdd:cd07775  216 GK-VTKEAAEETGLKEGTPVVVGGGDVQLGCLGL--------GVVRPGQ------TAVLGGSFWQQEVnTAAPVTDPAMN 280
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 323 GPYYSAMVPGFWLNEGGQSVTGKLIDHMVQghpAF-PELQAKATARCQSIYAYLNshldliKKAQ--PVGF-----LTVD 394
Cdd:cd07775  281 IRVNCHVIPDMWQAEGISFFPGLVMRWFRD---AFcAEEKEIAERLGIDAYDLLE------EMAKdvPPGSygimpIFSD 351
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 395 L-------HVWPDFhgnrspladltlkgmvTGLTLSQDLDDLAILYLATVQAIAFGTRFIIETMEAA-GHSLSTLFLCGG 466
Cdd:cd07775  352 VmnyknwrHAAPSF----------------LNLDIDPEKCNKATFFRAIMENAAIVSAGNLERIAEFsGIFPDSLVFAGG 415
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|
gi 755508662 467 LSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQIAV 516
Cdd:cd07775  416 ASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGAGIYSSLEEAV 465
PRK15027 PRK15027
xylulokinase; Provisional
21-483 3.13e-19

xylulokinase; Provisional


Pssm-ID: 184987 [Multi-domain]  Cd Length: 484  Bit Score: 90.41  E-value: 3.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  21 YVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAAC-----CLVTKEVVQGIDAHRIRGLGFDAT 95
Cdd:PRK15027   2 YIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATdramkALGDQHSLQDVKALGIAGQMHGAT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  96 cslvVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREICWDKAG 175
Cdd:PRK15027  82 ----LLDAQQRVL---------RPAILWNDGRCAQECALLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDK 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 176 HFfdLP-DFLSWKATGVTARSLCSLV-CKWTYSAEKGWDDSfwkMIGLEDLIDDNYSkignlVLLPGAALGIGLTPEAAR 253
Cdd:PRK15027 149 VL--LPkDYLRLRMTGEFASDMSDAAgTMWLDVAKRDWSDV---MLQACHLSRDQMP-----ALYEGSEITGALLPEVAK 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 254 ELGLPSgIAVAASLIDAHAGGLGVigadvrghGLTCEGQPVTSrlaviCGTSSCHMGISKDPVFVPGVWGPYYSAMVPGF 333
Cdd:PRK15027 219 AWGMAT-VPVVAGGGDNAAGAVGV--------GMVDANQAMLS-----LGTSGVYFAVSEGFLSKPESAVHSFCHALPQR 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 334 WlneggqsvtgKLIDHMVQGHPAFpELQAKATARcQSIYAYLNSHLDLIKKAQPVGFLtvdlhvwPDFHGNRSPLADLTL 413
Cdd:PRK15027 285 W----------HLMSVMLSAASCL-DWAAKLTGL-SNVPALIAAAQQADESAEPVWFL-------PYLSGERTPHNNPQA 345
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 414 KGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGGLSKNPLFVQMHADITGM 483
Cdd:PRK15027 346 KGVFFGLTHQHGPNELA---RAVLEGVGYALADGMDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQ 412
ASKHA_NBD_FGGY_GK cd07769
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ...
20-511 1.06e-18

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: 89.06  E-value: 1.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFdaTC- 96
Cdd:cd07769    1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAkaGISASDIAAIGI--TNq 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  97 --SLVVLDKefhplpvnHEGDSSRNVIMWLDHRAVSQVHRINETKH--RVLQYVGGVMSVEMQAPKLLWLKEN---LREI 169
Cdd:cd07769   79 reTTVVWDK--------KTGKPLYNAIVWQDRRTADICEELKAKGLeeRIREKTGLPLDPYFSATKIKWILDNvpgARER 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 170 CwdKAGHF-FDLPD-FLSWKATG----VT-----ARSLcsLvckwtYSAEKG-WDDSfwkmigLEDLIDdnyskignlvl 237
Cdd:cd07769  151 A--ERGELlFGTIDtWLIWKLTGgkvhVTdvtnaSRTM--L-----FNIHTLeWDDE------LLELFG----------- 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 238 LPGAALgigltPE---------AARELGLPSGIAVAASLIDAHAgglgvigADVrGHGLTCEGQpvtsrlaVIC--GT-S 305
Cdd:cd07769  205 IPRSML-----PEvrpssevfgYTDPEGLGAGIPIAGILGDQQA-------ALF-GQGCFEPGM-------AKNtyGTgC 264
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 306 SCHMGISKDPVFV-PGV-----WG----PYYSAmvpgfwlnEGGQSVTGKLIDHMVQGhpafpelqakatarcqsiyayl 375
Cdd:cd07769  265 FLLMNTGEKPVPSkNGLlttiaWQiggkVTYAL--------EGSIFIAGAAIQWLRDN---------------------- 314
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 376 nshLDLIKKAQPVGFL--TVD----LHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIE 449
Cdd:cd07769  315 ---LGLIEDAAETEELarSVEdnggVYFVPAFSGLGAPYWDPDARGAIVGLTRGTTKAHIV---RAALESIAYQTRDVLE 388
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755508662 450 TMEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTS 511
Cdd:cd07769  389 AMEKdSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAAYLAGLAVGFWKD 451
GlpK COG0554
Glycerol kinase [Energy production and conversion];
18-513 5.53e-18

Glycerol kinase [Energy production and conversion];


Pssm-ID: 440320 [Multi-domain]  Cd Length: 496  Bit Score: 86.66  E-value: 5.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  18 SRYYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFD-- 93
Cdd:COG0554    2 KKYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAkaGISAEDIAAIGITnq 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  94 -ATCslVVLDKEF-HPLpvnHegdssrNVIMWLDHRAVSQVHRINETKH--RVLQYVGGVMSVEMQAPKLLWLKEN---L 166
Cdd:COG0554   82 rETT--VVWDRKTgKPL---Y------NAIVWQDRRTADICEELKADGLedLIREKTGLVLDPYFSATKIKWILDNvpgA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 167 REicwdKA--GH-FFDLPD-FLSWKATG----VT-----ARSLCslvckwtYSAEKG-WDDSFWKMIGLedliddnyski 232
Cdd:COG0554  151 RE----RAeaGElLFGTIDsWLIWKLTGgkvhVTdvtnaSRTML-------FNIHTLdWDDELLELFGI----------- 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 233 gnlvllPGAALgigltPE---------AARELGLPSGIAVAASLIDAHAgglgvigADVrGHGLTCEG------------ 291
Cdd:COG0554  209 ------PRSML-----PEvrpssevfgETDPDLFGAEIPIAGIAGDQQA-------ALF-GQACFEPGmakntygtgcfl 269
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 292 ------QPVTSR---LAVICgtsschmgiskdpvfvpgvWG----PYYsAMvpgfwlnEGGQSVTGKLIDhmvqghpafp 358
Cdd:COG0554  270 lmntgdEPVRSKnglLTTIA-------------------WGlggkVTY-AL-------EGSIFVAGAAVQ---------- 312
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 359 elqakatarcqsiyaYLNSHLDLIKKAQPVGFL--TVD----LHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAil 432
Cdd:COG0554  313 ---------------WLRDGLGLIDSAAESEALarSVEdnggVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIA-- 375
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 433 yLATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTS 511
Cdd:COG0554  376 -RAALESIAYQTRDVLDAMEAdSGIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGFWKS 454

                 ..
gi 755508662 512 VQ 513
Cdd:COG0554  455 LE 456
ASKHA_NBD_FGGY_GK5-like cd07793
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ...
20-512 3.65e-16

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: 81.07  E-value: 3.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFdAT-- 95
Cdd:cd07793    1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKnaGLTPEDIAAIGI-STqr 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  96 CSLVVLDKE----FHplpvnhegdssrNVIMWLDHRAVSQVHRINE-TKHRVLQYVGGVM-----------------SVE 153
Cdd:cd07793   80 NTFLTWDKKtgkpLH------------NFITWQDLRAAELCESWNRsLLLKALRGGSKFLhfltrnkrflaasvlkfSTA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 154 MQAPKLLWLKENLREICWDKAGH---FFDLPDFLSWKATG----VTARSLCSLVckwtysaekgwddsfwkmiGLEDLID 226
Cdd:cd07793  148 HVSIRLLWILQNNPELKEAAEKGellFGTIDTWLLWKLTGgkvhATDYSNASAT-------------------GLFDPFT 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 227 DNYSK-IGNLVLLPGAALgigltPEaarelglpsgiavaaslIDAHAGGLGVIGADVRGHGLtcegqPVTSrlavICGTS 305
Cdd:cd07793  209 LEWSPiLLSLFGIPSSIL-----PE-----------------VKDTSGDFGSTDPSIFGAEI-----PITA----VVADQ 257
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 306 SCHMgiskdpvFVPGVWGPYYSAMVPG---FW-LNEGGQ---SVTG--KLIDHMVQGHPAF-PELQAKATARC----QSI 371
Cdd:cd07793  258 QAAL-------FGECCFDKGDVKITMGtgtFIdINTGSKphaSVKGlyPLVGWKIGGEITYlAEGNASDTGTVidwaKSI 330
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 372 yAYLNSHLDLIKKAQPVGfLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAIlylATVQAIAFGTRFIIETM 451
Cdd:cd07793  331 -GLFDDPSETEDIAESVE-DTNGVYFVPAFSGLQAPYNDPTACAGFIGLTPSTTKAHLVR---AILESIAFRVKQLLETM 405
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755508662 452 EA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSV 512
Cdd:cd07793  406 EKeTSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSK 467
PRK10331 PRK10331
L-fuculokinase; Provisional
25-515 9.46e-15

L-fuculokinase; Provisional


Pssm-ID: 182383 [Multi-domain]  Cd Length: 470  Bit Score: 76.61  E-value: 9.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  25 DVGTGSVRAALVDQRGLLLAFAEQP----IKKWEPQFnhHEQSSEDIW---AACClvtKEVVQGIDAHRIRGL-----GF 92
Cdd:PRK10331   8 DCGATNVRAIAVDRQGKIVARASTPnasdIAAENSDW--HQWSLDAILqrfADCC---RQINSELTECHIRGItvttfGV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  93 DATcslvvldkefhplPVNHEGDSSRNVIMWLDHRAVSQVHRI-NETKHRVLQYVGGVMSVEMQAP-KLLWLKENLREIc 170
Cdd:PRK10331  83 DGA-------------LVDKQGNLLYPIISWKCPRTAAVMENIeRYISAQQLQQISGVGAFSFNTLyKLVWLKENHPQL- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 171 WDKAGHFFDLPDFLSWKATGV--TARSLCSlVCKWTYSAEKGWDDSFWKMIGL-EDL---IDDNYSKIGNlvllpgaalg 244
Cdd:PRK10331 149 LEQAHAWLFISSLINHRLTGEftTDITMAG-TSQMLDIQQRDFSPEILQATGLsRRLfprLVEAGEQIGT---------- 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 245 igLTPEAARELGLPSGIAVAASlidAHAGGLGVIGAdvrGHGLtceGQPV-----------------TSRLAVICGtSSC 307
Cdd:PRK10331 218 --LQPSAAALLGLPVGIPVISA---GHDTQFALFGS---GAGQ---NQPVlssgtweilmvrsaqvdTSLLSQYAG-STC 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 308 HMGiSKDPVFVPGVWgpyysamvpgfWLNEGGQSVTGKLIdhmvqghpaFPELQAKATarcqsiyaylnshldLIKKAQP 387
Cdd:PRK10331 286 ELD-SQSGLYNPGMQ-----------WLASGVLEWVRKLF---------WTAETPYQT---------------MIEEARA 329
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 388 VGFLTVDLHVWPDFHGNRspladltlKGMVTGLTLSQDLDDlaiLYLATVQAIAFGTRFIIETMEAAGH-SLSTLFLCGG 466
Cdd:PRK10331 330 IPPGADGVKMQCDLLACQ--------NAGWQGVTLNTTRGH---FYRAALEGLTAQLKRNLQVLEKIGHfKASELLLVGG 398
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 755508662 467 LSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQIA 515
Cdd:PRK10331 399 GSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQA 447
ASKHA_NBD_FGGY_GK1-3-like cd07792
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ...
21-514 1.35e-14

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: 76.02  E-value: 1.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  21 YVG-IDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAAC--CL---VTKEVVQGIDAHRIRGLGFda 94
Cdd:cd07792    2 LVGaIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVyeCIeeaVEKLKALGISPSDIKAIGI-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  95 TC---SLVVLDKEfhplpvnhEGDSSRNVIMWLDHRAVSQVHR----INETKHRVLQYVGGVMSVEMQAPKLLWLKENLR 167
Cdd:cd07792   80 TNqreTTVVWDKS--------TGKPLYNAIVWLDTRTSDTVEElsakTPGGKDHFRKKTGLPISTYFSAVKLRWLLDNVP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 168 EI---------------CWdkaghffdlpdfLSWKATG----------VTARSLCSLV----CKWtysaekgwDDSFWKM 218
Cdd:cd07792  152 EVkkavddgrllfgtvdSW------------LIWNLTGgknggvhvtdVTNASRTMLMnlrtLQW--------DPELCEF 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 219 IGLedliddnyskignlvllPGAALgigltPE---AARELGLPS-----GIAVAASLIDAHAgglgvigADVrGHGLTCE 290
Cdd:cd07792  212 FGI-----------------PMSIL-----PEirsSSEVYGKIAsgplaGVPISGCLGDQQA-------ALV-GQGCFKP 261
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 291 GQ------------------PVTSRlaviCG--TSSCH-MGISKDPVFvpgvwgpyysAMvpgfwlnEGGQSVTGKLIDh 349
Cdd:cd07792  262 GEakntygtgcfllyntgeePVFSK----HGllTTVAYkLGPDAPPVY----------AL-------EGSIAIAGAAVQ- 319
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 350 mvqghpafpelqakatarcqsiyaYLNSHLDLIKKAQPVGFL--TVD----LHVWPDFHGNRSPLADLTLKGMVTGLTLS 423
Cdd:cd07792  320 ------------------------WLRDNLGIISSASEVETLaaSVPdtggVYFVPAFSGLFAPYWRPDARGTIVGLTQF 375
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 424 QDLDDLAilyLATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILG 502
Cdd:cd07792  376 TTKAHIA---RAALEAVCFQTREILDAMNKdSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIAA 452
                        570
                 ....*....|..
gi 755508662 503 ACASGDFTSVQI 514
Cdd:cd07792  453 GLAVGVWKSLDE 464
ASKHA_NBD_FGGY_SHK cd07777
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ...
20-501 1.94e-14

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: 75.34  E-value: 1.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  20 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKWEPQ--FNHHEQSSEDIWAAcclvTKEVVQGIDAH---RIRGLGFd 93
Cdd:cd07777    1 NVLGIDIGTTSIKAALLDlESGRILESVSRPTPAPISSddPGRSEQDPEKILEA----VRNLIDELPREylsDVTGIGI- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  94 aTC---SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINETKHRVLQYVGGV-MSVEMQAPKLLWLKENLREI 169
Cdd:cd07777   76 -TGqmhGIVLWDEDGNPV---------SPLITWQDQRCSEEFLGGLSTYGEELLPKSGMrLKPGYGLATLFWLLRNGPLP 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 170 cwDKAGHFFDLPDFLSWKATGvTARSLCSLVCK--WTY--SAEKGWDDSFWKMIGLEDLIddnYSKIGNlvllPGAALGi 245
Cdd:cd07777  146 --SKADRAGTIGDYIVARLTG-LPKPVMHPTNAasWGLfdLETGTWNKDLLEALGLPVIL---LPEIVP----SGEIVG- 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 246 GLTPEaarelgLPSGIAVAASLIDAHAGglgVIGADVRGHGltcegqpvtsRLAVICGTSScHMGISKDPVFVPGVWG-- 323
Cdd:cd07777  215 TLSSA------LPKGIPVYVALGDNQAS---VLGSGLNEEN----------DAVLNIGTGA-QLSFLTPKFELSGSVEir 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 324 PYYSamvpGFWLNeggqSVT----GKLIDHMVQghpAFPELQAKATARC--QSIYAYLNShLDLIKKAQPvgfLTVDlhv 397
Cdd:cd07777  275 PFFD----GRYLL----VAAslpgGRALAVLVD---FLREWLRELGGSLsdDEIWEKLDE-LAESEESSD---LSVD--- 336
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 398 wPDFHGNRSplaDLTLKGMVTGLTLsqdlDDLAI--LYLATVQAIAFGTRFIIETMEAAGHSLSTLFLCGG-LSKNPLFV 474
Cdd:cd07777  337 -PTFFGERH---DPEGRGSITNIGE----SNFTLgnLFRALCRGIAENLHEMLPRLDLDLSGIERIVGSGGaLRKNPVLR 408
                        490       500
                 ....*....|....*....|....*..
gi 755508662 475 QMHADITGMPVVLSQEVESVLVGAAIL 501
Cdd:cd07777  409 RIIEKRFGLPVVLSEGSEEAAVGAALL 435
PTZ00294 PTZ00294
glycerol kinase-like protein; Provisional
21-530 5.01e-14

glycerol kinase-like protein; Provisional


Pssm-ID: 240348 [Multi-domain]  Cd Length: 504  Bit Score: 74.63  E-value: 5.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  21 YVG-IDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQGIdahRIRGLGFDATC--- 96
Cdd:PTZ00294   3 YIGsIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKL---REKGPSFKIKAigi 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  97 -----SLVVLDKefhplpvnHEGDSSRNVIMWLDHRAVSQVHRINET--KHRVLQYVGG-VMSVEMQAPKLLWLKENLRE 168
Cdd:PTZ00294  80 tnqreTVVAWDK--------VTGKPLYNAIVWLDTRTYDIVNELTKKygGSNFFQKITGlPISTYFSAFKIRWMLENVPA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 169 IcwDKAGH-----FFDLPDFLSWKATG-------VTARSLCSLVCKWTYSaekgWDDSFWKMIGL--EDL--IDDNYSKI 232
Cdd:PTZ00294 152 V--KDAVKegtllFGTIDTWLIWNLTGgkshvtdVTNASRTFLMNIKTLK----WDEELLNKFGIpkETLpeIKSSSENF 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 233 GNLVLLPGAALgigltpeaarelglpSGIAVAASLIDAHAGGLGvigadvrgHGLTCEGQPVTSRlavicGTSsCH--MG 310
Cdd:PTZ00294 226 GTISGEAVPLL---------------EGVPITGCIGDQQAALIG--------HGCFEKGDAKNTY-----GTG-CFllMN 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 311 ISKDPVFVP-GVWGpyysamVPGFWLNEGGQSVtgklidHMVQGhpafpelqakATARCQSIYAYLNSHLDLIKKAQPVG 389
Cdd:PTZ00294 277 TGTEIVFSKhGLLT------TVCYQLGPNGPTV------YALEG----------SIAVAGAGVEWLRDNMGLISHPSEIE 334
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 390 FL------TVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETME-AAGHSLSTLF 462
Cdd:PTZ00294 335 KLarsvkdTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIV---RAALEAIALQTNDVIESMEkDAGIELNSLR 411
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 463 LCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQI--AVPREHGPLLHPCLSA 530
Cdd:PTZ00294 412 VDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLEEvkKLIRRSNSTFSPQMSA 481
FGGY_EcGK_like cd07786
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ...
20-512 5.77e-14

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: 74.06  E-value: 5.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  20 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFD---A 94
Cdd:cd07786    1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAkaGIRASDIAAIGITnqrE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  95 TCslVVLDKEfhplpvnhEGDSSRNVIMWLDHRAVSQVHRINETKH--RVLQYVGGVMSVEMQAPKLLWLKEN---LREI 169
Cdd:cd07786   81 TT--VVWDRE--------TGKPVYNAIVWQDRRTADICEELKAEGHeeMIREKTGLVLDPYFSATKIRWILDNvpgARER 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 170 cwDKAGH-FFDLPD-FLSWKATG----VT-----ARSLcslvckwTYSAEKG-WDDsfwkmiGLEDLIDdnyskignlvl 237
Cdd:cd07786  151 --AERGElAFGTIDsWLIWKLTGgkvhATdvtnaSRTM-------LFNIHTLeWDD------ELLELFG----------- 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 238 LPGAALgigltPE---------AARELGLPSGIAVAASLIDAHAgglgvigADVrGHGLTCEGQpvtsrlaVIC--GTSS 306
Cdd:cd07786  205 IPASML-----PEvkpssevfgYTDPDLLGAEIPIAGIAGDQQA-------ALF-GQACFEPGM-------AKNtyGTGC 264
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 307 -CHMGISKDPVFVPG------VWG----PYYsAMvpgfwlnEGGQSVTGKLIDhmvqghpafpelqakatarcqsiyaYL 375
Cdd:cd07786  265 fMLMNTGEKPVRSKNgllttiAWQlggkVTY-AL-------EGSIFIAGAAVQ-------------------------WL 311
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 376 NSHLDLIKKAQPVGFL--TVD----LHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIE 449
Cdd:cd07786  312 RDGLGLIESAAETEALarSVPdnggVYFVPAFTGLGAPYWDPDARGAIFGLTRGTTRAHIA---RAALESIAYQTRDLLE 388
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755508662 450 TMEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSV 512
Cdd:cd07786  389 AMEAdSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSL 452
PRK10939 PRK10939
autoinducer-2 (AI-2) kinase; Provisional
20-511 6.70e-14

autoinducer-2 (AI-2) kinase; Provisional


Pssm-ID: 182853 [Multi-domain]  Cd Length: 520  Bit Score: 74.27  E-value: 6.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  20 YYVGIDVGTGSVRAALVDQRGLLLAFAEqpiKKW----EPQF-NHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLgf 92
Cdd:PRK10939   4 YLMALDAGTGSIRAVIFDLNGNQIAVGQ---AEWrhlaVPDVpGSMEFDLEKNWQLACQCIRQALQkaGIPASDIAAV-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  93 dATCSL----VVLDKEFHPLpvnhegdssrnvimW----LDHRAVSQV----HRINETKHRVLQYVGGVMSVEmQAPKLL 160
Cdd:PRK10939  79 -SATSMregiVLYDRNGTEI--------------WacanVDARASREVselkELHNNFEEEVYRCSGQTLALG-ALPRLL 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 161 WLKENLREIcWDKAGHFFDLPDFLSWKATGVTA--------RSLCSLVckwtysaEKGWDDSFWKMIGledLIDDNYSKi 232
Cdd:PRK10939 143 WLAHHRPDI-YRQAHTITMISDWIAYMLSGELAvdpsnagtTGLLDLV-------TRDWDPALLEMAG---LRADILPP- 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 233 gnlVLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGT-------- 304
Cdd:PRK10939 211 ---VKETGTVLG-HVTAKAAAETGLRAGTPVVMGGGDVQLGCLGL--------GVVRPGQ-----TAVLGGTfwqqvvnl 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 305 ----SSCHMGISKDPvfvpgvwgpyysAMVPGFWLNEGGQSVTGkLIdhMVQGHPAF-PELQAKATARCQSIYAYLNshl 379
Cdd:PRK10939 274 papvTDPNMNIRINP------------HVIPGMVQAESISFFTG-LT--MRWFRDAFcAEEKLLAERLGIDAYSLLE--- 335
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 380 dliKKAQ--PVGFLTVdLHVWPD-------FHGNRSPLadltlkgmvtGLTLSQDLDDLAILYLATVQAIAFGTRFIIET 450
Cdd:PRK10939 336 ---EMASrvPVGSHGI-IPIFSDvmrfkswYHAAPSFI----------NLSIDPEKCNKATLFRALEENAAIVSACNLQQ 401
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755508662 451 MEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTS 511
Cdd:PRK10939 402 IAAfSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEATALGCAIAAGVGAGIYSS 463
glpK PRK00047
glycerol kinase GlpK;
396-507 2.04e-10

glycerol kinase GlpK;


Pssm-ID: 234594 [Multi-domain]  Cd Length: 498  Bit Score: 62.92  E-value: 2.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 396 HVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFV 474
Cdd:PRK00047 344 YVVPAFTGLGAPYWDSDARGAIFGLTRGTTKEHII---RATLESIAYQTRDVLDAMQAdSGIRLKELRVDGGAVANNFLM 420
                         90       100       110
                 ....*....|....*....|....*....|...
gi 755508662 475 QMHADITGMPVVLSQEVESVLVGAAILGACASG 507
Cdd:PRK00047 421 QFQADILGVPVERPVVAETTALGAAYLAGLAVG 453
PLN02295 PLN02295
glycerol kinase
21-514 3.96e-08

glycerol kinase


Pssm-ID: 215166 [Multi-domain]  Cd Length: 512  Bit Score: 55.86  E-value: 3.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  21 YVG-IDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAAcclVTKEVVQGIDAHRIRGLGFDATCSLV 99
Cdd:PLN02295   1 FVGaIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILES---VLTCIAKALEKAAAKGHNVDSGLKAI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 100 VL--DKEFHPLPVNHEGDSSRNVIMWLDHRAVSQVHRINETKH----RVLQYVGGVMSVEMQAPKLLWLKENLREICWD- 172
Cdd:PLN02295  78 GItnQRETTVAWSKSTGRPLYNAIVWMDSRTSSICRRLEKELSggrkHFVETCGLPISTYFSATKLLWLLENVDAVKEAv 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 173 KAGH--FFDLPDFLSWKATGVTARSL----CSLVCKWTYSAEKG--WDDSFWKMIGL--EDL--IDDNYSKIGnlvllpG 240
Cdd:PLN02295 158 KSGDalFGTIDSWLIWNLTGGASGGVhvtdVTNASRTMLMNLKTldWDKPTLEALGIpaEILpkIVSNSEVIG------T 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 241 AALGIGLtpeaarelglpSGIAVAASLIDAHAGGLGvigadvrghgltcegqpvtsrlavicgtSSCHMGISKDpVFVPG 320
Cdd:PLN02295 232 IAKGWPL-----------AGVPIAGCLGDQHAAMLG----------------------------QRCRPGEAKS-TYGTG 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 321 VWgpyysaMVpgfwLNEGGQSVTGKlidHMVQGHPAFpELQAKATARcqsiYA-------------YLNSHLDLIKKAQP 387
Cdd:PLN02295 272 CF------IL----LNTGEEVVPSK---HGLLTTVAY-KLGPDAPTN----YAlegsvaiagaavqWLRDNLGIIKSASE 333
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 388 VGFL--TVD----LHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAilyLATVQAIAFGTRFIIETM------EAAG 455
Cdd:PLN02295 334 IEALaaTVDdtggVYFVPAFSGLFAPRWRDDARGVCVGITRFTNKAHIA---RAVLESMCFQVKDVLDAMrkdageEKSH 410
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755508662 456 HSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSQEVESVLVGAAILGACASGDFTSVQI 514
Cdd:PLN02295 411 KGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTEEEI 469
ASKHA_NBD_FGGY_NaCK-like cd07772
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ...
24-501 7.16e-07

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: 51.49  E-value: 7.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662  24 IDVGTGSVRAALVDQRGLLLAFAEQPIK-KWEPQFNHHEqsSEDIWAACCLVTKEVVQGidaHRIRGLGFdaTC---SLV 99
Cdd:cd07772    5 FDIGKTNKKLLLFDENGEVLAERSTPNPeIEEDGYPCED--VEAIWEWLLDSLAELAKR---HRIDAINF--TThgaTFA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 100 VLDKEFHP-LPV---NHEGDSSrnvimwldhravsqvhrINEtkhrvlQY--------------VGGVMSVEMQapkLLW 161
Cdd:cd07772   78 LLDENGELaLPVydyEKPIPDE-----------------INE------AYyaergpfeetgsppLPGGLNLGKQ---LYW 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 162 LKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVC--------KWTYS---AEKGWDDSFWKMigledliddnys 230
Cdd:cd07772  132 LKREKPEL-FARAKTILPLPQYWAWRLTGKAASEITSLGChtdlwdfeKNEYSslvKKEGWDKLFPPL------------ 198
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 231 kignlvLLPGAALGIgLTPEAARELGLPSGIAVAASLIDAHAgglgvigadvrghgltcegqpvtSRLAvicgtsscHMG 310
Cdd:cd07772  199 ------RKAWEVLGP-LRPDLARRTGLPKDIPVGCGIHDSNA-----------------------ALLP--------YLA 240
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 311 ISKDPvFV---PGVWgpyYSAMVPGFWLNEGGQSVTGKLIDHM-VQGHPA----FP-----ELQAKataRCQSIYAYLNS 377
Cdd:cd07772  241 AGKEP-FTllsTGTW---CIAMNPGNDLPLTELDLARDCLYNLdVFGRPVktarFMggreyERLVE---RIAKSFPQLPS 313
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755508662 378 HLDLIKkaqpvgFLTVDLHVWPDFHGNRSPLADLTLKGMVTGLTLSQDLDDLAILYLATVQAIAfgtrfiietMEAAGHS 457
Cdd:cd07772  314 LADLAK------LLARGTFALPSFAPGGGPFPGSGGRGVLSAFPSAEEAYALAILYLALMTDYA---------LDLLGSG 378
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 755508662 458 LSTLFLCGGLSKNPLFVQMHADI-TGMPVVLSQEVESVLVGAAIL 501
Cdd:cd07772  379 VGRIIVEGGFAKNPVFLRLLAALrPDQPVYLSDDSEGTALGAALL 423
ASKHA_NBD_FGGY_RhaB-like cd07771
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ...
440-513 3.26e-06

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: 49.45  E-value: 3.26e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755508662 440 IAFGTRFIIETMEA-AGHSLSTLFLCGGLSKNPLFVQMHADITGMPVVLSqEVESVLVGAAILGACASGDFTSVQ 513
Cdd:cd07771  378 LALKYAKTIEELEElTGKRIDRIHIVGGGSRNALLCQLTADATGLPVIAG-PVEATAIGNLLVQLIALGEIKSLE 451
NagC COG1940
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ...
19-92 5.57e-03

Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];


Pssm-ID: 441543 [Multi-domain]  Cd Length: 306  Bit Score: 39.11  E-value: 5.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755508662  19 RYYVGIDVGTGSVRAALVDQRGLLLAFAEQPIkkwepqfnHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGF 92
Cdd:COG1940    5 GYVIGIDIGGTKIKAALVDLDGEVLARERIPT--------PAGAGPEAVLEAIAELIEELLAeaGISRGRILGIGI 72
 
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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