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Conserved domains on  [gi|446197531|ref|WP_000275386|]
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MULTISPECIES: xylulokinase [Enterobacteriaceae]

Protein Classification

xylulokinase( domain architecture ID 11487572)

xylulokinase catalyzes the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P) and ADP

CATH:  3.30.420.40
EC:  2.7.1.17
Gene Ontology:  GO:0005524|GO:0005998|GO:0004856
PubMed:  8800467|7781919
SCOP:  3000092

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PRK15027 PRK15027
xylulokinase; Provisional
1-484 0e+00

xylulokinase; Provisional


:

Pssm-ID: 184987 [Multi-domain]  Cd Length: 484  Bit Score: 1043.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   1 MYIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQDVKALGIAGQMHGA 80
Cdd:PRK15027   1 MYIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQDVKALGIAGQMHGA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  81 TLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRLRM 160
Cdd:PRK15027  81 TLLDAQQRVLRPAILWNDGRCAQECALLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRLRM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 161 TGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGMATVPVVAGGGDNAAGAVG 240
Cdd:PRK15027 161 TGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVAKAWGMATVPVVAGGGDNAAGAVG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 241 VGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWVAKLTGLCNVPALIAAAQQA 320
Cdd:PRK15027 241 VGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWAAKLTGLSNVPALIAAAQQA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 321 DESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGIKPQSVTLIGGGARSE 400
Cdd:PRK15027 321 DESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGIKPQSVTLIGGGARSE 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 401 YWRQMLADISGQQLDYRTGGDVGPALGAARLAQIAANPEKSLIELLPQLPLEQSHLPDAQRYAAYQPRRETFRRLYQQLL 480
Cdd:PRK15027 401 YWRQMLADISGQQLDYRTGGDVGPALGAARLAQIAANPEKSLIELLPQLPLEQSHLPDAQRYAAYQPRRETFRRLYQQLL 480

                 ....
gi 446197531 481 PLMA 484
Cdd:PRK15027 481 PLMA 484
 
Name Accession Description Interval E-value
PRK15027 PRK15027
xylulokinase; Provisional
1-484 0e+00

xylulokinase; Provisional


Pssm-ID: 184987 [Multi-domain]  Cd Length: 484  Bit Score: 1043.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   1 MYIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQDVKALGIAGQMHGA 80
Cdd:PRK15027   1 MYIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQDVKALGIAGQMHGA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  81 TLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRLRM 160
Cdd:PRK15027  81 TLLDAQQRVLRPAILWNDGRCAQECALLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRLRM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 161 TGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGMATVPVVAGGGDNAAGAVG 240
Cdd:PRK15027 161 TGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVAKAWGMATVPVVAGGGDNAAGAVG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 241 VGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWVAKLTGLCNVPALIAAAQQA 320
Cdd:PRK15027 241 VGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWAAKLTGLSNVPALIAAAQQA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 321 DESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGIKPQSVTLIGGGARSE 400
Cdd:PRK15027 321 DESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGIKPQSVTLIGGGARSE 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 401 YWRQMLADISGQQLDYRTGGDVGPALGAARLAQIAANPEKSLIELLPQLPLEQSHLPDAQRYAAYQPRRETFRRLYQQLL 480
Cdd:PRK15027 401 YWRQMLADISGQQLDYRTGGDVGPALGAARLAQIAANPEKSLIELLPQLPLEQSHLPDAQRYAAYQPRRETFRRLYQQLL 480

                 ....
gi 446197531 481 PLMA 484
Cdd:PRK15027 481 PLMA 484
XylB TIGR01312
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of ...
3-477 0e+00

D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of carbohydrate kinases. The member from Klebsiella pneumoniae, designated DalK (see , was annotated erroneously in GenBank as D-arabinitol kinase but is authentic D-xylulose kinase. D-xylulose kinase (XylB) generally is found with xylose isomerase (XylA) and acts in xylose utilization. [Energy metabolism, Sugars]


Pssm-ID: 273550 [Multi-domain]  Cd Length: 481  Bit Score: 693.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531    3 IGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSL--QDVKALGIAGQMHGA 80
Cdd:TIGR01312   1 LGIDLGTSGVKALLVDEQGEVIASGSAPHTVISPHPGWSEQDPEDWWDATEEAIKELLEQASEmgQDIKGIGISGQMHGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   81 TLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRV--ITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRL 158
Cdd:TIGR01312  81 VLLDANGEVLRPAILWNDTRTAQECEELEAELGDERVleITGNLALPGFTAPKLLWVRKHEPEVFARIAKVMLPKDYLRY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  159 RMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGM-ATVPVVAGGGDNAAG 237
Cdd:TIGR01312 161 RLTGEYVTEYSDASGTGWFDVAKRAWSKELLDALDLPESQLPELIESSEKAGTVRPEVAARLGLsAGVPVAAGGGDNAAG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  238 AVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWVAKLTGLCNVPALIAAA 317
Cdd:TIGR01312 241 AIGTGTVDPGDAMMSLGTSGVVYAVTDKPLPDPAGAVHGFCHALPGGWLPMGVTLSATSSLEWFRELFGKEDVEALNELA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  318 QQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVV-HACGIKPQSVTLIGGG 396
Cdd:TIGR01312 321 EQSPPGAEGVTFLPYLNGERTPHLDPQARGSFIGLTHNTTRADLTRAVLEGVTFALRDSLDILrEAGGIPIQSIRLIGGG 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  397 ARSEYWRQMLADISGQQLDYRTgGDVGPALGAARLAQIAANpEKSLIELLPQLPLEQSH--LPDAQRYAAYQPRRETFRR 474
Cdd:TIGR01312 401 AKSPAWRQMLADIFGTPVDVPE-GEEGPALGAAILAAWALG-EKDLAALCSEAVVKQTEsvLPIAENVEAYEELYERYKK 478

                  ...
gi 446197531  475 LYQ 477
Cdd:TIGR01312 479 LYQ 481
ASKHA_NBD_FGGY_EcXK-like cd07808
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ...
1-476 0e+00

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: 627.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   1 MYIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQH--SLQDVKALGIAGQMH 78
Cdd:cd07808    1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAgiSPSDIAAIGLTGQMH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  79 GATLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRV-ITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLR 157
Cdd:cd07808   81 GLVLLDKNGRPLRPAILWNDQRSAAECEELEARLGDEILiITGNPPLPGFTLPKLLWLKENEPEIFARIRKILLPKDYLR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 158 LRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGMAT-VPVVAGGGDNAA 236
Cdd:cd07808  161 YRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEAAEELGLPEgTPVVAGAGDNAA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 237 GAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWVAKLTGLCNVP--ALI 314
Cdd:cd07808  241 AALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLHTFPHAVPGKWYAMGVTLSAGLSLRWLRDLFGPDRESfdELD 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 315 AAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGIKPQSVTLIG 394
Cdd:cd07808  321 AEAAKVPPGSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVLKELGIKVKEIRLIG 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 395 GGARSEYWRQMLADISGQQLDYRTGGDvGPALGAARLAQIAANPEKSLIELLPQL-PLEQSHLPDAQRYAAYQPRRETFR 473
Cdd:cd07808  401 GGAKSPLWRQILADVLGVPVVVPAEEE-GSAYGAALLAAVGAGVFDDLEEAAAACiKIEKTIEPDPERHEAYDELYARYR 479

                 ...
gi 446197531 474 RLY 476
Cdd:cd07808  480 ELY 482
XylB COG1070
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ...
1-484 0e+00

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: 602.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   1 MYIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQH--SLQDVKALGIAGQMH 78
Cdd:COG1070    2 YVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAgvDPEEIAAIGVSGQMH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  79 GATLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRV--ITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYL 156
Cdd:COG1070   82 GLVLLDADGEPLRPAILWNDTRAAAEAAELREELGEEALyeITGNPLHPGFTAPKLLWLKENEPEIFARIAKVLLPKDYL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 157 RLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGM-ATVPVVAGGGDNA 235
Cdd:COG1070  162 RYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEAAAETGLpAGTPVVAGAGDNA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 236 AGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWVAKLTG---LCNVPA 312
Cdd:COG1070  242 AAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFCHAVPGRWLPMGATNNGGSALRWFRDLFAdgeLDDYEE 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 313 LIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGIKPQSVTL 392
Cdd:COG1070  322 LNALAAEVPPGADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEALEEAGVKIDRIRA 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 393 IGGGARSEYWRQMLADISGQQLdYRTGGDVGPALGAARLAQIAANPEKSLIELLPQL-PLEQSHLPDAQRYAAYQPRRET 471
Cdd:COG1070  402 TGGGARSPLWRQILADVLGRPV-EVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMvRVGETIEPDPENVAAYDELYER 480
                        490
                 ....*....|...
gi 446197531 472 FRRLYQQLLPLMA 484
Cdd:COG1070  481 YRELYPALKPLFE 493
FGGY_N pfam00370
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ...
1-227 3.74e-108

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: 321.21  E-value: 3.74e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531    1 MYIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQH--SLQDVKALGIAGQMH 78
Cdd:pfam00370   1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLgiSLKQIKGIGISNQGH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   79 GATLLDAQQRVLRPAILWNDGRCAQECTLLEA--RVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYL 156
Cdd:pfam00370  81 GTVLLDKNDKPLYNAILWKDRRTAEIVENLKEegNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHKFLTIHDYL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446197531  157 RLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGM-ATVPV 227
Cdd:pfam00370 161 RWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMWGLdEGVPV 232
 
Name Accession Description Interval E-value
PRK15027 PRK15027
xylulokinase; Provisional
1-484 0e+00

xylulokinase; Provisional


Pssm-ID: 184987 [Multi-domain]  Cd Length: 484  Bit Score: 1043.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   1 MYIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQDVKALGIAGQMHGA 80
Cdd:PRK15027   1 MYIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQDVKALGIAGQMHGA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  81 TLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRLRM 160
Cdd:PRK15027  81 TLLDAQQRVLRPAILWNDGRCAQECALLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRLRM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 161 TGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGMATVPVVAGGGDNAAGAVG 240
Cdd:PRK15027 161 TGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVAKAWGMATVPVVAGGGDNAAGAVG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 241 VGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWVAKLTGLCNVPALIAAAQQA 320
Cdd:PRK15027 241 VGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWAAKLTGLSNVPALIAAAQQA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 321 DESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGIKPQSVTLIGGGARSE 400
Cdd:PRK15027 321 DESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGIKPQSVTLIGGGARSE 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 401 YWRQMLADISGQQLDYRTGGDVGPALGAARLAQIAANPEKSLIELLPQLPLEQSHLPDAQRYAAYQPRRETFRRLYQQLL 480
Cdd:PRK15027 401 YWRQMLADISGQQLDYRTGGDVGPALGAARLAQIAANPEKSLIELLPQLPLEQSHLPDAQRYAAYQPRRETFRRLYQQLL 480

                 ....
gi 446197531 481 PLMA 484
Cdd:PRK15027 481 PLMA 484
XylB TIGR01312
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of ...
3-477 0e+00

D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of carbohydrate kinases. The member from Klebsiella pneumoniae, designated DalK (see , was annotated erroneously in GenBank as D-arabinitol kinase but is authentic D-xylulose kinase. D-xylulose kinase (XylB) generally is found with xylose isomerase (XylA) and acts in xylose utilization. [Energy metabolism, Sugars]


Pssm-ID: 273550 [Multi-domain]  Cd Length: 481  Bit Score: 693.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531    3 IGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSL--QDVKALGIAGQMHGA 80
Cdd:TIGR01312   1 LGIDLGTSGVKALLVDEQGEVIASGSAPHTVISPHPGWSEQDPEDWWDATEEAIKELLEQASEmgQDIKGIGISGQMHGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   81 TLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRV--ITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRL 158
Cdd:TIGR01312  81 VLLDANGEVLRPAILWNDTRTAQECEELEAELGDERVleITGNLALPGFTAPKLLWVRKHEPEVFARIAKVMLPKDYLRY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  159 RMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGM-ATVPVVAGGGDNAAG 237
Cdd:TIGR01312 161 RLTGEYVTEYSDASGTGWFDVAKRAWSKELLDALDLPESQLPELIESSEKAGTVRPEVAARLGLsAGVPVAAGGGDNAAG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  238 AVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWVAKLTGLCNVPALIAAA 317
Cdd:TIGR01312 241 AIGTGTVDPGDAMMSLGTSGVVYAVTDKPLPDPAGAVHGFCHALPGGWLPMGVTLSATSSLEWFRELFGKEDVEALNELA 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  318 QQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVV-HACGIKPQSVTLIGGG 396
Cdd:TIGR01312 321 EQSPPGAEGVTFLPYLNGERTPHLDPQARGSFIGLTHNTTRADLTRAVLEGVTFALRDSLDILrEAGGIPIQSIRLIGGG 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  397 ARSEYWRQMLADISGQQLDYRTgGDVGPALGAARLAQIAANpEKSLIELLPQLPLEQSH--LPDAQRYAAYQPRRETFRR 474
Cdd:TIGR01312 401 AKSPAWRQMLADIFGTPVDVPE-GEEGPALGAAILAAWALG-EKDLAALCSEAVVKQTEsvLPIAENVEAYEELYERYKK 478

                  ...
gi 446197531  475 LYQ 477
Cdd:TIGR01312 479 LYQ 481
ASKHA_NBD_FGGY_EcXK-like cd07808
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ...
1-476 0e+00

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: 627.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   1 MYIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQH--SLQDVKALGIAGQMH 78
Cdd:cd07808    1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAgiSPSDIAAIGLTGQMH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  79 GATLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRV-ITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLR 157
Cdd:cd07808   81 GLVLLDKNGRPLRPAILWNDQRSAAECEELEARLGDEILiITGNPPLPGFTLPKLLWLKENEPEIFARIRKILLPKDYLR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 158 LRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGMAT-VPVVAGGGDNAA 236
Cdd:cd07808  161 YRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEAAEELGLPEgTPVVAGAGDNAA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 237 GAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWVAKLTGLCNVP--ALI 314
Cdd:cd07808  241 AALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLHTFPHAVPGKWYAMGVTLSAGLSLRWLRDLFGPDRESfdELD 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 315 AAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGIKPQSVTLIG 394
Cdd:cd07808  321 AEAAKVPPGSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVLKELGIKVKEIRLIG 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 395 GGARSEYWRQMLADISGQQLDYRTGGDvGPALGAARLAQIAANPEKSLIELLPQL-PLEQSHLPDAQRYAAYQPRRETFR 473
Cdd:cd07808  401 GGAKSPLWRQILADVLGVPVVVPAEEE-GSAYGAALLAAVGAGVFDDLEEAAAACiKIEKTIEPDPERHEAYDELYARYR 479

                 ...
gi 446197531 474 RLY 476
Cdd:cd07808  480 ELY 482
XylB COG1070
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ...
1-484 0e+00

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: 602.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   1 MYIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQH--SLQDVKALGIAGQMH 78
Cdd:COG1070    2 YVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAgvDPEEIAAIGVSGQMH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  79 GATLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRV--ITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYL 156
Cdd:COG1070   82 GLVLLDADGEPLRPAILWNDTRAAAEAAELREELGEEALyeITGNPLHPGFTAPKLLWLKENEPEIFARIAKVLLPKDYL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 157 RLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGM-ATVPVVAGGGDNA 235
Cdd:COG1070  162 RYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEAAAETGLpAGTPVVAGAGDNA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 236 AGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWVAKLTG---LCNVPA 312
Cdd:COG1070  242 AAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFCHAVPGRWLPMGATNNGGSALRWFRDLFAdgeLDDYEE 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 313 LIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGIKPQSVTL 392
Cdd:COG1070  322 LNALAAEVPPGADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEALEEAGVKIDRIRA 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 393 IGGGARSEYWRQMLADISGQQLdYRTGGDVGPALGAARLAQIAANPEKSLIELLPQL-PLEQSHLPDAQRYAAYQPRRET 471
Cdd:COG1070  402 TGGGARSPLWRQILADVLGRPV-EVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMvRVGETIEPDPENVAAYDELYER 480
                        490
                 ....*....|...
gi 446197531 472 FRRLYQQLLPLMA 484
Cdd:COG1070  481 YRELYPALKPLFE 493
ASKHA_NBD_FGGY_CvXK-like cd07805
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ...
3-473 2.29e-137

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: 404.59  E-value: 2.29e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   3 IGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQ--DVKALGIAGQMHGA 80
Cdd:cd07805    3 LAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDpsDIAAIAFSGQMQGV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  81 TLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQS---RVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLR 157
Cdd:cd07805   83 VPVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLGGIegyRLGGGNPPSGKDPLAKILWLKENEPEIYAKTHKFLDAKDYLN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 158 LRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWG-MATVPVVagggdnaa 236
Cdd:cd07805  163 FRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPEAAAELGlPAGTPVV-------- 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 237 gavgVGMVDA------------NQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWVAKL 304
Cdd:cd07805  235 ----GGGGDAaaaalgagaveeGDAHIYLGTSGWVAAHVPKPKTDPDHGIFTLASADPGRYLLAAEQETAGGALEWARDN 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 305 tgLC-------NVPALI-AAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADG 376
Cdd:cd07805  311 --LGgdedlgaDDYELLdELAAEAPPGSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLRWL 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 377 MDVVHACGIKPQSVTLIGGGARSEYWRQMLADISG---QQLDYRTggDVGpALGAARLAQIAANPEKSLIELLPQLPLEQ 453
Cdd:cd07805  389 LEALEKLTRKIDELRLVGGGARSDLWCQILADVLGrpvEVPENPQ--EAG-ALGAALLAAVGLGLLKSFDEAKALVKVEK 465
                        490       500
                 ....*....|....*....|
gi 446197531 454 SHLPDAQRYAAYQPRRETFR 473
Cdd:cd07805  466 VFEPDPENRARYDRLYEVFK 485
ASKHA_NBD_FGGY cd00366
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ...
1-432 2.34e-131

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: 385.77  E-value: 2.34e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   1 MYIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQH--SLQDVKALGIAGQMH 78
Cdd:cd00366    1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAgiDPSDIAAIGISGQMP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  79 GATLLDAQQRVLRPAILWNDGRcaqectllearvpqsrvitgnlmmpgftapkllwvqrhepeifrqiDKVLLPKDYLRL 158
Cdd:cd00366   81 GVVLVDADGNPLRPAIIWLDRR----------------------------------------------AKFLQPNDYIVF 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 159 RMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWG-MATVPVVAGGGDNAAG 237
Cdd:cd00366  115 RLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAAEETGlPAGTPVVAGGGDTAAA 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 238 AVGVGMVDANQAMLSLGTSGVYFAVSEGFLSkPESAVHSFCHALPQRWHLMSVMLSAASCLDWVAKLTGLCNVPA----- 312
Cdd:cd00366  195 ALGAGVVEPGDAVDSTGTSSVLSVCTDEPVP-PDPRLLNRCHVVPGLWLLEGAINTGGASLRWFRDEFGEEEDSDaeyeg 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 313 LIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGIKPQSVTL 392
Cdd:cd00366  274 LDELAAEVPPGSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEILEELGVKIKEIRV 353
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 446197531 393 IGGGARSEYWRQMLADISGqqLDYRTGGDV-GPALGAARLA 432
Cdd:cd00366  354 TGGGAKSRLWNQIKADVLG--VPVVVPEVAeGAALGAAILA 392
ASKHA_NBD_FGGY_BaXK-like cd07809
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ...
1-437 2.83e-124

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: 369.57  E-value: 2.83e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   1 MYIGIDLGTSGVKVILLN-EQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQH--SLQDVKALGIAGQM 77
Cdd:cd07809    1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAgaELRDVAAIGISGQM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  78 HGATLLDAQQRVLRPAILWNDGRCAQECTLLEARV-PQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYL 156
Cdd:cd07809   81 HGLVALDADGKVLRPAKLWCDTRTAPEAEELTEALgGKKCLLVGLNIPARFTASKLLWLKENEPEHYARIAKILLPHDYL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 157 RLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSR---DQMPALYEGSEITGALLPEVAKAWGMAT-VPVVAGGG 232
Cdd:cd07809  161 NWKLTGEKVTGLGDASGTFPIDPRTRDYDAELLAAIDPSRdlrDLLPEVLPAGEVAGRLTPEGAEELGLPAgIPVAPGEG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 233 DNAAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHAlPQRW-HLMSVMLSAASCLDWVAKLTGlCNVP 311
Cdd:cd07809  241 DNMTGALGTGVVNPGTVAVSLGTSGTAYGVSDKPVSDPHGRVATFCDS-TGGMlPLINTTNCLTAWTELFRELLG-VSYE 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 312 ALIAAAQQADESAEPVWFLPYLSGERTPhNNPQAKGVFFGLTH-QHGPNELARAVLEGVGYALADGMDVVHACGIKPQSV 390
Cdd:cd07809  319 ELDELAAQAPPGAGGLLLLPFLNGERTP-NLPHGRASLVGLTLsNFTRANLARAALEGATFGLRYGLDILRELGVEIDEI 397
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 446197531 391 TLIGGGARSEYWRQMLADISGQQLD-YRTGGDVgpALGAARLAQIAAN 437
Cdd:cd07809  398 RLIGGGSKSPVWRQILADVFGVPVVvPETGEGG--ALGAALQAAWGAG 443
ASKHA_NBD_FGGY_RrXK-like cd07804
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ...
1-436 1.21e-117

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: 352.98  E-value: 1.21e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   1 MYIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQ--HSLQDVKALGIAGqMH 78
Cdd:cd07804    1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKagISPKEIAAIGVSG-LV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  79 GATL-LDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRV--ITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDY 155
Cdd:cd07804   80 PALVpVDENGKPLRPAILYGDRRATEEIEWLNENIGEDRIfeITGNPLDSQSVGPKLLWIKRNEPEVFKKTRKFLGAYDY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 156 LRLRMTGEFASDMSDAAGTMWL-DVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGMAT-VPVVAGGGD 233
Cdd:cd07804  160 IVYKLTGEYVIDYSSAGNEGGLfDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTKEAAEETGLAEgTPVVAGTVD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 234 NAAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSfcHALPQRWHLMSVMLSAASCLDW-----------VA 302
Cdd:cd07804  240 AAASALSAGVVEPGDLLLMLGTAGDIGVVTDKLPTDPRLWLDY--HDIPGTYVLNGGMATSGSLLRWfrdefageeveAE 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 303 KLTGLCNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHA 382
Cdd:cd07804  318 KSGGDSAYDLLDEEAEKIPPGSDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYRALLEGVAYGLRHHLEVIRE 397
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446197531 383 CGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRtGGDVGPALGAARLAQIAA 436
Cdd:cd07804  398 AGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYV-KDTVGASLGDAFLAGVGV 450
ASKHA_NBD_FGGY_FK cd07773
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ...
1-437 2.89e-117

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: 351.50  E-value: 2.89e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   1 MYIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQDVKALGIAGQMHGA 80
Cdd:cd07773    1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGPDPIAAISVSSQGESG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  81 TLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRV--ITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRL 158
Cdd:cd07773   81 VPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEELyrITGLPPSPMYSLAKLLWLREHEPEIFAKAAKWLSVADYIAY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 159 RMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGMAT-VPVvagggdnaag 237
Cdd:cd07773  161 RLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEELGLPAgTPV---------- 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 238 avgV-------------GMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVH--SFCHALPQRWHLMSVMLSAASCLDWVA 302
Cdd:cd07773  231 ---VvgghdhlcaalgaGVIEPGDVLDSTGTAEALLAVVDEPPLDEMLAEGglSYGHHVPGGYYYLAGSLPGGALLEWFR 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 303 KLTGLCNVP--ALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVV 380
Cdd:cd07773  308 DLFGGDESDlaAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEAL 387
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446197531 381 HACGIKPQSVTLIGGGARSEYWRQMLADISGQQLdYRTGGDVGPALGAARLAQIAAN 437
Cdd:cd07773  388 EKAGIPIDEIRAVGGGARSPLWLQLKADILGRPI-EVPEVPEATALGAALLAGVGAG 443
ASKHA_NBD_FGGY_GntK cd07770
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ...
1-476 2.54e-112

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: 340.30  E-value: 2.54e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   1 MYIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQDVKALGIAGQMHGA 80
Cdd:cd07770    1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGGEVDAIGFSSAMHSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  81 TLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRV--ITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRL 158
Cdd:cd07770   81 LGVDEDGEPLTPVITWADTRAAEEAERLRKEGDGSELyrRTGCPIHPMYPLAKLLWLKEERPELFAKAAKFVSIKEYLLY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 159 RMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWG-MATVPVVAGGGDNAAG 237
Cdd:cd07770  161 RLTGELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFAERLGlLAGTPVVLGASDGALA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 238 AVGVGMVDANQAMLSLGTSG-VYFAVSEGFLSKPESAvhsFCHALPQRWHLMSVMLS-AASCLDWVAKLTGLCNVP--AL 313
Cdd:cd07770  241 NLGSGALDPGRAALTVGTSGaIRVVSDRPVLDPPGRL---WCYRLDENRWLVGGAINnGGNVLDWLRDTLLLSGDDyeEL 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 314 IAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGIKPQSVTLI 393
Cdd:cd07770  318 DKLAEAVPPGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKSIYEALEELAGPVKEIRAS 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 394 GGGARSEYWRQMLADISGQQLDYRTGGDvGPALGAARLAQIAANPEKSLiELLPQLPLEQSHLPDAQRYAAYQPRRETFR 473
Cdd:cd07770  398 GGFLRSPLWLQILADVLGRPVLVPEEEE-ASALGAALLALEALGLISSL-EADELVKIGKVVEPDPENHAIYAELYERFK 475

                 ...
gi 446197531 474 RLY 476
Cdd:cd07770  476 KLY 478
FGGY_N pfam00370
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ...
1-227 3.74e-108

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: 321.21  E-value: 3.74e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531    1 MYIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQH--SLQDVKALGIAGQMH 78
Cdd:pfam00370   1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLgiSLKQIKGIGISNQGH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   79 GATLLDAQQRVLRPAILWNDGRCAQECTLLEA--RVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYL 156
Cdd:pfam00370  81 GTVLLDKNDKPLYNAILWKDRRTAEIVENLKEegNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHKFLTIHDYL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446197531  157 RLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGM-ATVPV 227
Cdd:pfam00370 161 RWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMWGLdEGVPV 232
ASKHA_NBD_FGGY_EcLyxK-like cd07802
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ...
2-436 8.76e-108

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: 327.20  E-value: 8.76e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   2 YIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSL--QDVKALGIAGQMHG 79
Cdd:cd07802    2 LLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVdpSDIAGVGVTGHGNG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  80 ATLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRV--ITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLR 157
Cdd:cd07802   82 LYLVDKDGKPVRNAILSNDSRAADIVDRWEEDGTLEKVypLTGQPLWPGQPVALLRWLKENEPERYDRIRTVLFCKDWIR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 158 LRMTGEFASDMSDaAGTMWLDVAKRDWSDVMLQACDLS--RDQMPALYEGSEITGALLPEVAKAWG-MATVPVVAGGGDN 234
Cdd:cd07802  162 YRLTGEISTDYTD-AGSSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVTAEAAALTGlPEGTPVAAGAFDV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 235 AAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSfCHALPQRWHLMSVMLSAASCLDWV-------AKLTGL 307
Cdd:cd07802  241 VASALGAGAVDEGQLCVILGTWSINEVVTDEPVVPDSVGSNS-LHADPGLYLIVEASPTSASNLDWFldtllgeEKEAGG 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 308 CNVPALIAAAQQADESAEPVWFLPYLSGERTphnNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGiKP 387
Cdd:cd07802  320 SDYDELDELIAAVPPGSSGVIFLPYLYGSGA---NPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHRDHLERLLVAR-KP 395
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 446197531 388 QSVTLIGGGARSEYWRQMLADISGQQLDYRTGGDVGpALGAARLAQIAA 436
Cdd:cd07802  396 ETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELG-ALGAAICAAVAA 443
ASKHA_NBD_FGGY_SePSK_AtXK1-like cd07783
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ...
1-436 4.76e-100

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: 306.84  E-value: 4.76e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   1 MYIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQDVKALGIAGQMHGA 80
Cdd:cd07783    1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRPRRVVAIAVDGTSGTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  81 TLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRLRM 160
Cdd:cd07783   81 VLVDREGEPLRPAIMYNDARAVAEAEELAEAAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAKFLHQADWLAGRL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 161 TG-EFASDMSDAAgTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGM-ATVPVvagggdnaaga 238
Cdd:cd07783  161 TGdRGVTDYNNAL-KLGYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAEAAEELGLpAGTPV----------- 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 239 vGVGMVDANQAML------------SLGTSGVYFAVSEGFLSKPESAVHsfCHALPQRWHLMSVMLSA-ASCLDWVAKLT 305
Cdd:cd07783  229 -VAGTTDSIAAFLasgavrpgdavtSLGTTLVLKLLSDKRVPDPGGGVY--SHRHGDGYWLVGGASNTgGAVLRWFFSDD 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 306 GLcnvPALIAAAqqADESAEPVWFLPY-LSGERTPHNNPQAKGVFfgLTHQHGPNELARAVLEGVGYALADGMDVV-HAC 383
Cdd:cd07783  306 EL---AELSAQA--DPPGPSGLIYYPLpLRGERFPFWDPDARGFL--LPRPHDRAEFLRALLEGIAFIERLGYERLeELG 378
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446197531 384 GIKPQSVTLIGGGARSEYWRQMLADISGQQLdyRTGGDVGPALGAARLAQIAA 436
Cdd:cd07783  379 APPVEEVRTAGGGARNDLWNQIRADVLGVPV--VIAEEEEAALGAALLAAAGL 429
ASKHA_NBD_FGGY_YgcE-like cd07779
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ...
1-465 2.89e-93

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: 289.42  E-value: 2.89e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   1 MYIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSL--QDVKALGIAGQmh 78
Cdd:cd07779    1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVdpEDIAAIGLTSQ-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  79 GAT--LLDAQQRVLRPAILWNDGRcaqectllearvpqsrvitgnlmmpgftapkllwvqrhepeifrqIDKVLLPKDYL 156
Cdd:cd07779   79 RSTfvPVDEDGRPLRPAISWQDKR---------------------------------------------TAKFLTVQDYL 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 157 RLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGMAT-VPVvagggdna 235
Cdd:cd07779  114 LYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEAAEETGLPEgTPV-------- 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 236 agavgV-------------GMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWVA 302
Cdd:cd07779  186 -----VagggdqqcaalgaGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPGKWVLEGSINTGGSAVRWFR 260
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 303 KL--TGLCNVPALIAAA-----QQADES---AEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYA 372
Cdd:cd07779  261 DEfgQDEVAEKELGVSPyellnEEAAKSppgSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFE 340
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 373 LADGMDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQL----DYRTGgdvgpALGAARLAQIAANPEKSLIELLPQ 448
Cdd:cd07779  341 LRDNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVerpeTSEAT-----ALGAAILAAVGAGIYPDFEEAVKA 415
                        490
                 ....*....|....*...
gi 446197531 449 L-PLEQSHLPDAQRYAAY 465
Cdd:cd07779  416 MvRVTDTFEPDPENVAIY 433
ASKHA_NBD_FGGY_BaEryA-like cd24121
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ...
1-436 9.17e-90

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: 281.05  E-value: 9.17e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   1 MYIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSL--QDVKALGIAGQMH 78
Cdd:cd24121    1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVlpDRVAAIGVTGQGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  79 GATLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRV--ITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYL 156
Cdd:cd24121   81 GTWLVDEDGRPVRDAILWLDGRAADIVERWQADGIAEAVfeITGTGLFPGSQAAQLAWLKENEPERLERARTALHCKDWL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 157 RLRMTGEFASDMSDAAGTmWLDVAKRDWSDVMLQACDLS--RDQMPALYEGSEITGALLPEVAKAWGM-ATVPVVAGGGD 233
Cdd:cd24121  161 FYKLTGEIATDPSDASLT-FLDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPEAAAATGLpAGTPVVLGPFD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 234 NAAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRW-HLMSVMlSAASCLDWVAKLTGL----- 307
Cdd:cd24121  240 VVATALGSGAIEPGDACSILGTTGVHEVVVDEPDLEPEGVGYTICLGVPGRWlRAMANM-AGTPNLDWFLRELGEvlkeg 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 308 -----CNVPALI-AAAQQADESAEPVWFLPYLS--GERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALadgMDV 379
Cdd:cd24121  319 aepagSDLFQDLeELAASSPPGAEGVLYHPYLSpaGERAPFVNPNARAQFTGLSLEHTRADLLRAVYEGVALAM---RDC 395
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446197531 380 VHACGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTGGDVGpALGAARLAQIAA 436
Cdd:cd24121  396 YEHMGEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFG-ARGAAMNAAVAL 451
ASKHA_NBD_FGGY_L-RBK cd07781
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ...
2-479 1.68e-58

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: 200.84  E-value: 1.68e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   2 YIGIDLGTSGVKVILLNEQ-GEVVASQTE--KLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQ--DVKALGIAGQ 76
Cdd:cd07781    2 VIGIDFGTQSVRAGLVDLAdGEELASAVVpyPTGYIPPRPGWAEQNPADYWEALEEAVRGALAEAGVDpeDVVGIGVDTT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  77 mhGATLL--DAQQRVLRPAILWNDGRCAQECTLLEARvpQSRVITGNLMMPGFT------APKLLWVQRHEPEIFRQIDK 148
Cdd:cd07781   82 --SSTVVpvDEDGNPLAPAILWMDHRAQEEAAEINET--AHPALEYYLAYYGGVyssewmWPKALWLKRNAPEVYDAAYT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 149 VLLPKDYLRLRMTGEFASDMSdAAGTMWL-DVAKRDWSDVMLQACDLS----RDQMPALYEGS-EITGALLPEVAKAWGM 222
Cdd:cd07781  158 IVEACDWINARLTGRWVRSRC-AAGHKWMyNEWGGGPPREFLAALDPGllklREKLPGEVVPVgEPAGTLTAEAAERLGL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 223 -ATVPVVagggdnaagavgVGMVDANQAMLSL------------GTSGVYFAVSEGFLSKP------ESAVHsfchalPQ 283
Cdd:cd07781  237 pAGIPVA------------QGGIDAHMGAIGAgvvepgtlalimGTSTCHLMVSPKPVDIPgicgpvPDAVV------PG 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 284 RWHLMSVMLSAASCLDWVAKLTGLCN-------VPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQH 356
Cdd:cd07781  299 LYGLEAGQSAVGDIFAWFVRLFVPPAeergdsiYALLSEEAAKLPPGESGLVALDWFNGNRTPLVDPRLRGAIVGLTLGT 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 357 GPNELARAVLEGVGYALADGMDVVHACGIKPQSVTLIGGGA-RSEYWRQMLADISGQQLdYRTGGDVGPALGAARLAQIA 435
Cdd:cd07781  379 TPAHIYRALLEATAFGTRAIIERFEEAGVPVNRVVACGGIAeKNPLWMQIYADVLGRPI-KVPKSDQAPALGAAILAAVA 457
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 446197531 436 ANPEKSLIELLPQL-PLEQSHLPDAQRYAAYQPRRETFRRLYQQL 479
Cdd:cd07781  458 AGVYADIEEAADAMvRVDRVYEPDPENHAVYEELYALYKELYDAL 502
ASKHA_NBD_FGGY_YoaC-like cd07798
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ...
2-437 2.67e-55

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: 190.90  E-value: 2.67e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   2 YIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRP--HPLWSEQDPEQWWQATDRAMKALGDQH--SLQDVKALGIAGQM 77
Cdd:cd07798    2 YLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDddYPDAKEFDPEELWEKICEAIREALKKAgiSPEDISAVSSTSQR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  78 HGATLLDAQQRVLR--PAIlwnDGRCAQECTLLEARVPQSRVITGNLMMPGFTAP-KLLWVQRHEPEIFRQIDKVLLPKD 154
Cdd:cd07798   82 EGIVFLDKDGRELYagPNI---DARGVEEAAEIDDEFGEEIYTTTGHWPTELFPAaRLLWFKENRPEIFERIATVLSISD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 155 YLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGMAT-VPVVAGGGD 233
Cdd:cd07798  159 WIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAARELGLPEgTPVVVGGAD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 234 NAAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWVAKLtgLCNVPA- 312
Cdd:cd07798  239 TQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWTGCHLVPGKWVLESNAGVTGLNYQWLKEL--LYGDPEd 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 313 ----LIAAAQQADESAEPVwfLPYLSGERTPHNNPQAK--GVFFGLTHQHGPNE---LARAVLEGVGYALADGMDVVHA- 382
Cdd:cd07798  317 syevLEEEASEIPPGANGV--LAFLGPQIFDARLSGLKngGFLFPTPLSASELTrgdFARAILENIAFAIRANLEQLEEv 394
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446197531 383 CGIKPQSVTLIGGGARSEYWRQMLADISGQQLdYRTGGDVGPALGAARLAQIAAN 437
Cdd:cd07798  395 SGREIPYIILCGGGSRSALLCQILADVLGKPV-LVPEGREASALGAAICAAVGAG 448
ASKHA_NBD_FGGY_GK5-like cd07793
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ...
2-445 1.04e-48

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: 174.67  E-value: 1.04e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   2 YI-GIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMK-ALGD-QHSLQDVKALGIAGQMH 78
Cdd:cd07793    1 YIlAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKeALKNaGLTPEDIAAIGISTQRN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  79 GATLLDAQQ-RVLRPAILWNDGRCAQEC----------------TLLEARVPQSRVITGNLM--MPGFTAPKLLWVQRHE 139
Cdd:cd07793   81 TFLTWDKKTgKPLHNFITWQDLRAAELCeswnrslllkalrggsKFLHFLTRNKRFLAASVLkfSTAHVSIRLLWILQNN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 140 PEI----------FRQIDKVLLpkdylrLRMTG--EFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSE 207
Cdd:cd07793  161 PELkeaaekgellFGTIDTWLL------WKLTGgkVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSG 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 208 ITGALLPEVakawGMATVPVvagggdnaagAVGVGmvDANQAM------------LSLGTsGVYFAVSEGflSKPesavH 275
Cdd:cd07793  235 DFGSTDPSI----FGAEIPI----------TAVVA--DQQAALfgeccfdkgdvkITMGT-GTFIDINTG--SKP----H 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 276 SFCHAL-PQ-RWHLMS--------VMLSAASCLDWvAKLTGLCNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQA 345
Cdd:cd07793  292 ASVKGLyPLvGWKIGGeitylaegNASDTGTVIDW-AKSIGLFDDPSETEDIAESVEDTNGVYFVPAFSGLQAPYNDPTA 370
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 346 KGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHA-CGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTGGDVGp 424
Cdd:cd07793  371 CAGFIGLTPSTTKAHLVRAILESIAFRVKQLLETMEKeTSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMS- 449
                        490       500
                 ....*....|....*....|.
gi 446197531 425 ALGAARLAQIAANPEKSLIEL 445
Cdd:cd07793  450 ALGAAFLAGLASGIWKSKEEL 470
ASKHA_NBD_FGGY_GK cd07769
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ...
2-445 2.43e-42

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: 156.86  E-value: 2.43e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   2 YIG-IDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQ--DVKALGIAGQMH 78
Cdd:cd07769    1 YILaIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISasDIAAIGITNQRE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  79 GATLLDAQ-QRVLRPAILWNDGRCAQECTLLEARVPQSRV--ITGNLMMPGFTAPKLLWVQRHEPEI----------FRQ 145
Cdd:cd07769   81 TTVVWDKKtGKPLYNAIVWQDRRTADICEELKAKGLEERIreKTGLPLDPYFSATKIKWILDNVPGAreraergellFGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 146 IDKVLLPKdylrlrMTG--EFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKawgmA 223
Cdd:cd07769  161 IDTWLIWK------LTGgkVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTDPEGLG----A 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 224 TVPVvagggdnaagavgVGMVDANQA-----------------------MLSLGTSGVYFavSEGFLS----KPESAVhs 276
Cdd:cd07769  231 GIPI-------------AGILGDQQAalfgqgcfepgmakntygtgcflLMNTGEKPVPS--KNGLLTtiawQIGGKV-- 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 277 fCHALPqrwhlmSVMLSAASCLDWVAKLTGLCNVPALIAA-AQQAdESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQ 355
Cdd:cd07769  294 -TYALE------GSIFIAGAAIQWLRDNLGLIEDAAETEElARSV-EDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRG 365
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 356 HGPNELARAVLEGVGYALADGMDVVHA-CGIKPQSVTLIGGGARSEYWRQMLADISGQQLdyrtggdVGP------ALGA 428
Cdd:cd07769  366 TTKAHIVRAALESIAYQTRDVLEAMEKdSGIKLKELRVDGGATANNFLMQFQADILGVPV-------VRPkvaettALGA 438
                        490
                 ....*....|....*..
gi 446197531 429 ARLAQIAANPEKSLIEL 445
Cdd:cd07769  439 AYLAGLAVGFWKDLDEL 455
ASKHA_NBD_FGGY_SHK cd07777
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ...
1-432 8.25e-41

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: 151.61  E-value: 8.25e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   1 MYIGIDLGTSGVKVILLN-EQGEVVASQTEKLTVSRPH--PLWSEQDPEQWWQATDRAMKALgDQHSLQDVKALGIAGQM 77
Cdd:cd07777    1 NVLGIDIGTTSIKAALLDlESGRILESVSRPTPAPISSddPGRSEQDPEKILEAVRNLIDEL-PREYLSDVTGIGITGQM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  78 HGATLLDAQQRVLRPAILWNDGRCAQECTL-LEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPeIFRQIDKVLLPKDYL 156
Cdd:cd07777   80 HGIVLWDEDGNPVSPLITWQDQRCSEEFLGgLSTYGEELLPKSGMRLKPGYGLATLFWLLRNGP-LPSKADRAGTIGDYI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 157 RLRMTG--EFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKawgmaTVPVvagggdn 234
Cdd:cd07777  159 VARLTGlpKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLSSALPK-----GIPV------- 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 235 aagavGVGMVDaNQAM-------------LSLGTSG-VYFAVSEGFLSkpeSAVHSFChaLPQRWHLmsvmLSAAS---- 296
Cdd:cd07777  227 -----YVALGD-NQASvlgsglneendavLNIGTGAqLSFLTPKFELS---GSVEIRP--FFDGRYL----LVAASlpgg 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 297 ----CL-----DWVAKLTGLCNVPA----LIAAAQQADESaePVWFLPYLSGERTphnNPQAKGVFFGLTHQH-GPNELA 362
Cdd:cd07777  292 ralaVLvdflrEWLRELGGSLSDDEiwekLDELAESEESS--DLSVDPTFFGERH---DPEGRGSITNIGESNfTLGNLF 366
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446197531 363 RAVLEGVGYALADGMDVVHACGIKPQSVTLIGGGAR-SEYWRQMLADISGQQLDYRTGGDvGPALGAARLA 432
Cdd:cd07777  367 RALCRGIAENLHEMLPRLDLDLSGIERIVGSGGALRkNPVLRRIIEKRFGLPVVLSEGSE-EAAVGAALLA 436
PTZ00294 PTZ00294
glycerol kinase-like protein; Provisional
2-445 7.11e-36

glycerol kinase-like protein; Provisional


Pssm-ID: 240348 [Multi-domain]  Cd Length: 504  Bit Score: 139.34  E-value: 7.11e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   2 YIG-IDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAM----KALGDQHSLQDVKALGIAGQ 76
Cdd:PTZ00294   3 YIGsIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMneaiKKLREKGPSFKIKAIGITNQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  77 MHGATLLDAQQ-RVLRPAILWNDGRCAQECTLLEARVPQS---RVITGNLMMPGFTAPKLLWVQRHEPEI---------- 142
Cdd:PTZ00294  83 RETVVAWDKVTgKPLYNAIVWLDTRTYDIVNELTKKYGGSnffQKITGLPISTYFSAFKIRWMLENVPAVkdavkegtll 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 143 FRQIDKVLLPKdylrLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEvaKAWGM 222
Cdd:PTZ00294 163 FGTIDTWLIWN----LTGGKSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTISGE--AVPLL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 223 ATVPVVAGGGDNAAGAVGVGMVDANQAMLSLGTsGVYFAVSEGflskpESAVHSFCHAL-----------PQRWHLMSVM 291
Cdd:PTZ00294 237 EGVPITGCIGDQQAALIGHGCFEKGDAKNTYGT-GCFLLMNTG-----TEIVFSKHGLLttvcyqlgpngPTVYALEGSI 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 292 LSAASCLDWvakltgLCNVPALIAAAQQADESAEP------VWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAV 365
Cdd:PTZ00294 311 AVAGAGVEW------LRDNMGLISHPSEIEKLARSvkdtggVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAA 384
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 366 LEGVGYALAdgmDVVHA----CGIKPQSVTLIGGGARSEYWRQMLADISGQQLdYRTGGDVGPALGAARLAQIAANPEKS 441
Cdd:PTZ00294 385 LEAIALQTN---DVIESmekdAGIELNSLRVDGGLTKNKLLMQFQADILGKDI-VVPEMAETTALGAALLAGLAVGVWKS 460

                 ....
gi 446197531 442 LIEL 445
Cdd:PTZ00294 461 LEEV 464
PRK10331 PRK10331
L-fuculokinase; Provisional
6-415 1.49e-34

L-fuculokinase; Provisional


Pssm-ID: 182383 [Multi-domain]  Cd Length: 470  Bit Score: 134.77  E-value: 1.49e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   6 DLGTSGVKVILLNEQGEVVASQTEKlTVSRP---HPLWSEQDPEQWWQATDRAMKALGDQHSLQDVKALGIAGQMHGATL 82
Cdd:PRK10331   8 DCGATNVRAIAVDRQGKIVARASTP-NASDIaaeNSDWHQWSLDAILQRFADCCRQINSELTECHIRGITVTTFGVDGAL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  83 LDAQQRVLRPAILWNDGRCAQECTLLEARVPQSR--VITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRLRM 160
Cdd:PRK10331  87 VDKQGNLLYPIISWKCPRTAAVMENIERYISAQQlqQISGVGAFSFNTLYKLVWLKENHPQLLEQAHAWLFISSLINHRL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 161 TGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGM-ATVPVVAGGGDNAAGAV 239
Cdd:PRK10331 167 TGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQPSAAALLGLpVGIPVISAGHDTQFALF 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 240 GVGmVDANQAMLSLGTSGVYFAVSEgflsKPESAVHSFCHALPQRWHLMS------VMLSAASCLDWVAKL--TGLCNVP 311
Cdd:PRK10331 247 GSG-AGQNQPVLSSGTWEILMVRSA----QVDTSLLSQYAGSTCELDSQSglynpgMQWLASGVLEWVRKLfwTAETPYQ 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 312 ALIAAAQQADESAEPVWFLPYLSGERTphnnpqakGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHA-CGIKPQSV 390
Cdd:PRK10331 322 TMIEEARAIPPGADGVKMQCDLLACQN--------AGWQGVTLNTTRGHFYRAALEGLTAQLKRNLQVLEKiGHFKASEL 393
                        410       420
                 ....*....|....*....|....*
gi 446197531 391 TLIGGGARSEYWRQMLADISGQQLD 415
Cdd:PRK10331 394 LLVGGGSRNALWNQIKANMLDIPIK 418
GlpK COG0554
Glycerol kinase [Energy production and conversion];
2-466 1.04e-33

Glycerol kinase [Energy production and conversion];


Pssm-ID: 440320 [Multi-domain]  Cd Length: 496  Bit Score: 132.88  E-value: 1.04e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   2 YIG-IDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMK-ALGDQH-SLQDVKALGIAGQMH 78
Cdd:COG0554    4 YILaIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIReALAKAGiSAEDIAAIGITNQRE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  79 GATLLDAQQ-RVLRPAILWNDGRCAQECTLLEARVPQSRV--ITGNLMMPGFTAPKLLWVQRHEPEIfRQ---------- 145
Cdd:COG0554   84 TTVVWDRKTgKPLYNAIVWQDRRTADICEELKADGLEDLIreKTGLVLDPYFSATKIKWILDNVPGA-REraeagellfg 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 146 -IDKVLLpkdYlrlRMTG--EFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGallpEVAKAWGM 222
Cdd:COG0554  163 tIDSWLI---W---KLTGgkVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFG----ETDPDLFG 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 223 ATVPVVagggdnaagavgvGM----------------------------VDAN---QAMLS----LGTSG------VYFA 261
Cdd:COG0554  233 AEIPIA-------------GIagdqqaalfgqacfepgmakntygtgcfLLMNtgdEPVRSknglLTTIAwglggkVTYA 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 262 VsEGFlskpesavhsfchalpqrwhlmsvMLSAASCLDWVAKLTGLCNVPALIAA-AQQADeSAEPVWFLPYLSGERTPH 340
Cdd:COG0554  300 L-EGS------------------------IFVAGAAVQWLRDGLGLIDSAAESEAlARSVE-DNGGVYFVPAFTGLGAPY 353
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 341 NNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHA-CGIKPQSVTLIGGGARSEYWRQMLADISGQQLDyRtg 419
Cdd:COG0554  354 WDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEAdSGIPLKELRVDGGASANDLLMQFQADILGVPVE-R-- 430
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446197531 420 gdvgP------ALGAARLAQIAANPEKSLIELLPQLPLEQSHLP---DAQRYAAYQ 466
Cdd:COG0554  431 ----PkvtettALGAAYLAGLAVGFWKSLEELAALWKVDRRFEPqmdEEERERLYA 482
FGGY_EcGK_like cd07786
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ...
2-466 1.80e-33

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: 132.23  E-value: 1.80e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   2 YI-GIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQ--DVKALGIAGQMH 78
Cdd:cd07786    1 YIlAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRasDIAAIGITNQRE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  79 GATLLDAQQ-RVLRPAILWNDGRCAQECTLL-----EARVpqsRVITGNLMMPGFTAPKLLWVQRHEPE----------I 142
Cdd:cd07786   81 TTVVWDRETgKPVYNAIVWQDRRTADICEELkaeghEEMI---REKTGLVLDPYFSATKIRWILDNVPGareraergelA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 143 FRQIDKvllpkdYLRLRMTG--EFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGallpEVAKAW 220
Cdd:cd07786  158 FGTIDS------WLIWKLTGgkVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFG----YTDPDL 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 221 GMATVPVVagggdnaagavgvGMVDANQAML-------------SLGTS-------GVYFAVSE-GFLS--------KPE 271
Cdd:cd07786  228 LGAEIPIA-------------GIAGDQQAALfgqacfepgmaknTYGTGcfmlmntGEKPVRSKnGLLTtiawqlggKVT 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 272 SAvhsfchalpqrwhLMSVMLSAASCLDWVAKLTGLCNVPALIAA-AQQADESaEPVWFLPYLSGERTPHNNPQAKGVFF 350
Cdd:cd07786  295 YA-------------LEGSIFIAGAAVQWLRDGLGLIESAAETEAlARSVPDN-GGVYFVPAFTGLGAPYWDPDARGAIF 360
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 351 GLTHQHGPNELARAVLEGVGYALAdgmDVVHA----CGIKPQSVTLIGGGARSEYWRQMLADISGQQLdyrtggdVGP-- 424
Cdd:cd07786  361 GLTRGTTRAHIARAALESIAYQTR---DLLEAmeadSGIPLKELRVDGGASANDFLMQFQADILGVPV-------ERPkv 430
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 446197531 425 ----ALGAARLAQIAANPEKSLIELLPQLPLEQS---HLPDAQRYAAYQ 466
Cdd:cd07786  431 tettALGAAYLAGLAVGLWKSLDELAKLWQVDRRfepSMSEEEREALYA 479
ASKHA_NBD_FGGY_AI-2K cd07775
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ...
2-472 4.17e-33

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: 131.30  E-value: 4.17e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   2 YIGIDLGTSGVKVILLNEQGEVVA-SQTEKLTVSRP-HPLWSEQDPEQWWQATDRAMK-ALGD-QHSLQDVKALGIAGQM 77
Cdd:cd07775    2 LLALDAGTGSGRAVIFDLEGNQIAvAQREWRHKEVPdVPGSMDFDTEKNWKLICECIReALKKaGIAPKSIAAISTTSMR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  78 HGATLLDAQQRVLrpailWN----DGRCAQECTLLEARVPQSR----VITGNLMMPGfTAPKLLWVQRHEPEIFRQIDKV 149
Cdd:cd07775   82 EGIVLYDNEGEEI-----WAcanvDARAAEEVSELKELYNTLEeevyRISGQTFALG-AIPRLLWLKNNRPEIYRKAAKI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 150 LLPKDYLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGMAT-VPVV 228
Cdd:cd07775  156 TMLSDWIAYKLSGELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKEAAEETGLKEgTPVV 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 229 AGGGDNAAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWVAKltGLC 308
Cdd:cd07775  236 VGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPAMNIRVNCHVIPDMWQAEGISFFPGLVMRWFRD--AFC 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 309 NVPALIAAAQQAD------ESAEPV-----WFLPYLSGERTPHNNPQAKGVFFGLT---HQHGPNELARAVLEGVGYALA 374
Cdd:cd07775  314 AEEKEIAERLGIDaydlleEMAKDVppgsyGIMPIFSDVMNYKNWRHAAPSFLNLDidpEKCNKATFFRAIMENAAIVSA 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 375 DGMDVVHAC-GIKPQSVTLIGGGARSEYWRQMLADISGQQLdyrTGGDV--GPALGAARLAQIAANPEKSLIELLPQL-P 450
Cdd:cd07775  394 GNLERIAEFsGIFPDSLVFAGGASKGKLWCQILADVLGLPV---KVPVVkeATALGAAIAAGVGAGIYSSLEEAVESLvK 470
                        490       500
                 ....*....|....*....|..
gi 446197531 451 LEQSHLPDAQRYAAYQPRRETF 472
Cdd:cd07775  471 WEREYLPNPENHEVYQDLYEKW 492
ASKHA_NBD_FGGY_GK1-3-like cd07792
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ...
2-445 9.38e-31

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: 124.56  E-value: 9.38e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   2 YIG-IDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAM-------KALGdqHSLQDVKALGI 73
Cdd:cd07792    2 LVGaIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIeeaveklKALG--ISPSDIKAIGI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  74 AGQMHGATLLDAQQRV-LRPAILWNDGRCAQECTLLEARVPQS----RVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDK 148
Cdd:cd07792   80 TNQRETTVVWDKSTGKpLYNAIVWLDTRTSDTVEELSAKTPGGkdhfRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 149 vllpKD--------YLRLRMTGE-----FASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGallpE 215
Cdd:cd07792  160 ----GRllfgtvdsWLIWNLTGGknggvHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYG----K 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 216 VAKAWgMATVPVVagggdnaagavgvGMV-------------DANQAMLSLGTsGVYFAVSEGflskpESAVHSFCHAL- 281
Cdd:cd07792  232 IASGP-LAGVPIS-------------GCLgdqqaalvgqgcfKPGEAKNTYGT-GCFLLYNTG-----EEPVFSKHGLLt 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 282 ----------PQRWHLM-SVMLsAASCLDWVAKLTGLCNVPALIAA-AQQADESAEpVWFLPYLSGERTPHNNPQAKGVF 349
Cdd:cd07792  292 tvayklgpdaPPVYALEgSIAI-AGAAVQWLRDNLGIISSASEVETlAASVPDTGG-VYFVPAFSGLFAPYWRPDARGTI 369
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 350 FGLTH----QHgpneLARAVLEGVGYALADGMDVVHA-CGIKPQSVTLIGGGARSEYWRQMLADISGQQLdyrtggdVGP 424
Cdd:cd07792  370 VGLTQfttkAH----IARAALEAVCFQTREILDAMNKdSGIPLTSLRVDGGMTKNNLLMQIQADILGIPV-------ERP 438
                        490       500
                 ....*....|....*....|....*..
gi 446197531 425 ------ALGAARLAQIAANPEKSLIEL 445
Cdd:cd07792  439 smvettALGAAIAAGLAVGVWKSLDEL 465
FGGY_C pfam02782
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ...
249-436 1.76e-30

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: 117.04  E-value: 1.76e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  249 AMLSLGTSGVYFAVSEgflsKPESAVHSFCH-----ALPQRWHLMSVMLSAASCLDWVAKLTGL-------CNVP---AL 313
Cdd:pfam02782   1 LAISAGTSSFVLVETP----EPVLSVHGVWGpytneMLPGYWGLEGGQSAAGSLLAWLLQFHGLreelrdaGNVEslaEL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  314 IAAAQQADesAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHAC-GIKPQSVTL 392
Cdd:pfam02782  77 AALAAVAP--AGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQeGHPIDTIHV 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 446197531  393 IGGGARSEYWRQMLADISGQQLdYRTGGDVGPALGAARLAQIAA 436
Cdd:pfam02782 155 SGGGSRNPLLLQLLADALGLPV-VVPGPDEATALGAALLAAVAA 197
ASKHA_NBD_FGGY_RhaB-like cd07771
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ...
2-445 1.47e-24

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: 106.07  E-value: 1.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   2 YIGIDLGTSGVKVILlneqgevVASQTEKLT---VSR-PHPLWSEQDPEQW-----WQATDRAMKALGDQHslQDVKALG 72
Cdd:cd07771    2 YLAVDLGASSGRVIL-------GSLDGGKLEleeIHRfPNRPVEINGHLYWdidrlFDEIKEGLKKAAEQG--GDIDSIG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  73 IA--GQMHGatLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRV--ITGNLMMPGFTAPKLLWVQRHEPEIFRQIDK 148
Cdd:cd07771   73 IDtwGVDFG--LLDKNGELLGNPVHYRDPRTEGMMEELFEKISKEELyeRTGIQFQPINTLYQLYALKKEGPELLERADK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 149 VLLPKDYLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGMATVPVv 228
Cdd:cd07771  151 LLMLPDLLNYLLTGEKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLKPEVAEELGLKGIPV- 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 229 agggdnaagaVGVG------------MVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSF---CHA---------LPQR 284
Cdd:cd07771  230 ----------IAVAshdtasavaavpAEDEDAAFISSGTWSLIGVELDEPVITEEAFEAGFtneGGAdgtirllknITGL 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 285 W---HLMSVMLSAASCLDWvakltglcnvPALIAAAQQADESA------EPVWFLP---------YLsgERTPHNNPQAK 346
Cdd:cd07771  300 WllqECRREWEEEGKDYSY----------DELVALAEEAPPFGafidpdDPRFLNPgdmpeairaYC--RETGQPVPESP 367
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 347 GvffglthqhgpnELARAVLEGVGYALADGM-DVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQLdyRTGGDVGPA 425
Cdd:cd07771  368 G------------EIARCIYESLALKYAKTIeELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLPV--IAGPVEATA 433
                        490       500
                 ....*....|....*....|.
gi 446197531 426 LGAArLAQ-IAANPEKSLIEL 445
Cdd:cd07771  434 IGNL-LVQlIALGEIKSLEEG 453
PLN02295 PLN02295
glycerol kinase
2-437 2.52e-24

glycerol kinase


Pssm-ID: 215166 [Multi-domain]  Cd Length: 512  Bit Score: 105.94  E-value: 2.52e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   2 YIG-IDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAM-----KALGDQHSLQD-VKALGIA 74
Cdd:PLN02295   1 FVGaIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIakaleKAAAKGHNVDSgLKAIGIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  75 GQMHGATLLDAQQ-RVLRPAILWNDGRCAQECTLLEARVPQS----RVITGNLMMPGFTAPKLLWVQRHEPEI------- 142
Cdd:PLN02295  81 NQRETTVAWSKSTgRPLYNAIVWMDSRTSSICRRLEKELSGGrkhfVETCGLPISTYFSATKLLWLLENVDAVkeavksg 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 143 ---FRQIDKVLLpkdylrLRMTG-----EFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGallp 214
Cdd:PLN02295 161 dalFGTIDSWLI------WNLTGgasggVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIG---- 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 215 EVAKAWGMATVPVVAGggdnaagavgvgMVDANQAMLS-------------------LGTSGVYFAVSEGFLSK------ 269
Cdd:PLN02295 231 TIAKGWPLAGVPIAGC------------LGDQHAAMLGqrcrpgeakstygtgcfilLNTGEEVVPSKHGLLTTvayklg 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 270 PESAVhsfCHALPQrwhlmSVMLSAAScLDWVAKLTGLCNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVF 349
Cdd:PLN02295 299 PDAPT---NYALEG-----SVAIAGAA-VQWLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVC 369
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 350 FGLTHQHGPNELARAVLEGVGYALADGMDVVHA-CGIKPQSVTLI-----GGGARSEYWRQMLADISGQQL----DYRTg 419
Cdd:PLN02295 370 VGITRFTNKAHIARAVLESMCFQVKDVLDAMRKdAGEEKSHKGLFllrvdGGATANNLLMQIQADLLGSPVvrpaDIET- 448
                        490
                 ....*....|....*...
gi 446197531 420 gdvgPALGAARLAQIAAN 437
Cdd:PLN02295 449 ----TALGAAYAAGLAVG 462
glpK PRK00047
glycerol kinase GlpK;
2-466 5.57e-22

glycerol kinase GlpK;


Pssm-ID: 234594 [Multi-domain]  Cd Length: 498  Bit Score: 98.74  E-value: 5.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   2 YIG-IDLGTSGVKVILLNEQGEVVA-SQTEkLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQ--DVKALGIAGQM 77
Cdd:PRK00047   6 YILaLDQGTTSSRAIIFDHDGNIVSvAQKE-FTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISpdQIAAIGITNQR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  78 HGATLLDaqQRVLRP---AILWNDGRCAQECTLLEARvPQSRVI---TGNLMMPGFTAPKLLWVQRHEPE---------- 141
Cdd:PRK00047  85 ETTVVWD--KETGRPiynAIVWQDRRTADICEELKRD-GYEDYIrekTGLVIDPYFSGTKIKWILDNVEGareraekgel 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 142 IFRQIDKVLLPKdylrlrMTGE--FASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGallPEVAKA 219
Cdd:PRK00047 162 LFGTIDTWLVWK------LTGGkvHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYG---KTNPYG 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 220 WGMATVPVVagggdnaagavgvGMVDANQAML-------------SLGTsGVYFAVSEGflskpESAVHS-------FCH 279
Cdd:PRK00047 233 FFGGEVPIA-------------GIAGDQQAALfgqlcfepgmaknTYGT-GCFMLMNTG-----EKAVKSengllttIAW 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 280 ALPQRWHLM---SVMLsAASCLDWVAKLTGLCNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQH 356
Cdd:PRK00047 294 GIDGKVVYAlegSIFV-AGSAIQWLRDGLKIISDASDSEALARKVEDNDGVYVVPAFTGLGAPYWDSDARGAIFGLTRGT 372
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 357 GPNELARAVLEGVGYALADGMDVVHA-CGIKPQSVTLIGGGARSEYWRQMLADISGQQLdyrtggdVGP------ALGAA 429
Cdd:PRK00047 373 TKEHIIRATLESIAYQTRDVLDAMQAdSGIRLKELRVDGGAVANNFLMQFQADILGVPV-------ERPvvaettALGAA 445
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 446197531 430 RLAQIAANPEKSLIELLPQLPLEQS---HLPDAQRYAAYQ 466
Cdd:PRK00047 446 YLAGLAVGFWKDLDELKEQWKIDRRfepQMDEEEREKLYA 485
PRK10939 PRK10939
autoinducer-2 (AI-2) kinase; Provisional
5-482 9.98e-22

autoinducer-2 (AI-2) kinase; Provisional


Pssm-ID: 182853 [Multi-domain]  Cd Length: 520  Bit Score: 98.15  E-value: 9.98e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   5 IDLGTSGVKVILLNEQG-EVVASQTEKLTVSRPH-PLWSEQDPEQWWQATDRAMK-ALGD-QHSLQDVKALGIAGQMHGA 80
Cdd:PRK10939   8 LDAGTGSIRAVIFDLNGnQIAVGQAEWRHLAVPDvPGSMEFDLEKNWQLACQCIRqALQKaGIPASDIAAVSATSMREGI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  81 TLLDAQQRVLrpailWN----DGRCAQECTLLEARVP--QSRV--ITGNLMMPGfTAPKLLWVQRHEPEIFRQIDKVLLP 152
Cdd:PRK10939  88 VLYDRNGTEI-----WAcanvDARASREVSELKELHNnfEEEVyrCSGQTLALG-ALPRLLWLAHHRPDIYRQAHTITMI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 153 KDYLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGMAT-VPVVAGG 231
Cdd:PRK10939 162 SDWIAYMLSGELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTAKAAAETGLRAgTPVVMGG 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 232 GDNAAGAVGVGMVDANQAMLSLGTsgvyF-----AVSEGFlSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWVAKltG 306
Cdd:PRK10939 242 GDVQLGCLGLGVVRPGQTAVLGGT----FwqqvvNLPAPV-TDPNMNIRINPHVIPGMVQAESISFFTGLTMRWFRD--A 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 307 LCNVPALIAAAQQAD------ESAEPV-----WFLPYLSGERTPHNNPQAKGVFFGLT---HQHGPNELARAVLEGVGYA 372
Cdd:PRK10939 315 FCAEEKLLAERLGIDayslleEMASRVpvgshGIIPIFSDVMRFKSWYHAAPSFINLSidpEKCNKATLFRALEENAAIV 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 373 LADGMDVVHA-CGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTGGDVgPALGAARLAQIAANPEKSLIELLPQL-P 450
Cdd:PRK10939 395 SACNLQQIAAfSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEA-TALGCAIAAGVGAGIYSSLAETGERLvR 473
                        490       500       510
                 ....*....|....*....|....*....|..
gi 446197531 451 LEQSHLPDAQRYAAYQPRRETFRRLYQQLLPL 482
Cdd:PRK10939 474 WERTFEPNPENHELYQEAKEKWQAVYADQLGL 505
ASKHA_NBD_FGGY_SpXK-like cd07776
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ...
1-470 5.37e-21

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


Pssm-ID: 466795 [Multi-domain]  Cd Length: 514  Bit Score: 95.70  E-value: 5.37e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   1 MYIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPH------------PLWSEQDPEQWWQATDRA---MKALGDQhsL 65
Cdd:cd07776    1 LYLGLDLSTQSLKAVVIDSDLKVVAEESVNFDSDLPEygtkggvhrdgdGGEVTSPVLMWVEALDLLlekLKAAGFD--F 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  66 QDVKALGIAGQMHG---------ATL--LDAQQRVLrpAIL-----------WNDGRCAQECTLLEARV--PQSRV-ITG 120
Cdd:cd07776   79 SRVKAISGSGQQHGsvywskgaeSALanLDPSKSLA--EQLegafsvpdspiWMDSSTTKQCRELEKAVggPEALAkLTG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 121 NLMMPGFTAPKLLWVQRHEPEIFRQIDKV---------LLpkdylrlrmTGEFAS-DMSDAAGTMWLDVAKRDWSDVMLQ 190
Cdd:cd07776  157 SRAYERFTGPQIAKIAQTDPEAYENTERIslvssflasLL---------LGRYAPiDESDGSGMNLMDIRSRKWSPELLD 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 191 AC---DLsRDQMPALYEGSEITGALLPEVAKAWGM--------------ATVpvvagggdnaagavgVGM-VDANQAMLS 252
Cdd:cd07776  228 AAtapDL-KEKLGELVPSSTVAGGISSYFVERYGFspdclvvaftgdnpASL---------------AGLgLEPGDVAVS 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 253 LGTSGVYFAVSEGFLSKPESavHSFCHALPQRWHLMsvMLsaasCL-------DWVAKLTGLCNVPALIAAAQQADESAE 325
Cdd:cd07776  292 LGTSDTVFLVLDEPKPGPEG--HVFANPVDPGSYMA--ML----CYkngslarERVRDRYAGGSWEKFNELLESTPPGNN 363
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 326 PVWFLPYLSGERTPHnnpqAKGVFFGLTHQHGPNEL------ARAVLEgvGYALAdgMdVVHA----CGIKPQSVTLIGG 395
Cdd:cd07776  364 GNLGLYFDEPEITPP----VPGGGRRFFGDDGVDAFfdpaveVRAVVE--SQFLS--M-RLHAerlgSDIPPTRILATGG 434
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 396 GARSEYWRQMLADISGQQLdYRTGGDVGPALGAARLAQIAANPEKSLIELLPQLPLEQSHL-----PDAQRYAAYQPRRE 470
Cdd:cd07776  435 ASANKAILQVLADVFGAPV-YTLDVANSAALGAALRAAHGLLCAGSGDFSPEFVVFSAEEPklvaePDPEAAEVYDKLLE 513
ASKHA_NBD_FGGY_D-RBK cd07782
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ...
2-478 1.55e-20

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: 94.52  E-value: 1.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   2 YIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQ--HSLQDVKALGIAgqmhg 79
Cdd:cd07782    2 YIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGagVDPEQVKGIGFD----- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  80 AT----LLDAQQRVL---------RPAILWNDGRC---AQECTLLEARVPQSrviTGNLMMPGFTAPKLLWVQRHEPEIF 143
Cdd:cd07782   77 ATcslvVLDAEGKPVsvspsgddeRNVILWMDHRAveeAERINATGHEVLKY---VGGKISPEMEPPKLLWLKENLPETW 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 144 RQIDKVL-LPkDYLRLRMTGefasdmSDAAG--TM---WLDVAKRD----WSDVMLQACDL------------SRDQMPa 201
Cdd:cd07782  154 AKAGHFFdLP-DFLTWKATG------SLTRSlcSLvckWTYLAHEGseggWDDDFFKEIGLedlvednfakigSVVLPP- 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 202 lyeGSEITGALLPEVAKAWGM-ATVPVvagggdnaagavGVGMVDANQamlslGTSGVYFAVSEGFLSKPESAVH----- 275
Cdd:cd07782  226 ---GEPVGGGLTAEAAKELGLpEGTPV------------GVSLIDAHA-----GGLGTLGADVGGLPCEADPLTRrlali 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 276 ---SFCH-ALPQRWHLM--------SVML----------SAA-SCLDWV-------------AKLTGlCNVPALIAA--A 317
Cdd:cd07782  286 cgtSSCHmAVSPEPVFVpgvwgpyySAMLpglwlneggqSATgALLDHIiethpaypelkeeAKAAG-KSIYEYLNErlE 364
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 318 QQADESAEPVWFL-------PYLSGERTPHNNPQAKGVFFGLTHQHGPNELAR---AVLEGVGYALADGMDVVHACGIKP 387
Cdd:cd07782  365 QLAEEKGLPLAYLtrdlhvlPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAYGTRHIIEAMNAAGHKI 444
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 388 QSVTLIGGGARSEYWRQMLADISGQQLdyrtggdVGPA------LGAARLAQIAANPEKSLIELLPQL-PLEQSHLPDAQ 460
Cdd:cd07782  445 DTIFMCGGLSKNPLFVQLHADVTGCPV-------VLPKepeavlLGAAILGAVASGDFPSLWDAMAAMsGPGKVVEPNEE 517
                        570
                 ....*....|....*...
gi 446197531 461 RYAAYQPRRETFRRLYQQ 478
Cdd:cd07782  518 LKKYHDRKYEVFLKMYED 535
ASKHA_NBD_FGGY_RBK-like cd07768
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ...
2-479 8.16e-19

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: 89.22  E-value: 8.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   2 YIGIDLGTSGVKVILLN-EQGEVVASQTEKLTV-SRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQ--DVKALGIAGQM 77
Cdd:cd07768    2 GIGVDVGTSSARAGVYDlYAGLEMAQEPVPYYQdSSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDayEVKGCGVDATC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  78 HGATL-LDAQQRVLRPA-------ILWNDGRCAQECTLLEARVPQSRV-ITGNLMMPGFTAPKLLWVQRHEPEIFRQIDK 148
Cdd:cd07768   82 SLAIFdREGTPLMALIPypnednvIFWMDHSAVNEAQWINMQCPQQLLdYLGGKISPEMGVPKLKYFLDEYSHLRDKHFH 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 149 VLLPKDYLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEI------TGALLPEVAKAWGM 222
Cdd:cd07768  162 IFDLHDYIAYELTRLYEWNICGLLGKENLDGEESGWSSSFFKNIDPRLEHLTTTKNLPSNvpigttSGVALPEMAEKMGL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 223 ---ATVPVVAGGGDNAAGAVGVGMVDANQAMLSlGTSGVYFAVS------EGFLSKPESAVhsfchaLPQRWHLMSVMLS 293
Cdd:cd07768  242 hpgTAVVVSCIDAHASWFAVASPHLETSLFMIA-GTSSCHMYGTtisdriPGVWGPFDTII------DPDYSVYEAGQSA 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 294 AASCLDWVAKlTGLCnVPALI----------AAAQQADESAEPVWF-------LPYLSGERTPHNNPQAKGVFFGLTHQH 356
Cdd:cd07768  315 TGKLIEHLFE-SHPC-ARKFDealkkgadiyQVLEQTIRQIEKNNGlsihiltLDMFFGNRSEFADPRLKGSFIGESLDT 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 357 GPNELA---RAVLEGVGYALADGMDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQLdYRTGGDVGPALGAARLAQ 433
Cdd:cd07768  393 SMLNLTykyIAILEALAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAI-IKPKENMMGILGAAVLAK 471
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446197531 434 IAANpEKSLIELLPQLPLEQSHL-----PDAQRYAAYQPRRetfRRLYQQL 479
Cdd:cd07768  472 VAAG-KKQLADSITEADISNDRKsetfePLAYRLGADYILL---YKLLCVK 518
ASKHA_NBD_FGGY_NaCK-like cd07772
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ...
5-221 6.57e-15

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: 76.53  E-value: 6.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   5 IDLGTSGVKVILLNEQGEVVASQTEKLTVSrPHPLWSEQDPEQWWQATDRAMKALGDQHslqDVKALGIAGqmHGAT--L 82
Cdd:cd07772    5 FDIGKTNKKLLLFDENGEVLAERSTPNPEI-EEDGYPCEDVEAIWEWLLDSLAELAKRH---RIDAINFTT--HGATfaL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  83 LDAQQRVLRP--AILWN-DGRCAQEctLLEARVPqsRVITGNLMMPGFT--APKLLWVQRHEPEIFRQIDKVL-LPkDYL 156
Cdd:cd07772   79 LDENGELALPvyDYEKPiPDEINEA--YYAERGP--FEETGSPPLPGGLnlGKQLYWLKREKPELFARAKTILpLP-QYW 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446197531 157 RLRMTGEFASDMSdAAGT---MWlDVAKRDWSDVmLQACDLSRdQMPALYEGSEITGALLPEVAKAWG 221
Cdd:cd07772  154 AWRLTGKAASEIT-SLGChtdLW-DFEKNEYSSL-VKKEGWDK-LFPPLRKAWEVLGPLRPDLARRTG 217
PRK04123 PRK04123
ribulokinase; Provisional
315-479 2.62e-11

ribulokinase; Provisional


Pssm-ID: 235221 [Multi-domain]  Cd Length: 548  Bit Score: 65.64  E-value: 2.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 315 AAAQQADESAEPVwfLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGIKPQSVTLIG 394
Cdd:PRK04123 369 AAKQPPGEHGLVA--LDWFNGRRTPLADQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECFEDQGVPVEEVIAAG 446
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531 395 GGAR-SEYWRQMLADISGQQLDYRTgGDVGPALGAARLAQIAANPEKSLIELLPQL--PLEQSHLPDAQRYAAYQPRRET 471
Cdd:PRK04123 447 GIARkNPVLMQIYADVLNRPIQVVA-SDQCPALGAAIFAAVAAGAYPDIPEAQQAMasPVEKTYQPDPENVARYEQLYQE 525

                 ....*...
gi 446197531 472 FRRLYQQL 479
Cdd:PRK04123 526 YKQLHDYF 533
ASKHA_NBD_FGGY_MPA43-like cd07778
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ...
2-142 2.13e-07

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: 53.18  E-value: 2.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   2 YIGIDLGTSGVKVILLNEQGEVVASQTEKLT-VSRPHPLWS-EQDPEQWWQATDRAMKALGDQHSLQDVKALGIAgqmhg 79
Cdd:cd07778    2 GIGIDVGSTSVRIGIFDYHGTLLATSERPISyKQDPKDLWFvTQSSTEIWKAIKTALKELIEELSDYIVSGIGVS----- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  80 ATL------LDAQQRVLRP-------------AILWNDGRCAQECTLLEARVPQSRVI-TGNLMMPGFTAPKLLWVQRHE 139
Cdd:cd07778   77 ATCsmvvmqRDSDTSYLVPynviheksnpdqdIIFWMDHRASEETQWLNNILPDDILDyLGGGFIPEMAIPKLKYLIDLI 156

                 ...
gi 446197531 140 PEI 142
Cdd:cd07778  157 KED 159
PLN02669 PLN02669
xylulokinase
1-191 6.37e-07

xylulokinase


Pssm-ID: 178274 [Multi-domain]  Cd Length: 556  Bit Score: 51.69  E-value: 6.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   1 MYIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSE---QDPEQ----------WWQATDRAMKALGDQH-SLQ 66
Cdd:PLN02669   9 LFLGFDSSTQSLKATVLDSNLRIVASEIVHFDSDLPHYGTKDgvyRDPKVngrivsptlmWVEALDLLLQKLAKEKfPFH 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  67 DVKALGIAGQMHGA-----------TLLDAQQRV---LRPAI------LWNDGRCAQECTLLEARV---PQSRVITGNLM 123
Cdd:PLN02669  89 KVVAISGSGQQHGSvywrkgasavlKSLDPSKSLvaqLQDAFstkdspIWMDSSTTKQCREIEEAVggaAELSKLTGSRA 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446197531 124 MPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRLRMTGEFAS-DMSDAAGTMWLDVAKRDWSDVMLQA 191
Cdd:PLN02669 169 YERFTGPQIRKIYETQPEVYHDTERISLVSSFMASLLVGDYASiDETDGAGMNLMDIEKRCWSKAALEA 237
NagC COG1940
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ...
1-98 8.97e-06

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: 47.58  E-value: 8.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   1 MYIGIDLGTSGVKVILLNEQGEVVASQtekltvSRPHPlwSEQDPEQWWQATDRAMKALGDQH--SLQDVKALGIAgqMH 78
Cdd:COG1940    6 YVIGIDIGGTKIKAALVDLDGEVLARE------RIPTP--AGAGPEAVLEAIAELIEELLAEAgiSRGRILGIGIG--VP 75
                         90       100
                 ....*....|....*....|...
gi 446197531  79 GatLLDAQQ-RVLRPAIL--WND 98
Cdd:COG1940   76 G--PVDPETgVVLNAPNLpgWRG 96
rhaB PRK10640
rhamnulokinase; Provisional
82-189 3.07e-04

rhamnulokinase; Provisional


Pssm-ID: 182609 [Multi-domain]  Cd Length: 471  Bit Score: 43.17  E-value: 3.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531  82 LLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRVI--TGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRLR 159
Cdd:PRK10640  70 LLDKQGQRVGLPVSYRDSRTDGVMAQAQQQLGKRDIYrrSGIQFLPFNTLYQLRALTEQQPELIAQVAHALLIPDYFSYR 149
                         90       100       110
                 ....*....|....*....|....*....|
gi 446197531 160 MTGEFASDMSDAAGTMWLDVAKRDWSDVML 189
Cdd:PRK10640 150 LTGKMNWEYTNATTTQLVNINSDDWDESLL 179
ASKHA_ATPase_ROK cd23763
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ...
3-98 1.98e-03

ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family corresponds to a group of proteins including sugar kinases, transcriptional repressors, and yet uncharacterized open reading frames. ROK family sugar kinases phosphorylate a range of structurally distinct hexoses including the key carbon source D-glucose, various glucose epimers, and several acetylated hexosamines. The sugar kinases include N-acetyl-D-glucosamine kinase (NAGK; EC 2.7.1.59), polyphosphate glucokinase (PPGK; EC 2.7.1.63/EC 2.7.1.2), glucokinase (GLK; EC 2.7.1.2), fructokinase (FRK; EC 2.7.1.4), hexokinase (HK; EC 2.7.1.1), D-allose kinase (AlsK; EC 2.7.1.55), bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE; EC 3.2.1.183/EC 2.7.1.60), N-acetylmannosamine kinase (NanK; EC 2.7.1.60), beta-glucoside kinase (BglK; EC 2.7.1.85), and N-acetylglucosamine kinase (EC 2.7.1.59). The family also contains the repressor proteins, such as N-acetylglucosamine repressor (NagC), xylose repressor (XylR), cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and protein Mlc. ROK kinases harbor a conserved N-terminal ATP binding motif of sequence DxGxT, while ROK repressors possess a N-terminal extension that contains a canonical helix-turn-helix DNA binding motif. The ROK family proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.


Pssm-ID: 466849 [Multi-domain]  Cd Length: 239  Bit Score: 39.75  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446197531   3 IGIDLGTSGVKVILLNEQGEVVASQTEKLTvsrphplwSEQDPEQWWQATDRAMKALGDQHSL-QDVKALGIAgqMHGat 81
Cdd:cd23763    1 IGIDIGGTKIRAALVDLDGEILARERVPTP--------AEEGPEAVLDRIAELIEELLAEAGVrERILGIGIG--VPG-- 68
                         90       100
                 ....*....|....*....|
gi 446197531  82 LLDAQQ-RVLRPAIL--WND 98
Cdd:cd23763   69 PVDPETgIVLFAPNLpwWKN 88
ASKHA_NBD_O66634-like_rpt1 cd24034
nucleotide-binding domain (NBD) of the first repeat of Aquifex aeolicus hypothetical protein ...
2-30 5.98e-03

nucleotide-binding domain (NBD) of the first repeat of Aquifex aeolicus hypothetical protein O66634 and similar proteins; The family includes a group of uncharacterized proteins similar to Aquifex aeolicus hypothetical protein O66634, which contains two copies of the BcrAD/BadFG-like domain, suggesting that the family may structurally dimerize. The model corresponds to the first copy of the BcrAD/BadFG-like domain.


Pssm-ID: 466884 [Multi-domain]  Cd Length: 258  Bit Score: 38.34  E-value: 5.98e-03
                         10        20
                 ....*....|....*....|....*....
gi 446197531   2 YIGIDLGTSGVKVILLNEQGEVVASQTEK 30
Cdd:cd24034    1 YLGIDIGSTTVKAVVLDEKGNIVFSDYER 29
 
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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