|
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: 1042.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 1 MYIGIDLGTSGVKVILLNEQGEVVAAQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQDVKALGIAGQMHGA 80
Cdd:PRK15027 1 MYIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQDVKALGIAGQMHGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 81 TLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRLRM 160
Cdd:PRK15027 81 TLLDAQQRVLRPAILWNDGRCAQECALLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRLRM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 161 TGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGMATVPVVAGGGDNAAGAVG 240
Cdd:PRK15027 161 TGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVAKAWGMATVPVVAGGGDNAAGAVG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 241 VGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWAAKLTGLSNVPALIAAAQQA 320
Cdd:PRK15027 241 VGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWAAKLTGLSNVPALIAAAQQA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 321 DESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGIKPQSVTLIGGGARSE 400
Cdd:PRK15027 321 DESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGIKPQSVTLIGGGARSE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 401 YWRQMLADISGQQLDYRTGGDVGPALGAARLAQIAANPEKSLIELLPQLPLEQSHLPDAQRYAAYQPRRETFRRLYQQLL 480
Cdd:PRK15027 401 YWRQMLADISGQQLDYRTGGDVGPALGAARLAQIAANPEKSLIELLPQLPLEQSHLPDAQRYAAYQPRRETFRRLYQQLL 480
|
....
gi 16131435 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: 690.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 3 IGIDLGTSGVKVILLNEQGEVVAAQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSL--QDVKALGIAGQMHGA 80
Cdd:TIGR01312 1 LGIDLGTSGVKALLVDEQGEVIASGSAPHTVISPHPGWSEQDPEDWWDATEEAIKELLEQASEmgQDIKGIGISGQMHGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 81 TLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRV--ITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRL 158
Cdd:TIGR01312 81 VLLDANGEVLRPAILWNDTRTAQECEELEAELGDERVleITGNLALPGFTAPKLLWVRKHEPEVFARIAKVMLPKDYLRY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 159 RMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGM-ATVPVVAGGGDNAAG 237
Cdd:TIGR01312 161 RLTGEYVTEYSDASGTGWFDVAKRAWSKELLDALDLPESQLPELIESSEKAGTVRPEVAARLGLsAGVPVAAGGGDNAAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 238 AVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWAAKLTGLSNVPALIAAA 317
Cdd:TIGR01312 241 AIGTGTVDPGDAMMSLGTSGVVYAVTDKPLPDPAGAVHGFCHALPGGWLPMGVTLSATSSLEWFRELFGKEDVEALNELA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 318 QQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVV-HACGIKPQSVTLIGGG 396
Cdd:TIGR01312 321 EQSPPGAEGVTFLPYLNGERTPHLDPQARGSFIGLTHNTTRADLTRAVLEGVTFALRDSLDILrEAGGIPIQSIRLIGGG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 397 ARSEYWRQMLADISGQQLDYRTgGDVGPALGAARLAQIAANpEKSLIELLPQLPLEQSH--LPDAQRYAAYQPRRETFRR 474
Cdd:TIGR01312 401 AKSPAWRQMLADIFGTPVDVPE-GEEGPALGAAILAAWALG-EKDLAALCSEAVVKQTEsvLPIAENVEAYEELYERYKK 478
|
...
gi 16131435 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: 623.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 1 MYIGIDLGTSGVKVILLNEQGEVVAAQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQH--SLQDVKALGIAGQMH 78
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAgiSPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 79 GATLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRV-ITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLR 157
Cdd:cd07808 81 GLVLLDKNGRPLRPAILWNDQRSAAECEELEARLGDEILiITGNPPLPGFTLPKLLWLKENEPEIFARIRKILLPKDYLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 158 LRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGMAT-VPVVAGGGDNAA 236
Cdd:cd07808 161 YRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEAAEELGLPEgTPVVAGAGDNAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 237 GAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWAAKLTGLSNVP--ALI 314
Cdd:cd07808 241 AALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLHTFPHAVPGKWYAMGVTLSAGLSLRWLRDLFGPDRESfdELD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 315 AAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGIKPQSVTLIG 394
Cdd:cd07808 321 AEAAKVPPGSEGLLFLPYLSGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVLKELGIKVKEIRLIG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 395 GGARSEYWRQMLADISGQQLDYRTGGDvGPALGAARLAQIAANPEKSLIELLPQL-PLEQSHLPDAQRYAAYQPRRETFR 473
Cdd:cd07808 401 GGAKSPLWRQILADVLGVPVVVPAEEE-GSAYGAALLAAVGAGVFDDLEEAAAACiKIEKTIEPDPERHEAYDELYARYR 479
|
...
gi 16131435 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: 599.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 1 MYIGIDLGTSGVKVILLNEQGEVVAAQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQH--SLQDVKALGIAGQMH 78
Cdd:COG1070 2 YVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAgvDPEEIAAIGVSGQMH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 79 GATLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRV--ITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYL 156
Cdd:COG1070 82 GLVLLDADGEPLRPAILWNDTRAAAEAAELREELGEEALyeITGNPLHPGFTAPKLLWLKENEPEIFARIAKVLLPKDYL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 157 RLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGM-ATVPVVAGGGDNA 235
Cdd:COG1070 162 RYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEAAAETGLpAGTPVVAGAGDNA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 236 AGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWAAKLTG---LSNVPA 312
Cdd:COG1070 242 AAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFCHAVPGRWLPMGATNNGGSALRWFRDLFAdgeLDDYEE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 313 LIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGIKPQSVTL 392
Cdd:COG1070 322 LNALAAEVPPGADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEALEEAGVKIDRIRA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 393 IGGGARSEYWRQMLADISGQQLdYRTGGDVGPALGAARLAQIAANPEKSLIELLPQL-PLEQSHLPDAQRYAAYQPRRET 471
Cdd:COG1070 402 TGGGARSPLWRQILADVLGRPV-EVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMvRVGETIEPDPENVAAYDELYER 480
|
490
....*....|...
gi 16131435 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 |
4.07e-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: 403.82 E-value: 4.07e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 3 IGIDLGTSGVKVILLNEQGEVVAAQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQ--DVKALGIAGQMHGA 80
Cdd:cd07805 3 LAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDpsDIAAIAFSGQMQGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 81 TLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQS---RVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLR 157
Cdd:cd07805 83 VPVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLGGIegyRLGGGNPPSGKDPLAKILWLKENEPEIYAKTHKFLDAKDYLN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 158 LRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWG-MATVPVVagggdnaa 236
Cdd:cd07805 163 FRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPEAAAELGlPAGTPVV-------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 237 gavgVGMVDA------------NQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWAAKL 304
Cdd:cd07805 235 ----GGGGDAaaaalgagaveeGDAHIYLGTSGWVAAHVPKPKTDPDHGIFTLASADPGRYLLAAEQETAGGALEWARDN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 305 TGLSNVP------ALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMD 378
Cdd:cd07805 311 LGGDEDLgaddyeLLDELAAEAPPGSNGLLFLPWLNGERSPVEDPNARGAFIGLSLEHTRADLARAVLEGVAFNLRWLLE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 379 VVHACGIKPQSVTLIGGGARSEYWRQMLADISG---QQLDYRTggDVGpALGAARLAQIAANPEKSLIELLPQLPLEQSH 455
Cdd:cd07805 391 ALEKLTRKIDELRLVGGGARSDLWCQILADVLGrpvEVPENPQ--EAG-ALGAALLAAVGLGLLKSFDEAKALVKVEKVF 467
|
490
....*....|....*...
gi 16131435 456 LPDAQRYAAYQPRRETFR 473
Cdd:cd07805 468 EPDPENRARYDRLYEVFK 485
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
1-432 |
6.57e-130 |
|
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: 381.91 E-value: 6.57e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 1 MYIGIDLGTSGVKVILLNEQGEVVAAQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQH--SLQDVKALGIAGQMH 78
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAgiDPSDIAAIGISGQMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 79 GATLLDAQQRVLRPAILWNDGRcaqectllearvpqsrvitgnlmmpgftapkllwvqrhepeifrqiDKVLLPKDYLRL 158
Cdd:cd00366 81 GVVLVDADGNPLRPAIIWLDRR----------------------------------------------AKFLQPNDYIVF 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 159 RMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWG-MATVPVVAGGGDNAAG 237
Cdd:cd00366 115 RLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAAEETGlPAGTPVVAGGGDTAAA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 238 AVGVGMVDANQAMLSLGTSGVYFAVSEGFLSkPESAVHSFCHALPQRWHLMSVMLSAASCLDWAAKLTGLSNVPA----- 312
Cdd:cd00366 195 ALGAGVVEPGDAVDSTGTSSVLSVCTDEPVP-PDPRLLNRCHVVPGLWLLEGAINTGGASLRWFRDEFGEEEDSDaeyeg 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 313 LIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGIKPQSVTL 392
Cdd:cd00366 274 LDELAAEVPPGSDGLIFLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEILEELGVKIKEIRV 353
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 16131435 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 |
9.60e-123 |
|
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: 365.72 E-value: 9.60e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 1 MYIGIDLGTSGVKVILLN-EQGEVVAAQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQH--SLQDVKALGIAGQM 77
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAgaELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 78 HGATLLDAQQRVLRPAILWNDGRCAQECTLLEARV-PQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYL 156
Cdd:cd07809 81 HGLVALDADGKVLRPAKLWCDTRTAPEAEELTEALgGKKCLLVGLNIPARFTASKLLWLKENEPEHYARIAKILLPHDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 157 RLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSR---DQMPALYEGSEITGALLPEVAKAWGMAT-VPVVAGGG 232
Cdd:cd07809 161 NWKLTGEKVTGLGDASGTFPIDPRTRDYDAELLAAIDPSRdlrDLLPEVLPAGEVAGRLTPEGAEELGLPAgIPVAPGEG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 233 DNAAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHAlPQRW-HLMSVMLSAASCLDWAAKLTGLSnVP 311
Cdd:cd07809 241 DNMTGALGTGVVNPGTVAVSLGTSGTAYGVSDKPVSDPHGRVATFCDS-TGGMlPLINTTNCLTAWTELFRELLGVS-YE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 312 ALIAAAQQADESAEPVWFLPYLSGERTPhNNPQAKGVFFGLTH-QHGPNELARAVLEGVGYALADGMDVVHACGIKPQSV 390
Cdd:cd07809 319 ELDELAAQAPPGAGGLLLLPFLNGERTP-NLPHGRASLVGLTLsNFTRANLARAALEGATFGLRYGLDILRELGVEIDEI 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 16131435 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 |
7.18e-118 |
|
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: 353.37 E-value: 7.18e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 1 MYIGIDLGTSGVKVILLNEQGEVVAAQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQ--HSLQDVKALGIAGqMH 78
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKagISPKEIAAIGVSG-LV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 79 GATL-LDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRV--ITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDY 155
Cdd:cd07804 80 PALVpVDENGKPLRPAILYGDRRATEEIEWLNENIGEDRIfeITGNPLDSQSVGPKLLWIKRNEPEVFKKTRKFLGAYDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 156 LRLRMTGEFASDMSDAAGTMWL-DVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGMAT-VPVVAGGGD 233
Cdd:cd07804 160 IVYKLTGEYVIDYSSAGNEGGLfDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTKEAAEETGLAEgTPVVAGTVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 234 NAAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSfcHALPQRWHLMSVMLSAASCLDW-----------AA 302
Cdd:cd07804 240 AAASALSAGVVEPGDLLLMLGTAGDIGVVTDKLPTDPRLWLDY--HDIPGTYVLNGGMATSGSLLRWfrdefageeveAE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 303 KLTGLSNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHA 382
Cdd:cd07804 318 KSGGDSAYDLLDEEAEKIPPGSDGLIVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYRALLEGVAYGLRHHLEVIRE 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 16131435 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 |
3.87e-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: 351.12 E-value: 3.87e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 1 MYIGIDLGTSGVKVILLNEQGEVVAAQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQDVKALGIAGQMHGA 80
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGPDPIAAISVSSQGESG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 81 TLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRV--ITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRL 158
Cdd:cd07773 81 VPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEELyrITGLPPSPMYSLAKLLWLREHEPEIFAKAAKWLSVADYIAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 159 RMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGMAT-VPVvagggdnaag 237
Cdd:cd07773 161 RLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEELGLPAgTPV---------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 238 avgV-------------GMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVH--SFCHALPQRWHLMSVMLSAASCLDWAA 302
Cdd:cd07773 231 ---VvgghdhlcaalgaGVIEPGDVLDSTGTAEALLAVVDEPPLDEMLAEGglSYGHHVPGGYYYLAGSLPGGALLEWFR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 303 KLTGL--SNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVV 380
Cdd:cd07773 308 DLFGGdeSDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEAL 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131435 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 |
6.29e-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: 339.15 E-value: 6.29e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 1 MYIGIDLGTSGVKVILLNEQGEVVAAQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQDVKALGIAGQMHGA 80
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGGEVDAIGFSSAMHSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 81 TLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRV--ITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRL 158
Cdd:cd07770 81 LGVDEDGEPLTPVITWADTRAAEEAERLRKEGDGSELyrRTGCPIHPMYPLAKLLWLKEERPELFAKAAKFVSIKEYLLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 159 RMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWG-MATVPVVAGGGDNAAG 237
Cdd:cd07770 161 RLTGELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFAERLGlLAGTPVVLGASDGALA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 238 AVGVGMVDANQAMLSLGTSG-VYFAVSEGFLSKPESAvhsFCHALPQRWHLMSVMLS-AASCLDWAAKLTGLSNVP--AL 313
Cdd:cd07770 241 NLGSGALDPGRAALTVGTSGaIRVVSDRPVLDPPGRL---WCYRLDENRWLVGGAINnGGNVLDWLRDTLLLSGDDyeEL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 314 IAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGIKPQSVTLI 393
Cdd:cd07770 318 DKLAEAVPPGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKSIYEALEELAGPVKEIRAS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 394 GGGARSEYWRQMLADISGQQLDYRTGGDvGPALGAARLAQIAANPEKSLiELLPQLPLEQSHLPDAQRYAAYQPRRETFR 473
Cdd:cd07770 398 GGFLRSPLWLQILADVLGRPVLVPEEEE-ASALGAALLALEALGLISSL-EADELVKIGKVVEPDPENHAIYAELYERFK 475
|
...
gi 16131435 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 |
6.66e-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: 320.44 E-value: 6.66e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 1 MYIGIDLGTSGVKVILLNEQGEVVAAQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQH--SLQDVKALGIAGQMH 78
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLgiSLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 79 GATLLDAQQRVLRPAILWNDGRCAQECTLLEA--RVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYL 156
Cdd:pfam00370 81 GTVLLDKNDKPLYNAILWKDRRTAEIVENLKEegNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHKFLTIHDYL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131435 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 |
1.85e-107 |
|
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: 326.43 E-value: 1.85e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 2 YIGIDLGTSGVKVILLNEQGEVVAAQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSL--QDVKALGIAGQMHG 79
Cdd:cd07802 2 LLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVdpSDIAGVGVTGHGNG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 80 ATLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRV--ITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLR 157
Cdd:cd07802 82 LYLVDKDGKPVRNAILSNDSRAADIVDRWEEDGTLEKVypLTGQPLWPGQPVALLRWLKENEPERYDRIRTVLFCKDWIR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 158 LRMTGEFASDMSDaAGTMWLDVAKRDWSDVMLQACDLS--RDQMPALYEGSEITGALLPEVAKAWG-MATVPVVAGGGDN 234
Cdd:cd07802 162 YRLTGEISTDYTD-AGSSLLDLDTGEYDDELLDLLGIEelKDKLPPLVPSTEIAGRVTAEAAALTGlPEGTPVAAGAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 235 AAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSfCHALPQRWHLMSVMLSAASCLDWA-------AKLTGL 307
Cdd:cd07802 241 VASALGAGAVDEGQLCVILGTWSINEVVTDEPVVPDSVGSNS-LHADPGLYLIVEASPTSASNLDWFldtllgeEKEAGG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 308 SNVPALIAAAQQADESAEPVWFLPYLSGERTphnNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGiKP 387
Cdd:cd07802 320 SDYDELDELIAAVPPGSSGVIFLPYLYGSGA---NPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHRDHLERLLVAR-KP 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 16131435 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 |
2.04e-99 |
|
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: 305.30 E-value: 2.04e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 1 MYIGIDLGTSGVKVILLNEQGEVVAAQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQDVKALGIAGQMHGA 80
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRPRRVVAIAVDGTSGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 81 TLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRLRM 160
Cdd:cd07783 81 VLVDREGEPLRPAIMYNDARAVAEAEELAEAAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAKFLHQADWLAGRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 161 TG-EFASDMSDAAgTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGM-ATVPVvagggdnaaga 238
Cdd:cd07783 161 TGdRGVTDYNNAL-KLGYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAEAAEELGLpAGTPV----------- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 239 vGVGMVDANQAML------------SLGTSGVYFAVSEGFLSKPESAVHsfCHALPQRWHLMSVMLSA-ASCLDWAAKLT 305
Cdd:cd07783 229 -VAGTTDSIAAFLasgavrpgdavtSLGTTLVLKLLSDKRVPDPGGGVY--SHRHGDGYWLVGGASNTgGAVLRWFFSDD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 306 GLsnvPALIAAAqqADESAEPVWFLPY-LSGERTPHNNPQAKGVFfgLTHQHGPNELARAVLEGVGYALADGMDVV-HAC 383
Cdd:cd07783 306 EL---AELSAQA--DPPGPSGLIYYPLpLRGERFPFWDPDARGFL--LPRPHDRAEFLRALLEGIAFIERLGYERLeELG 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 16131435 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 |
6.55e-94 |
|
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: 291.34 E-value: 6.55e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 1 MYIGIDLGTSGVKVILLNEQGEVVAAQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSL--QDVKALGIAGQmh 78
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVdpEDIAAIGLTSQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 79 GAT--LLDAQQRVLRPAILWNDGRcaqectllearvpqsrvitgnlmmpgftapkllwvqrhepeifrqIDKVLLPKDYL 156
Cdd:cd07779 79 RSTfvPVDEDGRPLRPAISWQDKR---------------------------------------------TAKFLTVQDYL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 157 RLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGMAT-VPVvagggdna 235
Cdd:cd07779 114 LYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEAAEETGLPEgTPV-------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 236 agavgV-------------GMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDW-- 300
Cdd:cd07779 186 -----VagggdqqcaalgaGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPGKWVLEGSINTGGSAVRWfr 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 301 --------AAKLTGLSNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYA 372
Cdd:cd07779 261 defgqdevAEKELGVSPYELLNEEAAKSPPGSDGLLFLPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFE 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 373 LADGMDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQL----DYRTGgdvgpALGAARLAQIAANPEKSLIELLPQ 448
Cdd:cd07779 341 LRDNLEAMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVerpeTSEAT-----ALGAAILAAVGAGIYPDFEEAVKA 415
|
490
....*....|....*...
gi 16131435 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 |
5.72e-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: 281.82 E-value: 5.72e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 1 MYIGIDLGTSGVKVILLNEQGEVVAAQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQ--HSLQDVKALGIAGQMH 78
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKldVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 79 GATLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRV--ITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYL 156
Cdd:cd24121 81 GTWLVDEDGRPVRDAILWLDGRAADIVERWQADGIAEAVfeITGTGLFPGSQAAQLAWLKENEPERLERARTALHCKDWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 157 RLRMTGEFASDMSDAAGTmWLDVAKRDWSDVMLQACDLS--RDQMPALYEGSEITGALLPEVAKAWGM-ATVPVVAGGGD 233
Cdd:cd24121 161 FYKLTGEIATDPSDASLT-FLDFRTRQYDDEVLDLLGLEelRHLLPPIRPGTEVIGPLTPEAAAATGLpAGTPVVLGPFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 234 NAAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRW-HLMSVMlSAASCLDWAAKL-------- 304
Cdd:cd24121 240 VVATALGSGAIEPGDACSILGTTGVHEVVVDEPDLEPEGVGYTICLGVPGRWlRAMANM-AGTPNLDWFLRElgevlkeg 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 305 ---TGLSNVPALIAAAQQADESAEPVWFLPYLS--GERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALadgMDV 379
Cdd:cd24121 319 aepAGSDLFQDLEELAASSPPGAEGVLYHPYLSpaGERAPFVNPNARAQFTGLSLEHTRADLLRAVYEGVALAM---RDC 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131435 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 |
8.24e-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: 198.91 E-value: 8.24e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 2 YIGIDLGTSGVKVILLNEQ-GEVVA--AQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQ--DVKALGIAGQ 76
Cdd:cd07781 2 VIGIDFGTQSVRAGLVDLAdGEELAsaVVPYPTGYIPPRPGWAEQNPADYWEALEEAVRGALAEAGVDpeDVVGIGVDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 77 mhGATLL--DAQQRVLRPAILWNDGRCAQECTLLEARvpQSRVITGNLMMPGFT------APKLLWVQRHEPEIFRQIDK 148
Cdd:cd07781 82 --SSTVVpvDEDGNPLAPAILWMDHRAQEEAAEINET--AHPALEYYLAYYGGVyssewmWPKALWLKRNAPEVYDAAYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 149 VLLPKDYLRLRMTGEFASDMSdAAGTMWL-DVAKRDWSDVMLQACDLS----RDQMPALYEGS-EITGALLPEVAKAWGM 222
Cdd:cd07781 158 IVEACDWINARLTGRWVRSRC-AAGHKWMyNEWGGGPPREFLAALDPGllklREKLPGEVVPVgEPAGTLTAEAAERLGL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 223 -ATVPVVagggdnaagavgVGMVDANQAMLSL------------GTSGVYFAVSEGFLSKP------ESAVHsfchalPQ 283
Cdd:cd07781 237 pAGIPVA------------QGGIDAHMGAIGAgvvepgtlalimGTSTCHLMVSPKPVDIPgicgpvPDAVV------PG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 284 RWHLMSVMLSAASCLDWAAKL-------TGLSNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQH 356
Cdd:cd07781 299 LYGLEAGQSAVGDIFAWFVRLfvppaeeRGDSIYALLSEEAAKLPPGESGLVALDWFNGNRTPLVDPRLRGAIVGLTLGT 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 357 GPNELARAVLEGVGYALADGMDVVHACGIKPQSVTLIGGGA-RSEYWRQMLADISGQQLdYRTGGDVGPALGAARLAQIA 435
Cdd:cd07781 379 TPAHIYRALLEATAFGTRAIIERFEEAGVPVNRVVACGGIAeKNPLWMQIYADVLGRPI-KVPKSDQAPALGAAILAAVA 457
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 16131435 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 |
7.32e-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: 189.74 E-value: 7.32e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 2 YIGIDLGTSGVKVILLNEQGEVVAAQTEKLTVSRP--HPLWSEQDPEQWWQATDRAMKALGDQH--SLQDVKALGIAGQM 77
Cdd:cd07798 2 YLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDddYPDAKEFDPEELWEKICEAIREALKKAgiSPEDISAVSSTSQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 78 HGATLLDAQQRVLR--PAIlwnDGRCAQECTLLEARVPQSRVITGNLMMPGFTAP-KLLWVQRHEPEIFRQIDKVLLPKD 154
Cdd:cd07798 82 EGIVFLDKDGRELYagPNI---DARGVEEAAEIDDEFGEEIYTTTGHWPTELFPAaRLLWFKENRPEIFERIATVLSISD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 155 YLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGMAT-VPVVAGGGD 233
Cdd:cd07798 159 WIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAARELGLPEgTPVVVGGAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 234 NAAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDWAAKL--TGLSNVP 311
Cdd:cd07798 239 TQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWTGCHLVPGKWVLESNAGVTGLNYQWLKELlyGDPEDSY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 312 ALI-AAAQQADESAEPVwfLPYLSGERTPHNNPQAK--GVFFGLTHQHGPNE---LARAVLEGVGYALADGMDVVHA-CG 384
Cdd:cd07798 319 EVLeEEASEIPPGANGV--LAFLGPQIFDARLSGLKngGFLFPTPLSASELTrgdFARAILENIAFAIRANLEQLEEvSG 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 16131435 385 IKPQSVTLIGGGARSEYWRQMLADISGQQLdYRTGGDVGPALGAARLAQIAAN 437
Cdd:cd07798 397 REIPYIILCGGGSRSALLCQILADVLGKPV-LVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
2-445 |
9.33e-49 |
|
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: 9.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 2 YI-GIDLGTSGVKVILLNEQGEVVAAQTEKLTVSRPHPLWSEQDPEQWWQATDRAMK-ALGD-QHSLQDVKALGIAGQMH 78
Cdd:cd07793 1 YIlAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKeALKNaGLTPEDIAAIGISTQRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 79 GATLLDAQQ-RVLRPAILWNDGRCAQEC----------------TLLEARVPQSRVITGNLM--MPGFTAPKLLWVQRHE 139
Cdd:cd07793 81 TFLTWDKKTgKPLHNFITWQDLRAAELCeswnrslllkalrggsKFLHFLTRNKRFLAASVLkfSTAHVSIRLLWILQNN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 140 PEI----------FRQIDKVLLpkdylrLRMTG--EFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSE 207
Cdd:cd07793 161 PELkeaaekgellFGTIDTWLL------WKLTGgkVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDTSG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 208 ITGALLPEVakawGMATVPVvagggdnaagAVGVGmvDANQAM------------LSLGTsGVYFAVSEGflSKPesavH 275
Cdd:cd07793 235 DFGSTDPSI----FGAEIPI----------TAVVA--DQQAALfgeccfdkgdvkITMGT-GTFIDINTG--SKP----H 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 276 SFCHAL-PQ-RWHLMS--------VMLSAASCLDWAAKLTGLSNVPALIAAAQQADESaEPVWFLPYLSGERTPHNNPQA 345
Cdd:cd07793 292 ASVKGLyPLvGWKIGGeitylaegNASDTGTVIDWAKSIGLFDDPSETEDIAESVEDT-NGVYFVPAFSGLQAPYNDPTA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 346 KGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHA-CGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTGGDVGp 424
Cdd:cd07793 371 CAGFIGLTPSTTKAHLVRAILESIAFRVKQLLETMEKeTSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKNTEMS- 449
|
490 500
....*....|....*....|.
gi 16131435 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 |
2.64e-41 |
|
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: 154.16 E-value: 2.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 2 YIG-IDLGTSGVKVILLNEQGEVVAAQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQ--DVKALGIAGQMH 78
Cdd:cd07769 1 YILaIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISasDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 79 GATLLDAQ-QRVLRPAILWNDGRCAQECTLLEARVPQSRV--ITGNLMMPGFTAPKLLWVQRHEPEI----------FRQ 145
Cdd:cd07769 81 TTVVWDKKtGKPLYNAIVWQDRRTADICEELKAKGLEERIreKTGLPLDPYFSATKIKWILDNVPGAreraergellFGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 146 IDKVLLPKdylrlrMTG--EFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKawgmA 223
Cdd:cd07769 161 IDTWLIWK------LTGgkVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTDPEGLG----A 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 224 TVPVvagggdnaagavgVGMVDANQA-----------------------MLSLGTSGVYFavSEGFLS----KPESAVhs 276
Cdd:cd07769 231 GIPI-------------AGILGDQQAalfgqgcfepgmakntygtgcflLMNTGEKPVPS--KNGLLTtiawQIGGKV-- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 277 fCHALPqrwhlmSVMLSAASCLDWAAKLTGLSNVPALIAA-AQQAdESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQ 355
Cdd:cd07769 294 -TYALE------GSIFIAGAAIQWLRDNLGLIEDAAETEElARSV-EDNGGVYFVPAFSGLGAPYWDPDARGAIVGLTRG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 356 HGPNELARAVLEGVGYALADGMDVVHA-CGIKPQSVTLIGGGARSEYWRQMLADISGQQLdyrtggdVGP------ALGA 428
Cdd:cd07769 366 TTKAHIVRAALESIAYQTRDVLEAMEKdSGIKLKELRVDGGATANNFLMQFQADILGVPV-------VRPkvaettALGA 438
|
490
....*....|....*..
gi 16131435 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 |
2.81e-40 |
|
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: 150.06 E-value: 2.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 1 MYIGIDLGTSGVKVILLN-EQGEVVAAQTEKLTVSRPH--PLWSEQDPEQWWQATDRAMKALgDQHSLQDVKALGIAGQM 77
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDlESGRILESVSRPTPAPISSddPGRSEQDPEKILEAVRNLIDEL-PREYLSDVTGIGITGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 78 HGATLLDAQQRVLRPAILWNDGRCAQECTL-LEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPeIFRQIDKVLLPKDYL 156
Cdd:cd07777 80 HGIVLWDEDGNPVSPLITWQDQRCSEEFLGgLSTYGEELLPKSGMRLKPGYGLATLFWLLRNGP-LPSKADRAGTIGDYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 157 RLRMTG--EFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKawgmaTVPVvagggdn 234
Cdd:cd07777 159 VARLTGlpKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLSSALPK-----GIPV------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 235 aagavGVGMVDaNQAM-------------LSLGTSG-VYFAVSEGFLSkpeSAVHSFChaLPQRWHLmsvmLSAAS---- 296
Cdd:cd07777 227 -----YVALGD-NQASvlgsglneendavLNIGTGAqLSFLTPKFELS---GSVEIRP--FFDGRYL----LVAASlpgg 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 297 ----CL-----DWAAKLTGLSNVPA----LIAAAQQADESaePVWFLPYLSGERTphnNPQAKGVFFGLTHQH-GPNELA 362
Cdd:cd07777 292 ralaVLvdflrEWLRELGGSLSDDEiwekLDELAESEESS--DLSVDPTFFGERH---DPEGRGSITNIGESNfTLGNLF 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131435 363 RAVLEGVGYALADGMDVVHACGIKPQSVTLIGGGAR-SEYWRQMLADISGQQLDYRTGGDvGPALGAARLA 432
Cdd:cd07777 367 RALCRGIAENLHEMLPRLDLDLSGIERIVGSGGALRkNPVLRRIIEKRFGLPVVLSEGSE-EAAVGAALLA 436
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
2-445 |
1.09e-35 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 138.57 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 2 YIG-IDLGTSGVKVILLNEQGEVVAAQTEKLTVSRPHPLWSEQDPEQWWQATDRAM----KALGDQHSLQDVKALGIAGQ 76
Cdd:PTZ00294 3 YIGsIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMneaiKKLREKGPSFKIKAIGITNQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 77 MHGATLLDAQQ-RVLRPAILWNDGRCAQECTLLEARVPQS---RVITGNLMMPGFTAPKLLWVQRHEPEI---------- 142
Cdd:PTZ00294 83 RETVVAWDKVTgKPLYNAIVWLDTRTYDIVNELTKKYGGSnffQKITGLPISTYFSAFKIRWMLENVPAVkdavkegtll 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 143 FRQIDKVLLPKdylrLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEvaKAWGM 222
Cdd:PTZ00294 163 FGTIDTWLIWN----LTGGKSHVTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTISGE--AVPLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 223 ATVPVVAGGGDNAAGAVGVGMVDANQAMLSLGTsGVYFAVSEGflskpESAVHSFCHAL-----------PQRWHLMSVM 291
Cdd:PTZ00294 237 EGVPITGCIGDQQAALIGHGCFEKGDAKNTYGT-GCFLLMNTG-----TEIVFSKHGLLttvcyqlgpngPTVYALEGSI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 292 LSAASCLDWAAKLTGLSNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGY 371
Cdd:PTZ00294 311 AVAGAGVEWLRDNMGLISHPSEIEKLARSVKDTGGVVFVPAFSGLFAPYWRPDARGTIVGMTLKTTRAHIVRAALEAIAL 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131435 372 ALAdgmDVVHA----CGIKPQSVTLIGGGARSEYWRQMLADISGQQLdYRTGGDVGPALGAARLAQIAANPEKSLIEL 445
Cdd:PTZ00294 391 QTN---DVIESmekdAGIELNSLRVDGGLTKNKLLMQFQADILGKDI-VVPEMAETTALGAALLAGLAVGVWKSLEEV 464
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
6-415 |
2.47e-33 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 131.30 E-value: 2.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 6 DLGTSGVKVILLNEQGEVVAAQTEKlTVSRP---HPLWSEQDPEQWWQATDRAMKALGDQHSLQDVKALGIAGQMHGATL 82
Cdd:PRK10331 8 DCGATNVRAIAVDRQGKIVARASTP-NASDIaaeNSDWHQWSLDAILQRFADCCRQINSELTECHIRGITVTTFGVDGAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 83 LDAQQRVLRPAILWNDGRCAQECTLLEARVPQSR--VITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRLRM 160
Cdd:PRK10331 87 VDKQGNLLYPIISWKCPRTAAVMENIERYISAQQlqQISGVGAFSFNTLYKLVWLKENHPQLLEQAHAWLFISSLINHRL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 161 TGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGM-ATVPVVAGGGDNAAGAV 239
Cdd:PRK10331 167 TGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQPSAAALLGLpVGIPVISAGHDTQFALF 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 240 GVGmVDANQAMLSLGTSGVYFAVSEgflsKPESAVHSFCHALPQRWHLMS------VMLSAASCLDWAAKL--TGLSNVP 311
Cdd:PRK10331 247 GSG-AGQNQPVLSSGTWEILMVRSA----QVDTSLLSQYAGSTCELDSQSglynpgMQWLASGVLEWVRKLfwTAETPYQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 312 ALIAAAQQADESAEPVWFLPYLSGERTphnnpqakGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHA-CGIKPQSV 390
Cdd:PRK10331 322 TMIEEARAIPPGADGVKMQCDLLACQN--------AGWQGVTLNTTRGHFYRAALEGLTAQLKRNLQVLEKiGHFKASEL 393
|
410 420
....*....|....*....|....*
gi 16131435 391 TLIGGGARSEYWRQMLADISGQQLD 415
Cdd:PRK10331 394 LLVGGGSRNALWNQIKANMLDIPIK 418
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
2-466 |
1.32e-32 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 129.80 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 2 YIG-IDLGTSGVKVILLNEQGEVVA-AQTEkLTVSRPHPLWSEQDPEQWWQATDRAMK-ALGDQH-SLQDVKALGIAGQM 77
Cdd:COG0554 4 YILaIDQGTTSTRAILFDRDGNIVAvAQRE-FTQIYPQPGWVEHDPEEIWESVLAVIReALAKAGiSAEDIAAIGITNQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 78 HGATLLDAQQ-RVLRPAILWNDGRCAQECTLLEARVPQSRV--ITGNLMMPGFTAPKLLWVQRHEPEIfRQ--------- 145
Cdd:COG0554 83 ETTVVWDRKTgKPLYNAIVWQDRRTADICEELKADGLEDLIreKTGLVLDPYFSATKIKWILDNVPGA-REraeagellf 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 146 --IDKVLLpkdYlrlRMTG--EFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGallpEVAKAWG 221
Cdd:COG0554 162 gtIDSWLI---W---KLTGgkVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPRSMLPEVRPSSEVFG----ETDPDLF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 222 MATVPVVagggdnaagavgvGM----------------------------VDAN---QAMLS----LGTSG------VYF 260
Cdd:COG0554 232 GAEIPIA-------------GIagdqqaalfgqacfepgmakntygtgcfLLMNtgdEPVRSknglLTTIAwglggkVTY 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 261 AVsEGFlskpesavhsfchalpqrwhlmsvMLSAASCLDWAAKLTGLSNVPALIAA-AQQADeSAEPVWFLPYLSGERTP 339
Cdd:COG0554 299 AL-EGS------------------------IFVAGAAVQWLRDGLGLIDSAAESEAlARSVE-DNGGVYFVPAFTGLGAP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 340 HNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHA-CGIKPQSVTLIGGGARSEYWRQMLADISGQQLDyRt 418
Cdd:COG0554 353 YWDPDARGAIFGLTRGTTRAHIARAALESIAYQTRDVLDAMEAdSGIPLKELRVDGGASANDLLMQFQADILGVPVE-R- 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131435 419 ggdvgP------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 |
1.45e-32 |
|
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: 129.53 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 2 YI-GIDLGTSGVKVILLNEQGEVVA-AQTEkLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQ--DVKALGIAGQM 77
Cdd:cd07786 1 YIlAIDQGTTSSRAILFDHDGNIVAvAQRE-FTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRasDIAAIGITNQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 78 HGATLLDAQQ-RVLRPAILWNDGRCAQECTLL-----EARVpqsRVITGNLMMPGFTAPKLLWVQRHEPE---------- 141
Cdd:cd07786 80 ETTVVWDRETgKPVYNAIVWQDRRTADICEELkaeghEEMI---REKTGLVLDPYFSATKIRWILDNVPGareraergel 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 142 IFRQIDKvllpkdYLRLRMTG--EFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGallpEVAKA 219
Cdd:cd07786 157 AFGTIDS------WLIWKLTGgkVHATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFG----YTDPD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 220 WGMATVPVVagggdnaagavgvGMVDANQAML-------------SLGTS-------GVYFAVSE-GFLS--------KP 270
Cdd:cd07786 227 LLGAEIPIA-------------GIAGDQQAALfgqacfepgmaknTYGTGcfmlmntGEKPVRSKnGLLTtiawqlggKV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 271 ESAvhsfchalpqrwhLMSVMLSAASCLDWaakltgLSNVPALIAAAQQADESAE------PVWFLPYLSGERTPHNNPQ 344
Cdd:cd07786 294 TYA-------------LEGSIFIAGAAVQW------LRDGLGLIESAAETEALARsvpdngGVYFVPAFTGLGAPYWDPD 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 345 AKGVFFGLTHQHGPNELARAVLEGVGYALAdgmDVVHA----CGIKPQSVTLIGGGARSEYWRQMLADISGQQLdyrtgg 420
Cdd:cd07786 355 ARGAIFGLTRGTTRAHIARAALESIAYQTR---DLLEAmeadSGIPLKELRVDGGASANDFLMQFQADILGVPV------ 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 16131435 421 dVGP------ALGAARLAQIAANPEKSLIELLPQLPLEQS---HLPDAQRYAAYQ 466
Cdd:cd07786 426 -ERPkvtettALGAAYLAGLAVGLWKSLDELAKLWQVDRRfepSMSEEEREALYA 479
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
2-472 |
1.90e-31 |
|
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: 126.29 E-value: 1.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 2 YIGIDLGTSGVKVILLNEQGEVVA-AQTEKLTVSRP-HPLWSEQDPEQWWQATDRAMK-ALGD-QHSLQDVKALGIAGQM 77
Cdd:cd07775 2 LLALDAGTGSGRAVIFDLEGNQIAvAQREWRHKEVPdVPGSMDFDTEKNWKLICECIReALKKaGIAPKSIAAISTTSMR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 78 HGATLLDAQQRVLrpailWN----DGRCAQECTLLEARVPQSR----VITGNLMMPGfTAPKLLWVQRHEPEIFRQIDKV 149
Cdd:cd07775 82 EGIVLYDNEGEEI-----WAcanvDARAAEEVSELKELYNTLEeevyRISGQTFALG-AIPRLLWLKNNRPEIYRKAAKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 150 LLPKDYLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGMAT-VPVV 228
Cdd:cd07775 156 TMLSDWIAYKLSGELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKEAAEETGLKEgTPVV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 229 AGGGDNAAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLMSVMLSAASCLDW-------- 300
Cdd:cd07775 236 VGGGDVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPAMNIRVNCHVIPDMWQAEGISFFPGLVMRWfrdafcae 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 301 ---AAKLTGlsnvpalIAAAQQADESAEPV-----WFLPYLSGERTPHNNPQAKGVFFGLT---HQHGPNELARAVLEGV 369
Cdd:cd07775 316 ekeIAERLG-------IDAYDLLEEMAKDVppgsyGIMPIFSDVMNYKNWRHAAPSFLNLDidpEKCNKATFFRAIMENA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 370 GYALADGMDVVHAC-GIKPQSVTLIGGGARSEYWRQMLADISGQQLdyrTGGDV--GPALGAARLAQIAANPEKSLIELL 446
Cdd:cd07775 389 AIVSAGNLERIAEFsGIFPDSLVFAGGASKGKLWCQILADVLGLPV---KVPVVkeATALGAAIAAGVGAGIYSSLEEAV 465
|
490 500
....*....|....*....|....*..
gi 16131435 447 PQL-PLEQSHLPDAQRYAAYQPRRETF 472
Cdd:cd07775 466 ESLvKWEREYLPNPENHEVYQDLYEKW 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 |
9.65e-30 |
|
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: 121.48 E-value: 9.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 2 YIG-IDLGTSGVKVILLNEQGEVVAAQTEKLTVSRPHPLWSEQDPEQWWQATDRAM-------KALGdqHSLQDVKALGI 73
Cdd:cd07792 2 LVGaIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIeeaveklKALG--ISPSDIKAIGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 74 AGQMHGATLLDAQQRV-LRPAILWNDGRCAQECTLLEARVPQS----RVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDK 148
Cdd:cd07792 80 TNQRETTVVWDKSTGKpLYNAIVWLDTRTSDTVEELSAKTPGGkdhfRKKTGLPISTYFSAVKLRWLLDNVPEVKKAVDD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 149 vllpKD--------YLRLRMTGE-----FASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGallpE 215
Cdd:cd07792 160 ----GRllfgtvdsWLIWNLTGGknggvHVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEVYG----K 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 216 VAKAWgMATVPVVagggdnaagavgvGMV-------------DANQAMLSLGTsGVYFAVSEGflskpESAVHSFCHAL- 281
Cdd:cd07792 232 IASGP-LAGVPIS-------------GCLgdqqaalvgqgcfKPGEAKNTYGT-GCFLLYNTG-----EEPVFSKHGLLt 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 282 ----------PQRWHLM-SVMLsAASCLDWAAKLTGLSNVPALIAA-AQQADESAEpVWFLPYLSGERTPHNNPQAKGVF 349
Cdd:cd07792 292 tvayklgpdaPPVYALEgSIAI-AGAAVQWLRDNLGIISSASEVETlAASVPDTGG-VYFVPAFSGLFAPYWRPDARGTI 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 350 FGLTH----QHgpneLARAVLEGVGYALADGMDVVHA-CGIKPQSVTLIGGGARSEYWRQMLADISGQQLdyrtggdVGP 424
Cdd:cd07792 370 VGLTQfttkAH----IARAALEAVCFQTREILDAMNKdSGIPLTSLRVDGGMTKNNLLMQIQADILGIPV-------ERP 438
|
490 500
....*....|....*....|....*..
gi 16131435 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 |
1.36e-29 |
|
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: 114.73 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 249 AMLSLGTSGVYFAVSEgflsKPESAVHSFCH-----ALPQRWHLMSVMLSAASCLDW----------AAKLTGLSNVPAL 313
Cdd:pfam02782 1 LAISAGTSSFVLVETP----EPVLSVHGVWGpytneMLPGYWGLEGGQSAAGSLLAWllqfhglreeLRDAGNVESLAEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 314 IAAAQQADesAEPVWFLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHAC-GIKPQSVTL 392
Cdd:pfam02782 77 AALAAVAP--AGGLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQeGHPIDTIHV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16131435 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 |
9.11e-25 |
|
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: 106.46 E-value: 9.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 2 YIGIDLGTSGVKVILlneqGEVvaaQTEKLT---VSR-PHPLWSEQDPEQW-----WQATDRAMKALGDQHslQDVKALG 72
Cdd:cd07771 2 YLAVDLGASSGRVIL----GSL---DGGKLEleeIHRfPNRPVEINGHLYWdidrlFDEIKEGLKKAAEQG--GDIDSIG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 73 IA--GQMHGatLLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRV--ITGNLMMPGFTAPKLLWVQRHEPEIFRQIDK 148
Cdd:cd07771 73 IDtwGVDFG--LLDKNGELLGNPVHYRDPRTEGMMEELFEKISKEELyeRTGIQFQPINTLYQLYALKKEGPELLERADK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 149 VLLPKDYLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGMATVPVv 228
Cdd:cd07771 151 LLMLPDLLNYLLTGEKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLKPEVAEELGLKGIPV- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 229 agggdnaagaVGVG------------MVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSF---CHA---------LPQR 284
Cdd:cd07771 230 ----------IAVAshdtasavaavpAEDEDAAFISSGTWSLIGVELDEPVITEEAFEAGFtneGGAdgtirllknITGL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 285 WhlmsvMLSaaSCL-DWAAKLTGLSnVPALIAAAQQADESA------EPVWFLP---------YLsgERTPHNNPQAKGv 348
Cdd:cd07771 300 W-----LLQ--ECRrEWEEEGKDYS-YDELVALAEEAPPFGafidpdDPRFLNPgdmpeairaYC--RETGQPVPESPG- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 349 ffglthqhgpnELARAVLEGVGYALADGM-DVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQLdyRTGGDVGPALG 427
Cdd:cd07771 369 -----------EIARCIYESLALKYAKTIeELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLPV--IAGPVEATAIG 435
|
490
....*....|....*....
gi 16131435 428 AArLAQ-IAANPEKSLIEL 445
Cdd:cd07771 436 NL-LVQlIALGEIKSLEEG 453
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
2-437 |
5.19e-23 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 101.70 E-value: 5.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 2 YIG-IDLGTSGVKVILLNEQGEVVAAQTEKLTVSRPHPLWSEQDPEQWWQATDRAM-----KALGDQHSLQD-VKALGIA 74
Cdd:PLN02295 1 FVGaIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIakaleKAAAKGHNVDSgLKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 75 GQMHGATLLDAQQ-RVLRPAILWNDGRCAQECTLLEARVPQS----RVITGNLMMPGFTAPKLLWVQRHEPEI------- 142
Cdd:PLN02295 81 NQRETTVAWSKSTgRPLYNAIVWMDSRTSSICRRLEKELSGGrkhfVETCGLPISTYFSATKLLWLLENVDAVkeavksg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 143 ---FRQIDKVLLpkdylrLRMTG-----EFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGallp 214
Cdd:PLN02295 161 dalFGTIDSWLI------WNLTGgasggVHVTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIG---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 215 EVAKAWGMATVPVVAGggdnaagavgvgMVDANQAMLS-------------------LGTSGVYFAVSEGFLSK------ 269
Cdd:PLN02295 231 TIAKGWPLAGVPIAGC------------LGDQHAAMLGqrcrpgeakstygtgcfilLNTGEEVVPSKHGLLTTvayklg 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 270 PESAVhsfCHALPQrwhlmSVMLSAAScLDWAAKLTGLSNVPALIAAAQQADESAEPVWFLPYLSGERTPHNNPQAKGVF 349
Cdd:PLN02295 299 PDAPT---NYALEG-----SVAIAGAA-VQWLRDNLGIIKSASEIEALAATVDDTGGVYFVPAFSGLFAPRWRDDARGVC 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 350 FGLTHQHGPNELARAVLEGVGYALADGMDVVHA-CGIKPQSVTLI-----GGGARSEYWRQMLADISGQQL----DYRTg 419
Cdd:PLN02295 370 VGITRFTNKAHIARAVLESMCFQVKDVLDAMRKdAGEEKSHKGLFllrvdGGATANNLLMQIQADLLGSPVvrpaDIET- 448
|
490
....*....|....*...
gi 16131435 420 gdvgPALGAARLAQIAAN 437
Cdd:PLN02295 449 ----TALGAAYAAGLAVG 462
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
2-466 |
1.19e-22 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 100.67 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 2 YIG-IDLGTSGVKVILLNEQGEVVA-AQTEkLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQ--DVKALGIAGQM 77
Cdd:PRK00047 6 YILaLDQGTTSSRAIIFDHDGNIVSvAQKE-FTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISpdQIAAIGITNQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 78 HGATLLDaqQRVLRP---AILWNDGRCAQECTLLEARvPQSRVI---TGNLMMPGFTAPKLLWVQRHEPE---------- 141
Cdd:PRK00047 85 ETTVVWD--KETGRPiynAIVWQDRRTADICEELKRD-GYEDYIrekTGLVIDPYFSGTKIKWILDNVEGareraekgel 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 142 IFRQIDKVLLPKdylrlrMTGE--FASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGallPEVAKA 219
Cdd:PRK00047 162 LFGTIDTWLVWK------LTGGkvHVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYG---KTNPYG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 220 WGMATVPVVagggdnaagavgvGMVDANQAML-------------SLGTsGVYFAVSEGflskpESAVHS-------FCH 279
Cdd:PRK00047 233 FFGGEVPIA-------------GIAGDQQAALfgqlcfepgmaknTYGT-GCFMLMNTG-----EKAVKSengllttIAW 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 280 ALPQRWHLM---SVMLsAASCLDW---AAKLtgLSNVPALIAAAQQAdESAEPVWFLPYLSGERTPHNNPQAKGVFFGLT 353
Cdd:PRK00047 294 GIDGKVVYAlegSIFV-AGSAIQWlrdGLKI--ISDASDSEALARKV-EDNDGVYVVPAFTGLGAPYWDSDARGAIFGLT 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 354 HQHGPNELARAVLEGVGYALADGMDVVHA-CGIKPQSVTLIGGGARSEYWRQMLADISGQQLdyrtggdVGP------AL 426
Cdd:PRK00047 370 RGTTKEHIIRATLESIAYQTRDVLDAMQAdSGIRLKELRVDGGAVANNFLMQFQADILGVPV-------ERPvvaettAL 442
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 16131435 427 GAARLAQIAANPEKSLIELLPQLPLEQS---HLPDAQRYAAYQ 466
Cdd:PRK00047 443 GAAYLAGLAVGFWKDLDELKEQWKIDRRfepQMDEEEREKLYA 485
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
5-482 |
6.62e-22 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 98.54 E-value: 6.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 5 IDLGTSGVKVILLNEQG-EVVAAQTEKLTVSRPH-PLWSEQDPEQWWQATDRAMK-ALGD-QHSLQDVKALGIAGQMHGA 80
Cdd:PRK10939 8 LDAGTGSIRAVIFDLNGnQIAVGQAEWRHLAVPDvPGSMEFDLEKNWQLACQCIRqALQKaGIPASDIAAVSATSMREGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 81 TLLDAQQRVLrpailWN----DGRCAQECTLLEARVP--QSRV--ITGNLMMPGfTAPKLLWVQRHEPEIFRQIDKVLLP 152
Cdd:PRK10939 88 VLYDRNGTEI-----WAcanvDARASREVSELKELHNnfEEEVyrCSGQTLALG-ALPRLLWLAHHRPDIYRQAHTITMI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 153 KDYLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEITGALLPEVAKAWGMAT-VPVVAGG 231
Cdd:PRK10939 162 SDWIAYMLSGELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTAKAAAETGLRAgTPVVMGG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 232 GDNAAGAVGVGMVDANQAMLSLGTsgvyF-----AVSEGFlSKPESAVHSFCHALPQRWHLMSVMLSAASCLDW------ 300
Cdd:PRK10939 242 GDVQLGCLGLGVVRPGQTAVLGGT----FwqqvvNLPAPV-TDPNMNIRINPHVIPGMVQAESISFFTGLTMRWfrdafc 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 301 -----AAKLTGLSNVPALIAAAQQADESAEPVwfLPYLSGERTPHNNPQAKGVFFGLT---HQHGPNELARAVLEGVGYA 372
Cdd:PRK10939 317 aeeklLAERLGIDAYSLLEEMASRVPVGSHGI--IPIFSDVMRFKSWYHAAPSFINLSidpEKCNKATLFRALEENAAIV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 373 LADGMDVVHA-CGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTGGDVgPALGAARLAQIAANPEKSLIELLPQL-P 450
Cdd:PRK10939 395 SACNLQQIAAfSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEA-TALGCAIAAGVGAGIYSSLAETGERLvR 473
|
490 500 510
....*....|....*....|....*....|..
gi 16131435 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 |
5.27e-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: 5.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 1 MYIGIDLGTSGVKVILLNEQGEVVAAQTEKLTVSRPH------------PLWSEQDPEQWWQATDRA---MKALGDQhsL 65
Cdd:cd07776 1 LYLGLDLSTQSLKAVVIDSDLKVVAEESVNFDSDLPEygtkggvhrdgdGGEVTSPVLMWVEALDLLlekLKAAGFD--F 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 66 QDVKALGIAGQMHG---------ATL--LDAQQRVLrpAIL-----------WNDGRCAQECTLLEARV--PQSRV-ITG 120
Cdd:cd07776 79 SRVKAISGSGQQHGsvywskgaeSALanLDPSKSLA--EQLegafsvpdspiWMDSSTTKQCRELEKAVggPEALAkLTG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 121 NLMMPGFTAPKLLWVQRHEPEIFRQIDKV---------LLpkdylrlrmTGEFAS-DMSDAAGTMWLDVAKRDWSDVMLQ 190
Cdd:cd07776 157 SRAYERFTGPQIAKIAQTDPEAYENTERIslvssflasLL---------LGRYAPiDESDGSGMNLMDIRSRKWSPELLD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 191 AC---DLsRDQMPALYEGSEITGALLPEVAKAWGM--------------ATVpvvagggdnaagavgVGM-VDANQAMLS 252
Cdd:cd07776 228 AAtapDL-KEKLGELVPSSTVAGGISSYFVERYGFspdclvvaftgdnpASL---------------AGLgLEPGDVAVS 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 253 LGTSGVYFAVSEGFLSKPESavHSFCHALPQRWHLMsvML-------------SAASCLDWaakltglSNVPALIAAAQQ 319
Cdd:cd07776 292 LGTSDTVFLVLDEPKPGPEG--HVFANPVDPGSYMA--MLcykngslarervrDRYAGGSW-------EKFNELLESTPP 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 320 ADESaepVWFLPYLSGERTPHnnpqAKGVFFGLTHQHGPNEL------ARAVLEgvGYALAdgMdVVHA----CGIKPQS 389
Cdd:cd07776 361 GNNG---NLGLYFDEPEITPP----VPGGGRRFFGDDGVDAFfdpaveVRAVVE--SQFLS--M-RLHAerlgSDIPPTR 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 390 VTLIGGGARSEYWRQMLADISGQQLdYRTGGDVGPALGAARLAQIAANPEKSLIELLPQLPLEQSHL-----PDAQRYAA 464
Cdd:cd07776 429 ILATGGASANKAILQVLADVFGAPV-YTLDVANSAALGAALRAAHGLLCAGSGDFSPEFVVFSAEEPklvaePDPEAAEV 507
|
....*.
gi 16131435 465 YQPRRE 470
Cdd:cd07776 508 YDKLLE 513
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
2-478 |
5.48e-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: 92.60 E-value: 5.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 2 YIGIDLGTSGVKVILLNEQGEVVAAQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQ--HSLQDVKALGIAgqmhg 79
Cdd:cd07782 2 YIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGagVDPEQVKGIGFD----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 80 AT----LLDAQQRVL---------RPAILWNDGRC---AQECTLLEARVPQSrviTGNLMMPGFTAPKLLWVQRHEPEIF 143
Cdd:cd07782 77 ATcslvVLDAEGKPVsvspsgddeRNVILWMDHRAveeAERINATGHEVLKY---VGGKISPEMEPPKLLWLKENLPETW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 144 RQIDKVL-LPkDYLRLRMTGEFASDMSdaagTM---WLDVAKRD----WSDVMLQACDL------------SRDQMPaly 203
Cdd:cd07782 154 AKAGHFFdLP-DFLTWKATGSLTRSLC----SLvckWTYLAHEGseggWDDDFFKEIGLedlvednfakigSVVLPP--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 204 eGSEITGALLPEVAKAWGM-ATVPVvagggdnaagavGVGMVDAN---------------------QAMLSL--GTSGVY 259
Cdd:cd07782 226 -GEPVGGGLTAEAAKELGLpEGTPV------------GVSLIDAHagglgtlgadvgglpceadplTRRLALicGTSSCH 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 260 FAVSEGFLSKP------ESAVhsfchaLPQRW----------HLMSVML---SAASCLDWAAKLTGLSnVPALIAA--AQ 318
Cdd:cd07782 293 MAVSPEPVFVPgvwgpyYSAM------LPGLWlneggqsatgALLDHIIethPAYPELKEEAKAAGKS-IYEYLNErlEQ 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 319 QADESAEPVWFL-------PYLSGERTPHNNPQAKGVFFGLTHQHGPNELAR---AVLEGVGYALADGMDVVHACGIKPQ 388
Cdd:cd07782 366 LAEEKGLPLAYLtrdlhvlPDFHGNRSPLADPTLRGMISGLTLDTSLDDLALlylATLQALAYGTRHIIEAMNAAGHKID 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 389 SVTLIGGGARSEYWRQMLADISGQQLdyrtggdVGPA------LGAARLAQIAANPEKSLIELLPQL-PLEQSHLPDAQR 461
Cdd:cd07782 446 TIFMCGGLSKNPLFVQLHADVTGCPV-------VLPKepeavlLGAAILGAVASGDFPSLWDAMAAMsGPGKVVEPNEEL 518
|
570
....*....|....*..
gi 16131435 462 YAAYQPRRETFRRLYQQ 478
Cdd:cd07782 519 KKYHDRKYEVFLKMYED 535
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
2-479 |
2.44e-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: 90.76 E-value: 2.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 2 YIGIDLGTSGVKVILLN-EQG-EVVAAQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQ--DVKALGIAGQM 77
Cdd:cd07768 2 GIGVDVGTSSARAGVYDlYAGlEMAQEPVPYYQDSSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDayEVKGCGVDATC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 78 HGATL-LDAQQRVLRPA-------ILWNDGRCAQECTLLEARVPQSRV-ITGNLMMPGFTAPKLLWVQRHEPEIFRQIDK 148
Cdd:cd07768 82 SLAIFdREGTPLMALIPypnednvIFWMDHSAVNEAQWINMQCPQQLLdYLGGKISPEMGVPKLKYFLDEYSHLRDKHFH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 149 VLLPKDYLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACDLSRDQMPALYEGSEI------TGALLPEVAKAWGM 222
Cdd:cd07768 162 IFDLHDYIAYELTRLYEWNICGLLGKENLDGEESGWSSSFFKNIDPRLEHLTTTKNLPSNvpigttSGVALPEMAEKMGL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 223 ---ATVPVVAGGGDNAAGAVGVGMVDANQAMLSlGTSGVYFAVSE------GFLSKPESAVhsfchaLPQRWHLMSVMLS 293
Cdd:cd07768 242 hpgTAVVVSCIDAHASWFAVASPHLETSLFMIA-GTSSCHMYGTTisdripGVWGPFDTII------DPDYSVYEAGQSA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 294 AASCLDW-------AAKLTGLSNVPALI-AAAQQADESAEPVWF-------LPYLSGERTPHNNPQAKGVFFGLTHQHGP 358
Cdd:cd07768 315 TGKLIEHlfeshpcARKFDEALKKGADIyQVLEQTIRQIEKNNGlsihiltLDMFFGNRSEFADPRLKGSFIGESLDTSM 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 359 NELA---RAVLEGVGYALADGMDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQLdYRTGGDVGPALGAARLAQIA 435
Cdd:cd07768 395 LNLTykyIAILEALAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAI-IKPKENMMGILGAAVLAKVA 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 16131435 436 ANpEKSLIELLPQLPLEQSHL-----PDAQRYAAYQPRRetfRRLYQQL 479
Cdd:cd07768 474 AG-KKQLADSITEADISNDRKsetfePLAYRLGADYILL---YKLLCVK 518
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
5-221 |
2.21e-14 |
|
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: 74.99 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 5 IDLGTSGVKVILLNEQGEVVAAQTEKLTVSrPHPLWSEQDPEQWWQATDRAMKALGDQHslqDVKALGIAGqmHGAT--L 82
Cdd:cd07772 5 FDIGKTNKKLLLFDENGEVLAERSTPNPEI-EEDGYPCEDVEAIWEWLLDSLAELAKRH---RIDAINFTT--HGATfaL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 83 LDAQQRVLRP--AILWN-DGRCAQEctLLEARVPqsRVITGNLMMPGFT--APKLLWVQRHEPEIFRQIDKVL-LPkDYL 156
Cdd:cd07772 79 LDENGELALPvyDYEKPiPDEINEA--YYAERGP--FEETGSPPLPGGLnlGKQLYWLKREKPELFARAKTILpLP-QYW 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131435 157 RLRMTGEFASDMSdAAGT---MWlDVAKRDWSDVmLQACDLSRdQMPALYEGSEITGALLPEVAKAWG 221
Cdd:cd07772 154 AWRLTGKAASEIT-SLGChtdLW-DFEKNEYSSL-VKKEGWDK-LFPPLRKAWEVLGPLRPDLARRTG 217
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
315-479 |
3.04e-11 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 65.64 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 315 AAAQQADESAEPVwfLPYLSGERTPHNNPQAKGVFFGLTHQHGPNELARAVLEGVGYALADGMDVVHACGIKPQSVTLIG 394
Cdd:PRK04123 369 AAKQPPGEHGLVA--LDWFNGRRTPLADQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECFEDQGVPVEEVIAAG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 395 GGAR-SEYWRQMLADISGQQLDYRTgGDVGPALGAARLAQIAANPEKSLIELLPQL--PLEQSHLPDAQRYAAYQPRRET 471
Cdd:PRK04123 447 GIARkNPVLMQIYADVLNRPIQVVA-SDQCPALGAAIFAAVAAGAYPDIPEAQQAMasPVEKTYQPDPENVARYEQLYQE 525
|
....*...
gi 16131435 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 |
6.97e-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: 51.64 E-value: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 2 YIGIDLGTSGVKVILLNEQGEVVAAQTEKLT-VSRPHPLWS-EQDPEQWWQATDRAMKALGDQHSLQDVKALGIAgqmhg 79
Cdd:cd07778 2 GIGIDVGSTSVRIGIFDYHGTLLATSERPISyKQDPKDLWFvTQSSTEIWKAIKTALKELIEELSDYIVSGIGVS----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 80 ATL------LDAQQRVLRP-------------AILWNDGRCAQECTLLEARVPQSRVI-TGNLMMPGFTAPKLLWVQRHE 139
Cdd:cd07778 77 ATCsmvvmqRDSDTSYLVPynviheksnpdqdIIFWMDHRASEETQWLNNILPDDILDyLGGGFIPEMAIPKLKYLIDLI 156
|
...
gi 16131435 140 PEI 142
Cdd:cd07778 157 KED 159
|
|
| PLN02669 |
PLN02669 |
xylulokinase |
1-191 |
2.61e-06 |
|
xylulokinase
Pssm-ID: 178274 [Multi-domain] Cd Length: 556 Bit Score: 49.77 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 1 MYIGIDLGTSGVKVILLNEQGEVVAAQTEKLTVSRPHPLWSE---QDPEQ----------WWQATDRAMKALGDQH-SLQ 66
Cdd:PLN02669 9 LFLGFDSSTQSLKATVLDSNLRIVASEIVHFDSDLPHYGTKDgvyRDPKVngrivsptlmWVEALDLLLQKLAKEKfPFH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 67 DVKALGIAGQMHGA-----------TLLDAQQRV---LRPAI------LWNDGRCAQECTLLEARV---PQSRVITGNLM 123
Cdd:PLN02669 89 KVVAISGSGQQHGSvywrkgasavlKSLDPSKSLvaqLQDAFstkdspIWMDSSTTKQCREIEEAVggaAELSKLTGSRA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131435 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 |
1.88e-05 |
|
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: 46.43 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 1 MYIGIDLGTSGVKVILLNEQGEVVAaqteklTVSRPHPlwSEQDPEQWWQATDRAMKALGDQH--SLQDVKALGIAgqMH 78
Cdd:COG1940 6 YVIGIDIGGTKIKAALVDLDGEVLA------RERIPTP--AGAGPEAVLEAIAELIEELLAEAgiSRGRILGIGIG--VP 75
|
90 100
....*....|....*....|...
gi 16131435 79 GatLLDAQQ-RVLRPAIL--WND 98
Cdd:COG1940 76 G--PVDPETgVVLNAPNLpgWRG 96
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
82-189 |
3.13e-04 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 43.17 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 82 LLDAQQRVLRPAILWNDGRCAQECTLLEARVPQSRVI--TGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLRLR 159
Cdd:PRK10640 70 LLDKQGQRVGLPVSYRDSRTDGVMAQAQQQLGKRDIYrrSGIQFLPFNTLYQLRALTEQQPELIAQVAHALLIPDYFSYR 149
|
90 100 110
....*....|....*....|....*....|
gi 16131435 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 |
8.49e-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: 37.83 E-value: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131435 3 IGIDLGTSGVKVILLNEQGEVVAaqteklTVSRPHPlwSEQDPEQWWQATDRAMKALGDQHSL-QDVKALGIAgqMHGat 81
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILA------RERVPTP--AEEGPEAVLDRIAELIEELLAEAGVrERILGIGIG--VPG-- 68
|
90 100
....*....|....*....|
gi 16131435 82 LLDAQQ-RVLRPAIL--WND 98
Cdd:cd23763 69 PVDPETgIVLFAPNLpwWKN 88
|
|
| |
