|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
4-443 |
0e+00 |
|
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: 625.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 4 YWLGLDCGGSWLKAGLYDREGREAGVQRLPLCALSPQPGWAERDMAELWQCCMAVIRALLTHSGVSGEQIVGIGISAQGK 83
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 84 GLFLLDKNDKPLGNAILSSDRRAMEIVRRWQEDGIPEKLYPLTRQTLWTGHPVSLLRWLKEHEPERYAQIGCVMMTHDYL 163
Cdd:cd07802 81 GLYLVDKDGKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKENEPERYDRIRTVLFCKDWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 164 RWCLTGVKGCEESNISeSNLYNMSLGEYDPCLTDWLGIAEINHALPPVVGSAEICGEITAQTAALTGLKAGTPVVGGLFD 243
Cdd:cd07802 161 RYRLTGEISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEELKDKLPPLVPSTEIAGRVTAEAAALTGLPEGTPVAAGAFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 244 VVSTALCAGIEDEFTLNAVMGTWAVTSGITRGLRDGEAhPYVYGRYVNDGEFIVHEASPTSSGNLEWFTAQW-------G 316
Cdd:cd07802 240 VVASALGAGAVDEGQLCVILGTWSINEVVTDEPVVPDS-VGSNSLHADPGLYLIVEASPTSASNLDWFLDTLlgeekeaG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 317 EISFDEINQAVASLPKAGGDLFFLPFLYGSNAGLEMTSGFYGMQAIHTRAHLLQAIYEGVVFSHMTHLNRMRERFtDVHT 396
Cdd:cd07802 319 GSDYDELDELIAAVPPGSSGVIFLPYLYGSGANPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHRDHLERLLVAR-KPET 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 16131451 397 LRVTGGPAHSDVWMQMLADVSGLRIELPQVEETGCFGAALAARVGTG 443
Cdd:cd07802 398 IRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
3-492 |
8.42e-176 |
|
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: 503.21 E-value: 8.42e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 3 QYWLGLDCGGSWLKAGLYDREGREAGVQRLPLCALSPQPGWAERDMAELWQCCMAVIRALLTHSGVSGEQIVGIGISAQG 82
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 83 KGLFLLDKNDKPLGNAILSSDRRAMEIVRRWQEDGIPEKLYPLTRQTLWTGHPVSLLRWLKEHEPERYAQIGCVMMTHDY 162
Cdd:COG1070 81 HGLVLLDADGEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIAKVLLPKDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 163 LRWCLTGVKGCEESNISESNLYNMSLGEYDPCLTDWLGIAEinHALPPVVGSAEICGEITAQTAALTGLKAGTPVVGGLF 242
Cdd:COG1070 161 LRYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDR--ELLPELVPPGEVAGTLTAEAAAETGLPAGTPVVAGAG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 243 DVVSTALCAGIEDEFTLNAVMGTWAVTSGITRGLRDGEAHPYVYGRYVNDGEFIVHEASPTSSGNLEWFTAQWGE---IS 319
Cdd:COG1070 239 DNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFCHAVPGRWLPMGATNNGGSALRWFRDLFADgelDD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 320 FDEINQAVASLPKAGGDLFFLPFLYGSNAGL---EMTSGFYGMQAIHTRAHLLQAIYEGVVFSHMTHLNRMRERFTDVHT 396
Cdd:COG1070 319 YEELNALAAEVPPGADGLLFLPYLSGERTPHwdpNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEALEEAGVKIDR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 397 LRVTGGPAHSDVWMQMLADVSGLRIELPQVEETGCFGAALAARVGTGVYHNFSEAQRDLRHPVRTLLPDMTAHQLYQKKY 476
Cdd:COG1070 399 IRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMVRVGETIEPDPENVAAYDELY 478
|
490
....*....|....*.
gi 16131451 477 QRYQHLIAALQGFHAR 492
Cdd:COG1070 479 ERYRELYPALKPLFER 494
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
4-250 |
1.95e-128 |
|
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: 373.21 E-value: 1.95e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 4 YWLGLDCGGSWLKAGLYDREGREAGVQRLPLCALSPQPGWAERDMAELWQCCMAVIRALLTHSGVSGEQIVGIGISAQGK 83
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 84 GLFLLDKNDKPLGNAILSSDRRAMEIVRRWQEDGIPEKLYPLTRQTLWTGHPVSLLRWLKEHEPERYAQIGCVMMTHDYL 163
Cdd:pfam00370 81 GTVLLDKNDKPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHKFLTIHDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 164 RWCLTGVKGCEESNISESNLYNMSLGEYDPCLTDWLGIAEInhALPPVVGSAEICGEITAQTAALTGLKAGTPVVGGLFD 243
Cdd:pfam00370 161 RWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRD--HLPPLVESSEIYGELNPELAAMWGLDEGVPVVGGGGD 238
|
....*..
gi 16131451 244 VVSTALC 250
Cdd:pfam00370 239 QQAAAFG 245
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
4-480 |
6.46e-120 |
|
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: 360.32 E-value: 6.46e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 4 YWLGLDCGGSWLKAGLYDREGREAGV--QRLPLcaLSPQPGWAERDMAELWQCCMAVIRALLTHSGVSGEQIVGIGISAQ 81
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASasAEYPT--SSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 82 GKGLFLLDKNDKPLGNAILSSDRRAMEIVRRWQEDgIPEKLYPLTRQTLWTGHPVSLLRWLKEHEPERYAQIGCVMMTHD 161
Cdd:cd07808 79 MHGLVLLDKNGRPLRPAILWNDQRSAAECEELEAR-LGDEILIITGNPPLPGFTLPKLLWLKENEPEIFARIRKILLPKD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 162 YLRWCLTGVKGCEESNISESNLYNMSLGEYDPCLTDWLGIAEinHALPPVVGSAEICGEITAQTAALTGLKAGTPVVGGL 241
Cdd:cd07808 158 YLRYRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDP--SILPPIVESTEIVGTLTPEAAEELGLPEGTPVVAGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 242 FDVVSTALCAGIEDEFTLNAVMGTWAVTSGITRGLRDGEAHPYVYGRYVNDGEFIVHEASPTSSGNLEWFTAQWGE--IS 319
Cdd:cd07808 236 GDNAAAALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLHTFPHAVPGKWYAMGVTLSAGLSLRWLRDLFGPdrES 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 320 FDEINQAVASLPKAGGDLFFLPFLYGS-----NAglEMTSGFYGMQAIHTRAHLLQAIYEGVVFSHMTHLNRMRERFTDV 394
Cdd:cd07808 316 FDELDAEAAKVPPGSEGLLFLPYLSGErtpywDP--NARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVLKELGIKV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 395 HTLRVTGGPAHSDVWMQMLADVSGLRIELPQVEETGCFGAALAARVGTGVYHNFSEAQRDLRHPVRTLLPDMTAHQLYQK 474
Cdd:cd07808 394 KEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAACIKIEKTIEPDPERHEAYDE 473
|
....*.
gi 16131451 475 KYQRYQ 480
Cdd:cd07808 474 LYARYR 479
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
4-438 |
1.51e-114 |
|
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: 343.39 E-value: 1.51e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 4 YWLGLDCGGSWLKAGLYDREGREAGVQRLPLCALSPQPGWAERDMAELWQCCMAVIRALLTHSGVSGEQIVGIGISAQGK 83
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 84 GLFLLDKNDKPLGNAILSSDRRAmeivrrwqedgipeklypltrqtlwtghpvsllrwlkeheperyaqigCVMMTHDYL 163
Cdd:cd00366 81 GVVLVDADGNPLRPAIIWLDRRA------------------------------------------------KFLQPNDYI 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 164 RWCLTGVKGCEESNISESNLYNMSLGEYDPCLTDWLGIAEinHALPPVVGSAEICGEITAQTAALTGLKAGTPVVGGLFD 243
Cdd:cd00366 113 VFRLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPR--EKLPPIVESGEVVGRVTPEAAEETGLPAGTPVVAGGGD 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 244 VVSTALCAGIEDEFTLNAVMGTWAVTSGITRGLRDgeAHPYVYGRYVNDGEFIVHEASPTSSG-NLEWFTAQWGEISFDE 322
Cdd:cd00366 191 TAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEPVP--PDPRLLNRCHVVPGLWLLEGAINTGGaSLRWFRDEFGEEEDSD 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 323 IN------QAVASLPKAGGdLFFLPFLYGSNAGLEMTS---GFYGMQAIHTRAHLLQAIYEGVVFSHMTHLNRMRERFTD 393
Cdd:cd00366 269 AEyegldeLAAEVPPGSDG-LIFLPYLSGERSPIWDPAargVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEILEELGVK 347
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 16131451 394 VHTLRVTGGPAHSDVWMQMLADVSGLRIELPQVEETGCFGAALAA 438
Cdd:cd00366 348 IKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
4-479 |
5.15e-109 |
|
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: 332.18 E-value: 5.15e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 4 YWLGLDCGGSWLKAGLYDREGREAGVQRLPLCALSPQPGWAERDMAELWQC-CMAViRALLTHSGVSGEQIVGIGISAQG 82
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAvCRAT-RALLEKSGIDPSDIAAIAFSGQM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 83 KGLFLLDKNDKPLGNAILSSDRRAMEIVRRWQEDGIPEKLYPLTRQTLWTGH-PVSLLRWLKEHEPERYAQIGCVMMTHD 161
Cdd:cd07805 80 QGVVPVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLGGGNPPSGKdPLAKILWLKENEPEIYAKTHKFLDAKD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 162 YLRWCLTGVKGCEESNISESNLYNMSLGEYDPcltDWLGIAEINHA-LPPVVGSAEICGEITAQTAALTGLKAGTPVVGG 240
Cdd:cd07805 160 YLNFRLTGRAATDPSTASTTGLMDLRKRRWSE---ELLRAAGIDPDkLPELVPSTEVVGELTPEAAAELGLPAGTPVVGG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 241 LFDVVSTALCAGIEDEFTLNAVMGT--WAVTSgITRGLRDGEAHPYVYgRYVNDGEFIVHEASPTSSGNLEWFTAQW--- 315
Cdd:cd07805 237 GGDAAAAALGAGAVEEGDAHIYLGTsgWVAAH-VPKPKTDPDHGIFTL-ASADPGRYLLAAEQETAGGALEWARDNLggd 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 316 ---GEISFDEINQAVASLPKAGGDLFFLPFLYGSNAGLE---MTSGFYGMQAIHTRAHLLQAIYEGVVFSHMTHLNRMRE 389
Cdd:cd07805 315 edlGADDYELLDELAAEAPPGSNGLLFLPWLNGERSPVEdpnARGAFIGLSLEHTRADLARAVLEGVAFNLRWLLEALEK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 390 RFTDVHTLRVTGGPAHSDVWMQMLADVSGLRIELPQV-EETGCFGAALAARVGTGVYHNFSEAqRDLRHPVRTLLPDMTA 468
Cdd:cd07805 395 LTRKIDELRLVGGGARSDLWCQILADVLGRPVEVPENpQEAGALGAALLAAVGLGLLKSFDEA-KALVKVEKVFEPDPEN 473
|
490
....*....|.
gi 16131451 469 HQLYQKKYQRY 479
Cdd:cd07805 474 RARYDRLYEVF 484
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
4-443 |
3.55e-104 |
|
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: 318.80 E-value: 3.55e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 4 YWLGLDCGGSWLKAGLYDREGREAGVQRLPLCALSPQPGWAERDMAELWQCCMAVIRALLTHSGVSGEQIVGIGISAQGK 83
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 84 GLFLLDKNDKPLGNAILSSDRRAMEIVRRWQEDGIPEKLYPLTRQTLWTGHPVSLLRWLKEHEPERYAQIGCVMMTHDYL 163
Cdd:cd24121 81 GTWLVDEDGRPVRDAILWLDGRAADIVERWQADGIAEAVFEITGTGLFPGSQAAQLAWLKENEPERLERARTALHCKDWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 164 RWCLTGVKGCEESNISESnLYNMSLGEYDPCLTDWLGIAEINHALPPVVGSAEICGEITAQTAALTGLKAGTPVVGGLFD 243
Cdd:cd24121 161 FYKLTGEIATDPSDASLT-FLDFRTRQYDDEVLDLLGLEELRHLLPPIRPGTEVIGPLTPEAAAATGLPAGTPVVLGPFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 244 VVSTALCAGIEDEFTLNAVMGTWAVTSGITRGLR-DGEAHPYVY-----GRYVndgefivhEASPTSSG--NLEWFTAQW 315
Cdd:cd24121 240 VVATALGSGAIEPGDACSILGTTGVHEVVVDEPDlEPEGVGYTIclgvpGRWL--------RAMANMAGtpNLDWFLREL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 316 GEI-----------SFDEINQAVASLPKAGGDLFFLPFLygSNAG-----LEMTS--GFYGMQAIHTRAHLLQAIYEGVV 377
Cdd:cd24121 312 GEVlkegaepagsdLFQDLEELAASSPPGAEGVLYHPYL--SPAGerapfVNPNAraQFTGLSLEHTRADLLRAVYEGVA 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16131451 378 FSHMTHLNRMRERFTDvhtLRVTGGPAHSDVWMQMLADVSGLRIELPQVEETGCFGAALAARVGTG 443
Cdd:cd24121 390 LAMRDCYEHMGEDPGE---LRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
4-443 |
2.51e-102 |
|
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: 313.75 E-value: 2.51e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 4 YWLGLDCGGSWLKAGLYDREGREAGVQRLPLCALSPQPGWAERDMAELWQCCMAVIRALLthSGVSGEQIVGIGISAQGK 83
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAA--AQAGPDPIAAISVSSQGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 84 GLFLLDKNDKPLGNAILSSDRRAMEIVRRWQEDGIPEKLYPLTRQTLWTGHPVSLLRWLKEHEPERYAQIGCVMMTHDYL 163
Cdd:cd07773 79 SGVPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAKWLSVADYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 164 RWCLTGVKGCEESNISESNLYNMSLGEYDPCLTDWLGIAEinHALPPVVGSAEICGEITAQTAALTGLKAGTPVV-GGLf 242
Cdd:cd07773 159 AYRLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDA--SLLPELVPSGTVIGTVTPEAAEELGLPAGTPVVvGGH- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 243 DVVSTALCAGIEDEFTLNAVMGTWAVTSGITRGLRDGEAHP---YVYGRYVNDGEFIVHeASPTSSGNLEWFTAQ--WGE 317
Cdd:cd07773 236 DHLCAALGAGVIEPGDVLDSTGTAEALLAVVDEPPLDEMLAeggLSYGHHVPGGYYYLA-GSLPGGALLEWFRDLfgGDE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 318 ISFDEINQAVASLPKAGGDLFFLPFLYGSNA---GLEMTSGFYGMQAIHTRAHLLQAIYEGVVFSHMTHLNRMRERFTDV 394
Cdd:cd07773 315 SDLAAADELAEAAPPGPTGLLFLPHLSGSGTpdfDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEALEKAGIPI 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 16131451 395 HTLRVTGGPAHSDVWMQMLADVSGLRIELPQVEETGCFGAALAARVGTG 443
Cdd:cd07773 395 DEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
4-472 |
1.08e-95 |
|
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: 296.35 E-value: 1.08e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 4 YWLGLDCGGSWLKAGLYDREGREAGVQRLPLCALSPQPGWAERDMAELWQCCMAVIRALLTHSGVSGEQIVGIGISAQGK 83
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 84 GLFLLDKNDKPLGNAILSSDRRAmeivrrwqedgipeklypltrqtlwtghpvsllrwlkeheperyaqiGCVMMTHDYL 163
Cdd:cd07779 81 TFVPVDEDGRPLRPAISWQDKRT-----------------------------------------------AKFLTVQDYL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 164 RWCLTGVKGCEESNISESNLYNMSLGEYDPCLTDWLGIAEinHALPPVVGSAEICGEITAQTAALTGLKAGTPVVGGLFD 243
Cdd:cd07779 114 LYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDR--DKLPELVPPGTVIGTLTKEAAEETGLPEGTPVVAGGGD 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 244 VVSTALCAGIEDEFTLNAVMGTWAVTSGITRGLRDGEAHPYVYGRYVNDGEFIVhEASPTSSGN-LEWF----------T 312
Cdd:cd07779 192 QQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPGKWVL-EGSINTGGSaVRWFrdefgqdevaE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 313 AQWGEISFDEINQAVASLPKAGGDLFFLPFLYGSNA---GLEMTSGFYGMQAIHTRAHLLQAIYEGVVFSHMTHLNRMRE 389
Cdd:cd07779 271 KELGVSPYELLNEEAAKSPPGSDGLLFLPYLAGAGTpywNPEARGAFIGLTLSHTRAHLARAILEGIAFELRDNLEAMEK 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 390 RFTDVHTLRVTGGPAHSDVWMQMLADVSGLRIELPQVEETGCFGAALAARVGTGVYHNFSEAQRDLRHPVRTLLPDMTAH 469
Cdd:cd07779 351 AGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKAMVRVTDTFEPDPENV 430
|
...
gi 16131451 470 QLY 472
Cdd:cd07779 431 AIY 433
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
4-482 |
3.02e-90 |
|
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: 283.68 E-value: 3.02e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 4 YWLGLDCGGSWLKAGLYDREGR--EAGVQRLPLcaLSPQPGWAERDMAELWQCCMAVIRALLthSGVSGEQIVGIGISAQ 81
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRvvASSSAEYPL--IRPEPGWAEQDPEEILEAVLEALKEVL--AKLGGGEVDAIGFSSA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 82 GKGLFLLDKNDKPLGNAILSSDRRAMEIVRRWQEDGIPEKLYPLTrqtlwtG---HPVSL---LRWLKEHEPERYAQIGC 155
Cdd:cd07770 77 MHSLLGVDEDGEPLTPVITWADTRAAEEAERLRKEGDGSELYRRT------GcpiHPMYPlakLLWLKEERPELFAKAAK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 156 VMMTHDYLRWCLTGVKGCEESNISESNLYNMSLGEYDPCLTDWLGIAEINhaLPPVVGSAEICGEITAQTAALTGLKAGT 235
Cdd:cd07770 151 FVSIKEYLLYRLTGELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQ--LPELVDPTEVLPGLKPEFAERLGLLAGT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 236 PVVGGLFD-----VVSTALcagIEDEFTLNavMGTwavtSGITRGLRDgEAHPYVYGR----YVNDGEFIVHEASpTSSG 306
Cdd:cd07770 229 PVVLGASDgalanLGSGAL---DPGRAALT--VGT----SGAIRVVSD-RPVLDPPGRlwcyRLDENRWLVGGAI-NNGG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 307 N-LEWFTAQWG--EISFDEINQAVASLPKAGGDLFFLPFLYGSNA---GLEMTSGFYGMQAIHTRAHLLQAIYEGVVFSH 380
Cdd:cd07770 298 NvLDWLRDTLLlsGDDYEELDKLAEAVPPGSHGLIFLPYLAGERApgwNPDARGAFFGLTLNHTRADILRAVLEGVAFNL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 381 MTHLNRMRERFTDVHTLRVTGGPAHSDVWMQMLADVSGLRIELPQVEETGCFGAALAARVGTGVYHNFSEAqrDLRHPVR 460
Cdd:cd07770 378 KSIYEALEELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSLEAD--ELVKIGK 455
|
490 500
....*....|....*....|..
gi 16131451 461 TLLPDMTAHQLYQKKYQRYQHL 482
Cdd:cd07770 456 VVEPDPENHAIYAELYERFKKL 477
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
4-443 |
5.40e-84 |
|
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: 266.70 E-value: 5.40e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 4 YWLGLDCGGSWLKAGLYDREGREAGVQRLPLCALSPQPGWAERDMAELWQCCMAVIRALLTHSGVSGEQIVGIGISAQGK 83
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGLVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 84 GLFLLDKNDKPLGNAILSSDRRAMEIVRrWQEDGIPE-KLYPLTRQTLWTGHPVSLLRWLKEHEPERYAQIGCVMMTHDY 162
Cdd:cd07804 81 ALVPVDENGKPLRPAILYGDRRATEEIE-WLNENIGEdRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTRKFLGAYDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 163 LRWCLTGVKGCEESN-ISESNLYNMSLGEYDPCLTDWLGIAEinHALPPVVGSAEICGEITAQTAALTGLKAGTPVVGGL 241
Cdd:cd07804 160 IVYKLTGEYVIDYSSaGNEGGLFDIRKRTWDEELLEALGIDP--DLLPELVPSTEIVGEVTKEAAEETGLAEGTPVVAGT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 242 FDVVSTALCAGIEDEFTLNAVMGT---WAVtsgITRGLRDGEAHPYVY----GRYVNDGefivheaSPTSSG-NLEWF-- 311
Cdd:cd07804 238 VDAAASALSAGVVEPGDLLLMLGTagdIGV---VTDKLPTDPRLWLDYhdipGTYVLNG-------GMATSGsLLRWFrd 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 312 ---------TAQWGEISFDEINQAVASLPkAGGD-LFFLPFLYGsnaglEMT-------SG-FYGMQAIHTRAHLLQAIY 373
Cdd:cd07804 308 efageeveaEKSGGDSAYDLLDEEAEKIP-PGSDgLIVLPYFMG-----ERTpiwdpdaRGvIFGLTLSHTRAHLYRALL 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 374 EGVVFSHMTHLNRMRERFTDVHTLRVTGGPAHSDVWMQMLADVSGLRIELPQVEETGCFGAALAARVGTG 443
Cdd:cd07804 382 EGVAYGLRHHLEVIREAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| XylB |
TIGR01312 |
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of ... |
6-482 |
4.15e-82 |
|
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: 262.64 E-value: 4.15e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 6 LGLDCGGSWLKAGLYDREGREAGVQRLPLCALSPQPGWAERDMAELWQCCMAVIRALLTHSGVSGEQIVGIGISAQGKGL 85
Cdd:TIGR01312 1 LGIDLGTSGVKALLVDEQGEVIASGSAPHTVISPHPGWSEQDPEDWWDATEEAIKELLEQASEMGQDIKGIGISGQMHGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 86 FLLDKNDKPLGNAILSSDRRAMEIVRRWQEDGIPEKLYPLTRQTLWTGHPVSLLRWLKEHEPERYAQIGCVMMTHDYLRW 165
Cdd:TIGR01312 81 VLLDANGEVLRPAILWNDTRTAQECEELEAELGDERVLEITGNLALPGFTAPKLLWVRKHEPEVFARIAKVMLPKDYLRY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 166 CLTGVKGCEESNISESNLYNMSLGEYDpclTDWLGIAEINHA-LPPVVGSAEICGEITAQTAALTGLKAGTPVVGGLFDV 244
Cdd:TIGR01312 161 RLTGEYVTEYSDASGTGWFDVAKRAWS---KELLDALDLPESqLPELIESSEKAGTVRPEVAARLGLSAGVPVAAGGGDN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 245 VSTALCAGIEDEFTLNAVMGtwavTSGITRGLRDGeahpyvygrYVNDGEFIVH---EASPT---------SSGN-LEWF 311
Cdd:TIGR01312 238 AAGAIGTGTVDPGDAMMSLG----TSGVVYAVTDK---------PLPDPAGAVHgfcHALPGgwlpmgvtlSATSsLEWF 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 312 TAQWGEISFDEINQAVASLPKAGGDLFFLPFLYGS---NAGLEMTSGFYGMQAIHTRAHLLQAIYEGVVFSHMTHLNRMR 388
Cdd:TIGR01312 305 RELFGKEDVEALNELAEQSPPGAEGVTFLPYLNGErtpHLDPQARGSFIGLTHNTTRADLTRAVLEGVTFALRDSLDILR 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 389 ER-FTDVHTLRVTGGPAHSDVWMQMLADVSGLRIELPQVEETGCFGAALAARVGTGVYHNFSEAQrdlRHPVR---TLLP 464
Cdd:TIGR01312 385 EAgGIPIQSIRLIGGGAKSPAWRQMLADIFGTPVDVPEGEEGPALGAAILAAWALGEKDLAALCS---EAVVKqteSVLP 461
|
490
....*....|....*...
gi 16131451 465 DMTAHQLYQKKYQRYQHL 482
Cdd:TIGR01312 462 IAENVEAYEELYERYKKL 479
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
4-488 |
5.00e-75 |
|
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: 244.75 E-value: 5.00e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 4 YWLGLDCGGSWLKAGLYD-REGREAG--VQRLPLCALSPQPGWAERDMAELWQCCMAVIRALLTHSGVSGEQIVGIGISA 80
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELAsaVVPYPTGYIPPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 81 QGKGLFLLDKNDKPLGNAILSSDRRAMEIVRRWQEDGIPEKLYPLTrqtlWTGHPVS-------LLrWLKEHEPERYAQI 153
Cdd:cd07781 81 TSSTVVPVDEDGNPLAPAILWMDHRAQEEAAEINETAHPALEYYLA----YYGGVYSsewmwpkAL-WLKRNAPEVYDAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 154 GCVMMTHDYLRWCLTGVKGCEESNISESNLYNMSLGEYDPCLTDWLGI--AEINHALP-PVVGSAEICGEITAQTAALTG 230
Cdd:cd07781 156 YTIVEACDWINARLTGRWVRSRCAAGHKWMYNEWGGGPPREFLAALDPglLKLREKLPgEVVPVGEPAGTLTAEAAERLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 231 LKAGTPVVGGLFDVVSTALCAGIEDEFTLNAVMGTWAVTSGITRGLRDGeahPYVYGRY---VNDGeFIVHEASPTSSGN 307
Cdd:cd07781 236 LPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTSTCHLMVSPKPVDI---PGICGPVpdaVVPG-LYGLEAGQSAVGD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 308 -LEWF-------TAQWGEISFDEINQAVASLPKAGGDLFFLPFLYGS-----NAGLemTSGFYGMQAIHTRAHLLQAIYE 374
Cdd:cd07781 312 iFAWFvrlfvppAEERGDSIYALLSEEAAKLPPGESGLVALDWFNGNrtplvDPRL--RGAIVGLTLGTTPAHIYRALLE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 375 GVVFSHMTHLNRMRERFTDVHTLRVTGGPA-HSDVWMQMLADVSGLRIELPQVEETGCFGAALAARVGTGVYHNFSEAQR 453
Cdd:cd07781 390 ATAFGTRAIIERFEEAGVPVNRVVACGGIAeKNPLWMQIYADVLGRPIKVPKSDQAPALGAAILAAVAAGVYADIEEAAD 469
|
490 500 510
....*....|....*....|....*....|....*
gi 16131451 454 DLRHPVRTLLPDMTAHQLYQKKYQRYQHLIAALQG 488
Cdd:cd07781 470 AMVRVDRVYEPDPENHAVYEELYALYKELYDALGP 504
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
6-443 |
1.34e-68 |
|
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: 226.28 E-value: 1.34e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 6 LGLDCGGSWLKAGLYDRE-GREAGVQRLPLCALSPQPGWAERDMAELWQCCMAVIRALLTHSGVSGEQIVGIGISAQGKG 84
Cdd:cd07809 3 LGIDLGTQSIKAVLIDAEtGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQMHG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 85 LFLLDKNDKPLGNAIL----SSDRRAMEIVRRWQED-GIPEKLYPLTRqtlWTghpVSLLRWLKEHEPERYAQIGCVMMT 159
Cdd:cd07809 83 LVALDADGKVLRPAKLwcdtRTAPEAEELTEALGGKkCLLVGLNIPAR---FT---ASKLLWLKENEPEHYARIAKILLP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 160 HDYLRWCLTGVKGCEESNISESNLYNMSLGEYDPCLTDWLGIA-EINHALPPVVGSAEICGEITAQTAALTGLKAGTPVV 238
Cdd:cd07809 157 HDYLNWKLTGEKVTGLGDASGTFPIDPRTRDYDAELLAAIDPSrDLRDLLPEVLPAGEVAGRLTPEGAEELGLPAGIPVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 239 GGLFDVVSTALCAGIEDEFTLNAVMGTWAVTSGIT-RGLRDgeAHPYVYG-RYVNDGefIVHEASPTSSGN--LEWFTAQ 314
Cdd:cd07809 237 PGEGDNMTGALGTGVVNPGTVAVSLGTSGTAYGVSdKPVSD--PHGRVATfCDSTGG--MLPLINTTNCLTawTELFREL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 315 WGeISFDEINQAVASLPKAGGDLFFLPFLYG-SNAGLEMTSG-FYGMQ-AIHTRAHLLQAIYEGVVFSHMTHLNRMRERF 391
Cdd:cd07809 313 LG-VSYEELDELAAQAPPGAGGLLLLPFLNGeRTPNLPHGRAsLVGLTlSNFTRANLARAALEGATFGLRYGLDILRELG 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 16131451 392 TDVHTLRVTGGPAHSDVWMQMLADVSGLRIELPQVEETGCFGAALAARVGTG 443
Cdd:cd07809 392 VEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
4-442 |
3.01e-64 |
|
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: 214.39 E-value: 3.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 4 YWLGLDCGGSWLKAGLYDREGREAGVQRLPLCALSPQPGWAERDMAELWQCCMAVIRALLTHSGVSgeQIVGIGISAQGK 83
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRPR--RVVAIAVDGTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 84 GLFLLDKNDKPLGNAILSSDRRAMEIVRRWQEdgIPEKLYPLTRQTLWTGHPVSLLRWLKEHEPERYAQIGCVMMTHDYL 163
Cdd:cd07783 79 TLVLVDREGEPLRPAIMYNDARAVAEAEELAE--AAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAKFLHQADWL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 164 RWCLTGVKGC-EESNISESnLYNMSLGEYDPCLTDWLGIAEinHALPPVVGSAEICGEITAQTAALTGLKAGTPVVGGLF 242
Cdd:cd07783 157 AGRLTGDRGVtDYNNALKL-GYDPETGRWPSWLLALLGIPP--DLLPRVVAPGTVIGTLTAEAAEELGLPAGTPVVAGTT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 243 DVVSTALCAGIEDEFTLNAVMGTWAVTSGITRGLRDgEAHPYVYGRYVNDGEFIVHEASPTSSGNLEWFTaqwGEISFDE 322
Cdd:cd07783 234 DSIAAFLASGAVRPGDAVTSLGTTLVLKLLSDKRVP-DPGGGVYSHRHGDGYWLVGGASNTGGAVLRWFF---SDDELAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 323 INQAVASLPKAGgdLFFLPF-LYGS-----NAGLEmtsGFYgMQAIHTRAHLLQAIYEGVVFSHMTHLNRMRER-FTDVH 395
Cdd:cd07783 310 LSAQADPPGPSG--LIYYPLpLRGErfpfwDPDAR---GFL-LPRPHDRAEFLRALLEGIAFIERLGYERLEELgAPPVE 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 16131451 396 TLRVTGGPAHSDVWMQMLADVSGLRIELPQvEETGCFGAALAARVGT 442
Cdd:cd07783 384 EVRTAGGGARNDLWNQIRADVLGVPVVIAE-EEEAALGAALLAAAGL 429
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
4-443 |
1.06e-59 |
|
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: 202.84 E-value: 1.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 4 YWLGLDCGGSWLKAGLYDREGREAGVQRLPLCALSP--QPGWAERDMAELWQCCMAVIRALLTHSGVSGEQIVGIGISAQ 81
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDddYPDAKEFDPEELWEKICEAIREALKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 82 GKGLFLLDKNDKPL--GNAIlssDRRAMEIVRRWQEDGIPEKLYpltrqtlWTGHPVSL------LRWLKEHEPERYAQI 153
Cdd:cd07798 81 REGIVFLDKDGRELyaGPNI---DARGVEEAAEIDDEFGEEIYT-------TTGHWPTElfpaarLLWFKENRPEIFERI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 154 GCVMMTHDYLRWCLTGVKGCEESNISESNLYNMSLGEYDPCLTDWLGIAEinHALPPVVGSAEICGEITAQTAALTGLKA 233
Cdd:cd07798 151 ATVLSISDWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPP--EILPEIVPSGTVLGTVSEEAARELGLPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 234 GTPVVGGLFDVVSTALCAGIEDEFTLNAVMGTWAVTSGITRGLRDGEAHPYVYGRYVNDGEFIVhEASPTSSG-NLEWFT 312
Cdd:cd07798 229 GTPVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWTGCHLVPGKWVL-ESNAGVTGlNYQWLK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 313 ---AQWGEISFDEINQAVAS-LPKAGGDLFFLpflyGS---NAGLEMT--SGFYGMQAIH----TRAHLLQAIYEGVVFS 379
Cdd:cd07798 308 ellYGDPEDSYEVLEEEASEiPPGANGVLAFL----GPqifDARLSGLknGGFLFPTPLSaselTRGDFARAILENIAFA 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131451 380 HMTHLNRMRE-RFTDVHTLRVTGGPAHSDVWMQMLADVSGLRIELPQVEETGCFGAALAARVGTG 443
Cdd:cd07798 384 IRANLEQLEEvSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
4-479 |
5.40e-50 |
|
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: 178.30 E-value: 5.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 4 YWLGLDCGGSWLKAGLYDREGREAGVQRLPLCALSPQ--PGWAERDMAELWQCCMAVIRALLTHSGVSGEQIVGIGISAQ 81
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREWRHKEVPdvPGSMDFDTEKNWKLICECIREALKKAGIAPKSIAAISTTSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 82 GKGLFLLDKNDKPLGnAILSSDRRAMEIVRRWQE--DGIPEKLYPLTRQTLWTGHPVSLLrWLKEHEPERYAQIGCVMMT 159
Cdd:cd07775 81 REGIVLYDNEGEEIW-ACANVDARAAEEVSELKElyNTLEEEVYRISGQTFALGAIPRLL-WLKNNRPEIYRKAAKITML 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 160 HDYLRWCLTGVKGCEESNISESNLYNMSLGEYDPCLTDWLGI-AEInhaLPPVVGSAEICGEITAQTAALTGLKAGTPVV 238
Cdd:cd07775 159 SDWIAYKLSGELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLkADI---LPPVVESGTVIGKVTKEAAEETGLKEGTPVV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 239 GGLFDVVSTALCAGIEDEFTLNAVMGT-WAVTSGITRGLRDGEAHPYVYGRYVND---GEFIVHEASPTssgnLEWFTAQ 314
Cdd:cd07775 236 VGGGDVQLGCLGLGVVRPGQTAVLGGSfWQQEVNTAAPVTDPAMNIRVNCHVIPDmwqAEGISFFPGLV----MRWFRDA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 315 WGEisfDEINQAVaslpKAGGDLFFLpflygsnagLEMTS-----GFYGMQAI-----------H--------------- 363
Cdd:cd07775 312 FCA---EEKEIAE----RLGIDAYDL---------LEEMAkdvppGSYGIMPIfsdvmnyknwrHaapsflnldidpekc 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 364 TRAHLLQAIYEGVVFSHMTHLNRMRErFTDVH--TLRVTGGPAHSDVWMQMLADVSGLRIELPQVEETGCFGAALAARVG 441
Cdd:cd07775 376 NKATFFRAIMENAAIVSAGNLERIAE-FSGIFpdSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVG 454
|
490 500 510
....*....|....*....|....*....|....*...
gi 16131451 442 TGVYHNFSEAQRDLRHPVRTLLPDMTAHQLYQKKYQRY 479
Cdd:cd07775 455 AGIYSSLEEAVESLVKWEREYLPNPENHEVYQDLYEKW 492
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
1-480 |
1.02e-45 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 167.11 E-value: 1.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 1 MTQYWLGLDCGGSWLKAGLYDREGREAGVQRLPLCALSPQ--PGWAERDMAELWQCCMAVIRALLTHSGVSGEQIVGIGI 78
Cdd:PRK10939 1 SMSYLMALDAGTGSIRAVIFDLNGNQIAVGQAEWRHLAVPdvPGSMEFDLEKNWQLACQCIRQALQKAGIPASDIAAVSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 79 SAQGKGLFLLDKNDKPLGnAILSSDRRAMEIVRRWQED--GIPEKLYPLTRQTLWTGHPVSLLrWLKEHEPERYAQIGCV 156
Cdd:PRK10939 81 TSMREGIVLYDRNGTEIW-ACANVDARASREVSELKELhnNFEEEVYRCSGQTLALGALPRLL-WLAHHRPDIYRQAHTI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 157 MMTHDYLRWCLTGVKGCEESNISESNLYNMSLGEYDPCLTDWLGI-AEInhaLPPVVGSAEICGEITAQTAALTGLKAGT 235
Cdd:PRK10939 159 TMISDWIAYMLSGELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLrADI---LPPVKETGTVLGHVTAKAAAETGLRAGT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 236 PVVGGLFDVVSTALCAGIEDEFTLnAVMGT--WAVTSGITRGLRDGEA----HPYVYGRyVNDGEFIVheasptssgnle 309
Cdd:PRK10939 236 PVVMGGGDVQLGCLGLGVVRPGQT-AVLGGtfWQQVVNLPAPVTDPNMniriNPHVIPG-MVQAESIS------------ 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 310 WF---TAQWGEISFDEINQAVASlpKAGGDLFFLpflygsnagLE-MTS----GFYGMQAI-----------H------- 363
Cdd:PRK10939 302 FFtglTMRWFRDAFCAEEKLLAE--RLGIDAYSL---------LEeMASrvpvGSHGIIPIfsdvmrfkswyHaapsfin 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 364 --------TRAHLLQAIYEGVVFSHMTHLNRMrERFTDVHTLRV--TGGPAHSDVWMQMLADVSGLRIELPQVEETGCFG 433
Cdd:PRK10939 371 lsidpekcNKATLFRALEENAAIVSACNLQQI-AAFSGVFPSSLvfAGGGSKGKLWSQILADVTGLPVKVPVVKEATALG 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 16131451 434 AALAARVGTGVYHNFSEAQRDLRHPVRTLLPDMTAHQLYQKKYQRYQ 480
Cdd:PRK10939 450 CAIAAGVGAGIYSSLAETGERLVRWERTFEPNPENHELYQEAKEKWQ 496
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
4-480 |
8.43e-44 |
|
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: 161.58 E-value: 8.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 4 YWLGLDCGGSWLKAGLYDREGREAGVQRLPLCALSPQPGWAERDMAELWQCCMAVIRALLTHSGVSGEQIVGIGISAQgK 83
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQ-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 84 GLFLL-DK-NDKPLGNAILSSDRRAMEIVRRWQE-------DGIPEKLYPLTRQ---------TLWTGHPVSLLRWLKEH 145
Cdd:cd07793 80 NTFLTwDKkTGKPLHNFITWQDLRAAELCESWNRslllkalRGGSKFLHFLTRNkrflaasvlKFSTAHVSIRLLWILQN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 146 EPE--RYAQIGCVMM-THD-YLRWCLTG--VKGCEESNISESNLYNMSLGEYDPCLTDWLGIAEinHALPPVVGSAEICG 219
Cdd:cd07793 160 NPElkEAAEKGELLFgTIDtWLLWKLTGgkVHATDYSNASATGLFDPFTLEWSPILLSLFGIPS--SILPEVKDTSGDFG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 220 E-----------ITA----QTAALTG---LKAGtpvvgglfDVVSTalcagiedeftlnavMGT---WAVTSGitrglrd 278
Cdd:cd07793 238 StdpsifgaeipITAvvadQQAALFGeccFDKG--------DVKIT---------------MGTgtfIDINTG------- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 279 GEAHPYVYGRY------VNDGefIVH--EASPTSSGN-LEWFTAQWGEISFDEINQAVASLPKAGGdLFFLPFLYGSNAG 349
Cdd:cd07793 288 SKPHASVKGLYplvgwkIGGE--ITYlaEGNASDTGTvIDWAKSIGLFDDPSETEDIAESVEDTNG-VYFVPAFSGLQAP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 350 L---EMTSGFYGMQAIHTRAHLLQAIYEGVVF-SHMTHLNRMRERFTDVHTLRVTGGPAHSDVWMQMLADVSGLRIELPQ 425
Cdd:cd07793 365 YndpTACAGFIGLTPSTTKAHLVRAILESIAFrVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPK 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 16131451 426 VEETGCFGAALAARVGTGVYHNfSEAQRDLRHPVRTLLPDMTAhQLYQKKYQRYQ 480
Cdd:cd07793 445 NTEMSALGAAFLAGLASGIWKS-KEELKKLRKIEKIFEPKMDN-EKREELYKNWK 497
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
4-480 |
2.35e-43 |
|
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: 159.94 E-value: 2.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 4 YWLGLDCGGSWLKAGLYDREGREAGVQRLPLCALSPQPGWAERDMAELWQCCMAVIRALLTHSGVSGEQIVGIGISAQGK 83
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 84 GLFLLDKND-KPLGNAILSSDRRAMEIVRRWQEDGIPEKLypltRQTlwTGHPV------SLLRWLKEHEP---ERYAQI 153
Cdd:cd07769 81 TTVVWDKKTgKPLYNAIVWQDRRTADICEELKAKGLEERI----REK--TGLPLdpyfsaTKIKWILDNVPgarERAERG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 154 GCVMMTHD-YLRWCLTGVKG--CEESNISESNLYNMSLGEYDPCLTDWLGIAEInhALPPVVGSAEICGEITAqtaalTG 230
Cdd:cd07769 155 ELLFGTIDtWLIWKLTGGKVhvTDVTNASRTMLFNIHTLEWDDELLELFGIPRS--MLPEVRPSSEVFGYTDP-----EG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 231 LKAGTPVVG--------------------------GLFDVVSTalcagiedeftlnavmGTWAVTSgiTRGL-------R 277
Cdd:cd07769 228 LGAGIPIAGilgdqqaalfgqgcfepgmakntygtGCFLLMNT----------------GEKPVPS--KNGLlttiawqI 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 278 DGEAhpyVYgryvndgefiVHEASPTSSGN-LEWFTAQWGEI-SFDEINQAVASLPKAGGdLFFLPFLYG-------SNA 348
Cdd:cd07769 290 GGKV---TY----------ALEGSIFIAGAaIQWLRDNLGLIeDAAETEELARSVEDNGG-VYFVPAFSGlgapywdPDA 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 349 -GLemtsgFYGMQAIHTRAHLLQAIYEGVVFSHMTHLNRMRER-FTDVHTLRVTGGPAHSDVWMQMLADVSGLRIELPQV 426
Cdd:cd07769 356 rGA-----IVGLTRGTTKAHIVRAALESIAYQTRDVLEAMEKDsGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKV 430
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 16131451 427 EETGCFGAALAARVGTGVYHNFSEAqRDLRHPVRTLLPDMTAHQlYQKKYQRYQ 480
Cdd:cd07769 431 AETTALGAAYLAGLAVGFWKDLDEL-ASLWQVDKRFEPSMDEEE-RERLYRGWK 482
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
1-489 |
7.50e-42 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 155.99 E-value: 7.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 1 MTQYWLGLDCGGSWLKAGLYDREGREAGVQRLPLCALSPQPGWAERDMAELWQCCMAVIRALLTHSGVSGEQIVGIGISA 80
Cdd:COG0554 1 MKKYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISAEDIAAIGITN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 81 QGKGLFLLDKND-KPLGNAILSSDRRAMEIVRRWQEDGIPEKLypltRQTlwTGHPV------SLLRWLKEHEP---ERY 150
Cdd:COG0554 81 QRETTVVWDRKTgKPLYNAIVWQDRRTADICEELKADGLEDLI----REK--TGLVLdpyfsaTKIKWILDNVPgarERA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 151 AQiGCVMM-THD-YLRWCLTG--VKGCEESNISESNLYNMSLGEYDPCLTDWLGIAEinHALPPVVGSAEICGEITAqta 226
Cdd:COG0554 155 EA-GELLFgTIDsWLIWKLTGgkVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPR--SMLPEVRPSSEVFGETDP--- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 227 alTGLKAGTPVVG-------GLF--------DVVST------ALcagiedeftLNAvmGTWAVTSgiTRGL-------RD 278
Cdd:COG0554 229 --DLFGAEIPIAGiagdqqaALFgqacfepgMAKNTygtgcfLL---------MNT--GDEPVRS--KNGLlttiawgLG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 279 GEAhpyVYGryvndgefivHEASPTSSGNlewfTAQW-----GEI-SFDEINQAVASLPKAGGdLFFLPFLYG------- 345
Cdd:COG0554 294 GKV---TYA----------LEGSIFVAGA----AVQWlrdglGLIdSAAESEALARSVEDNGG-VYFVPAFTGlgapywd 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 346 SNA-----GLemTSGfygmqaiHTRAHLLQAIYEGVVFShmTH--LNRMRErftD----VHTLRVTGGPAHSDVWMQMLA 414
Cdd:COG0554 356 PDArgaifGL--TRG-------TTRAHIARAALESIAYQ--TRdvLDAMEA---DsgipLKELRVDGGASANDLLMQFQA 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16131451 415 DVSGLRIELPQVEETGCFGAALAARVGTGVYHNFSEAqRDLRHPVRTLLPDMTAHQLyQKKYQRYQHLIAALQGF 489
Cdd:COG0554 422 DILGVPVERPKVTETTALGAAYLAGLAVGFWKSLEEL-AALWKVDRRFEPQMDEEER-ERLYAGWKKAVERTLGW 494
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
2-482 |
1.51e-38 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 147.57 E-value: 1.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 2 TQYWLGLDCG-GSwLKAGLYD-REGREAG--VQRLPL----CALSPQPGWAERDMAELWQCCMAVIRALLTHSGVSGEQI 73
Cdd:COG1069 1 EKYVIGVDFGtDS-VRAVVVDaADGEELAsaVHPYPRwvigLYLPPPPDQARQHPLDYLEALEAAVREALAQAGVDPADV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 74 VGIGISAQGKGLFLLDKNDKPL-----------GNAILSSDRRAM-------EIVRRWQED------GI--PEKLYPltr 127
Cdd:COG1069 80 VGIGVDATGCTPVPVDADGTPLallpefaenphAMVILWKDHTAQeeaerinELAKARGEDylryvgGIisSEWFWP--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 128 qtlwtghpvSLLrWLKEHEPERYAQIGCVMMTHDYLRWCLTGvkgceesNISESN-------LYNMSLGEY--------- 191
Cdd:COG1069 157 ---------KIL-HLLREDPEVYEAADSFVELCDWITWQLTG-------SLKRSRctaghkaLWHAHEGGYpseeffaal 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 192 DPCLTDwlgIAE-INHalpPVVGSAEICGEITAQTAALTGLKAGTPVVGGLFDVVSTALCAGIEDEFTLNAVMGTWAVTS 270
Cdd:COG1069 220 DPLLDG---LADrLGT---EIYPLGEPAGTLTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGGVEPGTLVKVMGTSTCHM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 271 GITRGLRDgeaHPYVYGrYVNDG---EFIVHEASPTSSGNL-EWF------------TAQWGEIS-FDEINQAVASLPKA 333
Cdd:COG1069 294 LVSPEERF---VPGICG-QVDGSivpGMWGYEAGQSAVGDIfAWFvrllvppleyekEAEERGISlHPLLTEEAAKLPPG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 334 GGDLFFLPFLYGsN-------------AGLEMTSgfygmqaihTRAHLLQAIYEGVVFSHMTHLNRMRERFTDVHTLRVT 400
Cdd:COG1069 370 ESGLHALDWFNG-NrspladqrlkgviLGLTLGT---------DAEDIYRALVEATAFGTRAIIERFEEEGVPIDEIIAC 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 401 GG-PAHSDVWMQMLADVSGLRIELPQVEETGCFGAALAARVGTGVYHNFSEAQRDLRHPV-RTLLPDMTAHQLYQKKYQR 478
Cdd:COG1069 440 GGiATKNPLVMQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEEAMAAMGSGFdKVYTPDPENVAVYDALYAE 519
|
....
gi 16131451 479 YQHL 482
Cdd:COG1069 520 YLQL 523
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
4-480 |
1.02e-36 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 141.65 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 4 YWLGLDCGGSWLKAGLYDREGREAGVQRLPLCALSPQPGWAERDMAELWQC---CMAVIRALLTHSGVSGEqIVGIGISA 80
Cdd:PTZ00294 3 YIGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNvykCMNEAIKKLREKGPSFK-IKAIGITN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 81 QGKGLFLLDKN-DKPLGNAILSSDRRAMEIVRRWQEDGipeKLYPLTRQTlwTGHPVSL------LRWLKEHEPERYAQI 153
Cdd:PTZ00294 82 QRETVVAWDKVtGKPLYNAIVWLDTRTYDIVNELTKKY---GGSNFFQKI--TGLPISTyfsafkIRWMLENVPAVKDAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 154 G---CVMMTHD-YLRWCLTGVKG--CEESNISESNLYNMSLGEYDPCLTDWLGIAeiNHALPPVVGSAEICGEITAQTaa 227
Cdd:PTZ00294 157 KegtLLFGTIDtWLIWNLTGGKShvTDVTNASRTFLMNIKTLKWDEELLNKFGIP--KETLPEIKSSSENFGTISGEA-- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 228 lTGLKAGTPVVGGLFDVVSTALCAGIEDE-----------FTL-NAvmGTWAVTSG----ITRGLRDGEAHPYVYGRyvn 291
Cdd:PTZ00294 233 -VPLLEGVPITGCIGDQQAALIGHGCFEKgdakntygtgcFLLmNT--GTEIVFSKhgllTTVCYQLGPNGPTVYAL--- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 292 dgefivhEASPTSSGN-LEWFTAQWGEIS-FDEINQAVASLPKAGGDLF-------FLPFLYGSNAGlemtsGFYGMQAI 362
Cdd:PTZ00294 307 -------EGSIAVAGAgVEWLRDNMGLIShPSEIEKLARSVKDTGGVVFvpafsglFAPYWRPDARG-----TIVGMTLK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 363 HTRAHLLQAIYEGVVFSHMTHLNRM-RERFTDVHTLRVTGGPAHSDVWMQMLADVSGLRIELPQVEETGCFGAALAARVG 441
Cdd:PTZ00294 375 TTRAHIVRAALEAIALQTNDVIESMeKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLA 454
|
490 500 510
....*....|....*....|....*....|....*....
gi 16131451 442 TGVYHNFSEAQRDLRHPVRTLLPDMTAHQlYQKKYQRYQ 480
Cdd:PTZ00294 455 VGVWKSLEEVKKLIRRSNSTFSPQMSAEE-RKAIYKEWN 492
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
5-486 |
6.48e-36 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 139.33 E-value: 6.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 5 WLGLDCGGSWLKAGLYDREGREAGVQRLPLCALSPQPGWAERDMAELWQCCMAVIRALLTHSGVSGeqIVGIGISAQGKG 84
Cdd:PRK15027 2 YIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQD--VKALGIAGQMHG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 85 LFLLDKNDKPLGNAILSSDRRAMEivrrwqEDGIPEKLYPLTRQT----LWTGHPVSLLRWLKEHEPERYAQIGCVMMTH 160
Cdd:PRK15027 80 ATLLDAQQRVLRPAILWNDGRCAQ------ECALLEARVPQSRVItgnlMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 161 DYLRWCLTGVKGCEESNISESnlynMSLgeyDPCLTDW----LGIAEINH-ALPPVVGSAEICGEITAQTAALTGLKAgT 235
Cdd:PRK15027 154 DYLRLRMTGEFASDMSDAAGT----MWL---DVAKRDWsdvmLQACHLSRdQMPALYEGSEITGALLPEVAKAWGMAT-V 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 236 PVVGGLFDVVSTALCAGIEDEFTLNAVMGtwavTSGITRGLRDGeahpyvygrYVNDGEFIVH---EASP---------- 302
Cdd:PRK15027 226 PVVAGGGDNAAGAVGVGMVDANQAMLSLG----TSGVYFAVSEG---------FLSKPESAVHsfcHALPqrwhlmsvml 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 303 TSSGNLEWFTAQWGEISFDEINQAVASLPKAGGDLFFLPFLYGSNA---GLEMTSGFYGMQAIHTRAHLLQAIYEGVVFS 379
Cdd:PRK15027 293 SAASCLDWAAKLTGLSNVPALIAAAQQADESAEPVWFLPYLSGERTphnNPQAKGVFFGLTHQHGPNELARAVLEGVGYA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 380 HMTHLNRMRERFTDVHTLRVTGGPAHSDVWMQMLADVSGLRIELPQVEETG-CFGAALAARVGTGVYHNFSEAQRDLrhP 458
Cdd:PRK15027 373 LADGMDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTGGDVGpALGAARLAQIAANPEKSLIELLPQL--P 450
|
490 500
....*....|....*....|....*....
gi 16131451 459 V-RTLLPDMTAHQLYQKKYQRYQHLIAAL 486
Cdd:PRK15027 451 LeQSHLPDAQRYAAYQPRRETFRRLYQQL 479
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
4-480 |
1.03e-34 |
|
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: 135.70 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 4 YWLGLDCGGSWLKAGLYDREGREAGVQRLPLCALSPQPGWAERDMAELWQCCMAVIRALLTHSGVSGEQIVGIGISAQGK 83
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 84 GLFLLDKND-KPLGNAILSSDRRAMEIVRRWQEDG----IPEKlypltrqtlwTGHPV------SLLRWLKEHEPERYAQ 152
Cdd:cd07786 81 TTVVWDRETgKPVYNAIVWQDRRTADICEELKAEGheemIREK----------TGLVLdpyfsaTKIRWILDNVPGARER 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 153 I--GCVMM-THD-YLRWCLTG--VKGCEESNISESNLYNMSLGEYDPCLTDWLGIAEinHALPPVVGSAEICGEITA--- 223
Cdd:cd07786 151 AerGELAFgTIDsWLIWKLTGgkVHATDVTNASRTMLFNIHTLEWDDELLELFGIPA--SMLPEVKPSSEVFGYTDPdll 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 224 ------------QTAALTG--------LKA--GTpvvgGLFDVVSTalcagiedeftlnavmGTWAVTSG----ITRGLR 277
Cdd:cd07786 229 gaeipiagiagdQQAALFGqacfepgmAKNtyGT----GCFMLMNT----------------GEKPVRSKngllTTIAWQ 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 278 DGEAHPYVYgryvndgefivhEASPtssgnlewFTA----QW-----GEI-SFDEINQAVASLPKAGGdLFFLPflygsn 347
Cdd:cd07786 289 LGGKVTYAL------------EGSI--------FIAgaavQWlrdglGLIeSAAETEALARSVPDNGG-VYFVP------ 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 348 aglemtsGFYGMQAIH----------------TRAHLLQAIYEGVVFShmTH--LNRMRER-FTDVHTLRVTGGPAHSDV 408
Cdd:cd07786 342 -------AFTGLGAPYwdpdargaifgltrgtTRAHIARAALESIAYQ--TRdlLEAMEADsGIPLKELRVDGGASANDF 412
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131451 409 WMQMLADVSGLRIELPQVEETGCFGAALAARVGTGVYHNFSEAQRdLRHPVRTLLPDMTAHQLyQKKYQRYQ 480
Cdd:cd07786 413 LMQFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLDELAK-LWQVDRRFEPSMSEEER-EALYAGWK 482
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
8-479 |
2.89e-32 |
|
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: 129.18 E-value: 2.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 8 LDCGGSWLKAGLYDREGREAGVQRLPLCALSPQPGWAERDMAELWQC---CMAVIRALLTHSGVSGEQIVGIGISAQGKG 84
Cdd:cd07792 6 IDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESvyeCIEEAVEKLKALGISPSDIKAIGITNQRET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 85 LFLLDKN-DKPLGNAILSSDRRAMEIVRRWQEDGIPEKLYplTRQTlwTGHPVSL------LRWLKEHEPERYAQIG--- 154
Cdd:cd07792 86 TVVWDKStGKPLYNAIVWLDTRTSDTVEELSAKTPGGKDH--FRKK--TGLPISTyfsavkLRWLLDNVPEVKKAVDdgr 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 155 CVMMTHD-YLRWCLTGVKGCEE-----SNISESNLYNMSLGEYDPCLTDWLGIAEInhALPPVVGSAEICGEITaqtaal 228
Cdd:cd07792 162 LLFGTVDsWLIWNLTGGKNGGVhvtdvTNASRTMLMNLRTLQWDPELCEFFGIPMS--ILPEIRSSSEVYGKIA------ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 229 TGLKAGTPVVGGLFDvvSTALCAGiedeftlnavmgtwavtsgiTRGLRDGEAHPyVYGR----YVNDGEFIVH------ 298
Cdd:cd07792 234 SGPLAGVPISGCLGD--QQAALVG--------------------QGCFKPGEAKN-TYGTgcflLYNTGEEPVFskhgll 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 299 --------EASPTSSGnLE-----------WFTAQWGEI-SFDEINQAVASLPKAGGdLFFLP-FlygsnaglemtSGFY 357
Cdd:cd07792 291 ttvayklgPDAPPVYA-LEgsiaiagaavqWLRDNLGIIsSASEVETLAASVPDTGG-VYFVPaF-----------SGLF 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 358 -------------GMQAIHTRAHLLQAIYEGVVFSHMTHLNRM-RERFTDVHTLRVTGGPAHSDVWMQMLADVSGLRIEL 423
Cdd:cd07792 358 apywrpdargtivGLTQFTTKAHIARAALEAVCFQTREILDAMnKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVER 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131451 424 PQVEETGCFGAALAARVGTGVYhNFSEAQRDLRHPVRTLLPDMTAHQLYQKKYQRY 479
Cdd:cd07792 438 PSMVETTALGAAIAAGLAVGVW-KSLDELKSLNEGGRTVFEPQISEEERERRYKRW 492
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
4-438 |
3.64e-30 |
|
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: 121.95 E-value: 3.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 4 YWLGLDCGGSWLKAGLYDREGRE-AGVQRLPLCALSPQ--PGWAERDMAELWQCCMAVIRALLTHSGvsgEQIVGIGISA 80
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDLESGRiLESVSRPTPAPISSddPGRSEQDPEKILEAVRNLIDELPREYL---SDVTGIGITG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 81 QGKGLFLLDKNDKPLGNAILSSDRRAMEIVRrWQEDGIPEKLYPLTRQTLWTGHPVSLLRWLKEH--EPERYAQIGCVMm 158
Cdd:cd07777 78 QMHGIVLWDEDGNPVSPLITWQDQRCSEEFL-GGLSTYGEELLPKSGMRLKPGYGLATLFWLLRNgpLPSKADRAGTIG- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 159 thDYLRWCLTGvkgCEESNISESNLYnmSLGEYDPCLTDW-------LGIAEinHALPPVVGSAEICGEITAQtaaltgL 231
Cdd:cd07777 156 --DYIVARLTG---LPKPVMHPTNAA--SWGLFDLETGTWnkdlleaLGLPV--ILLPEIVPSGEIVGTLSSA------L 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 232 KAGTPVVGGLFD----VVSTALcaGIEDEFTLNavMGTwavtSG-ITRGLRDGEAHPYVYGR-YVNDGEFIVheASPTSS 305
Cdd:cd07777 221 PKGIPVYVALGDnqasVLGSGL--NEENDAVLN--IGT----GAqLSFLTPKFELSGSVEIRpFFDGRYLLV--AASLPG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 306 GN-LEW---FTAQW-----GEISFDEINQAVASL--PKAGGDLFFLPFLYGSNAGLEMTSGFYGmqaIH----TRAHLLQ 370
Cdd:cd07777 291 GRaLAVlvdFLREWlrelgGSLSDDEIWEKLDELaeSEESSDLSVDPTFFGERHDPEGRGSITN---IGesnfTLGNLFR 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131451 371 AIYEGVVFSHMTHLNRMRERFTDVHTLRVTGG-PAHSDVWMQMLADVSGLRIELPQVEETGCFGAALAA 438
Cdd:cd07777 368 ALCRGIAENLHEMLPRLDLDLSGIERIVGSGGaLRKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
4-477 |
1.26e-28 |
|
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: 118.79 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 4 YWLGLDCG-GSwLKAGLYDREGREAGVQRLPLCALSPQPGWAERDMAELWQCCMAVIRALLTHSGVSGEQIVGIGISAQG 82
Cdd:cd07782 1 YYIGVDVGtGS-ARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFDATC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 83 KgLFLLDKNDKPLG---------NAILSSDRRAMEivrrwQEDGIPEklypltrqtlwTGHPV--------SL------L 139
Cdd:cd07782 80 S-LVVLDAEGKPVSvspsgdderNVILWMDHRAVE-----EAERINA-----------TGHEVlkyvggkiSPemeppkL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 140 RWLKEHEPERYAQIGCVMMTHDYLRWCLTGVK-------GCEESNISESnlynMSLGEYDPCLTDWLGIAEI-------- 204
Cdd:cd07782 143 LWLKENLPETWAKAGHFFDLPDFLTWKATGSLtrslcslVCKWTYLAHE----GSEGGWDDDFFKEIGLEDLvednfaki 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 205 -NHALPPVVGSAeicGEITAQTAALTGLKAGTPVVGGLFD-----------VVSTALCAGIEDEFTLNAVMGTWAVTSGI 272
Cdd:cd07782 219 gSVVLPPGEPVG---GGLTAEAAKELGLPEGTPVGVSLIDahagglgtlgaDVGGLPCEADPLTRRLALICGTSSCHMAV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 273 TRglrdgEAH--PYVYGRY---------VNDG---------EFIV--HEASPTSSGNLEwftAQwGEISFDEINQAVASL 330
Cdd:cd07782 296 SP-----EPVfvPGVWGPYysamlpglwLNEGgqsatgallDHIIetHPAYPELKEEAK---AA-GKSIYEYLNERLEQL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 331 PKAGG--------DLFFLPFLYGSNA------------GLEMTSGF------Y--GMQAI--HTRaHLLQAiyegvvfsh 380
Cdd:cd07782 367 AEEKGlplayltrDLHVLPDFHGNRSpladptlrgmisGLTLDTSLddlallYlaTLQALayGTR-HIIEA--------- 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 381 mthlnrMRERFTDVHTLRVTGGPAHSDVWMQMLADVSGLRIELPQVEETGCFGAALAARVGTGVYHNFSEAQRDLRHPVR 460
Cdd:cd07782 437 ------MNAAGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWDAMAAMSGPGK 510
|
570
....*....|....*..
gi 16131451 461 TLLPDMTAHQLYQKKYQ 477
Cdd:cd07782 511 VVEPNEELKKYHDRKYE 527
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
1-482 |
7.69e-27 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 113.79 E-value: 7.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 1 MTQYWLGLDCGGSWLKAGLYD-REGREAG--VQRLPL----CALSPQPGWAERDMAELWQCCMAVIRALLTHSGVSGEQI 73
Cdd:PRK04123 1 MMAYVIGLDFGTDSVRALLVDcATGEELAtaVVEYPHwvkgRYLDLPPNQALQHPLDYIESLEAAIPAVLKEAGVDPAAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 74 VGIGI----------SAQGKGLFLLDK-NDKPLGNAILSSDRR----AMEIVRRWQEDGIPEklypLTRqtlWTGHPVS- 137
Cdd:PRK04123 81 VGIGVdftgstpapvDADGTPLALLPEfAENPHAMVKLWKDHTaqeeAEEINRLAHERGEAD----LSR---YIGGIYSs 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 138 ------LLRWLkEHEPERYAQIGCVMMTHDYLRWCLTGVKGCeeSNISESN-------LYNMSLGEY---------DPCL 195
Cdd:PRK04123 154 ewfwakILHVL-REDPAVYEAAASWVEACDWVVALLTGTTDP--QDIVRSRcaaghkaLWHESWGGLpsadffdalDPLL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 196 TDwlGIAEinhALP-PVVGSAEICGEITAQTAALTGLKAGTPVVGGLFDVVSTALCAGIEdEFTLNAVMGtwavTS---- 270
Cdd:PRK04123 231 AR--GLRD---KLFtETWTAGEPAGTLTAEWAQRLGLPEGVAVSVGAFDAHMGAVGAGAE-PGTLVKVMG----TStcdi 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 271 ----------GITrGLRDGEAHPYVYGryvndgefivHEASPTSSGNL-EWFT------------AQWGEISFDEINQAV 327
Cdd:PRK04123 301 lladkqravpGIC-GQVDGSIVPGLIG----------YEAGQSAVGDIfAWFArllvppeykdeaEARGKQLLELLTEAA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 328 ASLPKAGGDLFFLPFLYGS---NAGLEMTSGFYGMQAIHTRAHLLQAIYEGVVFSHMTHLNRMRERFTDVHTLRVTGG-P 403
Cdd:PRK04123 370 AKQPPGEHGLVALDWFNGRrtpLADQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECFEDQGVPVEEVIAAGGiA 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 404 AHSDVWMQMLADVSGLRIELPQVEETGCFGAALAARVGTGVYHNFSEAQRDLRHPV-RTLLPDMTAHQLYQKKYQRYQHL 482
Cdd:PRK04123 450 RKNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDIPEAQQAMASPVeKTYQPDPENVARYEQLYQEYKQL 529
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
19-479 |
1.17e-24 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 107.09 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 19 LYDREGREAGVQRLPLCALSPQPGWAERDMAELWQCCMAVIRALLTHSGVSGEQIVG----IGISAQGKGLFLLDKND-K 93
Cdd:PLN02295 16 IYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKGHNVDSglkaIGITNQRETTVAWSKSTgR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 94 PLGNAILSSDRRAMEIVRRWQED--GIPEKLypltRQTlwTGHPVSL------LRWLKEHEPERYAQI----GCVMMTHD 161
Cdd:PLN02295 96 PLYNAIVWMDSRTSSICRRLEKElsGGRKHF----VET--CGLPISTyfsatkLLWLLENVDAVKEAVksgdALFGTIDS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 162 YLRWCLTGVKGCEE-----SNISESNLYNMSLGEYDPCLTDWLGIAEinHALPPVVGSAEICGEITAqtaalTGLKAGTP 236
Cdd:PLN02295 170 WLIWNLTGGASGGVhvtdvTNASRTMLMNLKTLDWDKPTLEALGIPA--EILPKIVSNSEVIGTIAK-----GWPLAGVP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 237 VVGGLFDVVSTAL---CAGIEDEFT--------LNAvmGTWAVTSgiTRGL------RDGEAHPYVYGRyvndgefivhE 299
Cdd:PLN02295 243 IAGCLGDQHAAMLgqrCRPGEAKSTygtgcfilLNT--GEEVVPS--KHGLlttvayKLGPDAPTNYAL----------E 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 300 ASPTSSG-NLEWFTAQWGEI-SFDEINQAVASLPKAGGdLFFLPFLygsnaglemtSGFY-------------GMQAIHT 364
Cdd:PLN02295 309 GSVAIAGaAVQWLRDNLGIIkSASEIEALAATVDDTGG-VYFVPAF----------SGLFaprwrddargvcvGITRFTN 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 365 RAHLLQAIYEGVVFSHMTHLNRMR------ERFTDVHTLRVTGGPAHSDVWMQMLADVSGLRIELPQVEETGCFGAALAA 438
Cdd:PLN02295 378 KAHIARAVLESMCFQVKDVLDAMRkdageeKSHKGLFLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAA 457
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 16131451 439 RVGTGVYHNFSEAQRDLRHPVRTLLPDMTAhQLYQKKYQRY 479
Cdd:PLN02295 458 GLAVGLWTEEEIFASEKWKNTTTFRPKLDE-EERAKRYASW 497
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
1-489 |
2.68e-24 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 105.68 E-value: 2.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 1 MTQYWLGLDCGGSWLKAGLYDREGREAGVQRLPLCALSPQPGWAERDMAELWQCCMAVIRALLTHSGVSGEQIVGIGISA 80
Cdd:PRK00047 3 MKKYILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGITN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 81 QGKGLFLLDKND-KPLGNAILSSDRRAMEIVRRWQEDGIPEKLypltRQTlwTGHPV------SLLRWLKEHEP---ERy 150
Cdd:PRK00047 83 QRETTVVWDKETgRPIYNAIVWQDRRTADICEELKRDGYEDYI----REK--TGLVIdpyfsgTKIKWILDNVEgarER- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 151 AQIGCVMM-THD-YLRWCLTG--VKGCEESNISESNLYNMSLGEYDPCLTDWLGI-AEInhaLPPVVGSAEICGEITA-- 223
Cdd:PRK00047 156 AEKGELLFgTIDtWLVWKLTGgkVHVTDYTNASRTMLFNIHTLDWDDELLELLDIpRSM---LPEVRPSSEVYGKTNPyg 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 224 --------------QTAALTGLKA----------GTpvvgGLFDVVSTA-------------LCAGIEDEFTLnAVMGTW 266
Cdd:PRK00047 233 ffggevpiagiagdQQAALFGQLCfepgmakntyGT----GCFMLMNTGekavksengllttIAWGIDGKVVY-ALEGSI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 267 AVTSGITRGLRDG----------EAhpyvYGRYV--NDGEFIVheasPTSSGnleWFTAQWGeisfdeinqavaslPKAG 334
Cdd:PRK00047 308 FVAGSAIQWLRDGlkiisdasdsEA----LARKVedNDGVYVV----PAFTG---LGAPYWD--------------SDAR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 335 GDLFflpflygsnaGLemTSGfygmqaiHTRAHLLQAIYEGVVFSHMTHLNRMrERFTDVH--TLRVTGGPAHSDVWMQM 412
Cdd:PRK00047 363 GAIF----------GL--TRG-------TTKEHIIRATLESIAYQTRDVLDAM-QADSGIRlkELRVDGGAVANNFLMQF 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16131451 413 LADVSGLRIELPQVEETGCFGAALAARVGTGVYHNFSEAqRDLRHPVRTLLPDMTAHQLyQKKYQRYQHLIAALQGF 489
Cdd:PRK00047 423 QADILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDEL-KEQWKIDRRFEPQMDEEER-EKLYAGWKKAVKRTLAW 497
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
47-422 |
3.32e-24 |
|
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase (EC 2.7.1.5), also known as L-rhamnulose kinase, ATP:L-rhamnulose phosphotransferase, L-rhamnulose 1-kinase, or rhamnulose kinase, is an enzyme involved in the second step in rhamnose catabolism. It catalyzes the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Rhamnulokinase exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. The subfamily also includes Streptococcus pneumoniae L-fuculose k fuculose Kinase inase (FcsK) that uses ATP to phosphorylate fuculose creating fuculose-1-phosphate, and Alkalihalobacillus clausii bifunctional enzyme RhaA/RhaB. Members of this subfamily belong to the FGGY family of carbohydrate kinases.
Pssm-ID: 466791 [Multi-domain] Cd Length: 460 Bit Score: 104.92 E-value: 3.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 47 DMAELWQCCMAVIRALLTHsgvsGEQIVGIGISAQGKGLFLLDKNDKPLGNAILSSDRRAMEIVRRWQEDGIPEKLYPLT 126
Cdd:cd07771 46 DIDRLFDEIKEGLKKAAEQ----GGDIDSIGIDTWGVDFGLLDKNGELLGNPVHYRDPRTEGMMEELFEKISKEELYERT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 127 RQTLWTGHPVSLLRWLKEHEPERYAQIGCVMMTHDYLRWCLTGVKGCEESNISESNLYNMSLGEYDPCLTDWLGIAEinH 206
Cdd:cd07771 122 GIQFQPINTLYQLYALKKEGPELLERADKLLMLPDLLNYLLTGEKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPR--D 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 207 ALPPVVGSAEICGEITAQTAALTGLKaGTPVV-GGLFDVVSTALCAGIEDEFTLNAVMGTWAVTsGI--TRGLRDGEAhp 283
Cdd:cd07771 200 LFPPIVPPGTVLGTLKPEVAEELGLK-GIPVIaVASHDTASAVAAVPAEDEDAAFISSGTWSLI-GVelDEPVITEEA-- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 284 YVYGrYVN----DGEFIVHEasptssgNL-----------EWfTAQWGEISFDEINQAVASLPKAGG------DLFFLPF 342
Cdd:cd07771 276 FEAG-FTNeggaDGTIRLLK-------NItglwllqecrrEW-EEEGKDYSYDELVALAEEAPPFGAfidpddPRFLNPG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 343 lygsnaglEMtsgfygMQAI------------HTRAHLLQAIYEGVVFSHMTHLNRMRERF-TDVHTLRVTGGPAHSDVW 409
Cdd:cd07771 347 --------DM------PEAIraycretgqpvpESPGEIARCIYESLALKYAKTIEELEELTgKRIDRIHIVGGGSRNALL 412
|
410
....*....|...
gi 16131451 410 MQMLADVSGLRIE 422
Cdd:cd07771 413 CQLTADATGLPVI 425
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
6-474 |
5.45e-24 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 104.73 E-value: 5.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 6 LGLDCGGSWLKAGLYDREGREAGVQRLPlCALSP---QPGWAERDMAELWQ----CCMAVIrallthSGVSGEQIVGIGI 78
Cdd:PRK10331 5 LVLDCGATNVRAIAVDRQGKIVARASTP-NASDIaaeNSDWHQWSLDAILQrfadCCRQIN------SELTECHIRGITV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 79 SAQGKGLFLLDKNDKPLGNAILSSDRRAMEIVRRWQEDGIPEKLYPLTR------QTLWTghpvslLRWLKEHEPERYAQ 152
Cdd:PRK10331 78 TTFGVDGALVDKQGNLLYPIISWKCPRTAAVMENIERYISAQQLQQISGvgafsfNTLYK------LVWLKENHPQLLEQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 153 IGCVMMTHDYLRWCLTGVKGCEESNISESNLYNMSLGEYDPCLTDWLGIAEiNHaLPPVVGSAEICGEITAQTAALTGLK 232
Cdd:PRK10331 152 AHAWLFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSR-RL-FPRLVEAGEQIGTLQPSAAALLGLP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 233 AGTPVVGGLFDVVSTALCAGIE-DEFTLNAvmGTWAVTSgitrgLRDGEAHPYVYGRYvnDGEFIVHEASP--------- 302
Cdd:PRK10331 230 VGIPVISAGHDTQFALFGSGAGqNQPVLSS--GTWEILM-----VRSAQVDTSLLSQY--AGSTCELDSQSglynpgmqw 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 303 TSSGNLEWFTAQW--GEISFDE-INQAVASLPKAGGDLFFLPFLYGSNAGLEmtsgfyGMQAIHTRAHLLQAIYEGVVFS 379
Cdd:PRK10331 301 LASGVLEWVRKLFwtAETPYQTmIEEARAIPPGADGVKMQCDLLACQNAGWQ------GVTLNTTRGHFYRAALEGLTAQ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 380 HMTHLNRMRE--RFTDVHTLRVTGGpAHSDVWMQMLADVSGLRIELPQVEETGCFGAALAARVGTGVYHNFSEAQRDLRH 457
Cdd:PRK10331 375 LKRNLQVLEKigHFKASELLLVGGG-SRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQARAQMKY 453
|
490
....*....|....*..
gi 16131451 458 PVRTLLPDmTAHQLYQK 474
Cdd:PRK10331 454 QYRYFYPQ-TEPEFIEE 469
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
4-479 |
7.01e-22 |
|
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: 98.47 E-value: 7.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 4 YWLGLDCGGSWLKAGLYD-REGREAGVQRLPLCA-LSPQPGWAERDMAELWQCCMAVIRALLTHSGVSGEQIVGIGISAQ 81
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDlYAGLEMAQEPVPYYQdSSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGVDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 82 GKgLFLLDKNDKPL---------GNAILSSDRRAMEIVRRWQEDGiPEKLYPLTRQTLWTGHPVSLLRWLKEHEPERYAQ 152
Cdd:cd07768 81 CS-LAIFDREGTPLmalipypneDNVIFWMDHSAVNEAQWINMQC-PQQLLDYLGGKISPEMGVPKLKYFLDEYSHLRDK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 153 IGCVMMTHDYLRWCLTGVkgcEESNIsESNLYNMSL----GEYDPCLTDWLGIAEINHA----LPPVVGSAEICGEITAQ 224
Cdd:cd07768 159 HFHIFDLHDYIAYELTRL---YEWNI-CGLLGKENLdgeeSGWSSSFFKNIDPRLEHLTttknLPSNVPIGTTSGVALPE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 225 TAALTGLKAGTPVVGGLFDV-VSTALCAGIEDEFTLNAVMGTwavTSGITRGLRDGEAHPYVYGRYVN--DGEFIVHEAS 301
Cdd:cd07768 235 MAEKMGLHPGTAVVVSCIDAhASWFAVASPHLETSLFMIAGT---SSCHMYGTTISDRIPGVWGPFDTiiDPDYSVYEAG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 302 PTSSGNL-EWF------------TAQWGEISFDEINQAVASLPKAGG---DLFFLPFLYGSN---AGLEMTSGFYGMQ-- 360
Cdd:cd07768 312 QSATGKLiEHLfeshpcarkfdeALKKGADIYQVLEQTIRQIEKNNGlsiHILTLDMFFGNRsefADPRLKGSFIGESld 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 361 -AIHTRAHLLQAIYEGVVFSHMTHLNRMRERFTDVHTLRVTGGPAHSDVWMQMLADVSGLRIELPQVEETGCFGAALAAR 439
Cdd:cd07768 392 tSMLNLTYKYIAILEALAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGILGAAVLAK 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 16131451 440 VGTGV---YHNFSEAQRDLRHPVRTLLPDMTAHQ-LYQKKYQRY 479
Cdd:cd07768 472 VAAGKkqlADSITEADISNDRKSETFEPLAYRLGaDYILLYKLL 515
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
259-438 |
1.66e-17 |
|
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: 80.83 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 259 LNAVMGTWAVTSGITRG-LRDGEAHPYVYGRYVNDGEFIVHEASPTSSGNLEWFTAQWGEI----------SFDEINQAV 327
Cdd:pfam02782 1 LAISAGTSSFVLVETPEpVLSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLReelrdagnveSLAELAALA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 328 ASLPkaGGDLFFLPFLYGSNA-GLE--MTSGFYGMQAIHTRAHLLQAIYEGVVFSHMTHLNRMRERF-TDVHTLRVTGGP 403
Cdd:pfam02782 81 AVAP--AGGLLFYPDFSGNRApGADpgARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEgHPIDTIHVSGGG 158
|
170 180 190
....*....|....*....|....*....|....*
gi 16131451 404 AHSDVWMQMLADVSGLRIELPQVEETGCFGAALAA 438
Cdd:pfam02782 159 SRNPLLLQLLADALGLPVVVPGPDEATALGAALLA 193
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
8-269 |
3.22e-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: 74.60 E-value: 3.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 8 LDCGGSWLKAGLYDREGREAGVQRLPLCALsPQPGWAERDMAELWQCCMAVIRALlthsgVSGEQIVGIGISAQGKGLFL 87
Cdd:cd07772 5 FDIGKTNKKLLLFDENGEVLAERSTPNPEI-EEDGYPCEDVEAIWEWLLDSLAEL-----AKRHRIDAINFTTHGATFAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 88 LDKNDKPLG------NAILSSDRRAMEIVRrwqeDGIPEklypltrqtlwTGHPVSL--------LRWLKEHEPERYAQI 153
Cdd:cd07772 79 LDENGELALpvydyeKPIPDEINEAYYAER----GPFEE-----------TGSPPLPgglnlgkqLYWLKREKPELFARA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 154 GCVMMTHDYLRWCLTGVKGCEESNIS-ESNLYNMSLGEYdpclTDWLGIAEINHALPPVVGSAEICGEITAQTAALTGLK 232
Cdd:cd07772 144 KTILPLPQYWAWRLTGKAASEITSLGcHTDLWDFEKNEY----SSLVKKEGWDKLFPPLRKAWEVLGPLRPDLARRTGLP 219
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 16131451 233 AGTPVVGGLFDvvSTA-----LCAGiEDEFTLNAVmGTWAVT 269
Cdd:cd07772 220 KDIPVGCGIHD--SNAallpyLAAG-KEPFTLLST-GTWCIA 257
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
59-266 |
3.52e-13 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 71.29 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 59 IRALLTHSGVSGEQIVGIGISAQGKGLFLLDKNDKPLGNAILSSDRRAMEIVRRWQEDGIPEKLYP------LTRQTLWT 132
Cdd:PRK10640 42 IRLGLNKVCEEGIRIDSIGIDTWGVDYVLLDKQGQRVGLPVSYRDSRTDGVMAQAQQQLGKRDIYRrsgiqfLPFNTLYQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 133 ghpvslLRWLKEHEPERYAQIGCVMMTHDYLRWCLTGVKGCEESNISESNLYNMSLGEYDPCLTDWLGIAEINHALP--- 209
Cdd:PRK10640 122 ------LRALTEQQPELIAQVAHALLIPDYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGAPKAWFGRPthp 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 210 ---------------PVV-------GSAEICGEITAQTAA--------LTGLKAGTPVVGglfdvvSTALCAGIEDE--- 256
Cdd:PRK10640 196 gnvighwicpqgneiPVVavashdtASAVIASPLNDSDAAylssgtwsLMGFESQTPFTN------DTALAANITNEgga 269
|
250
....*....|....
gi 16131451 257 ----FTLNAVMGTW 266
Cdd:PRK10640 270 egryRVLKNIMGLW 283
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-82 |
6.66e-06 |
|
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];
Pssm-ID: 441543 [Multi-domain] Cd Length: 306 Bit Score: 47.97 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 1 MTQYWLGLDCGGSWLKAGLYDREGREAGVQRLPLCALSPQPGWAERdMAELwqccmavIRALLTHSGVSGEQIVGIGISA 80
Cdd:COG1940 3 DAGYVIGIDIGGTKIKAALVDLDGEVLARERIPTPAGAGPEAVLEA-IAEL-------IEELLAEAGISRGRILGIGIGV 74
|
..
gi 16131451 81 QG 82
Cdd:COG1940 75 PG 76
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
167-474 |
1.94e-03 |
|
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. The subfamily includes XKs mainly from eukaryote. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466795 [Multi-domain] Cd Length: 514 Bit Score: 40.62 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 167 LTG-VKGCEESNISESNLYNMSLGEYDPCLTDWLGIAEINHALPPVVGSAEICGEI------------TAQTAALTG--- 230
Cdd:cd07776 196 LLGrYAPIDESDGSGMNLMDIRSRKWSPELLDAATAPDLKEKLGELVPSSTVAGGIssyfverygfspDCLVVAFTGdnp 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 231 -LKAGTPVVGGlfDVvstALCAGieDEFTLNAVMGTwavtsgitrGLRDGEAHpyVYGRYVNDGEF---IVheaspTSSG 306
Cdd:cd07776 276 aSLAGLGLEPG--DV---AVSLG--TSDTVFLVLDE---------PKPGPEGH--VFANPVDPGSYmamLC-----YKNG 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 307 NL--EWFTAQWGEISFDEINQAVASLPKAGGDLFFLPFLYGsnaglEMT-------SGFYGMQAIH---TRAHLLQAIYE 374
Cdd:cd07776 333 SLarERVRDRYAGGSWEKFNELLESTPPGNNGNLGLYFDEP-----EITppvpgggRRFFGDDGVDaffDPAVEVRAVVE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131451 375 GVVFSHMTHLNRMRERfTDVHTLRVTGGPAHSDVWMQMLADVSGLRIELPQVEETGCFGAALAARVGTGVYHNFSEAQRD 454
Cdd:cd07776 408 SQFLSMRLHAERLGSD-IPPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAGSGDFSPEF 486
|
330 340
....*....|....*....|....
gi 16131451 455 LRHPVRTLL----PDMTAHQLYQK 474
Cdd:cd07776 487 VVFSAEEPKlvaePDPEAAEVYDK 510
|
|
| |
