|
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 ... |
3-441 |
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: 606.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 3 YYLGIDCGGTFIKAALISESGEVISLARENVSVLSEQAGYAEREMEALWQVCAKVVKQVIAQSHIAATSIKGVGISAQGK 82
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 83 GVFLLDKQHKPLGRAITSSDQRALHIVKQWQAEGIPQALYPITRQTLWTGHPVSILRWLKEHEPERYSNIGAVLMSHDYL 162
Cdd:cd07802 81 GLYLVDKDGKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKENEPERYDRIRTVLFCKDWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 163 RFCLTGELYCEETNISeSNLYNMQTGKYDEQLAEKLGLQNILEKLPPVIAPNQVAGFVTEDAAKLTGLVVGTPVVGGLFD 242
Cdd:cd07802 161 RYRLTGEISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEELKDKLPPLVPSTEIAGRVTAEAAALTGLPEGTPVAAGAFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 243 VVSTAYCAGLTDETKLNVVLGTWSVVSGITDHIDESQTlPFVYGKYAKAGQFIVHEASPTSAGNLEWFLKQWAN------ 316
Cdd:cd07802 240 VVASALGAGAVDEGQLCVILGTWSINEVVTDEPVVPDS-VGSNSLHADPGLYLIVEASPTSASNLDWFLDTLLGeekeag 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 317 -VSYQQLNEQIAALPPAASSVLFVPFLYGSNAGLGMQAAFYGMQAHHTQAHLLQAICEGVLFSLMTHLERMRIRFPhADT 395
Cdd:cd07802 319 gSDYDELDELIAAVPPGSSGVIFLPYLYGSGANPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHRDHLERLLVARK-PET 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1407948402 396 LRVTGGPAKSAVWMQMLADLSGMRLEIPNVEETGCLGAAMMAMQGA 441
Cdd:cd07802 398 IRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAA 443
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
2-484 |
7.88e-179 |
|
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: 510.53 E-value: 7.88e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 2 NYYLGIDCGGTFIKAALISESGEVISLARENVSVLSEQAGYAEREMEALWQVCAKVVKQVIAQSHIAATSIKGVGISAQG 81
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 82 KGVFLLDKQHKPLGRAITSSDQRALHIVKQWQAEGIPQALYPITRQTLWTGHPVSILRWLKEHEPERYSNIGAVLMSHDY 161
Cdd:COG1070 81 HGLVLLDADGEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIAKVLLPKDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 162 LRFCLTGELYCEETNISESNLYNMQTGKYDEQLAEKLGLQniLEKLPPVIAPNQVAGFVTEDAAKLTGLVVGTPVVGGLF 241
Cdd:COG1070 161 LRYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGID--RELLPELVPPGEVAGTLTAEAAAETGLPAGTPVVAGAG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 242 DVVSTAYCAGLTDETKLNVVLGTWSVVSGITDHIDESQTLPFVYGKYAKAGQFIVHEASPTSAGNLEWFLKQWA---NVS 318
Cdd:COG1070 239 DNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFCHAVPGRWLPMGATNNGGSALRWFRDLFAdgeLDD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 319 YQQLNEQIAALPPAASSVLFVPFLYGSNAGL---GMQAAFYGMQAHHTQAHLLQAICEGVLFSLMTHLERMRIRFPHADT 395
Cdd:COG1070 319 YEELNALAAEVPPGADGLLFLPYLSGERTPHwdpNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEALEEAGVKIDR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 396 LRVTGGPAKSAVWMQMLADLSGMRLEIPNVEETGCLGAAMMAMQGATATQDEQILQNDM----SIYVPNVQNYAAYQAKY 471
Cdd:COG1070 399 IRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMvrvgETIEPDPENVAAYDELY 478
|
490
....*....|...
gi 1407948402 472 QRYQRLVNALKQV 484
Cdd:COG1070 479 ERYRELYPALKPL 491
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
3-477 |
8.16e-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: 359.54 E-value: 8.16e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 3 YYLGIDCGGTFIKAALISESGEVISLARENVSVLSEQAGYAEREMEALWQVCAKVVKQVIAQSHIAATSIKGVGISAQGK 82
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 83 GVFLLDKQHKPLGRAITSSDQRAlhiVKQWQA--EGIPQALYPITRQTLWTGHPVSILRWLKEHEPERYSNIGAVLMSHD 160
Cdd:cd07808 81 GLVLLDKNGRPLRPAILWNDQRS---AAECEEleARLGDEILIITGNPPLPGFTLPKLLWLKENEPEIFARIRKILLPKD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 161 YLRFCLTGELYCEETNISESNLYNMQTGKYDEQLAEKLGLQniLEKLPPVIAPNQVAGFVTEDAAKLTGLVVGTPVVGGL 240
Cdd:cd07808 158 YLRYRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLD--PSILPPIVESTEIVGTLTPEAAEELGLPEGTPVVAGA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 241 FDVVSTAYCAGLTDETKLNVVLGTWSVVSGITD--HIDESQTLpFVYgKYAKAGQFIVHEASPTSAGNLEWFLKQWA--N 316
Cdd:cd07808 236 GDNAAAALGAGVVEPGDALISLGTSGVVFAPTDkpVPDPKGRL-HTF-PHAVPGKWYAMGVTLSAGLSLRWLRDLFGpdR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 317 VSYQQLNEQIAALPPAASSVLFVPFLYG-------SNAglgmQAAFYGMQAHHTQAHLLQAICEGVLFSLMTHLERMRIR 389
Cdd:cd07808 314 ESFDELDAEAAKVPPGSEGLLFLPYLSGertpywdPNA----RGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVLKEL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 390 FPHADTLRVTGGPAKSAVWMQMLADLSGMRLEIPNVEETGCLGAAMMAMQGATATQDEQILQNDMS----IYVPNVQNYA 465
Cdd:cd07808 390 GIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAACIkiekTIEPDPERHE 469
|
490
....*....|..
gi 1407948402 466 AYQAKYQRYQRL 477
Cdd:cd07808 470 AYDELYARYREL 481
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
3-437 |
3.05e-115 |
|
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: 344.55 E-value: 3.05e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 3 YYLGIDCGGTFIKAALISESGEVISLARENVSVLSEQAGYAEREMEALWQVCAKVVKQVIAQSHIAATSIKGVGISAQGK 82
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQMP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 83 GVFLLDKQHKPLGRAITSSDQRAlhivkqwqaegipqalypitrqtlwtghpvsilrwlkeheperysnigAVLMSHDYL 162
Cdd:cd00366 81 GVVLVDADGNPLRPAIIWLDRRA------------------------------------------------KFLQPNDYI 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 163 RFCLTGELYCEETNISESNLYNMQTGKYDEQLAEKLGLqnILEKLPPVIAPNQVAGFVTEDAAKLTGLVVGTPVVGGLFD 242
Cdd:cd00366 113 VFRLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGI--PREKLPPIVESGEVVGRVTPEAAEETGLPAGTPVVAGGGD 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 243 VVSTAYCAGLTDETKLNVVLGTWSVVSGITDHIDESQTLPFVYGkYAKAGQFIVHEASPTSAGNLEWFLKQWAN-----V 317
Cdd:cd00366 191 TAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEPVPPDPRLLNRC-HVVPGLWLLEGAINTGGASLRWFRDEFGEeedsdA 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 318 SYQQLNEQIAALPPAASSVLFVPFLYGSNAGL---GMQAAFYGMQAHHTQAHLLQAICEGVLFSLMTHLERMRIRFPHAD 394
Cdd:cd00366 270 EYEGLDELAAEVPPGSDGLIFLPYLSGERSPIwdpAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEILEELGVKIK 349
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1407948402 395 TLRVTGGPAKSAVWMQMLADLSGMRLEIPNVEETGCLGAAMMA 437
Cdd:cd00366 350 EIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
3-438 |
9.94e-111 |
|
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: 335.36 E-value: 9.94e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 3 YYLGIDCGGTFIKAALISESGEVISLARENVSVLSEQAGYAEREMEALWQVCAKVVKQVIAQSHIAATSIKGVGISAQGK 82
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 83 GVFLLDKQHKPLGRAITSSDQRALHIVKQWQAEGIPQALYPITRQTLWTGHPVSILRWLKEHEPERYSNIGAVLMSHDYL 162
Cdd:cd24121 81 GTWLVDEDGRPVRDAILWLDGRAADIVERWQADGIAEAVFEITGTGLFPGSQAAQLAWLKENEPERLERARTALHCKDWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 163 RFCLTGELyceETNISESNL--YNMQTGKYDEQLAEKLGLQNILEKLPPVIAPNQVAGFVTEDAAKLTGLVVGTPVVGGL 240
Cdd:cd24121 161 FYKLTGEI---ATDPSDASLtfLDFRTRQYDDEVLDLLGLEELRHLLPPIRPGTEVIGPLTPEAAAATGLPAGTPVVLGP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 241 FDVVSTAYCAGLTDETKLNVVLGTWSVVSGITDHIDESQ-----TLPFVY-GKYAKagqfivheASPTSAG--NLEWFLK 312
Cdd:cd24121 238 FDVVATALGSGAIEPGDACSILGTTGVHEVVVDEPDLEPegvgyTICLGVpGRWLR--------AMANMAGtpNLDWFLR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 313 QWANV-----------SYQQLNEQIAALPPAASSVLFVPFLygSNAGL-------GMQAAFYGMQAHHTQAHLLQAICEG 374
Cdd:cd24121 310 ELGEVlkegaepagsdLFQDLEELAASSPPGAEGVLYHPYL--SPAGErapfvnpNARAQFTGLSLEHTRADLLRAVYEG 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1407948402 375 VLFSLMTHLERMRIRfphADTLRVTGGPAKSAVWMQMLADLSGMRLEIPNVEETGCLGAAMMAM 438
Cdd:cd24121 388 VALAMRDCYEHMGED---PGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAA 448
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
3-437 |
3.86e-106 |
|
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: 323.00 E-value: 3.86e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 3 YYLGIDCGGTFIKAALISESGEVISLARENVSVLSEQAGYAEREMEALWQVCAKVVKQVIAQShiAATSIKGVGISAQGK 82
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQA--GPDPIAAISVSSQGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 83 GVFLLDKQHKPLGRAITSSDQRALHIVKQWQAEGIPQALYPITRQTLWTGHPVSILRWLKEHEPERYSNIGAVLMSHDYL 162
Cdd:cd07773 79 SGVPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAKWLSVADYI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 163 RFCLTGELYCEETNISESNLYNMQTGKYDEQLAEKLGLQniLEKLPPVIAPNQVAGFVTEDAAKLTGLVVGTPVV-GGLf 241
Cdd:cd07773 159 AYRLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGID--ASLLPELVPSGTVIGTVTPEAAEELGLPAGTPVVvGGH- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 242 DVVSTAYCAGLTDETKLNVVLGTWSVVSGITDHIDESQTLP---FVYGKYAKAGQFIVHeASPTSAGNLEWFLKQWAN-- 316
Cdd:cd07773 236 DHLCAALGAGVIEPGDVLDSTGTAEALLAVVDEPPLDEMLAeggLSYGHHVPGGYYYLA-GSLPGGALLEWFRDLFGGde 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 317 VSYQQLNEQIAALPPAASSVLFVPFLYGSNA---GLGMQAAFYGMQAHHTQAHLLQAICEGVLFSLMTHLERMRIRFPHA 393
Cdd:cd07773 315 SDLAAADELAEAAPPGPTGLLFLPHLSGSGTpdfDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEALEKAGIPI 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1407948402 394 DTLRVTGGPAKSAVWMQMLADLSGMRLEIPNVEETGCLGAAMMA 437
Cdd:cd07773 395 DEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLA 438
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
3-474 |
6.11e-105 |
|
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: 321.39 E-value: 6.11e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 3 YYLGIDCGGTFIKAALISESGEVISLARENVSVLSEQAGYAEREMEALWQVCAKVVKQVIAQSHIAATSIKGVGISAQGK 82
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 83 GVFLLDKQHKPLGRAITSSDQRALHivkqwQAEGIPQALYPITRQTLWTGHPVS----I--LRWLKEHEPERYSNIGAVL 156
Cdd:cd07805 81 GVVPVDKDGNPLRNAIIWSDTRAAE-----EAEEIAGGLGGIEGYRLGGGNPPSgkdpLakILWLKENEPEIYAKTHKFL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 157 MSHDYLRFCLTGELYCEETNISESNLYNMQTGKYDEQLAEKLGLqnILEKLPPVIAPNQVAGFVTEDAAKLTGLVVGTPV 236
Cdd:cd07805 156 DAKDYLNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGI--DPDKLPELVPSTEVVGELTPEAAAELGLPAGTPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 237 VGGLFDVVSTAYCAGLTDETKLNVVLGTWSVVSGITDH--IDESQ---TLPfvygkYAKAGQFIVHeASPTSAG-NLEWF 310
Cdd:cd07805 234 VGGGGDAAAAALGAGAVEEGDAHIYLGTSGWVAAHVPKpkTDPDHgifTLA-----SADPGRYLLA-AEQETAGgALEWA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 311 LKQWA------NVSYQQLNEQIAALPPAASSVLFVPFLYGSNAGL---GMQAAFYGMQAHHTQAHLLQAICEGVLFSLMT 381
Cdd:cd07805 308 RDNLGgdedlgADDYELLDELAAEAPPGSNGLLFLPWLNGERSPVedpNARGAFIGLSLEHTRADLARAVLEGVAFNLRW 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 382 HLERMRIRFPHADTLRVTGGPAKSAVWMQMLADLSGMRLEIP-NVEETGCLGAAMMAMQGA---TATQDEQILQNDMSIY 457
Cdd:cd07805 388 LLEALEKLTRKIDELRLVGGGARSDLWCQILADVLGRPVEVPeNPQEAGALGAALLAAVGLgllKSFDEAKALVKVEKVF 467
|
490
....*....|....*..
gi 1407948402 458 VPNVQNYAAYQAKYQRY 474
Cdd:cd07805 468 EPDPENRARYDRLYEVF 484
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
3-249 |
1.32e-101 |
|
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: 304.26 E-value: 1.32e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 3 YYLGIDCGGTFIKAALISESGEVISLARENVSVLSEQAGYAEREMEALWQVCAKVVKQVIAQSHIAATSIKGVGISAQGK 82
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 83 GVFLLDKQHKPLGRAITSSDQRALHIVKQWQAEGIPQALYPITRQTLWTGHPVSILRWLKEHEPERYSNIGAVLMSHDYL 162
Cdd:pfam00370 81 GTVLLDKNDKPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHKFLTIHDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 163 RFCLTGELYCEETNISESNLYNMQTGKYDEQLAEKLGLQNilEKLPPVIAPNQVAGFVTEDAAKLTGLVVGTPVVGGLFD 242
Cdd:pfam00370 161 RWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPR--DHLPPLVESSEIYGELNPELAAMWGLDEGVPVVGGGGD 238
|
....*..
gi 1407948402 243 VVSTAYC 249
Cdd:pfam00370 239 QQAAAFG 245
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
3-441 |
6.75e-101 |
|
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: 309.84 E-value: 6.75e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 3 YYLGIDCGGTFIKAALISESGEVISLARENVSVLSEQAGYAEREMEALWQVCAKVVKQVIAQSHIAATSIKGVGISAQGK 82
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGLVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 83 GVFLLDKQHKPLGRAITSSDQRAlhiVKQ--WQAEGIP-QALYPITRQTLWTGHPVSILRWLKEHEPERYSNIGAVLMSH 159
Cdd:cd07804 81 ALVPVDENGKPLRPAILYGDRRA---TEEieWLNENIGeDRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTRKFLGAY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 160 DYLRFCLTGELYCEETN-ISESNLYNMQTGKYDEQLAEKLGLqnILEKLPPVIAPNQVAGFVTEDAAKLTGLVVGTPVVG 238
Cdd:cd07804 158 DYIVYKLTGEYVIDYSSaGNEGGLFDIRKRTWDEELLEALGI--DPDLLPELVPSTEIVGEVTKEAAEETGLAEGTPVVA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 239 GLFDVVSTAYCAGLTDETKLNVVLGTWSVVSGITDHIDESQTLPFVYgkYAKAGQFIVHEASPTSAGNLEWFLKQWANV- 317
Cdd:cd07804 236 GTVDAAASALSAGVVEPGDLLLMLGTAGDIGVVTDKLPTDPRLWLDY--HDIPGTYVLNGGMATSGSLLRWFRDEFAGEe 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 318 ----------SYQQLNEQIAALPPAASSVLFVPFLYG-------SNAglgmQAAFYGMQAHHTQAHLLQAICEGVLFSLM 380
Cdd:cd07804 314 veaeksggdsAYDLLDEEAEKIPPGSDGLIVLPYFMGertpiwdPDA----RGVIFGLTLSHTRAHLYRALLEGVAYGLR 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1407948402 381 THLERMRIRFPHADTLRVTGGPAKSAVWMQMLADLSGMRLEIPNVEETGCLGAAMMAMQGA 441
Cdd:cd07804 390 HHLEVIREAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGV 450
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
3-478 |
9.67e-99 |
|
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: 305.25 E-value: 9.67e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 3 YYLGIDCGGTFIKAALISESGEVISLARENVSVLSEQAGYAEREMEALWQVCAKVVKQVIAQSHiaATSIKGVGISAQGK 82
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLG--GGEVDAIGFSSAMH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 83 GVFLLDKQHKPLGRAITSSDQRALHIVKQWQAEGIPQALYPITrqtlwtG---HPVS---ILRWLKEHEPERYSNIgAVL 156
Cdd:cd07770 79 SLLGVDEDGEPLTPVITWADTRAAEEAERLRKEGDGSELYRRT------GcpiHPMYplaKLLWLKEERPELFAKA-AKF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 157 MS-HDYLRFCLTGELYCEETNISESNLYNMQTGKYDEQLAEKLGLQniLEKLPPVIAPNQVAGFVTEDAAKLTGLVVGTP 235
Cdd:cd07770 152 VSiKEYLLYRLTGELVTDYSTASGTGLLNIHTLDWDEEALELLGID--EEQLPELVDPTEVLPGLKPEFAERLGLLAGTP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 236 VVGGLFDVVSTAYCAGLTDETKLNVVLGTwsvvSG----ITDH--IDESQTLpFVYgkYAKAGQFIVHEASpTSAGN-LE 308
Cdd:cd07770 230 VVLGASDGALANLGSGALDPGRAALTVGT----SGairvVSDRpvLDPPGRL-WCY--RLDENRWLVGGAI-NNGGNvLD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 309 WFLKQWAN--VSYQQLNEQIAALPPAASSVLFVPFLYGSNA---GLGMQAAFYGMQAHHTQAHLLQAICEGVLFSLMTHL 383
Cdd:cd07770 302 WLRDTLLLsgDDYEELDKLAEAVPPGSHGLIFLPYLAGERApgwNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKSIY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 384 ERMRIRFPHADTLRVTGGPAKSAVWMQMLADLSGMRLEIPNVEETGCLGAAMMAM--QGATATQDEQILQNDMSIYVPNV 461
Cdd:cd07770 382 EALEELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALeaLGLISSLEADELVKIGKVVEPDP 461
|
490
....*....|....*..
gi 1407948402 462 QNYAAYQAKYQRYQRLV 478
Cdd:cd07770 462 ENHAIYAELYERFKKLY 478
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
3-467 |
1.01e-93 |
|
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli sugar kinase YgcE. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466798 [Multi-domain] Cd Length: 433 Bit Score: 290.96 E-value: 1.01e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 3 YYLGIDCGGTFIKAALISESGEVISLARENVSVLSEQAGYAEREMEALWQVCAKVVKQVIAQSHIAATSIKGVGISAQGK 82
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 83 GVFLLDKQHKPLGRAITSSDQRALHIvkqwqaegipqalypitrqtlwtghpvsilrwlkeheperysnigavLMSHDYL 162
Cdd:cd07779 81 TFVPVDEDGRPLRPAISWQDKRTAKF-----------------------------------------------LTVQDYL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 163 RFCLTGELYCEETNISESNLYNMQTGKYDEQLAEKLGLQniLEKLPPVIAPNQVAGFVTEDAAKLTGLVVGTPVVGGLFD 242
Cdd:cd07779 114 LYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGID--RDKLPELVPPGTVIGTLTKEAAEETGLPEGTPVVAGGGD 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 243 vvstAYCA----GLTDETKLNVVLGTWSVVSGITDHIDESQTLPFVYGKYAKAGQFIVhEAS-PTSAGNLEWFLKQWANV 317
Cdd:cd07779 192 ----QQCAalgaGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPGKWVL-EGSiNTGGSAVRWFRDEFGQD 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 318 ----------SYQQLNEQIAALPPAASSVLFVPFLYGSNAGLGMQAA---FYGMQAHHTQAHLLQAICEGVLFSLMTHLE 384
Cdd:cd07779 267 evaekelgvsPYELLNEEAAKSPPGSDGLLFLPYLAGAGTPYWNPEArgaFIGLTLSHTRAHLARAILEGIAFELRDNLE 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 385 RMRIRFPHADTLRVTGGPAKSAVWMQMLADLSGMRLEIPNVEETGCLGAAMMAMQGATATQDEQILQNDM----SIYVPN 460
Cdd:cd07779 347 AMEKAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKAMvrvtDTFEPD 426
|
....*..
gi 1407948402 461 VQNYAAY 467
Cdd:cd07779 427 PENVAIY 433
|
|
| XylB |
TIGR01312 |
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of ... |
5-479 |
1.65e-87 |
|
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: 276.50 E-value: 1.65e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 5 LGIDCGGTFIKAALISESGEVISLARENVSVLSEQAGYAEREMEALWQVCAKVVKQVIAQSHIAATSIKGVGISAQGKGV 84
Cdd:TIGR01312 1 LGIDLGTSGVKALLVDEQGEVIASGSAPHTVISPHPGWSEQDPEDWWDATEEAIKELLEQASEMGQDIKGIGISGQMHGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 85 FLLDKQHKPLGRAITSSDQRALHIVKQWQAEGIPQALYPITRQTLWTGHPVSILRWLKEHEPERYSNIGAVLMSHDYLRF 164
Cdd:TIGR01312 81 VLLDANGEVLRPAILWNDTRTAQECEELEAELGDERVLEITGNLALPGFTAPKLLWVRKHEPEVFARIAKVMLPKDYLRY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 165 CLTGELYCEETNISESNLYNMQTGKYDEQLAEKLGLQniLEKLPPVIAPNQVAGFVTEDAAKLTGLVVGTPVVGGLFDVV 244
Cdd:TIGR01312 161 RLTGEYVTEYSDASGTGWFDVAKRAWSKELLDALDLP--ESQLPELIESSEKAGTVRPEVAARLGLSAGVPVAAGGGDNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 245 STAYCAGLTDETKLNVVLGTWSVVSGITDHIDESQTLPFVYGKYAKAGQFivHEASPT-SAGN-LEWFLKQWANVSYQQL 322
Cdd:TIGR01312 239 AGAIGTGTVDPGDAMMSLGTSGVVYAVTDKPLPDPAGAVHGFCHALPGGW--LPMGVTlSATSsLEWFRELFGKEDVEAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 323 NEQIAALPPAASSVLFVPFLYGS---NAGLGMQAAFYGMQAHHTQAHLLQAICEGVLFSLMTHLERMRirfpHAD----- 394
Cdd:TIGR01312 317 NELAEQSPPGAEGVTFLPYLNGErtpHLDPQARGSFIGLTHNTTRADLTRAVLEGVTFALRDSLDILR----EAGgipiq 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 395 TLRVTGGPAKSAVWMQMLADLSGMRLEIPNVEETGCLGAAMMAMQGAT----ATQDEQILQNDMSIYVPNVQNYAAYQAK 470
Cdd:TIGR01312 393 SIRLIGGGAKSPAWRQMLADIFGTPVDVPEGEEGPALGAAILAAWALGekdlAALCSEAVVKQTESVLPIAENVEAYEEL 472
|
....*....
gi 1407948402 471 YQRYQRLVN 479
Cdd:TIGR01312 473 YERYKKLYQ 481
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
3-442 |
2.24e-73 |
|
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: 238.60 E-value: 2.24e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 3 YYLGIDCGGTFIKAALI-SESGEVISLARENVSVLSEQAGYAEREMEALWQVCAKVVKQVIAQSHIAATSIKGVGISAQG 81
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIdAETGRVVASGSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 82 KGVFLLDKQHKPLGRAI----TSSDQRALHIVKQWQAEGIPQALYPItrQTLWTghpVSILRWLKEHEPERYSNIGAVLM 157
Cdd:cd07809 81 HGLVALDADGKVLRPAKlwcdTRTAPEAEELTEALGGKKCLLVGLNI--PARFT---ASKLLWLKENEPEHYARIAKILL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 158 SHDYLRFCLTGELYceeTNISESN---LYNMQTGKYDEQLAEKLGLQNIL-EKLPPVIAPNQVAGFVTEDAAKLTGLVVG 233
Cdd:cd07809 156 PHDYLNWKLTGEKV---TGLGDASgtfPIDPRTRDYDAELLAAIDPSRDLrDLLPEVLPAGEVAGRLTPEGAEELGLPAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 234 TPVVGGLFDVVSTAYCAGLTDETKLNVVLGTWSVVSGITDH--IDESQTlpfVYGkYAKAGQFIVHEASPTSAGN--LEW 309
Cdd:cd07809 233 IPVAPGEGDNMTGALGTGVVNPGTVAVSLGTSGTAYGVSDKpvSDPHGR---VAT-FCDSTGGMLPLINTTNCLTawTEL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 310 FLKQwANVSYQQLNEQIAALPPAASSVLFVPFLYG------SNAGlgmqAAFYGMQ-AHHTQAHLLQAICEGVLFSLMTH 382
Cdd:cd07809 309 FREL-LGVSYEELDELAAQAPPGAGGLLLLPFLNGertpnlPHGR----ASLVGLTlSNFTRANLARAALEGATFGLRYG 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 383 LERMRIRFPHADTLRVTGGPAKSAVWMQMLADLSGMRLEIPNVEETGCLGAAMMAMQGAT 442
Cdd:cd07809 384 LDILRELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
3-441 |
3.56e-71 |
|
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: 232.88 E-value: 3.56e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 3 YYLGIDCGGTFIKAALISESGEVISLARENVSVLSEQAGYAERE--MEALWQVCAKVVKQVIAQSHIAATSIKGVGISAQ 80
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYPDAKEfdPEELWEKICEAIREALKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 81 GKGVFLLDKQHKPLgRAITSSDQRAlhivKQWQAEgIPQALYpITRQTLWTGHPVSI-----LRWLKEHEPERYSNIGAV 155
Cdd:cd07798 81 REGIVFLDKDGREL-YAGPNIDARG----VEEAAE-IDDEFG-EEIYTTTGHWPTELfpaarLLWFKENRPEIFERIATV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 156 LMSHDYLRFCLTGELYCEETNISESNLYNMQTGKYDEQLAEKLGLQniLEKLPPVIAPNQVAGFVTEDAAKLTGLVVGTP 235
Cdd:cd07798 154 LSISDWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLP--PEILPEIVPSGTVLGTVSEEAARELGLPEGTP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 236 VVGGLFDVVSTAYCAGLTDETKLNVVLGTWSVVSGITDHIDESQTLPFVYGKYAKAGQFIVhEASPTSAG-NLEWF---L 311
Cdd:cd07798 232 VVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWTGCHLVPGKWVL-ESNAGVTGlNYQWLkelL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 312 KQWANVSYQQLNEQIAALPPAASSVL------FVPFLYGSNAGLGMQAAFYGMQAHHTQAHLLQAICEGVLFSLMTHLER 385
Cdd:cd07798 311 YGDPEDSYEVLEEEASEIPPGANGVLaflgpqIFDARLSGLKNGGFLFPTPLSASELTRGDFARAILENIAFAIRANLEQ 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1407948402 386 M-RIRFPHADTLRVTGGPAKSAVWMQMLADLSGMRLEIPNVEETGCLGAAMMAMQGA 441
Cdd:cd07798 391 LeEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGA 447
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
3-441 |
1.07e-70 |
|
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: 230.96 E-value: 1.07e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 3 YYLGIDCGGTFIKAALISESGEVISLARENVSVLSEQAGYAEREMEALWQVCAKVVKQVIAQSHIAatSIKGVGISAQGK 82
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRPR--RVVAIAVDGTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 83 GVFLLDKQHKPLGRAITSSDQRAlhivkQWQAEGIPQALYPITRQTLWTGHPVSIL---RWLKEHEPERYSNIGAVLMSH 159
Cdd:cd07783 79 TLVLVDREGEPLRPAIMYNDARA-----VAEAEELAEAAGAVAPRTGLAVSPSSSLaklLWLKRHEPEVLAKTAKFLHQA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 160 DYLRFCLTGELYC-EETNISESnLYNMQTGKYDEQLAEKLGLQniLEKLPPVIAPNQVAGFVTEDAAKLTGLVVGTPVVG 238
Cdd:cd07783 154 DWLAGRLTGDRGVtDYNNALKL-GYDPETGRWPSWLLALLGIP--PDLLPRVVAPGTVIGTLTAEAAEELGLPAGTPVVA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 239 GLFDVVSTAYCAGLTDETKLNVVLGTWSVVSGITD-HIDESQTLpfVYGKYAKAGQFIVHEASPTSAGNLEWFLKqwaNV 317
Cdd:cd07783 231 GTTDSIAAFLASGAVRPGDAVTSLGTTLVLKLLSDkRVPDPGGG--VYSHRHGDGYWLVGGASNTGGAVLRWFFS---DD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 318 SYQQLNEQIAalPPAASSVLFVPFLygsnaGLG---------MQAAFYGMqaHHTQAHLLQAICEGVLFslmthLERMRI 388
Cdd:cd07783 306 ELAELSAQAD--PPGPSGLIYYPLP-----LRGerfpfwdpdARGFLLPR--PHDRAEFLRALLEGIAF-----IERLGY 371
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1407948402 389 R------FPHADTLRVTGGPAKSAVWMQMLADLSGMRLEIPnVEETGCLGAAMMAMQGA 441
Cdd:cd07783 372 ErleelgAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIA-EEEEAALGAALLAAAGL 429
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
3-483 |
2.84e-66 |
|
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: 221.64 E-value: 2.84e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 3 YYLGIDCGGTFIKAALI-SESGEVISLARENV--SVLSEQAGYAEREMEALWQVCAKVVKQVIAQSHIAATSIKGVGISA 79
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVdLADGEELASAVVPYptGYIPPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 80 QGKGVFLLDKQHKPLGRAITSSDQRAlhivkQWQAEGIPQALYPITRQTL-WTGHPVS-------ILrWLKEHEPERYSN 151
Cdd:cd07781 81 TSSTVVPVDEDGNPLAPAILWMDHRA-----QEEAAEINETAHPALEYYLaYYGGVYSsewmwpkAL-WLKRNAPEVYDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 152 IgAVLMSH-DYLRFCLTGELYCEETNISESNLYNMQTGKYDEQLAEKLG--LQNILEKLP-PVIAPNQVAGFVTEDAAKL 227
Cdd:cd07781 155 A-YTIVEAcDWINARLTGRWVRSRCAAGHKWMYNEWGGGPPREFLAALDpgLLKLREKLPgEVVPVGEPAGTLTAEAAER 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 228 TGLVVGTPVVGGLFDVVSTAYCAGLTDETKLNVVLGTWSVVSGITDhidESQTLPFVYGKYAKA---GQFIVhEASPTSA 304
Cdd:cd07781 234 LGLPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTSTCHLMVSP---KPVDIPGICGPVPDAvvpGLYGL-EAGQSAV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 305 GN-LEWFLKQWANV-------SYQQLNEQIAALPPAASSVLFVPFLYGS-----NAGLgmQAAFYGMQAHHTQAHLLQAI 371
Cdd:cd07781 310 GDiFAWFVRLFVPPaeergdsIYALLSEEAAKLPPGESGLVALDWFNGNrtplvDPRL--RGAIVGLTLGTTPAHIYRAL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 372 CEGVLFSLMTHLERMRIRFPHADTLRVTGGPA-KSAVWMQMLADLSGMRLEIPNVEETGCLGAAMMAMQGATATQDEQIL 450
Cdd:cd07781 388 LEATAFGTRAIIERFEEAGVPVNRVVACGGIAeKNPLWMQIYADVLGRPIKVPKSDQAPALGAAILAAVAAGVYADIEEA 467
|
490 500 510
....*....|....*....|....*....|....*..
gi 1407948402 451 QNDM----SIYVPNVQNYAAYQAKYQRYQRLVNALKQ 483
Cdd:cd07781 468 ADAMvrvdRVYEPDPENHAVYEELYALYKELYDALGP 504
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
3-474 |
1.16e-52 |
|
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: 185.23 E-value: 1.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 3 YYLGIDCGGTFIKAALISESGEVISLARENVSVLSEQA--GYAEREMEALWQVCAKVVKQVIAQSHIAATSIKGVGISAQ 80
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREWRHKEVPDvpGSMDFDTEKNWKLICECIREALKKAGIAPKSIAAISTTSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 81 GKGVFLLDKQHKPLGrAITSSDQRALHIVKQWQA--EGIPQALYPITRQTLWTGHPvSILRWLKEHEPERYSNIGAVLMS 158
Cdd:cd07775 81 REGIVLYDNEGEEIW-ACANVDARAAEEVSELKElyNTLEEEVYRISGQTFALGAI-PRLLWLKNNRPEIYRKAAKITML 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 159 HDYLRFCLTGELYCEETNISESNLYNMQTGKYDEQLAEKLGLQNILekLPPVIAPNQVAGFVTEDAAKLTGLVVGTPVVG 238
Cdd:cd07775 159 SDWIAYKLSGELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADI--LPPVVESGTVIGKVTKEAAEETGLKEGTPVVV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 239 GLFDVVSTAYCAGLTDETKLNVVLGT--WSVVSGITDHIDES---QTLPfvygkYAKAGQFIVHEASPTSAGNLEWF--- 310
Cdd:cd07775 237 GGGDVQLGCLGLGVVRPGQTAVLGGSfwQQEVNTAAPVTDPAmniRVNC-----HVIPDMWQAEGISFFPGLVMRWFrda 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 311 ----LKQWANVS----YQQLNEQIAALPPAASsvlfvpflygsnaglGMQAAFYG-MQAHH------------------T 363
Cdd:cd07775 312 fcaeEKEIAERLgidaYDLLEEMAKDVPPGSY---------------GIMPIFSDvMNYKNwrhaapsflnldidpekcN 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 364 QAHLLQAICEGVLFSLMTHLERMRIRFPH-ADTLRVTGGPAKSAVWMQMLADLSGMRLEIPNVEETGCLGAAMMAMQGA- 441
Cdd:cd07775 377 KATFFRAIMENAAIVSAGNLERIAEFSGIfPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGAg 456
|
490 500 510
....*....|....*....|....*....|....*..
gi 1407948402 442 ----TATQDEQILQNDmSIYVPNVQNYAAYQAKYQRY 474
Cdd:cd07775 457 iyssLEEAVESLVKWE-REYLPNPENHEVYQDLYEKW 492
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
1-485 |
1.83e-46 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 169.03 E-value: 1.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 1 MNYYLGIDCGGTFIKAALISESGEVISLARENVSVLSEQ--AGYAEREMEALWQVCAKVVKQVIAQSHIAATSIKGVGIS 78
Cdd:PRK10939 2 MSYLMALDAGTGSIRAVIFDLNGNQIAVGQAEWRHLAVPdvPGSMEFDLEKNWQLACQCIRQALQKAGIPASDIAAVSAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 79 AQGKGVFLLDKQHKPLGrAITSSDQRALHIVKQWQA--EGIPQALYPITRQTLWTGHPVSILrWLKEHEPERYSNIGAVL 156
Cdd:PRK10939 82 SMREGIVLYDRNGTEIW-ACANVDARASREVSELKElhNNFEEEVYRCSGQTLALGALPRLL-WLAHHRPDIYRQAHTIT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 157 MSHDYLRFCLTGELYCEETNISESNLYNMQTGKYDEQLAEKLGLQniLEKLPPVIAPNQVAGFVTEDAAKLTGLVVGTPV 236
Cdd:PRK10939 160 MISDWIAYMLSGELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLR--ADILPPVKETGTVLGHVTAKAAAETGLRAGTPV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 237 VGGLFDVVSTAYCAGLTDETKLNVVLGT-WSVVSGITDHI-DESQTL---PFVYGKYAKAgqfivhEA-SPTSAGNLEWF 310
Cdd:PRK10939 238 VMGGGDVQLGCLGLGVVRPGQTAVLGGTfWQQVVNLPAPVtDPNMNIrinPHVIPGMVQA------ESiSFFTGLTMRWF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 311 -------LKQWA---NVS-YQQLNEQIAALPPAASSVLFVpFlygSNAglgMQaafYGMQAHH--------------TQA 365
Cdd:PRK10939 312 rdafcaeEKLLAerlGIDaYSLLEEMASRVPVGSHGIIPI-F---SDV---MR---FKSWYHAapsfinlsidpekcNKA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 366 HLLQAICEGVLFSLMTHLERMRiRF--PHADTLRVTGGPAKSAVWMQMLADLSGMRLEIPNVEETGCLGAAMMAMQGA-- 441
Cdd:PRK10939 382 TLFRALEENAAIVSACNLQQIA-AFsgVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEATALGCAIAAGVGAgi 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1407948402 442 ---TATQDEQILQNDMSiYVPNVQNYAAYQAKYQRYQRLVNA-LKQVD 485
Cdd:PRK10939 461 yssLAETGERLVRWERT-FEPNPENHELYQEAKEKWQAVYADqLGLVD 507
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
4-482 |
1.89e-46 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 168.22 E-value: 1.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 4 YLGIDCGGTFIKAALISESGEVISLARENVSVLSEQAGYAEREMEALWQVCAKVVKQVIAQSHIaaTSIKGVGISAQGKG 83
Cdd:PRK15027 2 YIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSL--QDVKALGIAGQMHG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 84 VFLLDKQHKPLGRAITSSDQRALHIVkQWQAEGIPQAlYPITRQTLWTGHPVSILRWLKEHEPERYSNIGAVLMSHDYLR 163
Cdd:PRK15027 80 ATLLDAQQRVLRPAILWNDGRCAQEC-ALLEARVPQS-RVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 164 FCLTGELYCEETNISESNLYNMQTGKYDEQLAEKLGLQNilEKLPPVIAPNQVAGFVTEDAAKLTGLvVGTPVVGGLFDV 243
Cdd:PRK15027 158 LRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSR--DQMPALYEGSEITGALLPEVAKAWGM-ATVPVVAGGGDN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 244 VSTAYCAGLTDETKLNVVLGTWSVVSGITDHI---DESQTLPFVygkYAKAGQFIVHEASPTSAGNLEWFLKQWANVSYQ 320
Cdd:PRK15027 235 AAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFlskPESAVHSFC---HALPQRWHLMSVMLSAASCLDWAAKLTGLSNVP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 321 QLneqIAALPPA---ASSVLFVPFLYGSNA---GLGMQAAFYGMQAHHTQAHLLQAICEGVLFSL---MTHLERMRIRfP 391
Cdd:PRK15027 312 AL---IAAAQQAdesAEPVWFLPYLSGERTphnNPQAKGVFFGLTHQHGPNELARAVLEGVGYALadgMDVVHACGIK-P 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 392 HADTLrvTGGPAKSAVWMQMLADLSGMRLEIPNVEETG-CLGAAMMAMQGATATQDEQILQNDMSI---YVPNVQNYAAY 467
Cdd:PRK15027 388 QSVTL--IGGGARSEYWRQMLADISGQQLDYRTGGDVGpALGAARLAQIAANPEKSLIELLPQLPLeqsHLPDAQRYAAY 465
|
490
....*....|....*
gi 1407948402 468 QAKYQRYQRLVNALK 482
Cdd:PRK15027 466 QPRRETFRRLYQQLL 480
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
3-437 |
3.61e-41 |
|
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466796 [Multi-domain] Cd Length: 436 Bit Score: 152.76 E-value: 3.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 3 YYLGIDCGGTFIKAALI-SESGEVISLARE--NVSVLSEQAGYAEREMEALWQVCAKVVKQVIAQSHIaatSIKGVGISA 79
Cdd:cd07777 1 NVLGIDIGTTSIKAALLdLESGRILESVSRptPAPISSDDPGRSEQDPEKILEAVRNLIDELPREYLS---DVTGIGITG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 80 QGKGVFLLDKQHKPLGRAITSSDQRALHIVKQwQAEGIPQALYPITRQTLWTGHPVSILRWLKEHEPERYSNiGAVLMSH 159
Cdd:cd07777 78 QMHGIVLWDEDGNPVSPLITWQDQRCSEEFLG-GLSTYGEELLPKSGMRLKPGYGLATLFWLLRNGPLPSKA-DRAGTIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 160 DYLRFCLTG--ELYCEETNISESNLYNMQTGKYDEQLAEKLGLQNILekLPPVIAPNQVAGFVTEDAAKltglvvGTPVV 237
Cdd:cd07777 156 DYIVARLTGlpKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVIL--LPEIVPSGEIVGTLSSALPK------GIPVY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 238 GGLFDVVSTAYCAGLTDETKLNVVLGTWSVVSGITDHIDES---QTLPFVYGKYAKAGQFIvheasptSAGN-LEW---F 310
Cdd:cd07777 228 VALGDNQASVLGSGLNEENDAVLNIGTGAQLSFLTPKFELSgsvEIRPFFDGRYLLVAASL-------PGGRaLAVlvdF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 311 LKQWA-----NVSYQQLNEQI--AALPPAASSVLFVPFLYGSNAGLGMQAAFYGMQAHH-TQAHLLQAICEGVLFSLMTH 382
Cdd:cd07777 301 LREWLrelggSLSDDEIWEKLdeLAESEESSDLSVDPTFFGERHDPEGRGSITNIGESNfTLGNLFRALCRGIAENLHEM 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1407948402 383 LERMRIRFPHADTLRVTGG-PAKSAVWMQMLADLSGMRLEIPNVEETGCLGAAMMA 437
Cdd:cd07777 381 LPRLDLDLSGIERIVGSGGaLRKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
3-479 |
1.68e-39 |
|
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: 149.25 E-value: 1.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 3 YYLGIDCGGTFIKAALISESGEVISLARENVSVLSEQAGYAEREMEALWQVCAKVVKQVIAQSHIAATSIKGVGISAQgK 82
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQ-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 83 GVFLL-DKQ-HKPLGRAITSSDQRALHIVKQWQ-------AEGIPQALYPITRQ---------TLWTGHPVSILRWLKEH 144
Cdd:cd07793 80 NTFLTwDKKtGKPLHNFITWQDLRAAELCESWNrslllkaLRGGSKFLHFLTRNkrflaasvlKFSTAHVSIRLLWILQN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 145 EPERYSnigavLMSHDYLRF-CL---------TGELYCEE-TNISESNLYNMQTGKYDEQLAEKLGLQniLEKLPPViap 213
Cdd:cd07793 160 NPELKE-----AAEKGELLFgTIdtwllwkltGGKVHATDySNASATGLFDPFTLEWSPILLSLFGIP--SSILPEV--- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 214 nqvagfvtEDAAKLTGL----VVGTP-----VVGglfDVVSTAYCAGLTDETKLNVVLGT---WSVVSGITDHIDESQTL 281
Cdd:cd07793 230 --------KDTSGDFGStdpsIFGAEipitaVVA---DQQAALFGECCFDKGDVKITMGTgtfIDINTGSKPHASVKGLY 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 282 PFVYGKYAKAGQFIVHEASPTSAGNLEWfLKQWANVSYQQLNEQIAALPPAASSVLFVPFLYGSNAGL---GMQAAFYGM 358
Cdd:cd07793 299 PLVGWKIGGEITYLAEGNASDTGTVIDW-AKSIGLFDDPSETEDIAESVEDTNGVYFVPAFSGLQAPYndpTACAGFIGL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 359 QAHHTQAHLLQAICEGVLFS---LMTHLER-MRIRFPHadtLRVTGGPAKSAVWMQMLADLSGMRLEIPNVEETGCLGAA 434
Cdd:cd07793 378 TPSTTKAHLVRAILESIAFRvkqLLETMEKeTSIKISS---IRVDGGVSNNDFILQLIADLLGKPVERPKNTEMSALGAA 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1407948402 435 MMAmqGATA---TQDEQI--LQNDMSIYVPNvQNYAAYQAKYQRYQRLVN 479
Cdd:cd07793 455 FLA--GLASgiwKSKEELkkLRKIEKIFEPK-MDNEKREELYKNWKKAVK 501
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
1-441 |
1.06e-35 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 138.24 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 1 MNYYLGIDCGGTFIKAALISESGEVIslARENVSVLSEQA----GYAEREMEALWQVCAKVVKQVIAQshIAATSIKGVG 76
Cdd:PRK10331 1 QDVILVLDCGATNVRAIAVDRQGKIV--ARASTPNASDIAaensDWHQWSLDAILQRFADCCRQINSE--LTECHIRGIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 77 ISAQGKGVFLLDKQHKPLGRAITSSDQRALHIVKQWQAEGIPQALYPITR------QTLWTghpvsiLRWLKEHEPERYS 150
Cdd:PRK10331 77 VTTFGVDGALVDKQGNLLYPIISWKCPRTAAVMENIERYISAQQLQQISGvgafsfNTLYK------LVWLKENHPQLLE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 151 NIGAVLMSHDYLRFCLTGELYCEETNISESNLYNMQTGKYDEQLAEKLGLQNILekLPPVIAPNQVAGFVTEDAAKLTGL 230
Cdd:PRK10331 151 QAHAWLFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRL--FPRLVEAGEQIGTLQPSAAALLGL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 231 VVGTPVVGGLFDVVSTAYCAGltdeTKLN-VVL--GTWSVVSGITDHIDESqtLPFVY-----------GKYAKAGQFIv 296
Cdd:PRK10331 229 PVGIPVISAGHDTQFALFGSG----AGQNqPVLssGTWEILMVRSAQVDTS--LLSQYagstceldsqsGLYNPGMQWL- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 297 heasptSAGNLEWFLKQW--ANVSYQQLNEQIAALPPAASSVLFVPFLYGSnaglgMQAAFYGMQAHHTQAHLLQAICEG 374
Cdd:PRK10331 302 ------ASGVLEWVRKLFwtAETPYQTMIEEARAIPPGADGVKMQCDLLAC-----QNAGWQGVTLNTTRGHFYRAALEG 370
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1407948402 375 VLFSLMTHLERM-RIRFPHADTLRVTGGPAKSAVWMQMLADLSGMRLEIPNVEETGCLGAAMMAMQGA 441
Cdd:PRK10331 371 LTAQLKRNLQVLeKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGV 438
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
1-477 |
3.59e-35 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 137.55 E-value: 3.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 1 MNYYLGIDCGGTFIKAALIS-ESGEVISLARENVS------VLSEQAGYAEREMEALWQVCAKVVKQVIAQSHIAATSIK 73
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDaADGEELASAVHPYPrwviglYLPPPPDQARQHPLDYLEALEAAVREALAQAGVDPADVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 74 GVGISAQGKGVFLLDKQHKPLgrAITSSDQRALH-IVKQWQ---AegIPQALYpITRQTLWTGHPVS------------- 136
Cdd:COG1069 81 GIGVDATGCTPVPVDADGTPL--ALLPEFAENPHaMVILWKdhtA--QEEAER-INELAKARGEDYLryvggiissewfw 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 137 --ILrWLKEHEPERYSNIgAVLMSH-DYLRFCLTGELyceetniSESN-------LYNMQTGKY-DEQLAEKLG--LQNI 203
Cdd:COG1069 156 pkIL-HLLREDPEVYEAA-DSFVELcDWITWQLTGSL-------KRSRctaghkaLWHAHEGGYpSEEFFAALDplLDGL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 204 LEKLP-PVIAPNQVAGFVTEDAAKLTGLVVGTPVVGGLFDVVSTAYCAGLTDETKLNVVLGTwsvvSgiTDHI---DESQ 279
Cdd:COG1069 227 ADRLGtEIYPLGEPAGTLTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGGVEPGTLVKVMGT----S--TCHMlvsPEER 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 280 TLPFVYGKYAKA---GqFIVHEASPTSAGNL-EWFLKQ--WA----------NVS-YQQLNEQIAALPPAASSVLFVPFL 342
Cdd:COG1069 301 FVPGICGQVDGSivpG-MWGYEAGQSAVGDIfAWFVRLlvPPleyekeaeerGISlHPLLTEEAAKLPPGESGLHALDWF 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 343 YG-----SNAGLgmQAAFYGMQAHHTQAHLLQAICEGVLFSLMTHLERMR-----IrfphaDTLRVTGG-PAKSAVWMQM 411
Cdd:COG1069 380 NGnrsplADQRL--KGVILGLTLGTDAEDIYRALVEATAFGTRAIIERFEeegvpI-----DEIIACGGiATKNPLVMQI 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1407948402 412 LADLSGMRLEIPNVEETGCLGAAMMAMQGATATQDEQILQNDMS-----IYVPNVQNYAAYQAKYQRYQRL 477
Cdd:COG1069 453 YADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEEAMAAMGsgfdkVYTPDPENVAVYDALYAEYLQL 523
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
3-478 |
2.71e-31 |
|
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: 126.04 E-value: 2.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 3 YYLGIDCGGTFIKAALISESGEVISLARENVSVLSEQAGYAEREMEALWQVCAKVVKQVIAQSHIAATSIKGVGISAQGK 82
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 83 GVFLLDKQ-HKPLGRAITSSDQRALHIVKQWQAEGipqaLYPITRQTlwTGHPV------SILRWLKEHEP---ERYSN- 151
Cdd:cd07769 81 TTVVWDKKtGKPLYNAIVWQDRRTADICEELKAKG----LEERIREK--TGLPLdpyfsaTKIKWILDNVPgarERAERg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 152 ---IGAVlmshD-YLRFCLT-GELY-CEETNISESNLYNMQTGKYDEQLAEKLGLQNILekLPPVIAPNQVAGFVTEDaa 225
Cdd:cd07769 155 ellFGTI----DtWLIWKLTgGKVHvTDVTNASRTMLFNIHTLEWDDELLELFGIPRSM--LPEVRPSSEVFGYTDPE-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 226 kltGLVVGTPVVG--G-----LF--------DVVSTaYCAGL-----TDETKL---NVVLGT--WSvvsgitdhIDEsqt 280
Cdd:cd07769 227 ---GLGAGIPIAGilGdqqaaLFgqgcfepgMAKNT-YGTGCfllmnTGEKPVpskNGLLTTiaWQ--------IGG--- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 281 lPFVYgkyakagqfiVHEASPTSAGN-LEWfLKQWANV--SYQQLnEQIAALPPAASSVLFVP-FlygsnAGLG-----M 351
Cdd:cd07769 292 -KVTY----------ALEGSIFIAGAaIQW-LRDNLGLieDAAET-EELARSVEDNGGVYFVPaF-----SGLGapywdP 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 352 QA--AFYGMQAHHTQAHLLQAICEGV------LFSLMTHLERMRIRfphadTLRVTGGPAKSAVWMQMLADLSGMRLEIP 423
Cdd:cd07769 354 DArgAIVGLTRGTTKAHIVRAALESIayqtrdVLEAMEKDSGIKLK-----ELRVDGGATANNFLMQFQADILGVPVVRP 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1407948402 424 NVEETGCLGAAMMAMQGATATQDEQILQNDMSI---YVPNVQNyAAYQAKYQRYQRLV 478
Cdd:cd07769 429 KVAETTALGAAYLAGLAVGFWKDLDELASLWQVdkrFEPSMDE-EERERLYRGWKKAV 485
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
3-438 |
3.08e-31 |
|
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: 125.33 E-value: 3.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 3 YYLGIDCGGTFIKAALISESGEVISLA---R-ENVSVlsEQAGYAEREMEALWQVCAKVVKQVIAQshiaATSIKGVGIS 78
Cdd:cd07771 1 NYLAVDLGASSGRVILGSLDGGKLELEeihRfPNRPV--EINGHLYWDIDRLFDEIKEGLKKAAEQ----GGDIDSIGID 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 79 AQGKGVFLLDKQHKPLGRAITSSDQRALHIVKQWQAEGIPQALYPITRQTLWTGHPVSILRWLKEHEPERYSNIGAVLMS 158
Cdd:cd07771 75 TWGVDFGLLDKNGELLGNPVHYRDPRTEGMMEELFEKISKEELYERTGIQFQPINTLYQLYALKKEGPELLERADKLLML 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 159 HDYLRFCLTGELYCEETNISESNLYNMQTGKYDEQLAEKLGLQniLEKLPPVIAPNQVAGFVTEDAAKLTGLvVGTPVV- 237
Cdd:cd07771 155 PDLLNYLLTGEKVAEYTIASTTQLLDPRTKDWSEELLEKLGLP--RDLFPPIVPPGTVLGTLKPEVAEELGL-KGIPVIa 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 238 GGLFDVVSTAYCAGLTDETKLNVVLGTWSVVSGITDHI---DESQTLPF-----VYGKYAK----AGQFIVHEasptsag 305
Cdd:cd07771 232 VASHDTASAVAAVPAEDEDAAFISSGTWSLIGVELDEPvitEEAFEAGFtneggADGTIRLlkniTGLWLLQE------- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 306 nlewFLKQWAN----VSYQQLNEQIAALPPAASsvLFVP----FLYGSNaglgMQAAF--Y----GMQAHHTQAHLLQAI 371
Cdd:cd07771 305 ----CRREWEEegkdYSYDELVALAEEAPPFGA--FIDPddprFLNPGD----MPEAIraYcretGQPVPESPGEIARCI 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1407948402 372 CEGVLFSLMTHLERMR----IRFphaDTLRVTGGPAKSAVWMQMLADLSGMRLEIPNVEET--GCLGAAMMAM 438
Cdd:cd07771 375 YESLALKYAKTIEELEeltgKRI---DRIHIVGGGSRNALLCQLTADATGLPVIAGPVEATaiGNLLVQLIAL 444
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
3-478 |
4.10e-31 |
|
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: 126.11 E-value: 4.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 3 YYLGIDCGGTFIKAALISESGEVISLARENVSVLSEQAGYAEREMEALWQVCAKVVKQVIAQSHIAATSIKGVGISAQGK 82
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFDATCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 83 GVfLLDKQHKPLgrAITSS-----------DQRALHivkqwQAEgipqalyPITRqtlwTGHPV--------SI------ 137
Cdd:cd07782 81 LV-VLDAEGKPV--SVSPSgddernvilwmDHRAVE-----EAE-------RINA----TGHEVlkyvggkiSPemeppk 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 138 LRWLKEHEPERYSNIGAVLMSHDYLRFCLTGE-------LYCEETNISESnlynMQTGKYDEQLAEKLGLQNILE----K 206
Cdd:cd07782 142 LLWLKENLPETWAKAGHFFDLPDFLTWKATGSltrslcsLVCKWTYLAHE----GSEGGWDDDFFKEIGLEDLVEdnfaK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 207 LPPVIAPNQ--VAGFVTEDAAKLTGLVVGTPVVGGLFD----------VVSTAYCAGLTD-ETKLNVVLGTWS---VVSg 270
Cdd:cd07782 218 IGSVVLPPGepVGGGLTAEAAKELGLPEGTPVGVSLIDahagglgtlgADVGGLPCEADPlTRRLALICGTSSchmAVS- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 271 itdhiDESQTLPFVYGKYAKA----------GQ--------FIV--HEASPTsagnlewfLKQWANVS----YQQLN--- 323
Cdd:cd07782 297 -----PEPVFVPGVWGPYYSAmlpglwlnegGQsatgalldHIIetHPAYPE--------LKEEAKAAgksiYEYLNerl 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 324 EQIAALPPAASSVL----FV-------------PFLYGSNAGLGMQAAFYGMQAHHTQAhlLQAICEGVlfslmTH-LER 385
Cdd:cd07782 364 EQLAEEKGLPLAYLtrdlHVlpdfhgnrspladPTLRGMISGLTLDTSLDDLALLYLAT--LQALAYGT-----RHiIEA 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 386 MRIRFPHADTLRVTGGPAKSAVWMQMLADLSGMRLEIPNVEETGCLGAAMMamqGATATQDEQILQNDM-------SIYV 458
Cdd:cd07782 437 MNAAGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAIL---GAVASGDFPSLWDAMaamsgpgKVVE 513
|
570 580
....*....|....*....|
gi 1407948402 459 PNVQNYAAYQAKYQRYQRLV 478
Cdd:cd07782 514 PNEELKKYHDRKYEVFLKMY 533
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
1-479 |
4.17e-27 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 113.92 E-value: 4.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 1 MNYYLGIDCGGTFIKAALISESGEVISLARENVSVLSEQAGYAEREMEALWQVCAKVVKQVIAQSHI--AATSIKGVGIS 78
Cdd:PTZ00294 1 MKYIGSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREkgPSFKIKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 79 AQGKGVFLLDKQH-KPLGRAITSSDQRALHIVKQWQAEGipqALYPITRQTlwTGHPVSI------LRWLKEHEPE---R 148
Cdd:PTZ00294 81 NQRETVVAWDKVTgKPLYNAIVWLDTRTYDIVNELTKKY---GGSNFFQKI--TGLPISTyfsafkIRWMLENVPAvkdA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 149 YSNIGAVLMSHD-YLRFCLTGE-LYCEE-TNISESNLYNMQTGKYDEQLAEKLGlqnILEKLPPVIAPN-QVAGFVTEDA 224
Cdd:PTZ00294 156 VKEGTLLFGTIDtWLIWNLTGGkSHVTDvTNASRTFLMNIKTLKWDEELLNKFG---IPKETLPEIKSSsENFGTISGEA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 225 aklTGLVVGTPVVGGLFDVVSTAYCAGLTDE--TK----------LNVvlGTWSVVSG----ITDHIDESQTLPFVY--- 285
Cdd:PTZ00294 233 ---VPLLEGVPITGCIGDQQAALIGHGCFEKgdAKntygtgcfllMNT--GTEIVFSKhgllTTVCYQLGPNGPTVYale 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 286 GKYAKAGQFIvheasptsagnlEW------FLKQWANVsyqqlnEQIAALPPAASSVLFVPFLYG-------SNAglgmQ 352
Cdd:PTZ00294 308 GSIAVAGAGV------------EWlrdnmgLISHPSEI------EKLARSVKDTGGVVFVPAFSGlfapywrPDA----R 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 353 AAFYGMQAHHTQAHLLQAICEGVLFSLMTHLERMRirfphADT------LRVTGGPAKSAVWMQMLADLSGMRLEIPNVE 426
Cdd:PTZ00294 366 GTIVGMTLKTTRAHIVRAALEAIALQTNDVIESME-----KDAgielnsLRVDGGLTKNKLLMQFQADILGKDIVVPEMA 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1407948402 427 ETGCLGAAMMAmqGATA------TQDEQILQNDMSIYVPNVQNyAAYQAKYQRYQRLVN 479
Cdd:PTZ00294 441 ETTALGAALLA--GLAVgvwkslEEVKKLIRRSNSTFSPQMSA-EERKAIYKEWNKAVE 496
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
1-482 |
1.83e-26 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 112.08 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 1 MNYYLGIDCGGTFIKAALISESGEVISLARENVSVLSEQAGYAEREMEALWQVCAKVVKQVIAQSHIAATSIKGVGISAQ 80
Cdd:COG0554 2 KKYILAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISAEDIAAIGITNQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 81 GKGVFLLDKQH-KPLGRAITSSDQRALHIVKQWQAEGipqaLYPITRQTlwTGHPV------SILRWLKEHEP---ERYS 150
Cdd:COG0554 82 RETTVVWDRKTgKPLYNAIVWQDRRTADICEELKADG----LEDLIREK--TGLVLdpyfsaTKIKWILDNVPgarERAE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 151 NiGAVLM----ShdYLRFCLT-GELY-CEETNISESNLYNMQTGKYDEQLAEKLGLQNILekLPPVIAPNQVAGFVTEDa 224
Cdd:COG0554 156 A-GELLFgtidS--WLIWKLTgGKVHvTDVTNASRTMLFNIHTLDWDDELLELFGIPRSM--LPEVRPSSEVFGETDPD- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 225 akltGLVVGTPVVG-------GLF--------DVVSTaYCAGltdetklNVVL---GTWSVVSG---ITD---HIDESQT 280
Cdd:COG0554 230 ----LFGAEIPIAGiagdqqaALFgqacfepgMAKNT-YGTG-------CFLLmntGDEPVRSKnglLTTiawGLGGKVT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 281 lpfvygkYAkagqfivHEASPTSAGNL-EWfLKQWANV--SYQQLnEQIAALPPAASSVLFVPFLygsnAGLG-----MQ 352
Cdd:COG0554 298 -------YA-------LEGSIFVAGAAvQW-LRDGLGLidSAAES-EALARSVEDNGGVYFVPAF----TGLGapywdPD 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 353 A--AFYGMQAHHTQAHLLQAICEGVLFSLMTHLERMRirfphADT------LRVTGGPAKSAVWMQMLADLSGMRLEIPN 424
Cdd:COG0554 358 ArgAIFGLTRGTTRAHIARAALESIAYQTRDVLDAME-----ADSgiplkeLRVDGGASANDLLMQFQADILGVPVERPK 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1407948402 425 VEETGCLGAAMMAMQGATATQDEQILQNDMSI---YVPNVQNyAAYQAKYQRYQRLVNALK 482
Cdd:COG0554 433 VTETTALGAAYLAGLAVGFWKSLEELAALWKVdrrFEPQMDE-EERERLYAGWKKAVERTL 492
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
258-438 |
3.58e-22 |
|
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: 93.93 E-value: 3.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 258 LNVVLGTWSVVSGITDHIDESQtlPFVYGKYAKA---GQFIVHEASPTSAGNLEWFLKQWA----------NVSYQQLNE 324
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLSV--HGVWGPYTNEmlpGYWGLEGGQSAAGSLLAWLLQFHGlreelrdagnVESLAELAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 325 QIAALPPAAssVLFVPFLYGSNAGLGMQAA---FYGMQAHHTQAHLLQAICEGVLFSLMTHLERMRIRFPHA-DTLRVTG 400
Cdd:pfam02782 79 LAAVAPAGG--LLFYPDFSGNRAPGADPGArgsITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPiDTIHVSG 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 1407948402 401 GPAKSAVWMQMLADLSGMRLEIPNVEETGCLGAAMMAM 438
Cdd:pfam02782 157 GGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAA 194
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
4-479 |
5.07e-21 |
|
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: 95.67 E-value: 5.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 4 YLG-IDCGGTFIKAALISESGEVISLARENVSVLSEQAGYAEREMEALWQVCAKVVKQVIAQ---SHIAATSIKGVGISA 79
Cdd:cd07792 2 LVGaIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEEAVEKlkaLGISPSDIKAIGITN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 80 QGKGVFLLDKQH-KPLGRAITSSDQRALHIVKQWQAEgipqalYPITRQTL--WTGHPVSI------LRWLKEHEPE--- 147
Cdd:cd07792 82 QRETTVVWDKSTgKPLYNAIVWLDTRTSDTVEELSAK------TPGGKDHFrkKTGLPISTyfsavkLRWLLDNVPEvkk 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 148 RYSN----IGAVlmshD-YLRFCLTGELYCEE-----TNISESNLYNMQTGKYDEQLAEKLGLQniLEKLPPVIAPNQVA 217
Cdd:cd07792 156 AVDDgrllFGTV----DsWLIWNLTGGKNGGVhvtdvTNASRTMLMNLRTLQWDPELCEFFGIP--MSILPEIRSSSEVY 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 218 GFVTEDAAKltglvvGTPVVGGLFDvvSTAYCAG---LTD-ETK----------LNVvlGTWSVVSG---ITdhidesqT 280
Cdd:cd07792 230 GKIASGPLA------GVPISGCLGD--QQAALVGqgcFKPgEAKntygtgcfllYNT--GEEPVFSKhglLT-------T 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 281 LPFVYGKYAKagqfiVH---EASPTSAGN-LEWFLKQWANVSYQQLNEQIAALPPAASSVLFVP-F--LYG----SNAgl 349
Cdd:cd07792 293 VAYKLGPDAP-----PVyalEGSIAIAGAaVQWLRDNLGIISSASEVETLAASVPDTGGVYFVPaFsgLFApywrPDA-- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 350 gmQAAFYGMQAHHTQAHLLQAICEGVLFSLMTHLERMRirfphAD------TLRVTGGPAKSAVWMQMLADLSGMRLEIP 423
Cdd:cd07792 366 --RGTIVGLTQFTTKAHIARAALEAVCFQTREILDAMN-----KDsgipltSLRVDGGMTKNNLLMQIQADILGIPVERP 438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 424 NVEETGCLGAAMMAMQGA----TATQDEQILQNDMSIYVPNVQNyAAYQAKYQRYQRLVN 479
Cdd:cd07792 439 SMVETTALGAAIAAGLAVgvwkSLDELKSLNEGGRTVFEPQISE-EERERRYKRWKKAVE 497
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
3-437 |
9.94e-20 |
|
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: 91.92 E-value: 9.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 3 YYLGIDCGGTFIKAALI--SESGEVISLARENVSVLSEQAGYAEREMEALWQVCAKVVKQVIAQSHIAATSIKGVGISAQ 80
Cdd:cd07768 1 YGIGVDVGTSSARAGVYdlYAGLEMAQEPVPYYQDSSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGVDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 81 GKgVFLLDKQHKPLGRAITSSDQRAlhiVKQW-------QAEGI----PQALYPITRQTLWTGHPVSILRWLKEHEPERY 149
Cdd:cd07768 81 CS-LAIFDREGTPLMALIPYPNEDN---VIFWmdhsavnEAQWInmqcPQQLLDYLGGKISPEMGVPKLKYFLDEYSHLR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 150 SNIGAVLMSHDYLRFCLTGElycEETNISES---NLYNMQTGKYDEQLAEKLGLQ---NILEKLPPVIAP-NQVAGFVTE 222
Cdd:cd07768 157 DKHFHIFDLHDYIAYELTRL---YEWNICGLlgkENLDGEESGWSSSFFKNIDPRlehLTTTKNLPSNVPiGTTSGVALP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 223 DAAKLTGLVVGTPVVGGLFDV-VSTAYCAGLTDETKLNVVLGTWSVVSGITDhidESQTLPFVYGKYAKA--GQFIVHEA 299
Cdd:cd07768 234 EMAEKMGLHPGTAVVVSCIDAhASWFAVASPHLETSLFMIAGTSSCHMYGTT---ISDRIPGVWGPFDTIidPDYSVYEA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 300 SPTSAGNL-EWF-------------LKQWANVsYQQLNE---QIAALPPAASSVLFVPFLYGSNAGLG---MQAAFYGMQ 359
Cdd:cd07768 311 GQSATGKLiEHLfeshpcarkfdeaLKKGADI-YQVLEQtirQIEKNNGLSIHILTLDMFFGNRSEFAdprLKGSFIGES 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 360 AHHTQ---AHLLQAICEGVLFSLMTHLERMRIRFPHADTLRVTGGPAKSAVWMQMLADLSGMRLEIPNVEETGCLGAAMM 436
Cdd:cd07768 390 LDTSMlnlTYKYIAILEALAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGILGAAVL 469
|
.
gi 1407948402 437 A 437
Cdd:cd07768 470 A 470
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
3-437 |
5.14e-18 |
|
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: 86.39 E-value: 5.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 3 YYLGIDCGGTFIKAALISESGEVISLARENVSVLSEQAGYAEREMEALWQVCAKVVKQVIAQSHIAATSIKGVGISAQGK 82
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 83 GVFLLDKQH-KPLGRAITSSDQRALHIVKQWQAEGipqaLYPITRQTlwTGHPV------SILRWLKEHEP---ERYSNi 152
Cdd:cd07786 81 TTVVWDRETgKPVYNAIVWQDRRTADICEELKAEG----HEEMIREK--TGLVLdpyfsaTKIRWILDNVPgarERAER- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 153 GAVLM----ShdYLRFCLTGEL--YCEETNISESNLYNMQTGKYDEQLAEKLGL-QNILeklpPVIAPNqVAGFVTEDAA 225
Cdd:cd07786 154 GELAFgtidS--WLIWKLTGGKvhATDVTNASRTMLFNIHTLEWDDELLELFGIpASML----PEVKPS-SEVFGYTDPD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 226 KLTGLVVGTPVVG----GLFDvvSTAYCAGLTDETklnvvLGTWS-VVSGITDHIDESQ-----TLPFVYG---KYAKag 292
Cdd:cd07786 227 LLGAEIPIAGIAGdqqaALFG--QACFEPGMAKNT-----YGTGCfMLMNTGEKPVRSKnglltTIAWQLGgkvTYAL-- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 293 qfivhEASPTSAGNL-EW------FLKQWANVsyqqlnEQIAALPPAASSVLFVPFLygsnAGLG-----MQA--AFYGM 358
Cdd:cd07786 298 -----EGSIFIAGAAvQWlrdglgLIESAAET------EALARSVPDNGGVYFVPAF----TGLGapywdPDArgAIFGL 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 359 QAHHTQAHLLQAICEGVLFSLMTHLERMRirfphAD------TLRVTGGPAKSAVWMQMLADLSGMRLEIPNVEETGCLG 432
Cdd:cd07786 363 TRGTTRAHIARAALESIAYQTRDLLEAME-----ADsgiplkELRVDGGASANDFLMQFQADILGVPVERPKVTETTALG 437
|
....*
gi 1407948402 433 AAMMA 437
Cdd:cd07786 438 AAYLA 442
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
47-477 |
2.11e-16 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 81.82 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 47 MEALwqvcAKVVKQVIAQSHIAATSIKGVGISAQGKGVFLLDKQHKPLgraitssdqrALH---------IVKQWQAEG- 116
Cdd:PRK04123 59 IESL----EAAIPAVLKEAGVDPAAVVGIGVDFTGSTPAPVDADGTPL----------ALLpefaenphaMVKLWKDHTa 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 117 IPQA--LYPITRQ------TLWTGHPVS-------ILRWLkEHEPERYSNIGAVLMSHDYLRFCLTGELYCEetNISESN 181
Cdd:PRK04123 125 QEEAeeINRLAHErgeadlSRYIGGIYSsewfwakILHVL-REDPAVYEAAASWVEACDWVVALLTGTTDPQ--DIVRSR 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 182 -------LYNMQTGKY-DEQLAEKL--GLQNIL-EKLP-PVIAPNQVAGFVTEDAAKLTGLVVGTPVVGGLFDVVSTAYC 249
Cdd:PRK04123 202 caaghkaLWHESWGGLpSADFFDALdpLLARGLrDKLFtETWTAGEPAGTLTAEWAQRLGLPEGVAVSVGAFDAHMGAVG 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 250 AGLTDETKLNVVlGTWS----------VVSGITDHIDESqTLPFVYGkYaKAGQfivheasptSA-GNL-EWFLKQWANV 317
Cdd:PRK04123 282 AGAEPGTLVKVM-GTSTcdilladkqrAVPGICGQVDGS-IVPGLIG-Y-EAGQ---------SAvGDIfAWFARLLVPP 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 318 SYQQ------------LNEQIAALPPAASSVLFVPFLYG-----SNAGLGMqaAFYGMQAHHTQAHLLQAICEGVLFSLM 380
Cdd:PRK04123 349 EYKDeaeargkqllelLTEAAAKQPPGEHGLVALDWFNGrrtplADQRLKG--VITGLTLGTDAPDIYRALIEATAFGTR 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 381 THLERMRIRFPHADTLRVTGG-PAKSAVWMQMLADLSGMRLEIPNVEETGCLGAAMMAMQGATATQDEQILQNDMS---- 455
Cdd:PRK04123 427 AIMECFEDQGVPVEEVIAAGGiARKNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDIPEAQQAMAspve 506
|
490 500
....*....|....*....|...
gi 1407948402 456 -IYVPNVQNYAAYQAKYQRYQRL 477
Cdd:PRK04123 507 kTYQPDPENVARYEQLYQEYKQL 529
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
39-454 |
2.42e-14 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 75.12 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 39 QAGYAEREMEALWQ---VC-AKVVKQVIAQSHIAATSIKGVGISAQGKGVFLLDKQH-KPLGRAITSSDQRALHIVKQWQ 113
Cdd:PLN02295 37 QAGWVEHDPMEILEsvlTCiAKALEKAAAKGHNVDSGLKAIGITNQRETTVAWSKSTgRPLYNAIVWMDSRTSSICRRLE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 114 AE--GIPQALypitRQTlwTGHPVSI------LRWLKEHEPERYSNI--GAVLMS--HDYLRFCLTGELYCEE-----TN 176
Cdd:PLN02295 117 KElsGGRKHF----VET--CGLPISTyfsatkLLWLLENVDAVKEAVksGDALFGtiDSWLIWNLTGGASGGVhvtdvTN 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 177 ISESNLYNMQTGKYDEQLAEKLGLQniLEKLPPVIAPNQVAGFVTEDaakltGLVVGTPVVGGLFDVVSTAY---C---- 249
Cdd:PLN02295 191 ASRTMLMNLKTLDWDKPTLEALGIP--AEILPKIVSNSEVIGTIAKG-----WPLAGVPIAGCLGDQHAAMLgqrCrpge 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 250 AGLTDETKLNVVLGTwsvvsgiTDHIDESQ-----TLPFVYGKyAKAGQFIVhEASPTSAG-NLEWFLKQWANVSYQQLN 323
Cdd:PLN02295 264 AKSTYGTGCFILLNT-------GEEVVPSKhglltTVAYKLGP-DAPTNYAL-EGSVAIAGaAVQWLRDNLGIIKSASEI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 324 EQIAALPPAASSVLFVPFLYGSNAGLGMQAA---FYGMQAHHTQAHLLQAICEGVLFSLMTHLERMrirfpHAD------ 394
Cdd:PLN02295 335 EALAATVDDTGGVYFVPAFSGLFAPRWRDDArgvCVGITRFTNKAHIARAVLESMCFQVKDVLDAM-----RKDageeks 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1407948402 395 -----TLRVTGGPAKSAVWMQMLADLSGMRLEIPNVEETGCLGAAMMAMQGATATQDEQILQNDM 454
Cdd:PLN02295 410 hkglfLLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTEEEIFASEK 474
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
7-437 |
4.08e-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: 74.22 E-value: 4.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 7 IDCGGTFIKAALISESGEVISLARENVSVLSEqAGYAEREMEALWQVCAKVVKQvIAQSHiaatSIKGVGISAQGKGVFL 86
Cdd:cd07772 5 FDIGKTNKKLLLFDENGEVLAERSTPNPEIEE-DGYPCEDVEAIWEWLLDSLAE-LAKRH----RIDAINFTTHGATFAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 87 LDKQHKPLgraitssdqralHIVKQWQAEGIP---QALYPITRQTLWTGHPVSI--------LRWLKEHEPERYSNIGAV 155
Cdd:cd07772 79 LDENGELA------------LPVYDYEKPIPDeinEAYYAERGPFEETGSPPLPgglnlgkqLYWLKREKPELFARAKTI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 156 LMSHDYLRFCLTGELYCEETNIS-ESNLYNMQTGKYdEQLAEKLGlqnILEKLPPVIAPNQVAGFVTEDAAKLTGLVVGT 234
Cdd:cd07772 147 LPLPQYWAWRLTGKAASEITSLGcHTDLWDFEKNEY-SSLVKKEG---WDKLFPPLRKAWEVLGPLRPDLARRTGLPKDI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 235 PVVGGLFDvvSTA----YCAGLTDETklnVVL--GTWSvvsgITDHIDESQTLPF------------VYGKYAKAGQF-- 294
Cdd:cd07772 223 PVGCGIHD--SNAallpYLAAGKEPF---TLLstGTWC----IAMNPGNDLPLTEldlardclynldVFGRPVKTARFmg 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 295 -IVHEaspTSAGNLEWFLKQWANVSY--QQLNEQIAALPPAASSVLFVPFLYGSNAGlgmqaAFYGmqahHTQAHLLQAI 371
Cdd:cd07772 294 gREYE---RLVERIAKSFPQLPSLADlaKLLARGTFALPSFAPGGGPFPGSGGRGVL-----SAFP----SAEEAYALAI 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1407948402 372 CEGVlfsLMTHLERMRIRFPhADTLRVTGGPAKSAVWMQMLADL-SGMRLEIPNVEETGCLGAAMMA 437
Cdd:cd07772 362 LYLA---LMTDYALDLLGSG-VGRIIVEGGFAKNPVFLRLLAALrPDQPVYLSDDSEGTALGAALLA 424
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
44-472 |
3.38e-13 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 71.29 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 44 EREM-EALWQVCAkvvkqviaqSHIAATSIkgvGISAQGKGVFLLDKQHKPLGRAITSSDQRALHIVKQWQAEGIPQALY 122
Cdd:PRK10640 39 ESAIrLGLNKVCE---------EGIRIDSI---GIDTWGVDYVLLDKQGQRVGLPVSYRDSRTDGVMAQAQQQLGKRDIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 123 PITRQTLWTGHPVSILRWLKEHEPERYSNIGAVLMSHDYLRFCLTGELYCEETNISESNLYNMQTGKYDEQLAEKLGLQ- 201
Cdd:PRK10640 107 RRSGIQFLPFNTLYQLRALTEQQPELIAQVAHALLIPDYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGAPk 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 202 NILEKlpPVIAPNQVAGFVTEDAAKLtglvvgtPVVG-GLFDVVSTAYCAGLTDETKLNVVLGTWSVVsGItdhidESQT 280
Cdd:PRK10640 187 AWFGR--PTHPGNVIGHWICPQGNEI-------PVVAvASHDTASAVIASPLNDSDAAYLSSGTWSLM-GF-----ESQT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 281 lPFVyGKYAKAgqfivheASPTSAGNLE------------WFLK---QWANVS-YQQLNEQIAALPPAASsvLFVP---- 340
Cdd:PRK10640 252 -PFT-NDTALA-------ANITNEGGAEgryrvlknimglWLLQrvlQERQITdLPALIAATAALPACRF--LINPnddr 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 341 FLYGSNAGLGMQAAF--YGMQAHHTQAHLLQAICEGVLFS---LMTHLERMRIR-FPHadtLRVTGGPAKSAVWMQMLAD 414
Cdd:PRK10640 321 FINPPSMCSEIQAACreTAQPVPESDAELARCIFDSLALLyadVLHELAQLRGEpFSQ---LHIVGGGCQNALLNQLCAD 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1407948402 415 LSGMRLEIPNVEET--GCLGAAMMAmQGATATQDE--QILQN--DMSIYVPNVQ-NYAAYQAKYQ 472
Cdd:PRK10640 398 ACGIRVIAGPVEAStlGNIGIQLMT-LDELNNVDDfrQVVSTnfPLTTFTPNPDsEIARHVAQFQ 461
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
3-448 |
2.19e-10 |
|
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: 62.58 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 3 YYLGIDCGGTFIKAALISESGEVIslARENVSVLSE------QAGYAERE----------M--EALWQVCAKVVKQVIAQ 64
Cdd:cd07776 1 LYLGLDLSTQSLKAVVIDSDLKVV--AEESVNFDSDlpeygtKGGVHRDGdggevtspvlMwvEALDLLLEKLKAAGFDF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 65 ShiaatSIKGVGISAQGKG-VFL----------LDKQ---HKPLGRAIT----------SSDQRALHIVKqwqAEGIPQA 120
Cdd:cd07776 79 S-----RVKAISGSGQQHGsVYWskgaesalanLDPSkslAEQLEGAFSvpdspiwmdsSTTKQCRELEK---AVGGPEA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 121 LYPIT--RQTL-WTGHpvSILRWLKEHePERYSNIGAV-LMShDYLRFCLTGElYC--EETNISESNLYNMQTGKYDEQL 194
Cdd:cd07776 151 LAKLTgsRAYErFTGP--QIAKIAQTD-PEAYENTERIsLVS-SFLASLLLGR-YApiDESDGSGMNLMDIRSRKWSPEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 195 AEKLGLQNILEKLPPVIAPNQVAG-----FVTEdaaklTGLVVGTPVVGGLFDVVSTAycAGLTDET-KLNVVLGTwsvv 268
Cdd:cd07776 226 LDAATAPDLKEKLGELVPSSTVAGgissyFVER-----YGFSPDCLVVAFTGDNPASL--AGLGLEPgDVAVSLGT---- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 269 sgitdhideSQTLpFVYGKYAK---AGQFIVHEASPTSA--------GNL--EWFLKQWANVSYQQLNEQIAALPPAASS 335
Cdd:cd07776 295 ---------SDTV-FLVLDEPKpgpEGHVFANPVDPGSYmamlcyknGSLarERVRDRYAGGSWEKFNELLESTPPGNNG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 336 VLFVPFLYG----SNAGLGMQAAFYG-MQAHHTQAHLLQAICEGVLFSLMTHLERMRIRFPHADTLrVTGGPAKSAVWMQ 410
Cdd:cd07776 365 NLGLYFDEPeitpPVPGGGRRFFGDDgVDAFFDPAVEVRAVVESQFLSMRLHAERLGSDIPPTRIL-ATGGASANKAILQ 443
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1407948402 411 MLADLSGM---RLEIPNveeTGCLGAAMMAMQGATATQDEQ 448
Cdd:cd07776 444 VLADVFGApvyTLDVAN---SAALGAALRAAHGLLCAGSGD 481
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-81 |
4.73e-09 |
|
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: 57.60 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 1 MNYYLGIDCGGTFIKAALISESGEVisLARENVSVLSEQAGyaeremEALWQVCAKVVKQVIAQSHIAATSIKGVGISAQ 80
Cdd:COG1940 4 AGYVIGIDIGGTKIKAALVDLDGEV--LARERIPTPAGAGP------EAVLEAIAELIEELLAEAGISRGRILGIGIGVP 75
|
.
gi 1407948402 81 G 81
Cdd:COG1940 76 G 76
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
3-437 |
3.20e-07 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 52.52 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 3 YYLGIDCGGTFIKAALISESGEVISLARENVSVLSEQAGYAEREMEALWQVCAKVVKQVIAQSHIAATSIKGVGISAQGK 82
Cdd:PRK00047 6 YILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGITNQRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 83 GVFLLDKQH-KPLGRAITSSDQRALHIVKQWQAEGIPQALypitRQTlwTGHPV------SILRWLKEHEP---ERYSNI 152
Cdd:PRK00047 86 TTVVWDKETgRPIYNAIVWQDRRTADICEELKRDGYEDYI----REK--TGLVIdpyfsgTKIKWILDNVEgarERAEKG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 153 GAVLMSHD-YLRFCLTGEL-----YceeTNISESNLYNMQTGKYDEQLaekLGLQNI-LEKLPPVIAPNQVAGFvTEDAA 225
Cdd:PRK00047 160 ELLFGTIDtWLVWKLTGGKvhvtdY---TNASRTMLFNIHTLDWDDEL---LELLDIpRSMLPEVRPSSEVYGK-TNPYG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 226 KLTGLVvgtPVVG--------------------------GLFDVVSTAycagltDETKL--NVVLGTwsVVSGITDHIde 277
Cdd:PRK00047 233 FFGGEV---PIAGiagdqqaalfgqlcfepgmakntygtGCFMLMNTG------EKAVKseNGLLTT--IAWGIDGKV-- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 278 sqtlpfVY---GKYAKAGQFIvheasptsagnlewflkQWanvsyqqLNEQIAALPPAASS------------VLFVP-F 341
Cdd:PRK00047 300 ------VYaleGSIFVAGSAI-----------------QW-------LRDGLKIISDASDSealarkvedndgVYVVPaF 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 342 lygsnAGLG-----MQA--AFYGMQAHHTQAHLLQAICEGVLFSLMTHLERMR----IRFPhadTLRVTGGPAKSAVWMQ 410
Cdd:PRK00047 350 -----TGLGapywdSDArgAIFGLTRGTTKEHIIRATLESIAYQTRDVLDAMQadsgIRLK---ELRVDGGAVANNFLMQ 421
|
490 500
....*....|....*....|....*..
gi 1407948402 411 MLADLSGMRLEIPNVEETGCLGAAMMA 437
Cdd:PRK00047 422 FQADILGVPVERPVVAETTALGAAYLA 448
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
3-81 |
5.70e-07 |
|
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and similar proteins; The family includes Fusobacterium nucleatum N-acetylmannosamine kinase (NanK; EC 2.7.1.60) and beta-glucoside kinase (BglK; EC 2.7.1.85) from Klebsiella pneumoniae and Listeria innocua. NanK catalyzes the second step of the sialic acid catabolic pathway, transferring a phosphate group from adenosine 5'-triphosphate to the C6 position of N-acetylmannosamine to generate N-acetylmannosamine 6-phosphate. Unlike other NanK enzymes and ROK family members, F. nucleatum NanK does not have a conserved zinc-binding site. BglK catalyzes the ATP-dependent phosphorylation of cellobiose to produce cellobiose-6'-P. It may have a dual role of kinase and transcriptional regulator of the cellobiose-PTS operon. The subfamily belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Members of this subfamily lack the cysteine-rich zinc-binding motif, which presents in other ROK families.
Pssm-ID: 466918 [Multi-domain] Cd Length: 294 Bit Score: 51.02 E-value: 5.70e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1407948402 3 YYLGIDCGGTFIKAALISESGEVISLArenvSVLSEQAGYAEREMEALwqvcakvvkQVIAQSHIAATSIKGVGISAQG 81
Cdd:cd24068 1 KILGIDIGGTKIKYGLVDADGEILEKD----SVPTPASKGGDAILERL---------LEIIAELKEKYDIEGIGISSAG 66
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
5-81 |
2.62e-05 |
|
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family corresponds to a group of proteins including sugar kinases, transcriptional repressors, and yet uncharacterized open reading frames. ROK family sugar kinases phosphorylate a range of structurally distinct hexoses including the key carbon source D-glucose, various glucose epimers, and several acetylated hexosamines. The sugar kinases include N-acetyl-D-glucosamine kinase (NAGK; EC 2.7.1.59), polyphosphate glucokinase (PPGK; EC 2.7.1.63/EC 2.7.1.2), glucokinase (GLK; EC 2.7.1.2), fructokinase (FRK; EC 2.7.1.4), hexokinase (HK; EC 2.7.1.1), D-allose kinase (AlsK; EC 2.7.1.55), bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE; EC 3.2.1.183/EC 2.7.1.60), N-acetylmannosamine kinase (NanK; EC 2.7.1.60), beta-glucoside kinase (BglK; EC 2.7.1.85), and N-acetylglucosamine kinase (EC 2.7.1.59). The family also contains the repressor proteins, such as N-acetylglucosamine repressor (NagC), xylose repressor (XylR), cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and protein Mlc. ROK kinases harbor a conserved N-terminal ATP binding motif of sequence DxGxT, while ROK repressors possess a N-terminal extension that contains a canonical helix-turn-helix DNA binding motif. The ROK family proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466849 [Multi-domain] Cd Length: 239 Bit Score: 45.53 E-value: 2.62e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1407948402 5 LGIDCGGTFIKAALISESGEVisLARENVSVLSEQAGyaeremEALWQVCAKVVKQVIAQSHIAAtSIKGVGISAQG 81
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEI--LARERVPTPAEEGP------EAVLDRIAELIEELLAEAGVRE-RILGIGIGVPG 68
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
3-81 |
5.18e-05 |
|
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7.1.2), also called glucose kinase, acts as an ATP-dependent kinase that phosphorylates glucose using ATP as a donor to give glucose-6-phosphate and ADP. It is highly specific for glucose. Glucokinases are found in invertebrates and microorganisms. They belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466912 [Multi-domain] Cd Length: 311 Bit Score: 45.36 E-value: 5.18e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1407948402 3 YYLGIDCGGTFIKAALISESGEVISLARENVSVLSEQagyaeremEALWQVCAKVVKQVIAQSHIAATSIKGVGISAQG 81
Cdd:cd24062 1 WIVGIDVGGTTIKMAFLTQEGEIVQKWEIPTNKLEGG--------ENIITDIAESIQQLLEELGYSKEDLIGIGVGVPG 71
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
3-81 |
1.79e-04 |
|
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This subfamily is composed of uncharacterized proteins belonging to the the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Members of this subfamily lack the cysteine-rich zinc-binding motif, which presents in other ROK families.
Pssm-ID: 466988 [Multi-domain] Cd Length: 286 Bit Score: 43.33 E-value: 1.79e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1407948402 3 YYLGIDCGGTFIKAALISESGEVISlaRENVSvlseqagYAEREMEALWQVCAKVVKQVIaqshiaaTSIKGVGISAQG 81
Cdd:cd24152 1 KYLVFDIGGTFIKYALVDENGNIIK--KGKIP-------TPKDSLEEFLDYIKKIIKRYD-------EEIDGIAISAPG 63
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
3-82 |
3.52e-04 |
|
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7.1.2), also called glucose kinase, acts as an ATP-dependent kinase that phosphorylates glucose using ATP as a donor to give glucose-6-phosphate and ADP. It is highly specific for glucose. Glucokinases are found in invertebrates and microorganisms. They belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466913 [Multi-domain] Cd Length: 308 Bit Score: 42.71 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 3 YYLGIDCGGTFIKAALISESGEVISLARENVSVLSEQAGYAEremealwQVCAKvVKQVIAQSHIAatSIKGVGISAQGK 82
Cdd:cd24063 1 YYVAVDIGGTWIRAGLVDEDGRILLKIRQPTPKTGDPGTVSE-------QVLGL-IETLLSKAGKD--SIEGIGVSSAGP 70
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
2-77 |
5.30e-04 |
|
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];
Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 41.79 E-value: 5.30e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1407948402 2 NYYLGIDCGGTFIKAALISESGEVISLARenvsvlSEQAGYAEREMEALWQVCAKVVKQVIAQSHIAAtSIKGVGI 77
Cdd:COG2971 1 PYILGVDGGGTKTRAVLVDADGEVLGRGR------AGGANPQSVGLEEALASLREALEEALAAAGDPA-DIEAVGF 69
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
2-72 |
8.72e-04 |
|
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1.55), also called allokinase, catalyzes the phosphorylation of D-allose to D-allose 6-phosphate. It has also low level glucokinase activity in vitro. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466920 [Multi-domain] Cd Length: 293 Bit Score: 41.38 E-value: 8.72e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1407948402 2 NYYLGIDCGGTFIKAALISESGEVISLARENvsvlSEQAGYAEREMEALwqvcAKVVKQVIAQS--HIAATSI 72
Cdd:cd24070 1 KYVLGIDIGGTNIRIGLVDEDGKLLDFEKVP----SKDLLRAGDPVEVL----ADLIREYIEEAglKPAAIVI 65
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| ASKHA_NBD_GspK-like |
cd24082 |
nucleotide-binding domain (NBD) of Vibrio cholerae glucosamine kinase GspK and similar ... |
3-79 |
1.20e-03 |
|
nucleotide-binding domain (NBD) of Vibrio cholerae glucosamine kinase GspK and similar proteins; The family includes a group of uncharacterized proteins similar to Vibrio cholerae glucosamine kinase GspK (EC 2.7.1.8), also called GlcN kinase. It acts as ATP-dependent kinase, which is specific for glucosamine. GspK does not show kinase activity with any other sugar.
Pssm-ID: 466932 [Multi-domain] Cd Length: 279 Bit Score: 40.59 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 3 YYLGIDCGGTFIKAALISESGEVISLAR---ENVSVLSEQAgyaeremealWQVCAKVVKQVIAQSHIAATSIKGVGISA 79
Cdd:cd24082 1 YFIGIDGGGTKCRARLADADGTVLGEATggpANLSSDLDQA----------WASILAAIKQALAQAGLDAAALSDLHAGL 70
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| ASKHA_NBD_eukNAGK-like |
cd24007 |
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) ... |
4-81 |
2.79e-03 |
|
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) family; The eukaryotic-type NAGK-like family includes a group of proteins similar to eukaryotic N-acetyl-D-glucosamine kinases, such as Vibrio cholerae glucosamine kinase GspK, Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK), Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase (KdgK) and Clostridium acetobutylicum N-acetylmuramic acid/N-acetylglucosamine kinase (MurK). NAGK (EC 2.7.1.59), also called GlcNAc kinase, converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. It is involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. NAGK also has ManNAc kinase activity. GspK (EC 2.7.1.8), also called GlcN kinase, acts as ATP-dependent kinase, which is specific for glucosamine. StHK is a novel hexokinase that can phosphorylate not only glucose but also GlcNAc, glucosamine, and mannose. KdgK (EC 2.7.1.45), also called 2-keto-3-deoxy-D-gluconate kinase, or KDG kinase, catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). It is specific for KDG. MurK (EC 2.7.1.-/EC 2.7.1.59), also known MurNAc/GlcNAc kinase, or murein sugar kinase, catalyzes the ATP-dependent phosphorylation of both cell wall (peptidoglycan) amino sugars, N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), at the 6-hydroxyl group. The eukaryotic-type N-acetylglucosamine kinase (NAGK) 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: 466857 [Multi-domain] Cd Length: 295 Bit Score: 39.60 E-value: 2.79e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1407948402 4 YLGIDCGGTFIKAALISESGEVISLARenvsvlSEQAGYAEREMEALWQVCAKVVKQVIAQsHIAATSIKGVGISAQG 81
Cdd:cd24007 1 VLGVDGGGTKTRAVLADEDGKILGRGK------GGPSNPASVGIEEAKENLKEAVREALSQ-AGSLGEIDAICLGLAG 71
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| ASKHA_NBD_BcrAD_BadFG_HgdC_HadI |
cd24036 |
nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and ... |
4-87 |
3.39e-03 |
|
nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and HgdC/HadI family includes BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins which are subunits of benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also contains some dehydratase activators, such as Acidaminococcus fermentans (R)-2-hydroxyglutaryl-CoA dehydratase activating ATPase (HgdC), Clostridioides difficile 2-hydroxyisocaproyl-CoA dehydratase activator (HadI), Clostridium sporogenes (R)-phenyllactate dehydratase activator (FldI), and Anaerotignum propionicum activator of lactoyl-CoA dehydratase (LcdC). Uncharacterized proteins, such as Escherichia coli protein YjiL and Methanocaldococcus jannaschii protein MJ0800, are also included in this family.
Pssm-ID: 466886 [Multi-domain] Cd Length: 250 Bit Score: 39.06 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1407948402 4 YLGIDCGGTFIKAALISESGEVisLARENVSVLSEQAGYAERemealwqvcakVVKQVIAQSHIAATSIKGVG------- 76
Cdd:cd24036 1 FAGIDVGSTTTKAVILDDKGKI--LGKAVIRTGTDPEKTAER-----------ALEEALEEAGLSREDIEYIVatgygrn 67
|
90 100
....*....|....*....|..
gi 1407948402 77 -----------ISAQGKGVFLL 87
Cdd:cd24036 68 svpfadktiteITCHARGAHFL 89
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