|
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 ... |
7-446 |
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: 605.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 7 FWLGIDCGGTYLKAGLYNSQGKEVCIERRSVATLSPRAGYAERDMHQLWQHCHKTVALLLKNSGADGGQIKGVGISAQGK 86
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 87 GLFLLDKQDRPLGNAILSSDRRALEIVQRWQQDGIPEKLYPHTRQTLWTGHPASLLRWVKENEPQRYQQIGSVMMAHDYL 166
Cdd:cd07802 81 GLYLVDKDGKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKENEPERYDRIRTVLFCKDWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 167 RWCLTGVKGCEESNISeSNLYNMNTGQYDPQLTRWLGISDIDGALPPIIGSAEICGEITAQAAALTGLTAGTPVVGGLFD 246
Cdd:cd07802 161 RYRLTGEISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEELKDKLPPLVPSTEIAGRVTAEAAALTGLPEGTPVAAGAFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 247 VVSTAICAGLHDEHTLNAVMGTWAVTSGIAHGIRDNEPfPYVYGRYVHPQQFIVHEASPTSSGNLEWLTAQW-------G 319
Cdd:cd07802 240 VVASALGAGAVDEGQLCVILGTWSINEVVTDEPVVPDS-VGSNSLHADPGLYLIVEASPTSASNLDWFLDTLlgeekeaG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 320 DMSFDEINHAVASLPKAESDVFFLPFLYGSNAGLEMTSGFYGLQALHTRAHLLQAVYEGVVFSHMTHLNRMLERFPhVQA 399
Cdd:cd07802 319 GSDYDELDELIAAVPPGSSGVIFLPYLYGSGANPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHRDHLERLLVARK-PET 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 505385654 400 LRVTGGPTHSDVWMQMLADVSGLAIELPQVEETGCSGAALAALVGTG 446
Cdd:cd07802 398 IRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
6-495 |
3.40e-172 |
|
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: 494.35 E-value: 3.40e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 6 PFWLGIDCGGTYLKAGLYNSQGKEVCIERRSVATLSPRAGYAERDMHQLWQHCHKTVALLLKNSGADGGQIKGVGISAQG 85
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 86 KGLFLLDKQDRPLGNAILSSDRRALEIVQRWQQDGIPEKLYPHTRQTLWTGHPASLLRWVKENEPQRYQQIGSVMMAHDY 165
Cdd:COG1070 81 HGLVLLDADGEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIAKVLLPKDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 166 LRWCLTGVKGCEESNISESNLYNMNTGQYDPQLTRWLGISdiDGALPPIIGSAEICGEITAQAAALTGLTAGTPVVGGLF 245
Cdd:COG1070 161 LRYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGID--RELLPELVPPGEVAGTLTAEAAAETGLPAGTPVVAGAG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 246 DVVSTAICAGLHDEHTLNAVMGTWAVTSGIAHGIRDNEPFPYVYGRYVHPQQFIVHEASPTSSGNLEWLTAQWGD---MS 322
Cdd:COG1070 239 DNAAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFCHAVPGRWLPMGATNNGGSALRWFRDLFADgelDD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 323 FDEINHAVASLPKAESDVFFLPFLYGSNAGL---EMTSGFYGLQALHTRAHLLQAVYEGVVFSHMTHLNRMLERFPHVQA 399
Cdd:COG1070 319 YEELNALAAEVPPGADGLLFLPYLSGERTPHwdpNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEALEEAGVKIDR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 400 LRVTGGPTHSDVWMQMLADVSGLAIELPQVEETGCSGAALAALVGTGLYPDFYAAQRALRHDIRMIEPDMRAHAAYQRKY 479
Cdd:COG1070 399 IRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMVRVGETIEPDPENVAAYDELY 478
|
490
....*....|....*.
gi 505385654 480 HRYQLLISALQGYHAR 495
Cdd:COG1070 479 ERYRELYPALKPLFER 494
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
9-483 |
5.10e-119 |
|
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: 358.00 E-value: 5.10e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 9 LGIDCGGTYLKAGLYNSQGKEVCIERRSVATLSPRAGYAERDMHQLWQHCHKTVALLLKNSGADGGQIKGVGISAQGKGL 88
Cdd:cd07808 3 LGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQMHGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 89 FLLDKQDRPLGNAILSSDRRALEIVqRWQQDGIPEKLYPHTRQTLWTGHPASLLRWVKENEPQRYQQIGSVMMAHDYLRW 168
Cdd:cd07808 83 VLLDKNGRPLRPAILWNDQRSAAEC-EELEARLGDEILIITGNPPLPGFTLPKLLWLKENEPEIFARIRKILLPKDYLRY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 169 CLTGVKGCEESNISESNLYNMNTGQYDPQLTRWLGIsDIDgALPPIIGSAEICGEITAQAAALTGLTAGTPVVGGLFDVV 248
Cdd:cd07808 162 RLTGELATDPSDASGTLLFDVEKREWSEELLEALGL-DPS-ILPPIVESTEIVGTLTPEAAEELGLPEGTPVVAGAGDNA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 249 STAICAGLHDEHTLNAVMGTWAVTSGIAHGIRDNEPFPYVYGRYVHPQQFIVHEASPTSSGNLEWLTAQWGDM--SFDEI 326
Cdd:cd07808 240 AAALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLHTFPHAVPGKWYAMGVTLSAGLSLRWLRDLFGPDreSFDEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 327 NHAVASLPKAESDVFFLPFLYGS-----NAglEMTSGFYGLQALHTRAHLLQAVYEGVVFShmthLNRMLERF----PHV 397
Cdd:cd07808 320 DAEAAKVPPGSEGLLFLPYLSGErtpywDP--NARGSFFGLSLSHTRAHLARAVLEGVAFS----LRDSLEVLkelgIKV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 398 QALRVTGGPTHSDVWMQMLADVSGLAIELPQVEETGCSGAALAALVGTGLYPDFYAAQRALRHDIRMIEPDMRAHAAYQR 477
Cdd:cd07808 394 KEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAACIKIEKTIEPDPERHEAYDE 473
|
....*.
gi 505385654 478 KYHRYQ 483
Cdd:cd07808 474 LYARYR 479
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
7-253 |
7.53e-108 |
|
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain.
Pssm-ID: 395295 [Multi-domain] Cd Length: 245 Bit Score: 320.82 E-value: 7.53e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 7 FWLGIDCGGTYLKAGLYNSQGKEVCIERRSVATLSPRAGYAERDMHQLWQHCHKTVALLLKNSGADGGQIKGVGISAQGK 86
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 87 GLFLLDKQDRPLGNAILSSDRRALEIVQRWQQDGIPEKLYPHTRQTLWTGHPASLLRWVKENEPQRYQQIGSVMMAHDYL 166
Cdd:pfam00370 81 GTVLLDKNDKPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHKFLTIHDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 167 RWCLTGVKGCEESNISESNLYNMNTGQYDPQLTRWLGISDIdgALPPIIGSAEICGEITAQAAALTGLTAGTPVVGGLFD 246
Cdd:pfam00370 161 RWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRD--HLPPLVESSEIYGELNPELAAMWGLDEGVPVVGGGGD 238
|
....*..
gi 505385654 247 VVSTAIC 253
Cdd:pfam00370 239 QQAAAFG 245
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
7-482 |
1.43e-106 |
|
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: 326.01 E-value: 1.43e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 7 FWLGIDCGGTYLKAGLYNSQGKEVCIERRSVATLSPRAGYAERDMHQLWQHCHKTVALLLKNSGADGGQIKGVGISAQGK 86
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 87 GLFLLDKQDRPLGNAILSSDRRALEIVQRWQQDGIPEKLYphtrqTLWTGHPAS----L--LRWVKENEPQRYQQIGSVM 160
Cdd:cd07805 81 GVVPVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGY-----RLGGGNPPSgkdpLakILWLKENEPEIYAKTHKFL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 161 MAHDYLRWCLTGVKGCEESNISESNLYNMNTGQYDPQLTRWLGIsDIDgALPPIIGSAEICGEITAQAAALTGLTAGTPV 240
Cdd:cd07805 156 DAKDYLNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGI-DPD-KLPELVPSTEVVGELTPEAAAELGLPAGTPV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 241 VGGLFDVVSTAICAGLHDEHTLNAVMGT--WAVTSgIAHGIRDNEPFPYVYgRYVHPQQFIVHEASPTSSGNLEWLTAQW 318
Cdd:cd07805 234 VGGGGDAAAAALGAGAVEEGDAHIYLGTsgWVAAH-VPKPKTDPDHGIFTL-ASADPGRYLLAAEQETAGGALEWARDNL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 319 GDM------SFDEINHAVASLPKAESDVFFLPFLYGSNAGLE---MTSGFYGLQALHTRAHLLQAVYEGVVFSHMTHLNR 389
Cdd:cd07805 312 GGDedlgadDYELLDELAAEAPPGSNGLLFLPWLNGERSPVEdpnARGAFIGLSLEHTRADLARAVLEGVAFNLRWLLEA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 390 MLERFPHVQALRVTGGPTHSDVWMQMLADVSGLAIELPQV-EETGCSGAALAALVGTGLYPDFYAAqRALRHDIRMIEPD 468
Cdd:cd07805 392 LEKLTRKIDELRLVGGGARSDLWCQILADVLGRPVEVPENpQEAGALGAALLAAVGLGLLKSFDEA-KALVKVEKVFEPD 470
|
490
....*....|....
gi 505385654 469 MRAHAAYQRKYHRY 482
Cdd:cd07805 471 PENRARYDRLYEVF 484
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
9-441 |
8.42e-104 |
|
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: 316.04 E-value: 8.42e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 9 LGIDCGGTYLKAGLYNSQGKEVCIERRSVATLSPRAGYAERDMHQLWQHCHKTVALLLKNSGADGGQIKGVGISAQGKGL 88
Cdd:cd00366 3 LGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQMPGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 89 FLLDKQDRPLGNAILSSDRRAleivqrwqqdgipeklyphtrqtlwtghpasllrwvkenepqryqqigSVMMAHDYLRW 168
Cdd:cd00366 83 VLVDADGNPLRPAIIWLDRRA------------------------------------------------KFLQPNDYIVF 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 169 CLTGVKGCEESNISESNLYNMNTGQYDPQLTRWLGISDidGALPPIIGSAEICGEITAQAAALTGLTAGTPVVGGLFDVV 248
Cdd:cd00366 115 RLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPR--EKLPPIVESGEVVGRVTPEAAEETGLPAGTPVVAGGGDTA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 249 STAICAGLHDEHTLNAVMGTWAVTSGIAHGIRDNEPFPYVYGrYVHPQQFIVHEASPTSSGNLEWLTAQWG-----DMSF 323
Cdd:cd00366 193 AAALGAGVVEPGDAVDSTGTSSVLSVCTDEPVPPDPRLLNRC-HVVPGLWLLEGAINTGGASLRWFRDEFGeeedsDAEY 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 324 DEINHAVASLPKAESDVFFLPFLYGSNAGLEMTS---GFYGLQALHTRAHLLQAVYEGVVFSHMTHLNRMLERFPHVQAL 400
Cdd:cd00366 272 EGLDELAAEVPPGSDGLIFLPYLSGERSPIWDPAargVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEILEELGVKIKEI 351
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 505385654 401 RVTGGPTHSDVWMQMLADVSGLAIELPQVEETGCSGAALAA 441
Cdd:cd00366 352 RVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
9-446 |
4.52e-102 |
|
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466793 [Multi-domain] Cd Length: 443 Bit Score: 313.37 E-value: 4.52e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 9 LGIDCGGTYLKAGLYNSQGKEVCIERRSVATLSPRAGYAERDMHQLWQHCHKTVALLLKNSGADggQIKGVGISAQGKGL 88
Cdd:cd07773 3 LGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGPD--PIAAISVSSQGESG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 89 FLLDKQDRPLGNAILSSDRRALEIVQRWQQDGIPEKLYPHTRQTLWTGHPASLLRWVKENEPQRYQQIGSVMMAHDYLRW 168
Cdd:cd07773 81 VPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAKWLSVADYIAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 169 CLTGVKGCEESNISESNLYNMNTGQYDPQLTRWLGISdiDGALPPIIGSAEICGEITAQAAALTGLTAGTPVV-GGLfDV 247
Cdd:cd07773 161 RLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGID--ASLLPELVPSGTVIGTVTPEAAEELGLPAGTPVVvGGH-DH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 248 VSTAICAGLHDEHTLNAVMGTWAVTSGIAHGIRDNEPFP---YVYGRYVHPQQFIVHeASPTSSGNLEWLTAQ--WGDMS 322
Cdd:cd07773 238 LCAALGAGVIEPGDVLDSTGTAEALLAVVDEPPLDEMLAeggLSYGHHVPGGYYYLA-GSLPGGALLEWFRDLfgGDESD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 323 FDEINHAVASLPKAESDVFFLPFLYGSNA---GLEMTSGFYGLQALHTRAHLLQAVYEGVVFshmtHLNRMLERF----P 395
Cdd:cd07773 317 LAAADELAEAAPPGPTGLLFLPHLSGSGTpdfDPDARGAFLGLTLGTTRADLLRAILEGLAF----ELRLNLEALekagI 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 505385654 396 HVQALRVTGGPTHSDVWMQMLADVSGLAIELPQVEETGCSGAALAALVGTG 446
Cdd:cd07773 393 PIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
7-446 |
7.65e-102 |
|
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: 313.02 E-value: 7.65e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 7 FWLGIDCGGTYLKAGLYNSQGKEVCIERRSVATLSPRAGYAERDMHQLWQHCHKTVALLLKNSGADGGQIKGVGISAQGK 86
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 87 GLFLLDKQDRPLGNAILSSDRRALEIVQRWQQDGIPEKLYPHTRQTLWTGHPASLLRWVKENEPQRYQQIGSVMMAHDYL 166
Cdd:cd24121 81 GTWLVDEDGRPVRDAILWLDGRAADIVERWQADGIAEAVFEITGTGLFPGSQAAQLAWLKENEPERLERARTALHCKDWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 167 RWCLTGVKGCEESNISESnLYNMNTGQYDPQLTRWLGISDIDGALPPIIGSAEICGEITAQAAALTGLTAGTPVVGGLFD 246
Cdd:cd24121 161 FYKLTGEIATDPSDASLT-FLDFRTRQYDDEVLDLLGLEELRHLLPPIRPGTEVIGPLTPEAAAATGLPAGTPVVLGPFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 247 VVSTAICAGLHDEHTLNAVMGTWAVTSGIAHGIRDN-EPFPYVygrYVHPQQFIVHEASPTSSG--NLEWLTAQWGDM-- 321
Cdd:cd24121 240 VVATALGSGAIEPGDACSILGTTGVHEVVVDEPDLEpEGVGYT---ICLGVPGRWLRAMANMAGtpNLDWFLRELGEVlk 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 322 ---------SFDEINHAVASLPKAESDVFFLPFLygSNAG-----LEMTS--GFYGLQALHTRAHLLQAVYEGVVFShmt 385
Cdd:cd24121 317 egaepagsdLFQDLEELAASSPPGAEGVLYHPYL--SPAGerapfVNPNAraQFTGLSLEHTRADLLRAVYEGVALA--- 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505385654 386 hlnrMLERFPH----VQALRVTGGPTHSDVWMQMLADVSGLAIELPQVEETGCSGAALAALVGTG 446
Cdd:cd24121 392 ----MRDCYEHmgedPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
7-475 |
3.74e-90 |
|
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: 282.10 E-value: 3.74e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 7 FWLGIDCGGTYLKAGLYNSQGKEVCIERRSVATLSPRAGYAERDMHQLWQHCHKTVALLLKNSGADGGQIKGVGISAQGK 86
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 87 GLFLLDKQDRPLGNAILSSDRRAleivqrwqqdgipeklyphtrqtlwtghpasllrwvkenepqRYqqigsVMMAHDYL 166
Cdd:cd07779 81 TFVPVDEDGRPLRPAISWQDKRT------------------------------------------AK-----FLTVQDYL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 167 RWCLTGVKGCEESNISESNLYNMNTGQYDPQLTRWLGIsDIDgALPPIIGSAEICGEITAQAAALTGLTAGTPVVGGLFD 246
Cdd:cd07779 114 LYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGI-DRD-KLPELVPPGTVIGTLTKEAAEETGLPEGTPVVAGGGD 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 247 VVSTAICAGLHDEHTLNAVMGTWAVTSGIAHG-IRDNEPFPYVYGrYVHPQQFIVhEASPTSSGN-LEWL---------- 314
Cdd:cd07779 192 QQCAALGAGVLEPGTASLSLGTAAVVIAVSDKpVEDPERRIPCNP-SAVPGKWVL-EGSINTGGSaVRWFrdefgqdeva 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 315 TAQWGDMSFDEINHAVASLPKAESDVFFLPFLYGSNA---GLEMTSGFYGLQALHTRAHLLQAVYEGVVFSHMTHLNRML 391
Cdd:cd07779 270 EKELGVSPYELLNEEAAKSPPGSDGLLFLPYLAGAGTpywNPEARGAFIGLTLSHTRAHLARAILEGIAFELRDNLEAME 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 392 ERFPHVQALRVTGGPTHSDVWMQMLADVSGLAIELPQVEETGCSGAALAALVGTGLYPDFYAAQRALRHDIRMIEPDMRA 471
Cdd:cd07779 350 KAGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKAMVRVTDTFEPDPEN 429
|
....
gi 505385654 472 HAAY 475
Cdd:cd07779 430 VAIY 433
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
9-483 |
5.83e-87 |
|
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: 275.20 E-value: 5.83e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 9 LGIDCGGTYLKAGLYNSQGKEVCIERRSVATLSPRAGYAERDMHQLWQHCHKTVALLLKNSGADggQIKGVGISAQGKGL 88
Cdd:cd07770 3 LGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGG--EVDAIGFSSAMHSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 89 FLLDKQDRPLGNAILSSDRRALEIVQRWQQDGIPEKLYPHTrqtlwtG---HPASL---LRWVKENEPQRYQQIGSVMMA 162
Cdd:cd07770 81 LGVDEDGEPLTPVITWADTRAAEEAERLRKEGDGSELYRRT------GcpiHPMYPlakLLWLKEERPELFAKAAKFVSI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 163 HDYLRWCLTGVKGCEESNISESNLYNMNTGQYDPQLTRWLGISDidGALPPIIGSAEICGEITAQAAALTGLTAGTPVVG 242
Cdd:cd07770 155 KEYLLYRLTGELVTDYSTASGTGLLNIHTLDWDEEALELLGIDE--EQLPELVDPTEVLPGLKPEFAERLGLLAGTPVVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 243 GLFDVVSTAICAGLHDEHTLNAVMGTwavtSGIAHGIRDnEPFPYVYGR----YVHPQQFIVHEASpTSSGN-LEWLTAQ 317
Cdd:cd07770 233 GASDGALANLGSGALDPGRAALTVGT----SGAIRVVSD-RPVLDPPGRlwcyRLDENRWLVGGAI-NNGGNvLDWLRDT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 318 WG--DMSFDEINHAVASLPKAESDVFFLPFLYGSNA---GLEMTSGFYGLQALHTRAHLLQAVYEGVVFSHMTHLNRMLE 392
Cdd:cd07770 307 LLlsGDDYEELDKLAEAVPPGSHGLIFLPYLAGERApgwNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKSIYEALEE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 393 RFPHVQALRVTGGPTHSDVWMQMLADVSGLAIELPQVEETGCSGAALAALVGTGLYPDFyaAQRALRHDIRMIEPDMRAH 472
Cdd:cd07770 387 LAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSL--EADELVKIGKVVEPDPENH 464
|
490
....*....|.
gi 505385654 473 AAYQRKYHRYQ 483
Cdd:cd07770 465 AIYAELYERFK 475
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
9-446 |
2.04e-82 |
|
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: 262.85 E-value: 2.04e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 9 LGIDCGGTYLKAGLYNSQGKEVCIERRSVATLSPRAGYAERDMHQLWQHCHKTVALLLKNSGADGGQIKGVGISAQGKGL 88
Cdd:cd07804 3 LGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGLVPAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 89 FLLDKQDRPLGNAILSSDRRALEIVQrWQQDGIPE-KLYPHTRQTLWTGHPASLLRWVKENEPQRYQQIGSVMMAHDYLR 167
Cdd:cd07804 83 VPVDENGKPLRPAILYGDRRATEEIE-WLNENIGEdRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTRKFLGAYDYIV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 168 WCLTGVKGCEESN-ISESNLYNMNTGQYDPQLTRWLGIsDIDgALPPIIGSAEICGEITAQAAALTGLTAGTPVVGGLFD 246
Cdd:cd07804 162 YKLTGEYVIDYSSaGNEGGLFDIRKRTWDEELLEALGI-DPD-LLPELVPSTEIVGEVTKEAAEETGLAEGTPVVAGTVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 247 VVSTAICAGLHDEHTLNAVMGTwAVTSGIAHgirDNEPFP--YVYGRYVHPQQFIVHEASPTSSGNLEWL---------- 314
Cdd:cd07804 240 AAASALSAGVVEPGDLLLMLGT-AGDIGVVT---DKLPTDprLWLDYHDIPGTYVLNGGMATSGSLLRWFrdefageeve 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 315 -TAQWGDMSFDEINHAVASLPkAESD-VFFLPFLYGsnaglEMT-------SG-FYGLQALHTRAHLLQAVYEGVVFSHM 384
Cdd:cd07804 316 aEKSGGDSAYDLLDEEAEKIP-PGSDgLIVLPYFMG-----ERTpiwdpdaRGvIFGLTLSHTRAHLYRALLEGVAYGLR 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505385654 385 THLNRMLERFPHVQALRVTGGPTHSDVWMQMLADVSGLAIELPQVEETGCSGAALAALVGTG 446
Cdd:cd07804 390 HHLEVIREAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| XylB |
TIGR01312 |
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of ... |
9-487 |
2.07e-76 |
|
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: 248.00 E-value: 2.07e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 9 LGIDCGGTYLKAGLYNSQGKEVCIERRSVATLSPRAGYAERDMHQLWQHCHKTVALLLKNSGADGGQIKGVGISAQGKGL 88
Cdd:TIGR01312 1 LGIDLGTSGVKALLVDEQGEVIASGSAPHTVISPHPGWSEQDPEDWWDATEEAIKELLEQASEMGQDIKGIGISGQMHGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 89 FLLDKQDRPLGNAILSSDRRALEIVQRWQQDGIPEKLYPHTRQTLWTGHPASLLRWVKENEPQRYQQIGSVMMAHDYLRW 168
Cdd:TIGR01312 81 VLLDANGEVLRPAILWNDTRTAQECEELEAELGDERVLEITGNLALPGFTAPKLLWVRKHEPEVFARIAKVMLPKDYLRY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 169 CLTGVKGCEESNISESNLYNMNTGQYDPQLtrwLGISDIDGA-LPPIIGSAEICGEITAQAAALTGLTAGTPVVGGLFDV 247
Cdd:TIGR01312 161 RLTGEYVTEYSDASGTGWFDVAKRAWSKEL---LDALDLPESqLPELIESSEKAGTVRPEVAARLGLSAGVPVAAGGGDN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 248 VSTAICAGLHDEHTLNAVMGtwavTSGIAHGIRDnepfpyvygRYVHPQQFIVH---EASPT---------SSGN-LEWL 314
Cdd:TIGR01312 238 AAGAIGTGTVDPGDAMMSLG----TSGVVYAVTD---------KPLPDPAGAVHgfcHALPGgwlpmgvtlSATSsLEWF 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 315 TAQWGDMSFDEINHAVASLPKAESDVFFLPFLYGS---NAGLEMTSGFYGLQALHTRAHLLQAVYEGVVFShmthLNRML 391
Cdd:TIGR01312 305 RELFGKEDVEALNELAEQSPPGAEGVTFLPYLNGErtpHLDPQARGSFIGLTHNTTRADLTRAVLEGVTFA----LRDSL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 392 ERFPH-----VQALRVTGGPTHSDVWMQMLADVSGLAIELPQVEETGCSGAALAALVGTGLYPDFYAAQRALRHDIRMIE 466
Cdd:TIGR01312 381 DILREaggipIQSIRLIGGGAKSPAWRQMLADIFGTPVDVPEGEEGPALGAAILAAWALGEKDLAALCSEAVVKQTESVL 460
|
490 500
....*....|....*....|.
gi 505385654 467 PDMRAHAAYQRKYHRYQLLIS 487
Cdd:TIGR01312 461 PIAENVEAYEELYERYKKLYQ 481
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
9-491 |
4.49e-69 |
|
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: 229.35 E-value: 4.49e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 9 LGIDCGGTYLKAGLYNSQ-GKEV--CIERRSVATLSPRAGYAERDMHQLWQHCHKTVALLLKNSGADGGQIKGVGISAQG 85
Cdd:cd07781 3 IGIDFGTQSVRAGLVDLAdGEELasAVVPYPTGYIPPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVDTTS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 86 KGLFLLDKQDRPLGNAILSSDRRALEivqrwQQDGIPEKLYPHTRQ-TLWTGHPAS-------LLrWVKENEPQRYQQIG 157
Cdd:cd07781 83 STVVPVDEDGNPLAPAILWMDHRAQE-----EAAEINETAHPALEYyLAYYGGVYSsewmwpkAL-WLKRNAPEVYDAAY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 158 SVMMAHDYLRWCLTGVKGCEESNISESNLYNMNTGQYDPQLTRWLGISDIDGA--LP-PIIGSAEICGEITAQAAALTGL 234
Cdd:cd07781 157 TIVEACDWINARLTGRWVRSRCAAGHKWMYNEWGGGPPREFLAALDPGLLKLRekLPgEVVPVGEPAGTLTAEAAERLGL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 235 TAGTPVVGGLFDVVSTAICAGLHDEHTLNAVMGTWAVTSGIAhgiRDNEPFPYVYGRY---VHPQQFIVhEASPTSSG-- 309
Cdd:cd07781 237 PAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTSTCHLMVS---PKPVDIPGICGPVpdaVVPGLYGL-EAGQSAVGdi 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 310 ------NLEWLTAQWGDMSFDEINHAVASLPKAESDVFFLPFLYGS-----NAGLemTSGFYGLQALHTRAHLLQAVYEG 378
Cdd:cd07781 313 fawfvrLFVPPAEERGDSIYALLSEEAAKLPPGESGLVALDWFNGNrtplvDPRL--RGAIVGLTLGTTPAHIYRALLEA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 379 VVFshmtHLNRMLERFP----HVQALRVTGGPT-HSDVWMQMLADVSGLAIELPQVEETGCSGAALAALVGTGLYPDFYA 453
Cdd:cd07781 391 TAF----GTRAIIERFEeagvPVNRVVACGGIAeKNPLWMQIYADVLGRPIKVPKSDQAPALGAAILAAVAAGVYADIEE 466
|
490 500 510
....*....|....*....|....*....|....*...
gi 505385654 454 AQRALRHDIRMIEPDMRAHAAYQRKYHRYQLLISALQG 491
Cdd:cd07781 467 AADAMVRVDRVYEPDPENHAVYEELYALYKELYDALGP 504
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
9-446 |
2.06e-66 |
|
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: 220.50 E-value: 2.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 9 LGIDCGGTYLKAGLYNSQGKEVCIE-RRSVATLSPRAGYAERDMHQLWQHCHKTVALLLKNSGADGGQIKGVGISAQGKG 87
Cdd:cd07809 3 LGIDLGTQSIKAVLIDAETGRVVASgSAPHENILIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQMHG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 88 LFLLDKQDRPLGNAILSSDRRALEIVQRwqqdgIPEKL-YPHTRQTL------WTghpASLLRWVKENEPQRYQQIGSVM 160
Cdd:cd07809 83 LVALDADGKVLRPAKLWCDTRTAPEAEE-----LTEALgGKKCLLVGlniparFT---ASKLLWLKENEPEHYARIAKIL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 161 MAHDYLRWCLTGVKGCEESNISESNLYNMNTGQYDPQLTRWLGISDIDGA-LPPIIGSAEICGEITAQAAALTGLTAGTP 239
Cdd:cd07809 155 LPHDYLNWKLTGEKVTGLGDASGTFPIDPRTRDYDAELLAAIDPSRDLRDlLPEVLPAGEVAGRLTPEGAEELGLPAGIP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 240 VVGGLFDVVSTAICAGLHDEHTLNAVMGtwavTSGIAHGIRDnEPFPYVYGR---YVHPQQFIVHEASPTSSGN--LEWL 314
Cdd:cd07809 235 VAPGEGDNMTGALGTGVVNPGTVAVSLG----TSGTAYGVSD-KPVSDPHGRvatFCDSTGGMLPLINTTNCLTawTELF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 315 TAQwGDMSFDEINHAVASLPKAESDVFFLPFLYG-SNAGLEMTSG-FYGLQ-ALHTRAHLLQAVYEGVVFSHMTHLNRML 391
Cdd:cd07809 310 REL-LGVSYEELDELAAQAPPGAGGLLLLPFLNGeRTPNLPHGRAsLVGLTlSNFTRANLARAALEGATFGLRYGLDILR 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 505385654 392 ERFPHVQALRVTGGPTHSDVWMQMLADVSGLAIELPQVEETGCSGAALAALVGTG 446
Cdd:cd07809 389 ELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
7-445 |
3.61e-58 |
|
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: 198.60 E-value: 3.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 7 FWLGIDCGGTYLKAGLYNSQGKEVCIERRSVATLSPRAGYAERDMHQLWQHCHKTVALLLKNsgADGGQIKGVGISAQGK 86
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAE--LRPRRVVAIAVDGTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 87 GLFLLDKQDRPLGNAILSSDRRALEIVQRWQQDGIPEKLYPHTRQTlwTGHPASLLRWVKENEPQRYQQIGSVMMAHDYL 166
Cdd:cd07783 79 TLVLVDREGEPLRPAIMYNDARAVAEAEELAEAAGAVAPRTGLAVS--PSSSLAKLLWLKRHEPEVLAKTAKFLHQADWL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 167 RWCLTGVKGC-EESNISESnLYNMNTGQYDPQLTRWLGISDidGALPPIIGSAEICGEITAQAAALTGLTAGTPVVGGLF 245
Cdd:cd07783 157 AGRLTGDRGVtDYNNALKL-GYDPETGRWPSWLLALLGIPP--DLLPRVVAPGTVIGTLTAEAAEELGLPAGTPVVAGTT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 246 DVVSTAICAGLHDEHTLNAVMGtwavTSGIAHGIRDNEPFPYVYGRYVHP---QQFIVHEASPTSSGNLEWLTaqwGDMS 322
Cdd:cd07783 234 DSIAAFLASGAVRPGDAVTSLG----TTLVLKLLSDKRVPDPGGGVYSHRhgdGYWLVGGASNTGGAVLRWFF---SDDE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 323 FDEINHAVAslPKAESDVFFLPF-LYGS-----NAGLEmtsGFYgLQALHTRAHLLQAVYEGVVFShmthLNRMLERF-- 394
Cdd:cd07783 307 LAELSAQAD--PPGPSGLIYYPLpLRGErfpfwDPDAR---GFL-LPRPHDRAEFLRALLEGIAFI----ERLGYERLee 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 505385654 395 ---PHVQALRVTGGPTHSDVWMQMLADVSGLAIELPQvEETGCSGAALAALVGT 445
Cdd:cd07783 377 lgaPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAE-EEEAALGAALLAAAGL 429
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
9-446 |
1.64e-57 |
|
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: 197.45 E-value: 1.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 9 LGIDCGGTYLKAGLYNSQGKEVCIERR----SVATLSPRAGYAerDMHQLWQHCHKTVALLLKNSGADGGQIKGVGISAQ 84
Cdd:cd07798 3 LVIDIGTGGGRCALVDSEGKIVAIAYReweyYTDDDYPDAKEF--DPEELWEKICEAIREALKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 85 GKGLFLLDKQDRPL--GNAIlssDRRALEIVQRWQQDGIPEKLYphtrqtlWTGH------PASLLRWVKENEPQRYQQI 156
Cdd:cd07798 81 REGIVFLDKDGRELyaGPNI---DARGVEEAAEIDDEFGEEIYT-------TTGHwptelfPAARLLWFKENRPEIFERI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 157 GSVMMAHDYLRWCLTGVKGCEESNISESNLYNMNTGQYDPQLTRWLGISdiDGALPPIIGSAEICGEITAQAAALTGLTA 236
Cdd:cd07798 151 ATVLSISDWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLP--PEILPEIVPSGTVLGTVSEEAARELGLPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 237 GTPVVGGLFDVVSTAICAGLHDEHTLNAVMGTWAVTSGIAHGIRDNEPFPYVYGRYVHPQQFIVhEASPTSSG-NLEWLT 315
Cdd:cd07798 229 GTPVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWTGCHLVPGKWVL-ESNAGVTGlNYQWLK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 316 ---AQWGDMSFDEINHAVASLPKAESDVffLPFLyGS---NAGLEMT--SGFYGLQALH----TRAHLLQAVYEGVVFSH 383
Cdd:cd07798 308 ellYGDPEDSYEVLEEEASEIPPGANGV--LAFL-GPqifDARLSGLknGGFLFPTPLSaselTRGDFARAILENIAFAI 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505385654 384 MTHLNRMLERFPH-VQALRVTGGPTHSDVWMQMLADVSGLAIELPQVEETGCSGAALAALVGTG 446
Cdd:cd07798 385 RANLEQLEEVSGReIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
9-482 |
4.86e-42 |
|
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: 156.34 E-value: 4.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 9 LGIDCGGTYLKAGLYNSQGKEVCIERRS-VATLSPR-AGYAERDMHQLWQHCHKTVALLLKNSGADGGQIKGVGISAQGK 86
Cdd:cd07775 3 LALDAGTGSGRAVIFDLEGNQIAVAQREwRHKEVPDvPGSMDFDTEKNWKLICECIREALKKAGIAPKSIAAISTTSMRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 87 GLFLLDKQDRPLGnAILSSDRRALEIVQRWQQ--DGIPEKLYPHTRQTLWTGHPASLLrWVKENEPQRYQQIGSVMMAHD 164
Cdd:cd07775 83 GIVLYDNEGEEIW-ACANVDARAAEEVSELKElyNTLEEEVYRISGQTFALGAIPRLL-WLKNNRPEIYRKAAKITMLSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 165 YLRWCLTGVKGCEESNISESNLYNMNTGQYDPQLTRWLGISDIdgALPPIIGSAEICGEITAQAAALTGLTAGTPVVGGL 244
Cdd:cd07775 161 WIAYKLSGELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKAD--ILPPVVESGTVIGKVTKEAAEETGLKEGTPVVVGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 245 FDVVSTAICAGLHDEHTLNAVMGT-WAVTSGIAHGIRDNEPFPYVyGRYVHPQQFIVhEASPTSSGnlewLTAQWGDMSF 323
Cdd:cd07775 239 GDVQLGCLGLGVVRPGQTAVLGGSfWQQEVNTAAPVTDPAMNIRV-NCHVIPDMWQA-EGISFFPG----LVMRWFRDAF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 324 --DEINHAVASlpkaesdvfflpflyGSNAGLEMT-------SGFYGLQAL-----------H---------------TR 368
Cdd:cd07775 313 caEEKEIAERL---------------GIDAYDLLEemakdvpPGSYGIMPIfsdvmnyknwrHaapsflnldidpekcNK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 369 AHLLQAVYEGVVFSHMTHLNRMLERFPHV-QALRVTGGPTHSDVWMQMLADVSGLAIELPQVEETGCSGAALAALVGTGL 447
Cdd:cd07775 378 ATFFRAIMENAAIVSAGNLERIAEFSGIFpDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGAGI 457
|
490 500 510
....*....|....*....|....*....|....*
gi 505385654 448 YPDFYAAQRALRHDIRMIEPDMRAHAAYQRKYHRY 482
Cdd:cd07775 458 YSSLEEAVESLVKWEREYLPNPENHEVYQDLYEKW 492
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
9-483 |
7.67e-38 |
|
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: 145.01 E-value: 7.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 9 LGIDCGGTYLKAGLYNSQGKEVCIERRSVATLSPRAGYAERDMHQLWQHCHKTVALLLKNSGADGGQIKGVGISAQgKGL 88
Cdd:cd07793 3 LAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQ-RNT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 89 FLL-DKQD-RPLGNAILSSDRRALEIVQRWQQ-------DGIPEKLYPHTRQ---------TLWTGHPASLLRWVKENEP 150
Cdd:cd07793 82 FLTwDKKTgKPLHNFITWQDLRAAELCESWNRslllkalRGGSKFLHFLTRNkrflaasvlKFSTAHVSIRLLWILQNNP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 151 QRYQQI--GSVMMA--HDYLRWCLTG--VKGCEESNISESNLYNMNTGQYDPQLTRWLGI-SDIdgaLPPIIGSAEICGE 223
Cdd:cd07793 162 ELKEAAekGELLFGtiDTWLLWKLTGgkVHATDYSNASATGLFDPFTLEWSPILLSLFGIpSSI---LPEVKDTSGDFGS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 224 -----------ITA----QAAALTG----------LTAGTpvvgGLFdvvstaicaglhdehtLNAVMGTWAVTSgiAHG 278
Cdd:cd07793 239 tdpsifgaeipITAvvadQQAALFGeccfdkgdvkITMGT----GTF----------------IDINTGSKPHAS--VKG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 279 IrdnepFPYVYGRYVHPQQFIVhEASPTSSGN-LEWLTaqwgdmSFDEINHAVASLPKAES-----DVFFLPFLYGSNAG 352
Cdd:cd07793 297 L-----YPLVGWKIGGEITYLA-EGNASDTGTvIDWAK------SIGLFDDPSETEDIAESvedtnGVYFVPAFSGLQAP 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 353 L---EMTSGFYGLQALHTRAHLLQAVYEGVVFSHMTHLNRMLERFPH-VQALRVTGGPTHSDVWMQMLADVSGLAIELPQ 428
Cdd:cd07793 365 YndpTACAGFIGLTPSTTKAHLVRAILESIAFRVKQLLETMEKETSIkISSIRVDGGVSNNDFILQLIADLLGKPVERPK 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 505385654 429 VEETGCSGAALAALVGTGLY---PDFyaaqRALRHDIRMIEPDMRAhAAYQRKYHRYQ 483
Cdd:cd07793 445 NTEMSALGAAFLAGLASGIWkskEEL----KKLRKIEKIFEPKMDN-EKREELYKNWK 497
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
9-483 |
4.99e-37 |
|
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: 142.61 E-value: 4.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 9 LGIDCGGTYLKAGLYNSQGKEVCIERRSVATLSPRAGYAERDMHQLWQHCHKTVALLLKNSGADGGQIKGVGISAQGKGL 88
Cdd:cd07769 3 LAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRETT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 89 FLLDKQD-RPLGNAILSSDRRALEIVQRWQQDGIPEKLyphtRQTlwTGHP------ASLLRWVKENEPQRYQQ------ 155
Cdd:cd07769 83 VVWDKKTgKPLYNAIVWQDRRTADICEELKAKGLEERI----REK--TGLPldpyfsATKIKWILDNVPGARERaergel 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 156 -IGSVmmahD-YLRWCLTGVKG--CEESNISESNLYNMNTGQYDPQLTRWLGISDIdgALPPIIGSAEICGEITA----- 226
Cdd:cd07769 157 lFGTI----DtWLIWKLTGGKVhvTDVTNASRTMLFNIHTLEWDDELLELFGIPRS--MLPEVRPSSEVFGYTDPeglga 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 227 ----------QAAALTGLTA----------GTpvvgGLFDVVSTaicaglhdehtlnavmGTWAVTSG------IAHGIr 280
Cdd:cd07769 231 gipiagilgdQQAALFGQGCfepgmakntyGT----GCFLLMNT----------------GEKPVPSKngllttIAWQI- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 281 DNEPfpyVYgryvhpqqfiVHEASPTSSGN-LEWLtaqwGDM-----SFDEINHAVASLPKAEsDVFFLPFLYG------ 348
Cdd:cd07769 290 GGKV---TY----------ALEGSIFIAGAaIQWL----RDNlglieDAAETEELARSVEDNG-GVYFVPAFSGlgapyw 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 349 -SNA-GLemtsgFYGLQALHTRAHLLQAVYEGVVFShMTHLNRMLER--FPHVQALRVTGGPTHSDVWMQMLADVSGLAI 424
Cdd:cd07769 352 dPDArGA-----IVGLTRGTTKAHIVRAALESIAYQ-TRDVLEAMEKdsGIKLKELRVDGGATANNFLMQFQADILGVPV 425
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 505385654 425 ELPQVEETGCSGAALAALVGTGLYPDFYAAQRALRHDiRMIEPDMRAHAAyQRKYHRYQ 483
Cdd:cd07769 426 VRPKVAETTALGAAYLAGLAVGFWKDLDELASLWQVD-KRFEPSMDEEER-ERLYRGWK 482
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
4-483 |
9.44e-36 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 139.37 E-value: 9.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 4 KEPFWLGIDCGGTYLKAGLYNSQGKEVCIERRSVATLS-PR-AGYAERDMHQLWQHCHKTVALLLKNSGADGGQIKGVGI 81
Cdd:PRK10939 1 SMSYLMALDAGTGSIRAVIFDLNGNQIAVGQAEWRHLAvPDvPGSMEFDLEKNWQLACQCIRQALQKAGIPASDIAAVSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 82 SAQGKGLFLLDKQDRPLGnAILSSDRRALEIVQRWQQD--GIPEKLYPHTRQTLWTGHPASLLrWVKENEPQRYQQIGSV 159
Cdd:PRK10939 81 TSMREGIVLYDRNGTEIW-ACANVDARASREVSELKELhnNFEEEVYRCSGQTLALGALPRLL-WLAHHRPDIYRQAHTI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 160 MMAHDYLRWCLTGVKGCEESNISESNLYNMNTGQYDPQLTRWLGI-SDIdgaLPPIIGSAEICGEITAQAAALTGLTAGT 238
Cdd:PRK10939 159 TMISDWIAYMLSGELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLrADI---LPPVKETGTVLGHVTAKAAAETGLRAGT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 239 PVVGGLFDVVSTAICAGLHDEHTLnAVMGT--WavtsgiahgirdnepfpyvygryvhpQQfIVHEASPTSSGNlewlta 316
Cdd:PRK10939 236 PVVMGGGDVQLGCLGLGVVRPGQT-AVLGGtfW--------------------------QQ-VVNLPAPVTDPN------ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 317 qwgdMSFdEIN-HAVASLPKAESDVFFlpflygsnAGL-----------------------------EMTS----GFYGL 362
Cdd:PRK10939 282 ----MNI-RINpHVIPGMVQAESISFF--------TGLtmrwfrdafcaeekllaerlgidayslleEMASrvpvGSHGI 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 363 -----QALH---------------------TRAHLLQAVYEGVVFSHMTHLNRmLERFPHVQALRV--TGGPTHSDVWMQ 414
Cdd:PRK10939 349 ipifsDVMRfkswyhaapsfinlsidpekcNKATLFRALEENAAIVSACNLQQ-IAAFSGVFPSSLvfAGGGSKGKLWSQ 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505385654 415 MLADVSGLAIELPQVEETGCSGAALAALVGTGLYPDFYAAQRALRHDIRMIEPDMRAHAAYQRKYHRYQ 483
Cdd:PRK10939 428 ILADVTGLPVKVPVVKEATALGCAIAAGVGAGIYSSLAETGERLVRWERTFEPNPENHELYQEAKEKWQ 496
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
8-487 |
1.81e-35 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 138.18 E-value: 1.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 8 WLGIDCGGTYLKAGLYNSQGKEVCIERRSVATLSPRAGYAERDMHQLWQHCHKTVALLLKNSGADGgqIKGVGISAQGKG 87
Cdd:PRK15027 2 YIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQD--VKALGIAGQMHG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 88 LFLLDKQDRPLGNAILSSDRRALEivqrwqQDGIPEKLYPHTRQT----LWTGHPASLLRWVKENEPQRYQQIGSVMMAH 163
Cdd:PRK15027 80 ATLLDAQQRVLRPAILWNDGRCAQ------ECALLEARVPQSRVItgnlMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 164 DYLRWCLTGVKGCEESnisesnlynmntgqyDPQLTRWLGISDID-------------GALPPIIGSAEICGEITAQAAA 230
Cdd:PRK15027 154 DYLRLRMTGEFASDMS---------------DAAGTMWLDVAKRDwsdvmlqachlsrDQMPALYEGSEITGALLPEVAK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 231 LTGLTAgTPVVGGLFDVVSTAICAGLHDEHTLNAVMGTWAVTSGIAHGIRDNePFPYVYGrYVH--PQQFIVHEASPTSS 308
Cdd:PRK15027 219 AWGMAT-VPVVAGGGDNAAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSK-PESAVHS-FCHalPQRWHLMSVMLSAA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 309 GNLEWLTAQWGDMSFDEINHAVASLPKAESDVFFLPFLYGSNA---GLEMTSGFYGLQALHTRAHLLQAVYEGVVFSHMT 385
Cdd:PRK15027 296 SCLDWAAKLTGLSNVPALIAAAQQADESAEPVWFLPYLSGERTphnNPQAKGVFFGLTHQHGPNELARAVLEGVGYALAD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 386 HLNRMLERFPHVQALRVTGGPTHSDVWMQMLADVSGLAIELPQVEETGCS-GAALAALVG-------TGLYPDFYAAQRA 457
Cdd:PRK15027 376 GMDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTGGDVGPAlGAARLAQIAanpekslIELLPQLPLEQSH 455
|
490 500 510
....*....|....*....|....*....|....
gi 505385654 458 LrhdirmiePDMRAHAAY--QRKYHR--YQLLIS 487
Cdd:PRK15027 456 L--------PDAQRYAAYqpRRETFRrlYQQLLP 481
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
5-485 |
3.93e-33 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 132.16 E-value: 3.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 5 EPFWLGIDCGGTYLKAGLYN-SQGKE----VCIERRSVA--TLSPRAGYAERDMHQLWQHCHKTVALLLKNSGADGGQIK 77
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDaADGEElasaVHPYPRWVIglYLPPPPDQARQHPLDYLEALEAAVREALAQAGVDPADVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 78 GVGISAQGKGLFLLDKQDRPL-----------GNAILSSDRRAL----EIVQRWQQDGIPeklyphtrqtlWTGHP---- 138
Cdd:COG1069 81 GIGVDATGCTPVPVDADGTPLallpefaenphAMVILWKDHTAQeeaeRINELAKARGED-----------YLRYVggii 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 139 ------ASLLrWVKENEPQRYQQIGSVMMAHDYLRWCLTGvkgceesNISESN-------LYNMNTGQY---------DP 196
Cdd:COG1069 150 ssewfwPKIL-HLLREDPEVYEAADSFVELCDWITWQLTG-------SLKRSRctaghkaLWHAHEGGYpseeffaalDP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 197 QLtrwlgiSDIDGALP-PIIGSAEICGEITAQAAALTGLTAGTPVVGGLFDVVSTAICAGLHDEHTLNAVMGTWAVTSGI 275
Cdd:COG1069 222 LL------DGLADRLGtEIYPLGEPAGTLTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGGVEPGTLVKVMGTSTCHMLV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 276 AhgirDNEPF-PYVYGRY---VHPQqFIVHEASPTSSGNL-EWLTAQ--W-----------GDMSFDEINHAVASLPKAE 337
Cdd:COG1069 296 S----PEERFvPGICGQVdgsIVPG-MWGYEAGQSAVGDIfAWFVRLlvPpleyekeaeerGISLHPLLTEEAAKLPPGE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 338 SDVFFLPFLYG-----SNAGLemTSGFYGLqALHTRA-HLLQAVYEGVVFShmthLNRMLERFP----HVQALRVTGG-P 406
Cdd:COG1069 371 SGLHALDWFNGnrsplADQRL--KGVILGL-TLGTDAeDIYRALVEATAFG----TRAIIERFEeegvPIDEIIACGGiA 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 407 THSDVWMQMLADVSGLAIELPQVEETGCSGAALAALVGTGLYPDFYAAQRALRHDI-RMIEPDMRAHAAYQRKYHRYQLL 485
Cdd:COG1069 444 TKNPLVMQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEEAMAAMGSGFdKVYTPDPENVAVYDALYAEYLQL 523
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
9-487 |
5.95e-33 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 131.25 E-value: 5.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 9 LGIDCGGTYLKAGLYNSQGKEVCIERRSVATLSPRAGYAERDMHQLWQHCHKTVALLLKNSGADGGQ--IKGVGISAQGK 86
Cdd:PTZ00294 5 GSIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKLREKGPSfkIKAIGITNQRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 87 GLFLLDKQ-DRPLGNAILSSDRRALEIVQRWQQDGIPEKLYPHTrqtlwTGHP------ASLLRWVKENEPQRYQQI--G 157
Cdd:PTZ00294 85 TVVAWDKVtGKPLYNAIVWLDTRTYDIVNELTKKYGGSNFFQKI-----TGLPistyfsAFKIRWMLENVPAVKDAVkeG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 158 SVMMA--HDYLRWCLTGVKG--CEESNISESNLYNMNTGQYDPQLTRWLGISdiDGALPPIIGSAEICGEITAQAaalTG 233
Cdd:PTZ00294 160 TLLFGtiDTWLIWNLTGGKShvTDVTNASRTFLMNIKTLKWDEELLNKFGIP--KETLPEIKSSSENFGTISGEA---VP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 234 LTAGTPVVGGLFDVVSTAICAGLHDEHTLNAVMGTWA---VTSG-------------IAHGIRDNEPFPYVYgryvhpqq 297
Cdd:PTZ00294 235 LLEGVPITGCIGDQQAALIGHGCFEKGDAKNTYGTGCfllMNTGteivfskhgllttVCYQLGPNGPTVYAL-------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 298 fivhEASPTSSGN-LEWLTAQWGDMS-FDEINHAVASLPKAESDVF-------FLPFLYGSNAG--LEMTsgfyglqaLH 366
Cdd:PTZ00294 307 ----EGSIAVAGAgVEWLRDNMGLIShPSEIEKLARSVKDTGGVVFvpafsglFAPYWRPDARGtiVGMT--------LK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 367 T-RAHLLQAVYEGVVFSHMTHLNRMLERFPH-VQALRVTGGPTHSDVWMQMLADVSGLAIELPQVEETGCSGAALAALVG 444
Cdd:PTZ00294 375 TtRAHIVRAALEAIALQTNDVIESMEKDAGIeLNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLA 454
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 505385654 445 TGLYPDFYAAQRALRHDIRMIEPDMRAhAAYQRKYHRYQLLIS 487
Cdd:PTZ00294 455 VGVWKSLEEVKKLIRRSNSTFSPQMSA-EERKAIYKEWNKAVE 496
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
9-483 |
1.26e-31 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 127.10 E-value: 1.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 9 LGIDCGGTYLKAGLYNSQGKEVCIERRSVATLSPRAGYAERDMHQLWQHCHKTVALLLKNSGADGGQIKGVGISAQGKGL 88
Cdd:COG0554 6 LAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISAEDIAAIGITNQRETT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 89 FLLDKQD-RPLGNAILSSDRRALEIVQRWQQDGIPEKLyphtRQTlwTG------HPASLLRWVKENEP---QRYQQ--- 155
Cdd:COG0554 86 VVWDRKTgKPLYNAIVWQDRRTADICEELKADGLEDLI----REK--TGlvldpyFSATKIKWILDNVPgarERAEAgel 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 156 -IGSVmmahD-YLRWCLTG--VKGCEESNISESNLYNMNTGQYDPQLTRWLGISdiDGALPPIIGSAEICGE-------- 223
Cdd:COG0554 160 lFGTI----DsWLIWKLTGgkVHVTDVTNASRTMLFNIHTLDWDDELLELFGIP--RSMLPEVRPSSEVFGEtdpdlfga 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 224 ---ITA----QAAALTGLTAGTPvvG--------GLFdvvstaicaglhdehtLNAVMGTWAVTSG------IAHGIrDN 282
Cdd:COG0554 234 eipIAGiagdQQAALFGQACFEP--GmakntygtGCF----------------LLMNTGDEPVRSKngllttIAWGL-GG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 283 EPfpyVYGryvhpqqfivHEASPTSSGNL-EWLtaqwGDM-----SFDEINHAVASLPKAEsDVFFLPFLYG-------S 349
Cdd:COG0554 295 KV---TYA----------LEGSIFVAGAAvQWL----RDGlglidSAAESEALARSVEDNG-GVYFVPAFTGlgapywdP 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 350 NA-----GLemTSGfyglqalHTRAHLLQAVYEGVVFShmTH--LNRMLE--RFPhVQALRVTGGPTHSDVWMQMLADVS 420
Cdd:COG0554 357 DArgaifGL--TRG-------TTRAHIARAALESIAYQ--TRdvLDAMEAdsGIP-LKELRVDGGASANDLLMQFQADIL 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505385654 421 GLAIELPQVEETGCSGAALAALVGTGLYPDfYAAQRALRHDIRMIEPDMRAHAAyQRKYHRYQ 483
Cdd:COG0554 425 GVPVERPKVTETTALGAAYLAGLAVGFWKS-LEELAALWKVDRRFEPQMDEEER-ERLYAGWK 485
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
7-441 |
2.19e-30 |
|
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466796 [Multi-domain] Cd Length: 436 Bit Score: 122.72 E-value: 2.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 7 FWLGIDCGGTYLKAGLYNSQGKEVcIERRSVATLSP----RAGYAERDMHQLWQHCHKTVALLLKNSGADggqIKGVGIS 82
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDLESGRI-LESVSRPTPAPissdDPGRSEQDPEKILEAVRNLIDELPREYLSD---VTGIGIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 83 AQGKGLFLLDKQDRPLGNAILSSDRRALEIvQRWQQDGIPEKLYPHTRQTLWTGHPASLLRWVKEN--EPQRYQQIGSVM 160
Cdd:cd07777 77 GQMHGIVLWDEDGNPVSPLITWQDQRCSEE-FLGGLSTYGEELLPKSGMRLKPGYGLATLFWLLRNgpLPSKADRAGTIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 161 mahDYLRWCLTgvkGCEESNISESN-----LYNMNTGQYDPQLTRWLGISDIdgALPPIIGSAEICGEITAQaaaltgLT 235
Cdd:cd07777 156 ---DYIVARLT---GLPKPVMHPTNaaswgLFDLETGTWNKDLLEALGLPVI--LLPEIVPSGEIVGTLSSA------LP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 236 AGTPVVGGLFDVVSTAICAGLHDEHTLNAVMGT-----WAVTSGIAHGirDNEPFPYVYGRYVHpqqfiVheASPTSSGN 310
Cdd:cd07777 222 KGIPVYVALGDNQASVLGSGLNEENDAVLNIGTgaqlsFLTPKFELSG--SVEIRPFFDGRYLL-----V--AASLPGGR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 311 -LEWLT---AQW-----GDMSFDEINHAVASL--PKAESDVFFLPFLYGSNAGLEMTSGFYGLQA--LHTRaHLLQAVYE 377
Cdd:cd07777 293 aLAVLVdflREWlrelgGSLSDDEIWEKLDELaeSEESSDLSVDPTFFGERHDPEGRGSITNIGEsnFTLG-NLFRALCR 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505385654 378 GVVFSHMTHLNRMLERFPHVQALRVTGG-PTHSDVWMQMLADVSGLAIELPQVEETGCSGAALAA 441
Cdd:cd07777 372 GIAENLHEMLPRLDLDLSGIERIVGSGGaLRKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
9-483 |
6.63e-29 |
|
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: 119.13 E-value: 6.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 9 LGIDCGGTYLKAGLYNSQGKEVCIERRSVATLSPRAGYAERDMHQLWQHCHKTVALLLKNSGADGGQIKGVGISAQGKGL 88
Cdd:cd07786 3 LAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRETT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 89 FLLDKQD-RPLGNAILSSDRRALEIVQRWQQDG----IPEKlyphtrqtlwTG---HP---ASLLRWVKENEPQRYQQI- 156
Cdd:cd07786 83 VVWDRETgKPVYNAIVWQDRRTADICEELKAEGheemIREK----------TGlvlDPyfsATKIRWILDNVPGARERAe 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 157 ------GSVmmahD-YLRWCLTG--VKGCEESNISESNLYNMNTGQYDPQLTRWLGISdiDGALPPIIGSAEICGE---- 223
Cdd:cd07786 153 rgelafGTI----DsWLIWKLTGgkVHATDVTNASRTMLFNIHTLEWDDELLELFGIP--ASMLPEVKPSSEVFGYtdpd 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 224 -------ITA----QAAALTG----------LTAGTpvvgGLFDVVSTaicaglhdehtlnavmGTWAVTSgiAHG---- 278
Cdd:cd07786 227 llgaeipIAGiagdQQAALFGqacfepgmakNTYGT----GCFMLMNT----------------GEKPVRS--KNGlltt 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 279 --IRDNEPFPYVYgryvhpqqfivhEASPTSSGNL-EWLTaqwgdmsfDE---INHAVASLPKAESdvffLPflygSNAG 352
Cdd:cd07786 285 iaWQLGGKVTYAL------------EGSIFIAGAAvQWLR--------DGlglIESAAETEALARS----VP----DNGG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 353 LEMTSGFYGLQALH----------------TRAHLLQAVYEGVVFShmTH--LNRMLERFPH-VQALRVTGGPTHSDVWM 413
Cdd:cd07786 337 VYFVPAFTGLGAPYwdpdargaifgltrgtTRAHIARAALESIAYQ--TRdlLEAMEADSGIpLKELRVDGGASANDFLM 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 414 QMLADVSGLAIELPQVEETGCSGAALAALVGTGLYPDFYAAQRALRHDiRMIEPDMRAHAAyQRKYHRYQ 483
Cdd:cd07786 415 QFQADILGVPVERPKVTETTALGAAYLAGLAVGLWKSLDELAKLWQVD-RRFEPSMSEEER-EALYAGWK 482
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
6-482 |
2.95e-28 |
|
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: 117.62 E-value: 2.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 6 PFWLGIDCGGTYLKAGLYNSQGKEVCIERRSVATLSPRAGYAERDMHQLWQH---CHKTVALLLKNSGADGGQIKGVGIS 82
Cdd:cd07792 1 PLVGAIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESvyeCIEEAVEKLKALGISPSDIKAIGIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 83 AQGKGLFLLDKQ-DRPLGNAILSSDRRALEIVQRWQQDGIPEKLypHTRQTlwTGHP------ASLLRWVKENEPQRYQQ 155
Cdd:cd07792 81 NQRETTVVWDKStGKPLYNAIVWLDTRTSDTVEELSAKTPGGKD--HFRKK--TGLPistyfsAVKLRWLLDNVPEVKKA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 156 I-------GSVmmahD-YLRWCLTGVKGCEE-----SNISESNLYNMNTGQYDPQLTRWLGISDIdgALPPIIGSAEICG 222
Cdd:cd07792 157 VddgrllfGTV----DsWLIWNLTGGKNGGVhvtdvTNASRTMLMNLRTLQWDPELCEFFGIPMS--ILPEIRSSSEVYG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 223 EITA--------------QAAALTG----------LTAGTpvvgGLFDVVSTaicaglhdehtlnavmGTWAVTSGiaHG 278
Cdd:cd07792 231 KIASgplagvpisgclgdQQAALVGqgcfkpgeakNTYGT----GCFLLYNT----------------GEEPVFSK--HG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 279 I---------RDNEPfpyVYGRyvhpqqfivhEASPTSSGN-LEWLTAQWGDM-SFDEINHAVASLPKAEsDVFFLP-Fl 346
Cdd:cd07792 289 LlttvayklgPDAPP---VYAL----------EGSIAIAGAaVQWLRDNLGIIsSASEVETLAASVPDTG-GVYFVPaF- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 347 ygsnaglemtSGFY-------------GLQALHTRAHLLQAVYEGVVFSHMTHLNRM-LERFPHVQALRVTGGPTHSDVW 412
Cdd:cd07792 354 ----------SGLFapywrpdargtivGLTQFTTKAHIARAALEAVCFQTREILDAMnKDSGIPLTSLRVDGGMTKNNLL 423
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 413 MQMLADVSGLAIELPQVEETGCSGAALAALVGTGLYPDFYAAQRALRHDIRMIEPDMrAHAAYQRKYHRY 482
Cdd:cd07792 424 MQIQADILGIPVERPSMVETTALGAAIAAGLAVGVWKSLDELKSLNEGGRTVFEPQI-SEEERERRYKRW 492
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
9-467 |
8.84e-26 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 109.73 E-value: 8.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 9 LGIDCGGTYLKAGLYNSQGKEVCieRRSVATLSpRAGYAERDMHQ-----LWQH----CHKTVALLlknsgaDGGQIKGV 79
Cdd:PRK10331 5 LVLDCGATNVRAIAVDRQGKIVA--RASTPNAS-DIAAENSDWHQwsldaILQRfadcCRQINSEL------TECHIRGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 80 GISAQGKGLFLLDKQDRPLGNAILSSDRRALEIVQRWQQDGIPEKLY------PHTRQTLWTghpaslLRWVKENEPQRY 153
Cdd:PRK10331 76 TVTTFGVDGALVDKQGNLLYPIISWKCPRTAAVMENIERYISAQQLQqisgvgAFSFNTLYK------LVWLKENHPQLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 154 QQIGSVMMAHDYLRWCLTGVKGCEESNISESNLYNMNTGQYDPQLTRWLGISDidGALPPIIGSAEICGEITAQAAALTG 233
Cdd:PRK10331 150 EQAHAWLFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSR--RLFPRLVEAGEQIGTLQPSAAALLG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 234 LTAGTPVvgglfdvvstaICAGlHDehTLNAVMGTWA------VTSG-----IAHGIRDNEPFPYVY-----------GR 291
Cdd:PRK10331 228 LPVGIPV-----------ISAG-HD--TQFALFGSGAgqnqpvLSSGtweilMVRSAQVDTSLLSQYagstceldsqsGL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 292 YVHPQQFIvheasptSSGNLEWLTAQW--GDMSFDEINHAVASLPKAESDVFFLPFLYGSnagleMTSGFYGLQALHTRA 369
Cdd:PRK10331 294 YNPGMQWL-------ASGVLEWVRKLFwtAETPYQTMIEEARAIPPGADGVKMQCDLLAC-----QNAGWQGVTLNTTRG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 370 HLLQAVYEGVVFSHMTHLnRMLERFPHVQA--LRVTGGPTHSDVWMQMLADVSGLAIELPQVEETGCSGAALAALVGTGL 447
Cdd:PRK10331 362 HFYRAALEGLTAQLKRNL-QVLEKIGHFKAseLLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGE 440
|
490 500
....*....|....*....|
gi 505385654 448 YPDFYAAQRALRHDIRMIEP 467
Cdd:PRK10331 441 FSSPEQARAQMKYQYRYFYP 460
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
7-479 |
2.53e-24 |
|
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: 106.08 E-value: 2.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 7 FWLGIDCGGTYLKAGLYNSQGKEVCIERRSVATLSPRAGYAERDMHQLWQHCHKTVALLLKNSGADGGQIKGVGISAQGK 86
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFDATCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 87 gLFLLDKQDRPLG---------NAILSSDRRALEIVQRwqqdgIPEklyphtrqtlwTGHPA--------SL------LR 143
Cdd:cd07782 81 -LVVLDAEGKPVSvspsgdderNVILWMDHRAVEEAER-----INA-----------TGHEVlkyvggkiSPemeppkLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 144 WVKENEPQRYQQIGSVMMAHDYLRWCLTGVK-------GCEESNISESnlynMNTGQYDPQLTRWLGISDIDGALPPIIG 216
Cdd:cd07782 144 WLKENLPETWAKAGHFFDLPDFLTWKATGSLtrslcslVCKWTYLAHE----GSEGGWDDDFFKEIGLEDLVEDNFAKIG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 217 SA-----EICGE-ITAQAAALTGLTAGTPVVGGLFD----------VVSTAICAGLHD-EHTLNAVMGTwavtsGIAHGI 279
Cdd:cd07782 220 SVvlppgEPVGGgLTAEAAKELGLPEGTPVGVSLIDahagglgtlgADVGGLPCEADPlTRRLALICGT-----SSCHMA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 280 RDNEP--FPYVYGRYVH---PQ---------------QFIV--HEASPTSSgnlEWLTAQwGDMSFDEINHAVASLPKAE 337
Cdd:cd07782 295 VSPEPvfVPGVWGPYYSamlPGlwlneggqsatgallDHIIetHPAYPELK---EEAKAA-GKSIYEYLNERLEQLAEEK 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 338 --------SDVFFLPFLYGSNA------------GLEMTSGFYGLQALHTRAhlLQAVYEGVvfSHMthLNRMLERFPHV 397
Cdd:cd07782 371 glplayltRDLHVLPDFHGNRSpladptlrgmisGLTLDTSLDDLALLYLAT--LQALAYGT--RHI--IEAMNAAGHKI 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 398 QALRVTGGPTHSDVWMQMLADVSGLAIELPQVEETGCSGAALAALVGTGLYPDFYAAQRALRHDIRMIEPDMRAHAAYQR 477
Cdd:cd07782 445 DTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWDAMAAMSGPGKVVEPNEELKKYHDR 524
|
..
gi 505385654 478 KY 479
Cdd:cd07782 525 KY 526
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
50-460 |
2.40e-23 |
|
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: 102.61 E-value: 2.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 50 DMHQLWQHChKTVallLKNSGADGGQIKGVGISAQGKGLFLLDKQDRPLGNAILSSDRRALEIVQRWQQDGIPEKLYPHT 129
Cdd:cd07771 46 DIDRLFDEI-KEG---LKKAAEQGGDIDSIGIDTWGVDFGLLDKNGELLGNPVHYRDPRTEGMMEELFEKISKEELYERT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 130 RQTLWTGHPASLLRWVKENEPQRYQQIGSVMMAHDYLRWCLTGVKGCEESNISESNLYNMNTGQYDPQLTRWLGI-SDId 208
Cdd:cd07771 122 GIQFQPINTLYQLYALKKEGPELLERADKLLMLPDLLNYLLTGEKVAEYTIASTTQLLDPRTKDWSEELLEKLGLpRDL- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 209 gaLPPIIGSAEICGEITAQAAALTGLtAGTPVV-GGLFDVVSTAICAGLHDEHTLNAVMGTWAVTsGI--AHGIRDNEPF 285
Cdd:cd07771 201 --FPPIVPPGTVLGTLKPEVAEELGL-KGIPVIaVASHDTASAVAAVPAEDEDAAFISSGTWSLI-GVelDEPVITEEAF 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 286 PY-------VYGRYVHPQQ----FIVHEAsptssgnLEWLTAQWGDMSFDEINHAVASLPKAES------DVFFLPFlyg 348
Cdd:cd07771 277 EAgftneggADGTIRLLKNitglWLLQEC-------RREWEEEGKDYSYDELVALAEEAPPFGAfidpddPRFLNPG--- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 349 snaglEMTS------GFYGLQALHTRAHLLQAVYEGVVFSHMTHLNRMLERFPH-VQALRVTGGPTHSDVWMQMLADVSG 421
Cdd:cd07771 347 -----DMPEairaycRETGQPVPESPGEIARCIYESLALKYAKTIEELEELTGKrIDRIHIVGGGSRNALLCQLTADATG 421
|
410 420 430
....*....|....*....|....*....|....*....
gi 505385654 422 LAIELPQVEETgCSGAALAALVGTGLYPDFYAAQRALRH 460
Cdd:cd07771 422 LPVIAGPVEAT-AIGNLLVQLIALGEIKSLEEGRELVRN 459
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
60-485 |
3.28e-22 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 99.92 E-value: 3.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 60 KTVALLLKNSGADGGQIKGVGI----------SAQGKGLFLLDK-QDRPLGNAILSSDRRAL----EIVQRWQQDGipEK 124
Cdd:PRK04123 64 AAIPAVLKEAGVDPAAVVGIGVdftgstpapvDADGTPLALLPEfAENPHAMVKLWKDHTAQeeaeEINRLAHERG--EA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 125 LYPHtrqtlWTGHP-------ASLLRWVKENePQRYQQIGSVMMAHDYLRWCLTGVKGCeeSNISESN-------LYNMN 190
Cdd:PRK04123 142 DLSR-----YIGGIyssewfwAKILHVLRED-PAVYEAAASWVEACDWVVALLTGTTDP--QDIVRSRcaaghkaLWHES 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 191 TGQY---------DPQLTRwlgisDIDGALP-PIIGSAEICGEITAQAAALTGLTAGTPVVGGLFDVVSTAICAGlHDEH 260
Cdd:PRK04123 214 WGGLpsadffdalDPLLAR-----GLRDKLFtETWTAGEPAGTLTAEWAQRLGLPEGVAVSVGAFDAHMGAVGAG-AEPG 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 261 TLNAVMGTwaVTSGIAHGIRDNEpFPYVYGRY---VHPqQFIVHEASPTSSGNL-EWLT------------AQWGDMSFD 324
Cdd:PRK04123 288 TLVKVMGT--STCDILLADKQRA-VPGICGQVdgsIVP-GLIGYEAGQSAVGDIfAWFArllvppeykdeaEARGKQLLE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 325 EINHAVASLPKAESDVFFLPFLYGS---NAGLEMTSGFYGLQALHTRAHLLQAVYEGVVFshmtHLNRMLERFPH----V 397
Cdd:PRK04123 364 LLTEAAAKQPPGEHGLVALDWFNGRrtpLADQRLKGVITGLTLGTDAPDIYRALIEATAF----GTRAIMECFEDqgvpV 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 398 QALRVTGG-PTHSDVWMQMLADVSGLAIELPQVEETGCSGAALAALVGTGLYPDFYAAQRALRHDIRM-IEPDMRAHAAY 475
Cdd:PRK04123 440 EEVIAAGGiARKNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDIPEAQQAMASPVEKtYQPDPENVARY 519
|
490
....*....|
gi 505385654 476 QRKYHRYQLL 485
Cdd:PRK04123 520 EQLYQEYKQL 529
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
7-482 |
1.84e-19 |
|
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family includes bacterial RBK, vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein), Saccharomyces cerevisiae D-ribulokinase YDR109C, and Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466788 [Multi-domain] Cd Length: 522 Bit Score: 91.15 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 7 FWLGIDCGGTYLKAGLYN-SQGKEVCIERRSVAT-LSPRAGYAERDMHQLWQHCHKTVALLLKNSGADGGQIKGVGISAQ 84
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDlYAGLEMAQEPVPYYQdSSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGVDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 85 GKgLFLLDKQ---------DRPLGNAILSSDRRALEIVQrWQQDGIPEKLYPHTRQTLWTGHPASLLRWVKENEPQRYQQ 155
Cdd:cd07768 81 CS-LAIFDREgtplmalipYPNEDNVIFWMDHSAVNEAQ-WINMQCPQQLLDYLGGKISPEMGVPKLKYFLDEYSHLRDK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 156 IGSVMMAHDYLRWCLTGVkgcEESNIsESNLYNMN----TGQYDPQLTRWLGISDIDGA----LPPIIGSAEICGEITAQ 227
Cdd:cd07768 159 HFHIFDLHDYIAYELTRL---YEWNI-CGLLGKENldgeESGWSSSFFKNIDPRLEHLTttknLPSNVPIGTTSGVALPE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 228 AAALTGLTAGTPVVGGLFDV-VSTAICAGLHDEHTLNAVMGTwavtsGIAH--GIRDNEPFPYVYGRY---VHPQqFIVH 301
Cdd:cd07768 235 MAEKMGLHPGTAVVVSCIDAhASWFAVASPHLETSLFMIAGT-----SSCHmyGTTISDRIPGVWGPFdtiIDPD-YSVY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 302 EASPTSSGNL-EWL-----TAQWGDMS----------FDEINHAVASLPKAESDVFFLPFLYGSN---AGLEMTSGFYGL 362
Cdd:cd07768 309 EAGQSATGKLiEHLfeshpCARKFDEAlkkgadiyqvLEQTIRQIEKNNGLSIHILTLDMFFGNRsefADPRLKGSFIGE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 363 QaLHTRAHLLQAVY----EGVVFSHMTHLNRMLERFPHVQALRVTGGPTHSDVWMQMLADVSGLAIELPQVEETGCSGAA 438
Cdd:cd07768 389 S-LDTSMLNLTYKYiailEALAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGILGAA 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 505385654 439 LAALVGTG---LYPDFYAAQRALRHDIRMIEPDMRAHAA-YQRKYHRY 482
Cdd:cd07768 468 VLAKVAAGkkqLADSITEADISNDRKSETFEPLAYRLGAdYILLYKLL 515
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
11-469 |
3.77e-19 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 90.14 E-value: 3.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 11 IDCGGTYLKAGLYNSQGKEVCIERRSVATLSPRAGYAERDMHQLWQHCHKTVALLLKNSGADGGQ----IKGVGISAQGK 86
Cdd:PLN02295 5 IDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQAGWVEHDPMEILESVLTCIAKALEKAAAKGHNvdsgLKAIGITNQRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 87 GLFLLDKQD-RPLGNAILSSDRRALEIVQRWQQDGIPEKlyPHTRQTlwTGHP------ASLLRWVKENEPQRYQQI--- 156
Cdd:PLN02295 85 TTVAWSKSTgRPLYNAIVWMDSRTSSICRRLEKELSGGR--KHFVET--CGLPistyfsATKLLWLLENVDAVKEAVksg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 157 ----GSVmmaHDYLRWCLTGVKGCEE-----SNISESNLYNMNTGQYDPQLTRWLGISDidGALPPIIGSAEICGEITAq 227
Cdd:PLN02295 161 dalfGTI---DSWLIWNLTGGASGGVhvtdvTNASRTMLMNLKTLDWDKPTLEALGIPA--EILPKIVSNSEVIGTIAK- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 228 aaalTGLTAGTPVVGGLFDVVSTAI---CAGLHDEHT--------LNAvmGTWAVTSG------IAHGIRDNEPFPYVYg 290
Cdd:PLN02295 235 ----GWPLAGVPIAGCLGDQHAAMLgqrCRPGEAKSTygtgcfilLNT--GEEVVPSKhgllttVAYKLGPDAPTNYAL- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 291 ryvhpqqfivhEASPTSSG-NLEWLTAQWGDM-SFDEINHAVASLPKAESdVFFLPFLygsnaglemtSGFY-------- 360
Cdd:PLN02295 308 -----------EGSVAIAGaAVQWLRDNLGIIkSASEIEALAATVDDTGG-VYFVPAF----------SGLFaprwrdda 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 361 -----GLQALHTRAHLLQAVYEGVVFSHMTHLNRML----ERFPHVQ--ALRVTGGPTHSDVWMQMLADVSGLAIELPQV 429
Cdd:PLN02295 366 rgvcvGITRFTNKAHIARAVLESMCFQVKDVLDAMRkdagEEKSHKGlfLLRVDGGATANNLLMQIQADLLGSPVVRPAD 445
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 505385654 430 EETGCSGAALAALVGTGLYPDFYAAQRALRHDIRMIEPDM 469
Cdd:PLN02295 446 IETTALGAAYAAGLAVGLWTEEEIFASEKWKNTTTFRPKL 485
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
2-469 |
7.81e-19 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 89.11 E-value: 7.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 2 SEKEPFWLGIDCGGTYLKAGLYNSQGKEVCIERRSVATLSPRAGYAERDMHQLWQHCHKTVALLLKNSGADGGQIKGVGI 81
Cdd:PRK00047 1 MMMKKYILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 82 SAQGKGLFLLDKQD-RPLGNAILSSDRRALEIVQRWQQDGIPEKLyphtRQTlwTGHP------ASLLRWVKENEP---Q 151
Cdd:PRK00047 81 TNQRETTVVWDKETgRPIYNAIVWQDRRTADICEELKRDGYEDYI----REK--TGLVidpyfsGTKIKWILDNVEgarE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 152 RYQQ----IGSVmmahD-YLRWCLTG--VKGCEESNISESNLYNMNTGQYDPQLtrwLGISDIDGA-LPPIIGSAEICGE 223
Cdd:PRK00047 155 RAEKgellFGTI----DtWLVWKLTGgkVHVTDYTNASRTMLFNIHTLDWDDEL---LELLDIPRSmLPEVRPSSEVYGK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 224 ITA----------------QAAALTGL----------TAGTpvvgGLFDVVSTaicaglhdehtlnavmGTWAVTSG--- 274
Cdd:PRK00047 228 TNPygffggevpiagiagdQQAALFGQlcfepgmaknTYGT----GCFMLMNT----------------GEKAVKSEngl 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 275 ---IAHGIrDNEPfpyVYGRyvhpqqfivhEASPTSSGN-LEWLTaqwgdmsfDE---INHA-----VASLPKAESDVFF 342
Cdd:PRK00047 288 lttIAWGI-DGKV---VYAL----------EGSIFVAGSaIQWLR--------DGlkiISDAsdseaLARKVEDNDGVYV 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 343 LPFLYG-------SNA-GLemtsgFYGLQALHTRAHLLQAVYEGVVFSHMTHLNRMLERFP-HVQALRVTGGPTHSDVWM 413
Cdd:PRK00047 346 VPAFTGlgapywdSDArGA-----IFGLTRGTTKEHIIRATLESIAYQTRDVLDAMQADSGiRLKELRVDGGAVANNFLM 420
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 505385654 414 QMLADVSGLAIELPQVEETGCSGAALAAlvgtGLYPDFYAAQRALRHDI---RMIEPDM 469
Cdd:PRK00047 421 QFQADILGVPVERPVVAETTALGAAYLA----GLAVGFWKDLDELKEQWkidRRFEPQM 475
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
262-444 |
9.41e-18 |
|
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: 81.60 E-value: 9.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 262 LNAVMGTWAVtsgiaHGIRDNEP------FPYVYGRYVHPQQFIVHEASPTSSGNLEWLTAQWGdmSFDEINHA-----V 330
Cdd:pfam02782 1 LAISAGTSSF-----VLVETPEPvlsvhgVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHG--LREELRDAgnvesL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 331 ASLPKAESD-----VFFLPFLYGSNA-GLE--MTSGFYGLQALHTRAHLLQAVYEGVVFSHMTHLNRMLERFPH-VQALR 401
Cdd:pfam02782 74 AELAALAAVapaggLLFYPDFSGNRApGADpgARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHpIDTIH 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505385654 402 VTGGPTHSDVWMQMLADVSGLAIELPQVEETGCSGAALAALVG 444
Cdd:pfam02782 154 VSGGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
66-285 |
6.97e-12 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 67.44 E-value: 6.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 66 LKNSGADGGQIKGVGISAQGKGLFLLDKQDRPLGNAILSSDRRALEIVQRWQQDGIPEKLYPHTR------QTLWTghpa 139
Cdd:PRK10640 46 LNKVCEEGIRIDSIGIDTWGVDYVLLDKQGQRVGLPVSYRDSRTDGVMAQAQQQLGKRDIYRRSGiqflpfNTLYQ---- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 140 slLRWVKENEPQRYQQIGSVMMAHDYLRWCLTGVKGCEESNISESNLYNMNTGQYDPQLTRWLGISdiDGALPPIIGSAE 219
Cdd:PRK10640 122 --LRALTEQQPELIAQVAHALLIPDYFSYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGAP--KAWFGRPTHPGN 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505385654 220 ICGE-ITAQAAALtgltagtPVVG-GLFDVVSTAICAGLHDEHTLNAVMGTWAVTsgiahGIRDNEPF 285
Cdd:PRK10640 198 VIGHwICPQGNEI-------PVVAvASHDTASAVIASPLNDSDAAYLSSGTWSLM-----GFESQTPF 253
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
11-272 |
4.04e-11 |
|
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: 64.97 E-value: 4.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 11 IDCGGTYLKAGLYNSQGKEVCIERRSVATLsPRAGYAERDMHQLWQHCHKTVALLLKNsgadgGQIKGVGISAQGKGLFL 90
Cdd:cd07772 5 FDIGKTNKKLLLFDENGEVLAERSTPNPEI-EEDGYPCEDVEAIWEWLLDSLAELAKR-----HRIDAINFTTHGATFAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 91 LDKQDRPLG------NAILSSDRRALEIvqrwQQDGIPEKLYPHTRQTLwtgHPASLLRWVKENEPQRYQQIGSVMMAHD 164
Cdd:cd07772 79 LDENGELALpvydyeKPIPDEINEAYYA----ERGPFEETGSPPLPGGL---NLGKQLYWLKREKPELFARAKTILPLPQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 165 YLRWCLTGVKGCEESNIS-ESNLYNMNTGQYdpqlTRWLGISDIDGALPPIIGSAEICGEITAQAAALTGLTAGTPVVGG 243
Cdd:cd07772 152 YWAWRLTGKAASEITSLGcHTDLWDFEKNEY----SSLVKKEGWDKLFPPLRKAWEVLGPLRPDLARRTGLPKDIPVGCG 227
|
250 260 270
....*....|....*....|....*....|...
gi 505385654 244 LFDvvSTAICA---GLHDEH-TLNAVmGTWAVT 272
Cdd:cd07772 228 IHD--SNAALLpylAAGKEPfTLLST-GTWCIA 257
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
9-85 |
8.33e-06 |
|
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];
Pssm-ID: 441543 [Multi-domain] Cd Length: 306 Bit Score: 47.58 E-value: 8.33e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505385654 9 LGIDCGGTYLKAGLYNSQGKevCIERRSVATlSPRAGYAErdmhqLWQHCHKTVALLLKNSGADGGQIKGVGISAQG 85
Cdd:COG1940 8 IGIDIGGTKIKAALVDLDGE--VLARERIPT-PAGAGPEA-----VLEAIAELIEELLAEAGISRGRILGIGIGVPG 76
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
9-85 |
6.87e-04 |
|
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: 41.77 E-value: 6.87e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505385654 9 LGIDCGGTYLKAGLYNSQGKEVCieRRSVATlsPRAGYAERDMHQLWQHCHKTValllknsgaDGGQIKGVGISAQG 85
Cdd:cd24068 3 LGIDIGGTKIKYGLVDADGEILE--KDSVPT--PASKGGDAILERLLEIIAELK---------EKYDIEGIGISSAG 66
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
374-477 |
4.27e-03 |
|
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. The subfamily includes XKs mainly from eukaryote. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466795 [Multi-domain] Cd Length: 514 Bit Score: 39.46 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385654 374 AVYEGVVFSHMTHLNRMLERFPHVQALrVTGGPTHSDVWMQMLADVSGLAIELPQVEETGCSGAALAA----LVGTGLYP 449
Cdd:cd07776 404 AVVESQFLSMRLHAERLGSDIPPTRIL-ATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAahglLCAGSGDF 482
|
90 100
....*....|....*....|....*...
gi 505385654 450 DFYAAQRALRHDIRMIEPDMRAHAAYQR 477
Cdd:cd07776 483 SPEFVVFSAEEPKLVAEPDPEAAEVYDK 510
|
|
| |
