|
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: 600.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 7 FWLGIDCGGTYLKAGLYNSQGKEFDIERQSVHTLSPQPGWAERDMAALWQHCATTLSRLLQRTGIRGEQIRGVGISAQGK 86
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGHGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 87 GLFLLDKNDQPLGTAILSSDRRAMEIVKRWQQDGIPQKLYPLTRQTLWTGHPASLLRWVKEHEPQRYAQIGCVMMGHDYL 166
Cdd:cd07802 81 GLYLVDKDGKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKENEPERYDRIRTVLFCKDWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 167 RWCLTGVKGCEESNISeSNLYHMTSGQYDPCLTQWLGISEIDAVLPPIVGSSQISGEITSQAAAITGLAAGTPVVGGLFD 246
Cdd:cd07802 161 RYRLTGEISTDYTDAG-SSLLDLDTGEYDDELLDLLGIEELKDKLPPLVPSTEIAGRVTAEAAALTGLPEGTPVAAGAFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 247 VVSTALCAGLDDEYTLNAVMGTWAVTSGITEGLRDNEAhPFVYGRYVNEGQYIVHEASPTSSGNLEWLTAQF-------G 319
Cdd:cd07802 240 VVASALGAGAVDEGQLCVILGTWSINEVVTDEPVVPDS-VGSNSLHADPGLYLIVEASPTSASNLDWFLDTLlgeekeaG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 320 DISFDEINKLVDSLPKATSDVFFLPFLYGSNAGLDMTSGFYGMQALHTRAHLLQAVYEGVVFSHMTHLNRMRERFtEVRS 399
Cdd:cd07802 319 GSDYDELDELIAAVPPGSSGVIFLPYLYGSGANPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHRDHLERLLVAR-KPET 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 751394705 400 LRVTGGPAHSPVWMQMLADVSGLPVELPQVEETGCFGAAIAALVGTG 446
Cdd:cd07802 398 IRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
8-495 |
1.28e-177 |
|
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: 507.83 E-value: 1.28e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 8 WLGIDCGGTYLKAGLYNSQGKEFDIERQSVHTLSPQPGWAERDMAALWQHCATTLSRLLQRTGIRGEQIRGVGISAQGKG 87
Cdd:COG1070 3 VLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQMHG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 88 LFLLDKNDQPLGTAILSSDRRAMEIVKRWQQDGIPQKLYPLTRQTLWTGHPASLLRWVKEHEPQRYAQIGCVMMGHDYLR 167
Cdd:COG1070 83 LVLLDADGEPLRPAILWNDTRAAAEAAELREELGEEALYEITGNPLHPGFTAPKLLWLKENEPEIFARIAKVLLPKDYLR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 168 WCLTGVKGCEESNISESNLYHMTSGQYDPCLTQWLGISEidAVLPPIVGSSQISGEITSQAAAITGLAAGTPVVGGLFDV 247
Cdd:COG1070 163 YRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDR--ELLPELVPPGEVAGTLTAEAAAETGLPAGTPVVAGAGDN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 248 VSTALCAGLDDEYTLNAVMGTWAVTSGITEGLRDNEAHPFVYGRYVNEGQYIVHEASPTSSGNLEWLTAQFGD---ISFD 324
Cdd:COG1070 241 AAAALGAGAVEPGDAAVSLGTSGVVFVVSDKPLPDPEGRVHTFCHAVPGRWLPMGATNNGGSALRWFRDLFADgelDDYE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 325 EINKLVDSLPKATSDVFFLPFLYGSNAGL---DMTSGFYGMQALHTRAHLLQAVYEGVVFSHMTHLNRMRERFTEVRSLR 401
Cdd:COG1070 321 ELNALAAEVPPGADGLLFLPYLSGERTPHwdpNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEALEEAGVKIDRIR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 402 VTGGPAHSPVWMQMLADVSGLPVELPQVEETGCFGAAIAALVGTGVYANFADAQQTLSYEMRTLMPDMNAHAAYQRKYYR 481
Cdd:COG1070 401 ATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMVRVGETIEPDPENVAAYDELYER 480
|
490
....*....|....
gi 751394705 482 YQILIEALQGFHAR 495
Cdd:COG1070 481 YRELYPALKPLFER 494
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
9-483 |
4.50e-124 |
|
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: 371.10 E-value: 4.50e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 9 LGIDCGGTYLKAGLYNSQGKEFDIERQSVHTLSPQPGWAERDMAALWQHCATTLSRLLQRTGIRGEQIRGVGISAQGKGL 88
Cdd:cd07808 3 LGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQMHGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 89 FLLDKNDQPLGTAILSSDRRAMEIVkRWQQDGIPQKLYPLTRQTLWTGHPASLLRWVKEHEPQRYAQIGCVMMGHDYLRW 168
Cdd:cd07808 83 VLLDKNGRPLRPAILWNDQRSAAEC-EELEARLGDEILIITGNPPLPGFTLPKLLWLKENEPEIFARIRKILLPKDYLRY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 169 CLTGVKGCEESNISESNLYHMTSGQYDPCLTQWLGISEidAVLPPIVGSSQISGEITSQAAAITGLAAGTPVVGGLFDVV 248
Cdd:cd07808 162 RLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDP--SILPPIVESTEIVGTLTPEAAEELGLPEGTPVVAGAGDNA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 249 STALCAGLDDEYTLNAVMGTWAVTSGITEGLRDNEAHPFVYGRYVNEGQYIVHEASPTSSGNLEWLTAQFG--DISFDEI 326
Cdd:cd07808 240 AAALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLHTFPHAVPGKWYAMGVTLSAGLSLRWLRDLFGpdRESFDEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 327 NKLVDSLPKATSDVFFLPFLYGS-----NAglDMTSGFYGMQALHTRAHLLQAVYEGVVFSHMTHLNRMRERFTEVRSLR 401
Cdd:cd07808 320 DAEAAKVPPGSEGLLFLPYLSGErtpywDP--NARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVLKELGIKVKEIR 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 402 VTGGPAHSPVWMQMLADVSGLPVELPQVEETGCFGAAIAALVGTGVYANFADAQQTLSYEMRTLMPDMNAHAAYQRKYYR 481
Cdd:cd07808 398 LIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAAACIKIEKTIEPDPERHEAYDELYAR 477
|
..
gi 751394705 482 YQ 483
Cdd:cd07808 478 YR 479
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
7-482 |
3.22e-110 |
|
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: 335.64 E-value: 3.22e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 7 FWLGIDCGGTYLKAGLYNSQGKEFDIERQSVHTLSPQPGWAERDMAALWQHCATTLSRLLQRTGIRGEQIRGVGISAQGK 86
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQMQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 87 GLFLLDKNDQPLGTAILSSDRRAMEIVKRWQQDGIPQKLYPLTRQTLWTGH-PASLLRWVKEHEPQRYAQIGCVMMGHDY 165
Cdd:cd07805 81 GVVPVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLGGGNPPSGKdPLAKILWLKENEPEIYAKTHKFLDAKDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 166 LRWCLTGVKGCEESNISESNLYHMTSGQYDPCLTQWLGISEidAVLPPIVGSSQISGEITSQAAAITGLAAGTPVVGGLF 245
Cdd:cd07805 161 LNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDP--DKLPELVPSTEVVGELTPEAAAELGLPAGTPVVGGGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 246 DVVSTALCAGLDDEYTLNAVMGT--WAVTSgITEGLRDNEAHPFVYgRYVNEGQYIVHEASPTSSGNLEWLTAQF----- 318
Cdd:cd07805 239 DAAAAALGAGAVEEGDAHIYLGTsgWVAAH-VPKPKTDPDHGIFTL-ASADPGRYLLAAEQETAGGALEWARDNLggded 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 319 -GDISFDEINKLVDSLPKATSDVFFLPFLYGSNAGLD---MTSGFYGMQALHTRAHLLQAVYEGVVFSHMTHLNRMRERF 394
Cdd:cd07805 317 lGADDYELLDELAAEAPPGSNGLLFLPWLNGERSPVEdpnARGAFIGLSLEHTRADLARAVLEGVAFNLRWLLEALEKLT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 395 TEVRSLRVTGGPAHSPVWMQMLADVSGLPVELPQV-EETGCFGAAIAALVGTGVYANFADAQQTLSYEmRTLMPDMNAHA 473
Cdd:cd07805 397 RKIDELRLVGGGARSDLWCQILADVLGRPVEVPENpQEAGALGAALLAAVGLGLLKSFDEAKALVKVE-KVFEPDPENRA 475
|
....*....
gi 751394705 474 AYQRKYYRY 482
Cdd:cd07805 476 RYDRLYEVF 484
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
7-253 |
4.83e-109 |
|
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: 323.91 E-value: 4.83e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 7 FWLGIDCGGTYLKAGLYNSQGKEFDIERQSVHTLSPQPGWAERDMAALWQHCATTLSRLLQRTGIRGEQIRGVGISAQGK 86
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSQLGISLKQIKGIGISNQGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 87 GLFLLDKNDQPLGTAILSSDRRAMEIVKRWQQDGIPQKLYPLTRQTLWTGHPASLLRWVKEHEPQRYAQIGCVMMGHDYL 166
Cdd:pfam00370 81 GTVLLDKNDKPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHKFLTIHDYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 167 RWCLTGVKGCEESNISESNLYHMTSGQYDPCLTQWLGISEIdaVLPPIVGSSQISGEITSQAAAITGLAAGTPVVGGLFD 246
Cdd:pfam00370 161 RWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRD--HLPPLVESSEIYGELNPELAAMWGLDEGVPVVGGGGD 238
|
....*..
gi 751394705 247 VVSTALC 253
Cdd:pfam00370 239 QQAAAFG 245
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
9-441 |
5.09e-109 |
|
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: 329.14 E-value: 5.09e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 9 LGIDCGGTYLKAGLYNSQGKEFDIERQSVHTLSPQPGWAERDMAALWQHCATTLSRLLQRTGIRGEQIRGVGISAQGKGL 88
Cdd:cd00366 3 LGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQMPGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 89 FLLDKNDQPLGTAILSSDRRAmeivkrwqqdgipqklypltrqtlwtghpasllrwvkehepqryaqigCVMMGHDYLRW 168
Cdd:cd00366 83 VLVDADGNPLRPAIIWLDRRA------------------------------------------------KFLQPNDYIVF 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 169 CLTGVKGCEESNISESNLYHMTSGQYDPCLTQWLGISEidAVLPPIVGSSQISGEITSQAAAITGLAAGTPVVGGLFDVV 248
Cdd:cd00366 115 RLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPR--EKLPPIVESGEVVGRVTPEAAEETGLPAGTPVVAGGGDTA 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 249 STALCAGLDDEYTLNAVMGTWAVTSGITEglRDNEAHPFVYGRY-VNEGQYIVHEASPTSSGNLEWLTAQFG-----DIS 322
Cdd:cd00366 193 AAALGAGVVEPGDAVDSTGTSSVLSVCTD--EPVPPDPRLLNRChVVPGLWLLEGAINTGGASLRWFRDEFGeeedsDAE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 323 FDEINKLVDSLPKATSDVFFLPFLYGSNAGLDMTS---GFYGMQALHTRAHLLQAVYEGVVFSHMTHLNRMRERFTEVRS 399
Cdd:cd00366 271 YEGLDELAAEVPPGSDGLIFLPYLSGERSPIWDPAargVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEILEELGVKIKE 350
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 751394705 400 LRVTGGPAHSPVWMQMLADVSGLPVELPQVEETGCFGAAIAA 441
Cdd:cd00366 351 IRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
7-446 |
7.11e-109 |
|
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: 331.13 E-value: 7.11e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 7 FWLGIDCGGTYLKAGLYNSQGKEFDIERQSVHTLSPQPGWAERDMAALWQHCATTLSRLLQRTGIRGEQIRGVGISAQGK 86
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 87 GLFLLDKNDQPLGTAILSSDRRAMEIVKRWQQDGIPQKLYPLTRQTLWTGHPASLLRWVKEHEPQRYAQIGCVMMGHDYL 166
Cdd:cd24121 81 GTWLVDEDGRPVRDAILWLDGRAADIVERWQADGIAEAVFEITGTGLFPGSQAAQLAWLKENEPERLERARTALHCKDWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 167 RWCLTGVKGCEESNISESNLYHMTsGQYDPCLTQWLGISEIDAVLPPIVGSSQISGEITSQAAAITGLAAGTPVVGGLFD 246
Cdd:cd24121 161 FYKLTGEIATDPSDASLTFLDFRT-RQYDDEVLDLLGLEELRHLLPPIRPGTEVIGPLTPEAAAATGLPAGTPVVLGPFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 247 VVSTALCAGLDDEYTLNAVMGTWAVTSGITEGLRDNEAHP---FVYGRyvnEGQYIVHEASPTSSGNLEWLTAQFGDI-- 321
Cdd:cd24121 240 VVATALGSGAIEPGDACSILGTTGVHEVVVDEPDLEPEGVgytICLGV---PGRWLRAMANMAGTPNLDWFLRELGEVlk 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 322 ---------SFDEINKLVDSLPKATSDVFFLPFLygSNAG-----LDMTS--GFYGMQALHTRAHLLQAVYEGVVFShmt 385
Cdd:cd24121 317 egaepagsdLFQDLEELAASSPPGAEGVLYHPYL--SPAGerapfVNPNAraQFTGLSLEHTRADLLRAVYEGVALA--- 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 751394705 386 hlnrMRERF----TEVRSLRVTGGPAHSPVWMQMLADVSGLPVELPQVEETGCFGAAIAALVGTG 446
Cdd:cd24121 392 ----MRDCYehmgEDPGELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
9-446 |
3.38e-105 |
|
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: 321.07 E-value: 3.38e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 9 LGIDCGGTYLKAGLYNSQGKEFDIERQSVHTLSPQPGWAERDMAALWQHCATTLSRLLQRTGirGEQIRGVGISAQGKGL 88
Cdd:cd07773 3 LGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAG--PDPIAAISVSSQGESG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 89 FLLDKNDQPLGTAILSSDRRAMEIVKRWQQDGIPQKLYPLTRQTLWTGHPASLLRWVKEHEPQRYAQIGCVMMGHDYLRW 168
Cdd:cd07773 81 VPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEELYRITGLPPSPMYSLAKLLWLREHEPEIFAKAAKWLSVADYIAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 169 CLTGVKGCEESNISESNLYHMTSGQYDPCLTQWLGISEidAVLPPIVGSSQISGEITSQAAAITGLAAGTPVV-GGLfDV 247
Cdd:cd07773 161 RLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDA--SLLPELVPSGTVIGTVTPEAAEELGLPAGTPVVvGGH-DH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 248 VSTALCAGLDDEYTLNAVMGTWAVTSGITEGLRDNEAHP---FVYGRYVNEGQYIVHeASPTSSGNLEWLTAQFG--DIS 322
Cdd:cd07773 238 LCAALGAGVIEPGDVLDSTGTAEALLAVVDEPPLDEMLAeggLSYGHHVPGGYYYLA-GSLPGGALLEWFRDLFGgdESD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 323 FDEINKLVDSLPKATSDVFFLPFLYGSNA---GLDMTSGFYGMQALHTRAHLLQAVYEGVVFSHMTHLNRMRERFTEVRS 399
Cdd:cd07773 317 LAAADELAEAAPPGPTGLLFLPHLSGSGTpdfDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEALEKAGIPIDE 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 751394705 400 LRVTGGPAHSPVWMQMLADVSGLPVELPQVEETGCFGAAIAALVGTG 446
Cdd:cd07773 397 IRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
7-475 |
2.87e-96 |
|
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: 297.89 E-value: 2.87e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 7 FWLGIDCGGTYLKAGLYNSQGKEFDIERQSVHTLSPQPGWAERDMAALWQHCATTLSRLLQRTGIRGEQIRGVGISAQGK 86
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 87 GLFLLDKNDQPLGTAILSSDRRAmeivkrwqqdgipqklypltrqtlwtghpasllrwvkehepQRYAQIgcvmmgHDYL 166
Cdd:cd07779 81 TFVPVDEDGRPLRPAISWQDKRT-----------------------------------------AKFLTV------QDYL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 167 RWCLTGVKGCEESNISESNLYHMTSGQYDPCLTQWLGISEidAVLPPIVGSSQISGEITSQAAAITGLAAGTPVVGGLFD 246
Cdd:cd07779 114 LYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDR--DKLPELVPPGTVIGTLTKEAAEETGLPEGTPVVAGGGD 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 247 VVSTALCAGLDDEYTLNAVMGTWAVTSGITEGLRDNEAHPFVYGRYVNEGQYIVhEASPTSSGN-LEWLTAQFGDI---- 321
Cdd:cd07779 192 QQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPGKWVL-EGSINTGGSaVRWFRDEFGQDevae 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 322 ------SFDEINKLVDSLPKATSDVFFLPFLYGSNA---GLDMTSGFYGMQALHTRAHLLQAVYEGVVFSHMTHLNRMRE 392
Cdd:cd07779 271 kelgvsPYELLNEEAAKSPPGSDGLLFLPYLAGAGTpywNPEARGAFIGLTLSHTRAHLARAILEGIAFELRDNLEAMEK 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 393 RFTEVRSLRVTGGPAHSPVWMQMLADVSGLPVELPQVEETGCFGAAIAALVGTGVYANFADAQQTLSYEMRTLMPDMNAH 472
Cdd:cd07779 351 AGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKAMVRVTDTFEPDPENV 430
|
...
gi 751394705 473 AAY 475
Cdd:cd07779 431 AIY 433
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
9-485 |
6.33e-89 |
|
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: 280.60 E-value: 6.33e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 9 LGIDCGGTYLKAGLYNSQGKEFDIERQSVHTLSPQPGWAERDMAALWQHCATTLSRLLQRTGIRgeQIRGVGISAQGKGL 88
Cdd:cd07770 3 LGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGG--EVDAIGFSSAMHSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 89 FLLDKNDQPLGTAILSSDRRAMEIVKRWQQDGIPQKLYPLTrqtlwtG---HPASL---LRWVKEHEPQRYAQIGCVM-M 161
Cdd:cd07770 81 LGVDEDGEPLTPVITWADTRAAEEAERLRKEGDGSELYRRT------GcpiHPMYPlakLLWLKEERPELFAKAAKFVsI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 162 GhDYLRWCLTGVKGCEESNISESNLYHMTSGQYDPCLTQWLGISEidAVLPPIVGSSQISGEITSQAAAITGLAAGTPVV 241
Cdd:cd07770 155 K-EYLLYRLTGELVTDYSTASGTGLLNIHTLDWDEEALELLGIDE--EQLPELVDPTEVLPGLKPEFAERLGLLAGTPVV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 242 GGLFDVVSTALCAGLDDEYTLNAVMGTwavtSG-----ITEGLRDNEAHPFVYgrYVNEGQYIVHEASpTSSGN-LEWLT 315
Cdd:cd07770 232 LGASDGALANLGSGALDPGRAALTVGT----SGairvvSDRPVLDPPGRLWCY--RLDENRWLVGGAI-NNGGNvLDWLR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 316 AQFG--DISFDEINKLVDSLPKATSDVFFLPFLYGSNA---GLDMTSGFYGMQALHTRAHLLQAVYEGVVFSHMTHLNRM 390
Cdd:cd07770 305 DTLLlsGDDYEELDKLAEAVPPGSHGLIFLPYLAGERApgwNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKSIYEAL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 391 RERFTEVRSLRVTGGPAHSPVWMQMLADVSGLPVELPQVEETGCFGAAIAALVGTGVYANFADAQQTLSYEmrTLMPDMN 470
Cdd:cd07770 385 EELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSLEADELVKIGK--VVEPDPE 462
|
490
....*....|....*
gi 751394705 471 AHAAYQRKYYRYQIL 485
Cdd:cd07770 463 NHAIYAELYERFKKL 477
|
|
| XylB |
TIGR01312 |
D-xylulose kinase; This model describes D-xylulose kinases, a subfamily of the FGGY family of ... |
9-485 |
2.48e-86 |
|
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: 273.81 E-value: 2.48e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 9 LGIDCGGTYLKAGLYNSQGKEFDIERQSVHTLSPQPGWAERDMAALWQHCATTLSRLLQRTGIRGEQIRGVGISAQGKGL 88
Cdd:TIGR01312 1 LGIDLGTSGVKALLVDEQGEVIASGSAPHTVISPHPGWSEQDPEDWWDATEEAIKELLEQASEMGQDIKGIGISGQMHGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 89 FLLDKNDQPLGTAILSSDRRAMEIVKRWQQDGIPQKLYPLTRQTLWTGHPASLLRWVKEHEPQRYAQIGCVMMGHDYLRW 168
Cdd:TIGR01312 81 VLLDANGEVLRPAILWNDTRTAQECEELEAELGDERVLEITGNLALPGFTAPKLLWVRKHEPEVFARIAKVMLPKDYLRY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 169 CLTGVKGCEESNISESNLYHMTSGQYDPCLTQWLGISEidAVLPPIVGSSQISGEITSQAAAITGLAAGTPVVGGLFDVV 248
Cdd:TIGR01312 161 RLTGEYVTEYSDASGTGWFDVAKRAWSKELLDALDLPE--SQLPELIESSEKAGTVRPEVAARLGLSAGVPVAAGGGDNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 249 STALCAGLDDEYTLNAVMGTWAVTSGITEGLR---DNEAHPFVYGRyvnEGQYivHEASPTSSGN--LEWLTAQFGDISF 323
Cdd:TIGR01312 239 AGAIGTGTVDPGDAMMSLGTSGVVYAVTDKPLpdpAGAVHGFCHAL---PGGW--LPMGVTLSATssLEWFRELFGKEDV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 324 DEINKLVDSLPKATSDVFFLPFLYGS---NAGLDMTSGFYGMQALHTRAHLLQAVYEGVVFSHMTHLNRMRER-FTEVRS 399
Cdd:TIGR01312 314 EALNELAEQSPPGAEGVTFLPYLNGErtpHLDPQARGSFIGLTHNTTRADLTRAVLEGVTFALRDSLDILREAgGIPIQS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 400 LRVTGGPAHSPVWMQMLADVSGLPVELPQVEETGCFGAAIAALVGTGVYANFADAQQTLSYEMRTLMPDMNAHAAYQRKY 479
Cdd:TIGR01312 394 IRLIGGGAKSPAWRQMLADIFGTPVDVPEGEEGPALGAAILAAWALGEKDLAALCSEAVVKQTESVLPIAENVEAYEELY 473
|
....*.
gi 751394705 480 YRYQIL 485
Cdd:TIGR01312 474 ERYKKL 479
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
9-446 |
2.03e-85 |
|
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: 270.55 E-value: 2.03e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 9 LGIDCGGTYLKAGLYNSQGKEFDIERQSVHTLSPQPGWAERDMAALWQHCATTLSRLLQRTGIRGEQIRGVGISAQGKGL 88
Cdd:cd07804 3 LGIDIGTTGTKGVLVDEDGKVLASASIEHDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGLVPAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 89 FLLDKNDQPLGTAILSSDRRAMEIVKRWQQDGIPQKLYPLTRQTLWTGHPASLLRWVKEHEPQRYAQIGCVMMGHDYLRW 168
Cdd:cd07804 83 VPVDENGKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITGNPLDSQSVGPKLLWIKRNEPEVFKKTRKFLGAYDYIVY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 169 CLTGVKGCEESN-ISESNLYHMTSGQYDPCLTQWLGISEidAVLPPIVGSSQISGEITSQAAAITGLAAGTPVVGGLFDV 247
Cdd:cd07804 163 KLTGEYVIDYSSaGNEGGLFDIRKRTWDEELLEALGIDP--DLLPELVPSTEIVGEVTKEAAEETGLAEGTPVVAGTVDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 248 VSTALCAGLDDEYTLNAVMGT---WAVtsgITEGLRDNEAHPFVYgrYVNEGQYIVHEASPTSSGNLEWLTAQF------ 318
Cdd:cd07804 241 AASALSAGVVEPGDLLLMLGTagdIGV---VTDKLPTDPRLWLDY--HDIPGTYVLNGGMATSGSLLRWFRDEFageeve 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 319 -----GDISFDEINKLVDSLPkATSD-VFFLPFLYG-------SNAgldmtSG-FYGMQALHTRAHLLQAVYEGVVFSHM 384
Cdd:cd07804 316 aeksgGDSAYDLLDEEAEKIP-PGSDgLIVLPYFMGertpiwdPDA-----RGvIFGLTLSHTRAHLYRALLEGVAYGLR 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 751394705 385 THLNRMRERFTEVRSLRVTGGPAHSPVWMQMLADVSGLPVELPQVEETGCFGAAIAALVGTG 446
Cdd:cd07804 390 HHLEVIREAGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
9-491 |
2.60e-68 |
|
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: 227.42 E-value: 2.60e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 9 LGIDCGGTYLKAGLYNSQ-GKE--FDIERQSVHTLSPQPGWAERDMAALWQHCATTLSRLLQRTGIRGEQIRGVGISAQG 85
Cdd:cd07781 3 IGIDFGTQSVRAGLVDLAdGEElaSAVVPYPTGYIPPRPGWAEQNPADYWEALEEAVRGALAEAGVDPEDVVGIGVDTTS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 86 KGLFLLDKNDQPLGTAILSSDRRAMEivkrwQQDGIPQKLYPLTRQTL-WTGHPAS-------LLrWVKEHEPQRYAQIG 157
Cdd:cd07781 83 STVVPVDEDGNPLAPAILWMDHRAQE-----EAAEINETAHPALEYYLaYYGGVYSsewmwpkAL-WLKRNAPEVYDAAY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 158 CVMMGHDYLRWCLTGVKGCEESNISESNLYHMTSGQYDPCLTQWLGI--SEIDAVLP-PIVGSSQISGEITSQAAAITGL 234
Cdd:cd07781 157 TIVEACDWINARLTGRWVRSRCAAGHKWMYNEWGGGPPREFLAALDPglLKLREKLPgEVVPVGEPAGTLTAEAAERLGL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 235 AAGTPVVGGLFDVVSTALCAGLDDEYTLNAVMGTWAVTSGITEglrdnEAHPF--VYGRY---VNEGQYIVhEASPTSSG 309
Cdd:cd07781 237 PAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTSTCHLMVSP-----KPVDIpgICGPVpdaVVPGLYGL-EAGQSAVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 310 N-LEWLTAQF-------GDISFDEINKLVDSLPKATSDVFFLPFLYGS-----NAGLdmTSGFYGMQALHTRAHLLQAVY 376
Cdd:cd07781 311 DiFAWFVRLFvppaeerGDSIYALLSEEAAKLPPGESGLVALDWFNGNrtplvDPRL--RGAIVGLTLGTTPAHIYRALL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 377 EGVVFSHMTHLNRMRERFTEVRSLRVTGGPA-HSPVWMQMLADVSGLPVELPQVEETGCFGAAIAALVGTGVYANFADAQ 455
Cdd:cd07781 389 EATAFGTRAIIERFEEAGVPVNRVVACGGIAeKNPLWMQIYADVLGRPIKVPKSDQAPALGAAILAAVAAGVYADIEEAA 468
|
490 500 510
....*....|....*....|....*....|....*.
gi 751394705 456 QTLSYEMRTLMPDMNAHAAYQRKYYRYQILIEALQG 491
Cdd:cd07781 469 DAMVRVDRVYEPDPENHAVYEELYALYKELYDALGP 504
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
9-446 |
3.25e-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: 220.11 E-value: 3.25e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 9 LGIDCGGTYLKAGLYNSQGKEFDIERQSVHTL-SPQPGWAERDMAALWQHCATTLSRLLQRTGIRGEQIRGVGISAQGKG 87
Cdd:cd07809 3 LGIDLGTQSIKAVLIDAETGRVVASGSAPHENiLIDPGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISGQMHG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 88 LFLLDKNDQPLGTAILSSDRRAMEI---------VKRWQQDGIPqklyPLTRqtlWTghpASLLRWVKEHEPQRYAQIGC 158
Cdd:cd07809 83 LVALDADGKVLRPAKLWCDTRTAPEaeeltealgGKKCLLVGLN----IPAR---FT---ASKLLWLKENEPEHYARIAK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 159 VMMGHDYLRWCLTGVKGCEESNISESNLYHMTSGQYDPCLTQWLGISEID-AVLPPIVGSSQISGEITSQAAAITGLAAG 237
Cdd:cd07809 153 ILLPHDYLNWKLTGEKVTGLGDASGTFPIDPRTRDYDAELLAAIDPSRDLrDLLPEVLPAGEVAGRLTPEGAEELGLPAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 238 TPVVGGLFDVVSTALCAGLDDEYTLNAVMGTWAVTSGITE-GLRDneAHPFVYG-RYVNEGqyIVHEASPTSSGN--LEW 313
Cdd:cd07809 233 IPVAPGEGDNMTGALGTGVVNPGTVAVSLGTSGTAYGVSDkPVSD--PHGRVATfCDSTGG--MLPLINTTNCLTawTEL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 314 LTAQFGdISFDEINKLVDSLPKATSDVFFLPFLYG-SNAGLDMTSG-FYGMQ-ALHTRAHLLQAVYEGVVFSHMTHLNRM 390
Cdd:cd07809 309 FRELLG-VSYEELDELAAQAPPGAGGLLLLPFLNGeRTPNLPHGRAsLVGLTlSNFTRANLARAALEGATFGLRYGLDIL 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 751394705 391 RERFTEVRSLRVTGGPAHSPVWMQMLADVSGLPVELPQVEETGCFGAAIAALVGTG 446
Cdd:cd07809 388 RELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
7-445 |
5.08e-66 |
|
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: 219.40 E-value: 5.08e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 7 FWLGIDCGGTYLKAGLYNSQGKEFDIERQSVHTLSPQPGWAERDMAALWQHCATTLSRLLQRtgIRGEQIRGVGISAQGK 86
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAE--LRPRRVVAIAVDGTSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 87 GLFLLDKNDQPLGTAILSSDRRAMEIVKRWQQdgIPQKLYPLTRQTLWTGHPASLLRWVKEHEPQRYAQIGCVMMGHDYL 166
Cdd:cd07783 79 TLVLVDREGEPLRPAIMYNDARAVAEAEELAE--AAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAKFLHQADWL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 167 RWCLTGVKGC-EESNISESnLYHMTSGQYDPCLTQWLGISEidAVLPPIVGSSQISGEITSQAAAITGLAAGTPVVGGLF 245
Cdd:cd07783 157 AGRLTGDRGVtDYNNALKL-GYDPETGRWPSWLLALLGIPP--DLLPRVVAPGTVIGTLTAEAAEELGLPAGTPVVAGTT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 246 DVVSTALCAGLDDEYTLNAVMGTWAVTSGITEGLRDNEAHpFVYGRYVNEGQYIVHEASPTSSGNLEWLtaqFGDISFDE 325
Cdd:cd07783 234 DSIAAFLASGAVRPGDAVTSLGTTLVLKLLSDKRVPDPGG-GVYSHRHGDGYWLVGGASNTGGAVLRWF---FSDDELAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 326 INKLVDSLPKatSDVFFLPF-LYGSNAGL---DMTSGFYGMQalHTRAHLLQAVYEGVVFSHMTHLNRMRER-FTEVRSL 400
Cdd:cd07783 310 LSAQADPPGP--SGLIYYPLpLRGERFPFwdpDARGFLLPRP--HDRAEFLRALLEGIAFIERLGYERLEELgAPPVEEV 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 751394705 401 RVTGGPAHSPVWMQMLADVSGLPVELPQvEETGCFGAAIAALVGT 445
Cdd:cd07783 386 RTAGGGARNDLWNQIRADVLGVPVVIAE-EEEAALGAALLAAAGL 429
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
9-446 |
8.67e-62 |
|
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: 208.62 E-value: 8.67e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 9 LGIDCGGTYLKAGLYNSQGKEFDIERQ--SVHTLSPQPGWAERDMAALWQHCATTLSRLLQRTGIRGEQIRGVGISAQGK 86
Cdd:cd07798 3 LVIDIGTGGGRCALVDSEGKIVAIAYRewEYYTDDDYPDAKEFDPEELWEKICEAIREALKKAGISPEDISAVSSTSQRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 87 GLFLLDKNDQPL--GTAIlssDRRAMEIVkrwqqDGIPQKLYPltRQTLWTGH------PASLLRWVKEHEPQRYAQIGC 158
Cdd:cd07798 83 GIVFLDKDGRELyaGPNI---DARGVEEA-----AEIDDEFGE--EIYTTTGHwptelfPAARLLWFKENRPEIFERIAT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 159 VMMGHDYLRWCLTGVKGCEESNISESNLYHMTSGQYDPCLTQWLGISEidAVLPPIVGSSQISGEITSQAAAITGLAAGT 238
Cdd:cd07798 153 VLSISDWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPP--EILPEIVPSGTVLGTVSEEAARELGLPEGT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 239 PVVGGLFDVVSTALCAGLDDEYTLNAVMGTWAVTSGITEGLRDNEAHPFVYGRYVNEGQYIVhEASPTSSG-NLEWLT-- 315
Cdd:cd07798 231 PVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERRLWTGCHLVPGKWVL-ESNAGVTGlNYQWLKel 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 316 -AQFGDISFDEINKLVDSLPKATSDV--FFLPFLYGSNAGLDMTSGFYGMQALH----TRAHLLQAVYEGVVFSHMTHLN 388
Cdd:cd07798 310 lYGDPEDSYEVLEEEASEIPPGANGVlaFLGPQIFDARLSGLKNGGFLFPTPLSaselTRGDFARAILENIAFAIRANLE 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 751394705 389 RMRE-RFTEVRSLRVTGGPAHSPVWMQMLADVSGLPVELPQVEETGCFGAAIAALVGTG 446
Cdd:cd07798 390 QLEEvSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
9-482 |
4.90e-48 |
|
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: 172.90 E-value: 4.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 9 LGIDCGGTYLKAGLYNSQGKEFDI-ERQSVHTLSPQ-PGWAERDMAALWQHCATTLSRLLQRTGIRGEQIRGVGISAQGK 86
Cdd:cd07775 3 LALDAGTGSGRAVIFDLEGNQIAVaQREWRHKEVPDvPGSMDFDTEKNWKLICECIREALKKAGIAPKSIAAISTTSMRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 87 GLFLLDKNDQPLgTAILSSDRRAMEIVKRWQQ--DGIPQKLYPLTRQTLWTGHPASLLrWVKEHEPQRYAQIGCVMMGHD 164
Cdd:cd07775 83 GIVLYDNEGEEI-WACANVDARAAEEVSELKElyNTLEEEVYRISGQTFALGAIPRLL-WLKNNRPEIYRKAAKITMLSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 165 YLRWCLTGVKGCEESNISESNLYHMTSGQYDPCLTQWLGISeiDAVLPPIVGSSQISGEITSQAAAITGLAAGTPVVGGL 244
Cdd:cd07775 161 WIAYKLSGELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLK--ADILPPVVESGTVIGKVTKEAAEETGLKEGTPVVVGG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 245 FDVvsTALCAGLDDEYTLNAVM---GTWA----VTSGITE---GLRDNeAHPfVYGRYVNEGqyIVHEASPTssgnLEW- 313
Cdd:cd07775 239 GDV--QLGCLGLGVVRPGQTAVlggSFWQqevnTAAPVTDpamNIRVN-CHV-IPDMWQAEG--ISFFPGLV----MRWf 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 314 ----------LTAQFGDISFDEINKLVDSLPK-------ATSDVF-FLPFLYGSNAGLDMT---SGFygmqalhTRAHLL 372
Cdd:cd07775 309 rdafcaeekeIAERLGIDAYDLLEEMAKDVPPgsygimpIFSDVMnYKNWRHAAPSFLNLDidpEKC-------NKATFF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 373 QAVYEGVVFSHMTHLNRMRErFTEVR--SLRVTGGPAHSPVWMQMLADVSGLPVELPQVEETGCFGAAIAALVGTGVYAN 450
Cdd:cd07775 382 RAIMENAAIVSAGNLERIAE-FSGIFpdSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGAGIYSS 460
|
490 500 510
....*....|....*....|....*....|..
gi 751394705 451 FADAQQTLSYEMRTLMPDMNAHAAYQRKYYRY 482
Cdd:cd07775 461 LEEAVESLVKWEREYLPNPENHEVYQDLYEKW 492
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
8-486 |
4.41e-43 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 159.36 E-value: 4.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 8 WLGIDCGGTYLKAGLYNSQGKEFDIERQSVHTLSPQPGWAERDMAALWQHCATTLSRLLQRTGIRGeqIRGVGISAQGKG 87
Cdd:PRK15027 2 YIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATDRAMKALGDQHSLQD--VKALGIAGQMHG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 88 LFLLDKNDQPLGTAILSSDRRAMEIVKrWQQDGIPQKlYPLTRQTLWTGHPASLLRWVKEHEPQRYAQIGCVMMGHDYLR 167
Cdd:PRK15027 80 ATLLDAQQRVLRPAILWNDGRCAQECA-LLEARVPQS-RVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDKVLLPKDYLR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 168 WCLTGVkgceesnisesnlyhMTSGQYDPCLTQWLGISEID-------------AVLPPIVGSSQISGEITSQAAAITGL 234
Cdd:PRK15027 158 LRMTGE---------------FASDMSDAAGTMWLDVAKRDwsdvmlqachlsrDQMPALYEGSEITGALLPEVAKAWGM 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 235 AAgTPVVGGLFDVVSTALCAGLDDEYTLNAVMGTWAVTSGITEGLRDN---EAHPFVYGRyvnEGQYIVHEASPTSSGNL 311
Cdd:PRK15027 223 AT-VPVVAGGGDNAAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKpesAVHSFCHAL---PQRWHLMSVMLSAASCL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 312 EWLTAQFGdisFDEINKLVDSLPKA---TSDVFFLPFLYGSNAGLDMTSG---FYGMQALHTRAHLLQAVYEGVVFSHMT 385
Cdd:PRK15027 299 DWAAKLTG---LSNVPALIAAAQQAdesAEPVWFLPYLSGERTPHNNPQAkgvFFGLTHQHGPNELARAVLEGVGYALAD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 386 HLNRMRERFTEVRSLRVTGGPAHSPVWMQMLADVSGLPVELPQVEETG-CFGAAIAALVGTGVYANFADAQQTLSYEmRT 464
Cdd:PRK15027 376 GMDVVHACGIKPQSVTLIGGGARSEYWRQMLADISGQQLDYRTGGDVGpALGAARLAQIAANPEKSLIELLPQLPLE-QS 454
|
490 500
....*....|....*....|....*.
gi 751394705 465 LMPDMNAHAAY--QRKYYR--YQILI 486
Cdd:PRK15027 455 HLPDAQRYAAYqpRRETFRrlYQQLL 480
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
9-483 |
6.86e-41 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 154.01 E-value: 6.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 9 LGIDCGGTYLKAGLYNSQGKEFDI-ERQSVHTLSPQ-PGWAERDMAALWQHCATTLSRLLQRTGIRGEQIRGVGISAQGK 86
Cdd:PRK10939 6 MALDAGTGSIRAVIFDLNGNQIAVgQAEWRHLAVPDvPGSMEFDLEKNWQLACQCIRQALQKAGIPASDIAAVSATSMRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 87 GLFLLDKNDQPLgTAILSSDRRAMEIVKRWQQD--GIPQKLYPLTRQTLWTGHPASLLrWVKEHEPQRYAQIGCVMMGHD 164
Cdd:PRK10939 86 GIVLYDRNGTEI-WACANVDARASREVSELKELhnNFEEEVYRCSGQTLALGALPRLL-WLAHHRPDIYRQAHTITMISD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 165 YLRWCLTGVKGCEESNISESNLYHMTSGQYDPCLTQWLGISeiDAVLPPIVGSSQISGEITSQAAAITGLAAGTPVVGGL 244
Cdd:PRK10939 164 WIAYMLSGELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLR--ADILPPVKETGTVLGHVTAKAAAETGLRAGTPVVMGG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 245 FDVVSTALCAGLDDEYTLNAVMGT-WAVTSGITEGLRDNEAHPFVYGRYVNE-GQYivhEASPTSSG-NLEWLTAQFGDI 321
Cdd:PRK10939 242 GDVQLGCLGLGVVRPGQTAVLGGTfWQQVVNLPAPVTDPNMNIRINPHVIPGmVQA---ESISFFTGlTMRWFRDAFCAE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 322 SFDEINKL-VDS---LPKATSDV----------FFLPFLYGS---------NAGLDmtsgfygmQALHTRAHLLQAVYEG 378
Cdd:PRK10939 319 EKLLAERLgIDAyslLEEMASRVpvgshgiipiFSDVMRFKSwyhaapsfiNLSID--------PEKCNKATLFRALEEN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 379 VVFSHMTHLNRMrERFTEVR--SLRVTGGPAHSPVWMQMLADVSGLPVELPQVEETGCFGAAIAALVGTGVYANFADAQQ 456
Cdd:PRK10939 391 AAIVSACNLQQI-AAFSGVFpsSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEATALGCAIAAGVGAGIYSSLAETGE 469
|
490 500
....*....|....*....|....*..
gi 751394705 457 TLSYEMRTLMPDMNAHAAYQRKYYRYQ 483
Cdd:PRK10939 470 RLVRWERTFEPNPENHELYQEAKEKWQ 496
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
9-450 |
5.38e-40 |
|
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: 151.18 E-value: 5.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 9 LGIDCGGTYLKAGLYNSQGKEFDIERQSVHTLSPQPGWAERDMAALWQHCATTLSRLLQRTGIRGEQIRGVGISAQgKGL 88
Cdd:cd07793 3 LAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQ-RNT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 89 FLL-DK-NDQPLGTAILSSDRRAMEIVKRWQQ-------DGIPQKLYPLTRQ---------TLWTGHPASLLRWVKEHEP 150
Cdd:cd07793 82 FLTwDKkTGKPLHNFITWQDLRAAELCESWNRslllkalRGGSKFLHFLTRNkrflaasvlKFSTAHVSIRLLWILQNNP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 151 --QRYAQIGCVMMG--HDYLRWCLTG--VKGCEESNISESNLYHMTSGQYDPCLTQWLGI-SEIdavLPPIVGSS----- 218
Cdd:cd07793 162 elKEAAEKGELLFGtiDTWLLWKLTGgkVHATDYSNASATGLFDPFTLEWSPILLSLFGIpSSI---LPEVKDTSgdfgs 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 219 ---QISGE---ITS----QAAAITG----------LAAGTpvvgGLFDVVST-----ALCAGLddeYTLNAvmgtWAVTS 273
Cdd:cd07793 239 tdpSIFGAeipITAvvadQQAALFGeccfdkgdvkITMGT----GTFIDINTgskphASVKGL---YPLVG----WKIGG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 274 GITeglrdneahpfvygrYVNEGQyiVHeasptSSGN-LEWL--TAQFGDISfdEINKLVDSLPKaTSDVFFLPFLYGSN 350
Cdd:cd07793 308 EIT---------------YLAEGN--AS-----DTGTvIDWAksIGLFDDPS--ETEDIAESVED-TNGVYFVPAFSGLQ 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 351 AGL-DMT--SGFYGMQALHTRAHLLQAVYEGVVF-SHMTHLNRMRERFTEVRSLRVTGGPAHSPVWMQMLADVSGLPVEL 426
Cdd:cd07793 363 APYnDPTacAGFIGLTPSTTKAHLVRAILESIAFrVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVER 442
|
490 500
....*....|....*....|....
gi 751394705 427 PQVEETGCFGAAIAALVGTGVYAN 450
Cdd:cd07793 443 PKNTEMSALGAAFLAGLASGIWKS 466
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
9-487 |
2.12e-38 |
|
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: 146.46 E-value: 2.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 9 LGIDCGGTYLKAGLYNSQGKEFDIERQSVHTLSPQPGWAERDMAALWQHCATTLSRLLQRTGIRGEQIRGVGISAQGKGL 88
Cdd:cd07769 3 LAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQRETT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 89 FLLDKND-QPLGTAILSSDRRAMEIVKRWQQDGipqkLYPLTRQTlwTGHP------ASLLRWVKEHEP--QRYAQIGCV 159
Cdd:cd07769 83 VVWDKKTgKPLYNAIVWQDRRTADICEELKAKG----LEERIREK--TGLPldpyfsATKIKWILDNVPgaRERAERGEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 160 MMGH-D-YLRWCLTGVKG--CEESNISESNLYHMTSGQYDPCLTQWLGISEidAVLPPIVGSSQISGEITSqaaaiTGLA 235
Cdd:cd07769 157 LFGTiDtWLIWKLTGGKVhvTDVTNASRTMLFNIHTLEWDDELLELFGIPR--SMLPEVRPSSEVFGYTDP-----EGLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 236 AGTPVVG--G-----LF--------DVVSTalcaglddeY-TLNAVM---GTWAVTSgiTEGL-------RDNEAHpfvy 289
Cdd:cd07769 230 AGIPIAGilGdqqaaLFgqgcfepgMAKNT---------YgTGCFLLmntGEKPVPS--KNGLlttiawqIGGKVT---- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 290 grYVNEGqyivheaSPTSSGN-LEWLTAQFGDI-SFDEINKLVDSLPKaTSDVFFLPFLYG-------SNA-GLdmtsgF 359
Cdd:cd07769 295 --YALEG-------SIFIAGAaIQWLRDNLGLIeDAAETEELARSVED-NGGVYFVPAFSGlgapywdPDArGA-----I 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 360 YGMQALHTRAHLLQAVYEGVVFSHMTHLNRMRER-FTEVRSLRVTGGPAHSPVWMQMLADVSGLPVELPQVEETGCFGAA 438
Cdd:cd07769 360 VGLTRGTTKAHIVRAALESIAYQTRDVLEAMEKDsGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTALGAA 439
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 751394705 439 IAALVGTGVYANFADAQQTLSYEmRTLMPDMNAHAAyQRKYYRYQILIE 487
Cdd:cd07769 440 YLAGLAVGFWKDLDELASLWQVD-KRFEPSMDEEER-ERLYRGWKKAVE 486
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
5-485 |
3.55e-36 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 140.64 E-value: 3.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 5 ETFWLGIDCGGTYLKAGLYN-SQGKE-----FDIER-QSVHTLSPQPGWAERDMAALWQHCATTLSRLLQRTGIRGEQIR 77
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDaADGEElasavHPYPRwVIGLYLPPPPDQARQHPLDYLEALEAAVREALAQAGVDPADVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 78 GVGISAQGKGLFLLDKNDQPLG-TAILSSDRRAMeiVKRWQqD--GIPQ--KLYPLTRQTlwtGHP-------------- 138
Cdd:COG1069 81 GIGVDATGCTPVPVDADGTPLAlLPEFAENPHAM--VILWK-DhtAQEEaeRINELAKAR---GEDylryvggiissewf 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 139 -ASLLrWVKEHEPQRYAQIGCVMMGHDYLRWCLTGvkgceesNISESN-------LYHMTSGQY---------DPCLtqw 201
Cdd:COG1069 155 wPKIL-HLLREDPEVYEAADSFVELCDWITWQLTG-------SLKRSRctaghkaLWHAHEGGYpseeffaalDPLL--- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 202 lgiSEIDAVLP-PIVGSSQISGEITSQAAAITGLAAGTPVVGGLFDVVSTALCAGLDDEYTLNAVMGT------------ 268
Cdd:COG1069 224 ---DGLADRLGtEIYPLGEPAGTLTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGGVEPGTLVKVMGTstchmlvspeer 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 269 -----W-AVTSGITEGLRDNEAhpfvygryvneGQ--------YIVHEASPtsSGNLEWLTAQFGDISFDEINKLVDSLP 334
Cdd:COG1069 301 fvpgiCgQVDGSIVPGMWGYEA-----------GQsavgdifaWFVRLLVP--PLEYEKEAEERGISLHPLLTEEAAKLP 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 335 KATSDVFFLPFLYGS---NAGLDMTSGFYGMqALHTRA-HLLQAVYEGVVFSHMTHLNRMRERFTEVRSLRVTGG-PAHS 409
Cdd:COG1069 368 PGESGLHALDWFNGNrspLADQRLKGVILGL-TLGTDAeDIYRALVEATAFGTRAIIERFEEEGVPIDEIIACGGiATKN 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 751394705 410 PVWMQMLADVSGLPVELPQVEETGCFGAAIAALVGTGVYANFADAQQTLSYEM-RTLMPDMNAHAAYQRKYYRYQIL 485
Cdd:COG1069 447 PLVMQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEEAMAAMGSGFdKVYTPDPENVAVYDALYAEYLQL 523
|
|
| GlpK |
COG0554 |
Glycerol kinase [Energy production and conversion]; |
9-492 |
6.89e-35 |
|
Glycerol kinase [Energy production and conversion];
Pssm-ID: 440320 [Multi-domain] Cd Length: 496 Bit Score: 136.73 E-value: 6.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 9 LGIDCGGTYLKAGLYNSQGKEFDIERQSVHTLSPQPGWAERDMAALWQHCATTLSRLLQRTGIRGEQIRGVGISAQGKGL 88
Cdd:COG0554 6 LAIDQGTTSTRAILFDRDGNIVAVAQREFTQIYPQPGWVEHDPEEIWESVLAVIREALAKAGISAEDIAAIGITNQRETT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 89 FLLDKND-QPLGTAILSSDRRAMEIVKRWQQDGipqkLYPLTRQTlwTG------HPASLLRWVKEHEP--QRYAQIGCV 159
Cdd:COG0554 86 VVWDRKTgKPLYNAIVWQDRRTADICEELKADG----LEDLIREK--TGlvldpyFSATKIKWILDNVPgaRERAEAGEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 160 MMGH-D-YLRWCLTG--VKGCEESNISESNLYHMTSGQYDPCLTQWLGISEidAVLPPIVGSSQISGEITSqaaaiTGLA 235
Cdd:COG0554 160 LFGTiDsWLIWKLTGgkVHVTDVTNASRTMLFNIHTLDWDDELLELFGIPR--SMLPEVRPSSEVFGETDP-----DLFG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 236 AGTPVVG-------GLF--------DVVSTalcaglddeY-T---LNAVMGTWAVTSgiTEGL-------RDNEAHpfvy 289
Cdd:COG0554 233 AEIPIAGiagdqqaALFgqacfepgMAKNT---------YgTgcfLLMNTGDEPVRS--KNGLlttiawgLGGKVT---- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 290 grYVNEGqyivheaSPTSSGNL-EWLTAQFGDI-SFDEINKLVDSLPkATSDVFFLPFLygsnAGL-----DMTS-G-FY 360
Cdd:COG0554 298 --YALEG-------SIFVAGAAvQWLRDGLGLIdSAAESEALARSVE-DNGGVYFVPAF----TGLgapywDPDArGaIF 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 361 GMQALHTRAHLLQAVYEGVVFShmTH--LNRMRERF-TEVRSLRVTGGPAHSPVWMQMLADVSGLPVELPQVEETGCFGA 437
Cdd:COG0554 364 GLTRGTTRAHIARAALESIAYQ--TRdvLDAMEADSgIPLKELRVDGGASANDLLMQFQADILGVPVERPKVTETTALGA 441
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 751394705 438 AIAALVGTGVYANFADAQQTLSYEmRTLMPDMNAHAAyQRKYYRYQILIEALQGF 492
Cdd:COG0554 442 AYLAGLAVGFWKSLEELAALWKVD-RRFEPQMDEEER-ERLYAGWKKAVERTLGW 494
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
9-487 |
1.14e-33 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 133.18 E-value: 1.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 9 LGIDCGGTYLKAGLYNSQGKEFDiERQSVHT-LSPQPGWAERDMAALWQHCATTLSRLLQRTGIRGEQ--IRGVGISAQG 85
Cdd:PTZ00294 5 GSIDQGTTSTRFIIFDEKGNVVS-SHQIPHEqITPHPGWLEHDPEEILRNVYKCMNEAIKKLREKGPSfkIKAIGITNQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 86 KGLFLLDKN-DQPLGTAILSSDRRAMEIVKRWQQD-GIPQKLYPLTRQTLWTGHPASLLRWVKEHEPQRYAQI--GCVMM 161
Cdd:PTZ00294 84 ETVVAWDKVtGKPLYNAIVWLDTRTYDIVNELTKKyGGSNFFQKITGLPISTYFSAFKIRWMLENVPAVKDAVkeGTLLF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 162 G--HDYLRWCLTGVKG--CEESNISESNLYHMTSGQYDPCLTQWLGISEidAVLPPIVGSSQISGEITSQAaaiTGLAAG 237
Cdd:PTZ00294 164 GtiDTWLIWNLTGGKShvTDVTNASRTFLMNIKTLKWDEELLNKFGIPK--ETLPEIKSSSENFGTISGEA---VPLLEG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 238 TPVVGGLFDVVSTALCAGLDDE------YTLNAVM----GTWAVTSG----ITEGLRDNEAHPFVYGRyvnegqyivhEA 303
Cdd:PTZ00294 239 VPITGCIGDQQAALIGHGCFEKgdakntYGTGCFLlmntGTEIVFSKhgllTTVCYQLGPNGPTVYAL----------EG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 304 SPTSSGN-LEWLTAQFGDIS-FDEINKLVDSLPKaTSDVFFLP-FlygsnAGL-------DMTSGFYGMQALHTRAHLLQ 373
Cdd:PTZ00294 309 SIAVAGAgVEWLRDNMGLIShPSEIEKLARSVKD-TGGVVFVPaF-----SGLfapywrpDARGTIVGMTLKTTRAHIVR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 374 AVYEGVVFSHMTHLNRM-RERFTEVRSLRVTGGPAHSPVWMQMLADVSGLPVELPQVEETGCFGAAIAALVGTGVYANFA 452
Cdd:PTZ00294 383 AALEAIALQTNDVIESMeKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTALGAALLAGLAVGVWKSLE 462
|
490 500 510
....*....|....*....|....*....|....*
gi 751394705 453 DAQQTLSYEMRTLMPDMNAhAAYQRKYYRYQILIE 487
Cdd:PTZ00294 463 EVKKLIRRSNSTFSPQMSA-EERKAIYKEWNKAVE 496
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
9-476 |
2.21e-30 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 123.21 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 9 LGIDCGGTYLKAGLYNSQGKEfdIERQSVHTLSPQ----PGWAERDMAALWQHCATTLSRLLqrTGIRGEQIRGVGISAQ 84
Cdd:PRK10331 5 LVLDCGATNVRAIAVDRQGKI--VARASTPNASDIaaenSDWHQWSLDAILQRFADCCRQIN--SELTECHIRGITVTTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 85 GKGLFLLDKNDQPLGTAILSSDRRAMEIVKRWQQDGIPQKLYPLTR------QTLWTghpaslLRWVKEHEPQRYAQIGC 158
Cdd:PRK10331 81 GVDGALVDKQGNLLYPIISWKCPRTAAVMENIERYISAQQLQQISGvgafsfNTLYK------LVWLKENHPQLLEQAHA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 159 VMMGHDYLRWCLTGVKGCEESNISESNLYHMTSGQYDPCLTQWLGISEidAVLPPIVGSSQISGEITSQAAAITGLAAGT 238
Cdd:PRK10331 155 WLFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSR--RLFPRLVEAGEQIGTLQPSAAALLGLPVGI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 239 PVvgglfdvvstaLCAGLDDEYtlnAVMGTWA------VTSGITEGLRDNEAHPFVYGRYVNEGQYIVHEASP------- 305
Cdd:PRK10331 233 PV-----------ISAGHDTQF---ALFGSGAgqnqpvLSSGTWEILMVRSAQVDTSLLSQYAGSTCELDSQSglynpgm 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 306 --TSSGNLEWLTAQF--GDISFDEINKLVDSLPKATSDVFFLPFLYGSnagldMTSGFYGMQALHTRAHLLQAVYEGVVF 381
Cdd:PRK10331 299 qwLASGVLEWVRKLFwtAETPYQTMIEEARAIPPGADGVKMQCDLLAC-----QNAGWQGVTLNTTRGHFYRAALEGLTA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 382 SHMTHLNRMRE--RFtEVRSLRVTGGPAHSPVWMQMLADVSGLPVELPQVEETGCFGAAIAALVGTGVYANFADAQQTLS 459
Cdd:PRK10331 374 QLKRNLQVLEKigHF-KASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQARAQMK 452
|
490
....*....|....*..
gi 751394705 460 YEMRTLMPDmNAHAAYQ 476
Cdd:PRK10331 453 YQYRYFYPQ-TEPEFIE 468
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
11-482 |
2.88e-30 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466802 [Multi-domain] Cd Length: 499 Bit Score: 123.40 E-value: 2.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 11 IDCGGTYLKAGLYNSQGKEFDIERQSVHTLSPQPGWAERDMAALWQHCATTLS---RLLQRTGIRGEQIRGVGISAQGKG 87
Cdd:cd07792 6 IDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVYECIEeavEKLKALGISPSDIKAIGITNQRET 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 88 LFLLDKN-DQPLGTAILSSDRRAMEIVKRWQQDgipqklYPLTRQTL--WTGHP------ASLLRWVKEHEPQRYAQI-- 156
Cdd:cd07792 86 TVVWDKStGKPLYNAIVWLDTRTSDTVEELSAK------TPGGKDHFrkKTGLPistyfsAVKLRWLLDNVPEVKKAVdd 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 157 GCVMMGH-D-YLRWCLTGVKGCEE-----SNISESNLYHMTSGQYDPCLTQWLGISEidAVLPPIVGSSQISGEITSqaa 229
Cdd:cd07792 160 GRLLFGTvDsWLIWNLTGGKNGGVhvtdvTNASRTMLMNLRTLQWDPELCEFFGIPM--SILPEIRSSSEVYGKIAS--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 230 aitGLAAGTPVVGGLFDVVSTALCAGLDDE------YTLNAVM----GTWAVTSgiTEGL---------RDNEAHpfvyg 290
Cdd:cd07792 235 ---GPLAGVPISGCLGDQQAALVGQGCFKPgeakntYGTGCFLlyntGEEPVFS--KHGLlttvayklgPDAPPV----- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 291 rYVNEGQYIVHEASptssgnLEWLTAQFGDI-SFDEINKLVDSLPKaTSDVFFLP-FlygsnAGL-------DMTSGFYG 361
Cdd:cd07792 305 -YALEGSIAIAGAA------VQWLRDNLGIIsSASEVETLAASVPD-TGGVYFVPaF-----SGLfapywrpDARGTIVG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 362 MQALHTRAHLLQAVYEGVVFSHMTHLNRM-RERFTEVRSLRVTGGPAHSPVWMQMLADVSGLPVELPQVEETGCFGAAIA 440
Cdd:cd07792 372 LTQFTTKAHIARAALEAVCFQTREILDAMnKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSMVETTALGAAIA 451
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 751394705 441 ALVGTGVYANFADAQQTLSYEMRTLMPDMNaHAAYQRKYYRY 482
Cdd:cd07792 452 AGLAVGVWKSLDELKSLNEGGRTVFEPQIS-EEERERRYKRW 492
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
7-441 |
1.72e-28 |
|
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: 117.32 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 7 FWLGIDCGGTYLKAGLYNSQGKEFdIERQSVHTLSPQ----PGWAERDMAALWQHCATTLSRLLQRTGIRgeqIRGVGIS 82
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDLESGRI-LESVSRPTPAPIssddPGRSEQDPEKILEAVRNLIDELPREYLSD---VTGIGIT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 83 AQGKGLFLLDKNDQPLGTAILSSDRRAMEIVKrwqqDGIPQKLYPLTRQT---LWTGHPASLLRWVKEH--EPQRYAQIG 157
Cdd:cd07777 77 GQMHGIVLWDEDGNPVSPLITWQDQRCSEEFL----GGLSTYGEELLPKSgmrLKPGYGLATLFWLLRNgpLPSKADRAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 158 CVMmghDYLRWCLTGvkgCEESNISESN-----LYHMTSGQYDPCLTQWLGISEIdaVLPPIVGSSQISGEITSQaaait 232
Cdd:cd07777 153 TIG---DYIVARLTG---LPKPVMHPTNaaswgLFDLETGTWNKDLLEALGLPVI--LLPEIVPSGEIVGTLSSA----- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 233 gLAAGTPVVGGLFDVVSTALCAGLDDEYTLNAVMGTWAVTSGITEGLRDN---EAHPFVYGRYVNegqyiVheASPTSSG 309
Cdd:cd07777 220 -LPKGIPVYVALGDNQASVLGSGLNEENDAVLNIGTGAQLSFLTPKFELSgsvEIRPFFDGRYLL-----V--AASLPGG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 310 NL---------EWLTAQFGDISFDEINKLVDSL--PKATSDVFFLPFLYGSNAGLDMTSGFYG-MQALHTRAHLLQAVYE 377
Cdd:cd07777 292 RAlavlvdflrEWLRELGGSLSDDEIWEKLDELaeSEESSDLSVDPTFFGERHDPEGRGSITNiGESNFTLGNLFRALCR 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 751394705 378 GVVFSHMTHLNRMRERFTEVRSLRVTGG-PAHSPVWMQMLADVSGLPVELPQVEETGCFGAAIAA 441
Cdd:cd07777 372 GIAENLHEMLPRLDLDLSGIERIVGSGGaLRKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
7-479 |
2.44e-28 |
|
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily includes vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein) and similar proteins, such as Saccharomyces cerevisiae D-ribulokinase YDR109C, Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.
Pssm-ID: 466800 [Multi-domain] Cd Length: 540 Bit Score: 118.02 E-value: 2.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 7 FWLGIDCGGTYLKAGLYNSQGKEFDIERQSVHTLSPQPGWAERDMAALWQHCATTLSRLLQRTGIRGEQIRGVGISAQGK 86
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEGAGVDPEQVKGIGFDATCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 87 gLFLLDKNDQPLGTA---------ILSSDRRAMEIVKRwqqdgipqklypLTRqtlwTGHPA--------SL------LR 143
Cdd:cd07782 81 -LVVLDAEGKPVSVSpsgddernvILWMDHRAVEEAER------------INA----TGHEVlkyvggkiSPemeppkLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 144 WVKEHEPQRYAQIGCVMMGHDYLRWCLTGVK-------GCEESNISESnlyhMTSGQYDPCLTQWLGISEI--------- 207
Cdd:cd07782 144 WLKENLPETWAKAGHFFDLPDFLTWKATGSLtrslcslVCKWTYLAHE----GSEGGWDDDFFKEIGLEDLvednfakig 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 208 DAVLPPivGSSQISGeITSQAAAITGLAAGTPVVGGLFD----------VVSTALCAGLDD-EYTLNAVMGTWAVTSGIT 276
Cdd:cd07782 220 SVVLPP--GEPVGGG-LTAEAAKELGLPEGTPVGVSLIDahagglgtlgADVGGLPCEADPlTRRLALICGTSSCHMAVS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 277 EglrdnEAH--PFVYGRY---------VNEG---------QYIV--HEASPTssgnLEWLTAQFGDISFDEINKLVDSLP 334
Cdd:cd07782 297 P-----EPVfvPGVWGPYysamlpglwLNEGgqsatgallDHIIetHPAYPE----LKEEAKAAGKSIYEYLNERLEQLA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 335 KA--------TSDVFFLPFLYGSNA------------GLDMTSGF------Y--GMQAL--HTRaHLLQAvyegvvfshm 384
Cdd:cd07782 368 EEkglplaylTRDLHVLPDFHGNRSpladptlrgmisGLTLDTSLddlallYlaTLQALayGTR-HIIEA---------- 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 385 thlnrMRERFTEVRSLRVTGGPAHSPVWMQMLADVSGLPVELPQVEETGCFGAAIAALVGTGVYANFADAQQTLSYEMRT 464
Cdd:cd07782 437 -----MNAAGHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWDAMAAMSGPGKV 511
|
570
....*....|....*
gi 751394705 465 LMPDMNAHAAYQRKY 479
Cdd:cd07782 512 VEPNEELKKYHDRKY 526
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
9-483 |
1.29e-27 |
|
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: 115.28 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 9 LGIDCGGTYLKAGLYNSQGKEFDIERQSVHTLSPQPGWAERDMAALWQHCATTLSRLLQRTGIRGEQIRGVGISAQGKGL 88
Cdd:cd07786 3 LAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQRETT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 89 FLLDKND-QPLGTAILSSDRRAMEIVKRWQQDGipqkLYPLTRQTlwTG---HP---ASLLRWVKEHEP--QRYAQIGCV 159
Cdd:cd07786 83 VVWDRETgKPVYNAIVWQDRRTADICEELKAEG----HEEMIREK--TGlvlDPyfsATKIRWILDNVPgaRERAERGEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 160 MMG--HDYLRWCLTG--VKGCEESNISESNLYHMTSGQYDPCLTQWLGISEidAVLPPIVGSSQISGEItsqaaAITGLA 235
Cdd:cd07786 157 AFGtiDSWLIWKLTGgkVHATDVTNASRTMLFNIHTLEWDDELLELFGIPA--SMLPEVKPSSEVFGYT-----DPDLLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 236 AGTPVVG-------GLF--------DVVSTalcaglddeYTLNAVM----GTWAVTSG----ITEGLRDNEAHpfvygRY 292
Cdd:cd07786 230 AEIPIAGiagdqqaALFgqacfepgMAKNT---------YGTGCFMlmntGEKPVRSKngllTTIAWQLGGKV-----TY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 293 VNEGQYIVHEASptssgnLEWLTAQFGDI-SFDEINKLVDSLPKaTSDVFFLPflygsnagldmtsGFYGMQALH----- 366
Cdd:cd07786 296 ALEGSIFIAGAA------VQWLRDGLGLIeSAAETEALARSVPD-NGGVYFVP-------------AFTGLGAPYwdpda 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 367 -----------TRAHLLQAVYEGVVFShmTH--LNRMRER-FTEVRSLRVTGGPAHSPVWMQMLADVSGLPVELPQVEET 432
Cdd:cd07786 356 rgaifgltrgtTRAHIARAALESIAYQ--TRdlLEAMEADsGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVTET 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 751394705 433 GCFGAAIAALVGTGVYANFADAQQTLSYEmRTLMPDMNAHAAyQRKYYRYQ 483
Cdd:cd07786 434 TALGAAYLAGLAVGLWKSLDELAKLWQVD-RRFEPSMSEEER-EALYAGWK 482
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
9-456 |
7.95e-27 |
|
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: 113.01 E-value: 7.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 9 LGIDCGGTYLKAGLYNSQGKEFDIE---RQSvHTLSPQPG---WaerDMAALWQHCATTLSRLLQRtgirGEQIRGVGIS 82
Cdd:cd07771 3 LAVDLGASSGRVILGSLDGGKLELEeihRFP-NRPVEINGhlyW---DIDRLFDEIKEGLKKAAEQ----GGDIDSIGID 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 83 AQGKGLFLLDKNDQPLGTAILSSDRRAMEIVKRWQQDGIPQKLYPLTRQTLWTGHPASLLRWVKEHEPQRYAQIGCVMMG 162
Cdd:cd07771 75 TWGVDFGLLDKNGELLGNPVHYRDPRTEGMMEELFEKISKEELYERTGIQFQPINTLYQLYALKKEGPELLERADKLLML 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 163 HDYLRWCLTGVKGCEESNISESNLYHMTSGQYDPCLTQWLGISeiDAVLPPIVGSSQISGEITSQAAAITGLaAGTPVV- 241
Cdd:cd07771 155 PDLLNYLLTGEKVAEYTIASTTQLLDPRTKDWSEELLEKLGLP--RDLFPPIVPPGTVLGTLKPEVAEELGL-KGIPVIa 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 242 GGLFDVVSTALCAGLDDEYTLNAVMGTWAVTSGITEGLRDNEAhPFVYGrYVNEGQY--------------IVHEAspts 307
Cdd:cd07771 232 VASHDTASAVAAVPAEDEDAAFISSGTWSLIGVELDEPVITEE-AFEAG-FTNEGGAdgtirllknitglwLLQEC---- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 308 sgnLEWLTAQFGDISFDEINKLVDSLPKATS------DVFFLPFlygsnaglDMTS------GFYGMQALHTRAHLLQAV 375
Cdd:cd07771 306 ---RREWEEEGKDYSYDELVALAEEAPPFGAfidpddPRFLNPG--------DMPEairaycRETGQPVPESPGEIARCI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 376 YEGVVFSHMTHLNRMRERF-TEVRSLRVTGGPAHSPVWMQMLADVSGLPVELPQVEETgCFGAAIAALVGTGVYANFADA 454
Cdd:cd07771 375 YESLALKYAKTIEELEELTgKRIDRIHIVGGGSRNALLCQLTADATGLPVIAGPVEAT-AIGNLLVQLIALGEIKSLEEG 453
|
..
gi 751394705 455 QQ 456
Cdd:cd07771 454 RE 455
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
59-489 |
2.64e-24 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 106.08 E-value: 2.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 59 ATTLSRLLQRTGIRGEQIRGVGI----------SAQGKGLFLLDK-NDQPLGTAILSSDRRAMEivkrwQQDGIPQklyp 127
Cdd:PRK04123 63 EAAIPAVLKEAGVDPAAVVGIGVdftgstpapvDADGTPLALLPEfAENPHAMVKLWKDHTAQE-----EAEEINR---- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 128 LTRQtlwtGHPASLLRW----------------VKEHEPQRYAQIGCVMMGHDYLRWCLTGVKGCeeSNISESN------ 185
Cdd:PRK04123 134 LAHE----RGEADLSRYiggiyssewfwakilhVLREDPAVYEAAASWVEACDWVVALLTGTTDP--QDIVRSRcaaghk 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 186 -LYHMTSGQY---------DPCLTQWLgiseiDAVLP-PIVGSSQISGEITSQAAAITGLAAGTPVVGGLFDVVSTALCA 254
Cdd:PRK04123 208 aLWHESWGGLpsadffdalDPLLARGL-----RDKLFtETWTAGEPAGTLTAEWAQRLGLPEGVAVSVGAFDAHMGAVGA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 255 GLDdEYTLNAVMGTWAVTSGITEGLR---------DNEAHPFVYGryVNEGQ--------YIVHEASPTSsgnLEWLTAQ 317
Cdd:PRK04123 283 GAE-PGTLVKVMGTSTCDILLADKQRavpgicgqvDGSIVPGLIG--YEAGQsavgdifaWFARLLVPPE---YKDEAEA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 318 FGDISFDEINKLVDSLPKATSDVFFLPFLYGS---NAGLDMTSGFYGMQaLHTRA-HLLQAVYEGVVFSHMTHLNRMRER 393
Cdd:PRK04123 357 RGKQLLELLTEAAAKQPPGEHGLVALDWFNGRrtpLADQRLKGVITGLT-LGTDApDIYRALIEATAFGTRAIMECFEDQ 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 394 FTEVRSLRVTGG-PAHSPVWMQMLADVSGLPVELPQVEETGCFGAAIAALVGTGVYANFADAQQTL-SYEMRTLMPDMNA 471
Cdd:PRK04123 436 GVPVEEVIAAGGiARKNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDIPEAQQAMaSPVEKTYQPDPEN 515
|
490
....*....|....*...
gi 751394705 472 HAAYQRKYYRYQILIEAL 489
Cdd:PRK04123 516 VARYEQLYQEYKQLHDYF 533
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
42-477 |
2.11e-21 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 97.08 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 42 PQPGWAERDMAALWQHCATTLSRLLQRTGIRGEQIRG----VGISAQGKGLFLLDKND-QPLGTAILSSDRRAMEIVKRW 116
Cdd:PLN02295 36 PQAGWVEHDPMEILESVLTCIAKALEKAAAKGHNVDSglkaIGITNQRETTVAWSKSTgRPLYNAIVWMDSRTSSICRRL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 117 QQD------------GIPQKLYpltrqtlwtgHPASLLRWVKEHEPQRYAQI--GCVMMG--HDYLRWCLTGVKGCEE-- 178
Cdd:PLN02295 116 EKElsggrkhfvetcGLPISTY----------FSATKLLWLLENVDAVKEAVksGDALFGtiDSWLIWNLTGGASGGVhv 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 179 ---SNISESNLYHMTSGQYDPCLTQWLGISEidAVLPPIVGSSQISGEITSqaaaiTGLAAGTPVVGGLFDVVSTAL--- 252
Cdd:PLN02295 186 tdvTNASRTMLMNLKTLDWDKPTLEALGIPA--EILPKIVSNSEVIGTIAK-----GWPLAGVPIAGCLGDQHAAMLgqr 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 253 CAGLDDEYT--------LNAvmGTWAVTSgiTEGLRDNEAH---PFVYGRYVNEGQYIVHEASptssgnLEWLTAQFGDI 321
Cdd:PLN02295 259 CRPGEAKSTygtgcfilLNT--GEEVVPS--KHGLLTTVAYklgPDAPTNYALEGSVAIAGAA------VQWLRDNLGII 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 322 -SFDEINKLVDSLPkATSDVFFLPFLYGSNAGL---DMTSGFYGMQALHTRAHLLQAVYEGVVFSHMTHLNRMRERFTEV 397
Cdd:PLN02295 329 kSASEIEALAATVD-DTGGVYFVPAFSGLFAPRwrdDARGVCVGITRFTNKAHIARAVLESMCFQVKDVLDAMRKDAGEE 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 398 RS------LRVTGGPAHSPVWMQMLADVSGLPVELPQVEETGCFGAAIAALVGTGVYAN---FADAQQTLSyemRTLMPD 468
Cdd:PLN02295 408 KShkglflLRVDGGATANNLLMQIQADLLGSPVVRPADIETTALGAAYAAGLAVGLWTEeeiFASEKWKNT---TTFRPK 484
|
....*....
gi 751394705 469 MNAHAAYQR 477
Cdd:PLN02295 485 LDEEERAKR 493
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
262-444 |
8.97e-21 |
|
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: 90.08 E-value: 8.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 262 LNAVMGTWAVTSGITEglrdnEAHPFVYGRY------VNEGQYIVHEASPTSSGNLEWLTAQFG---DISFDEINKLVDS 332
Cdd:pfam02782 1 LAISAGTSSFVLVETP-----EPVLSVHGVWgpytneMLPGYWGLEGGQSAAGSLLAWLLQFHGlreELRDAGNVESLAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 333 LPKATSD-----VFFLPFLYGSNA-GLD--MTSGFYGMQALHTRAHLLQAVYEGVVFSHMTHLNRMRERF-TEVRSLRVT 403
Cdd:pfam02782 76 LAALAAVapaggLLFYPDFSGNRApGADpgARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQEgHPIDTIHVS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 751394705 404 GGPAHSPVWMQMLADVSGLPVELPQVEETGCFGAAIAALVG 444
Cdd:pfam02782 156 GGGSRNPLLLQLLADALGLPVVVPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
7-481 |
2.30e-20 |
|
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family includes bacterial RBK, vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein), Saccharomyces cerevisiae D-ribulokinase YDR109C, and Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466788 [Multi-domain] Cd Length: 522 Bit Score: 93.84 E-value: 2.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 7 FWLGIDCGGTYLKAGLYN-SQGKEF-DIERQSVHTLSPQPGWAERDMAALWQHCATTLSRLLQRTGIRGEQIRGVGISAQ 84
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDlYAGLEMaQEPVPYYQDSSKKSWKFWQKSTEIIKALQKCVQKLNIREGVDAYEVKGCGVDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 85 GKgLFLLDKNDQPL---------GTAILSSDRRAMEIVKrWQQDGIPQKLYPLTRQTLWTGHPASLLRWVKEHEPQRYAQ 155
Cdd:cd07768 81 CS-LAIFDREGTPLmalipypneDNVIFWMDHSAVNEAQ-WINMQCPQQLLDYLGGKISPEMGVPKLKYFLDEYSHLRDK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 156 IGCVMMGHDYLRWCLTGVkgcEESNISES---NLYHMTSGQYDPCLTQWLGISEIDA----VLPPIVGSSQISGEITSQA 228
Cdd:cd07768 159 HFHIFDLHDYIAYELTRL---YEWNICGLlgkENLDGEESGWSSSFFKNIDPRLEHLtttkNLPSNVPIGTTSGVALPEM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 229 AAITGLAAGTPVVGGLFDV-VSTALCAGLDDEYTLNAVMGTwavTSGITEGLRDNEAHPFVYGRYVN--EGQYIVHEASP 305
Cdd:cd07768 236 AEKMGLHPGTAVVVSCIDAhASWFAVASPHLETSLFMIAGT---SSCHMYGTTISDRIPGVWGPFDTiiDPDYSVYEAGQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 306 TSSGNL-EWL------TAQFGDI---------SFDEINKLVDSLPKATSDVFFLPFLYGSN---AGLDMTSGFYGMQaLH 366
Cdd:cd07768 313 SATGKLiEHLfeshpcARKFDEAlkkgadiyqVLEQTIRQIEKNNGLSIHILTLDMFFGNRsefADPRLKGSFIGES-LD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 367 TRAHLLQAVY----EGVVFSHMTHLNRMRERFTEVRSLRVTGGPAHSPVWMQMLADVSGLPVELPQVEETGCFGAAIAAL 442
Cdd:cd07768 392 TSMLNLTYKYiailEALAFGTRLIIDTFQNEGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMMGILGAAVLAK 471
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 751394705 443 VGTGV---YANFADAQQTLSYEMRTLMPDMNAHAAYQRKYYR 481
Cdd:cd07768 472 VAAGKkqlADSITEADISNDRKSETFEPLAYRLGADYILLYK 513
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
11-441 |
1.00e-18 |
|
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: 88.47 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 11 IDCGGTYLKAGLYNSQGKEFDIERQSVhTLSPQPGWAERDMAALWQHCATTLSRLLQRtgirgEQIRGVGISAQGKGLFL 90
Cdd:cd07772 5 FDIGKTNKKLLLFDENGEVLAERSTPN-PEIEEDGYPCEDVEAIWEWLLDSLAELAKR-----HRIDAINFTTHGATFAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 91 LDKNDQPLgTAILSSDRramEIVKRWQQD------GIPQKLYPLTRQTLwtgHPASLLRWVKEHEPQRYAQIGCVMMGHD 164
Cdd:cd07772 79 LDENGELA-LPVYDYEK---PIPDEINEAyyaergPFEETGSPPLPGGL---NLGKQLYWLKREKPELFARAKTILPLPQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 165 YLRWCLTGVKGCEESNIS-ESNLYHMTSGQYdpclTQWLGISEIDAVLPPIVGSSQISGEITSQAAAITGLAAGTPVVGG 243
Cdd:cd07772 152 YWAWRLTGKAASEITSLGcHTDLWDFEKNEY----SSLVKKEGWDKLFPPLRKAWEVLGPLRPDLARRTGLPKDIPVGCG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 244 LFDvvSTA----LCAGLDDEYTLNAVmGTWAVT--SGITEGLRDNEAHP------FVYGRYVnegqyivheasPTS---S 308
Cdd:cd07772 228 IHD--SNAallpYLAAGKEPFTLLST-GTWCIAmnPGNDLPLTELDLARdclynlDVFGRPV-----------KTArfmG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 309 GN-LEWLTAQFGDiSFDEINKLVDSLPKATSDVFFLPflygsnaGLDMTSGFYGMQALHT----------RAHLLQAVYe 377
Cdd:cd07772 294 GReYERLVERIAK-SFPQLPSLADLAKLLARGTFALP-------SFAPGGGPFPGSGGRGvlsafpsaeeAYALAILYL- 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 751394705 378 gvvfSHMTH--LNRMRErftEVRSLRVTGGPAHSPVWMQMLADV-SGLPVELPQVEETGCFGAAIAA 441
Cdd:cd07772 365 ----ALMTDyaLDLLGS---GVGRIIVEGGFAKNPVFLRLLAALrPDQPVYLSDDSEGTALGAALLA 424
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
2-492 |
9.75e-18 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 85.65 E-value: 9.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 2 SEKETFWLGIDCGGTYLKAGLYNSQGKEFDIErQSVHT-LSPQPGWAERDMAALWQHCATTLSRLLQRTGIRGEQIRGVG 80
Cdd:PRK00047 1 MMMKKYILALDQGTTSSRAIIFDHDGNIVSVA-QKEFTqIFPQPGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 81 ISAQGKGLFLLDKND-QPLGTAILSSDRRAMEIVKRWQQDGIPQKLypltRQTlwTGHP------ASLLRWVKEHEP--Q 151
Cdd:PRK00047 80 ITNQRETTVVWDKETgRPIYNAIVWQDRRTADICEELKRDGYEDYI----REK--TGLVidpyfsGTKIKWILDNVEgaR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 152 RYAQIGCVMMGH-D-YLRWCLTG--VKGCEESNISESNLYHMTSGQYDPCLTQWLGISEidAVLPPIVGSSQISGEITS- 226
Cdd:PRK00047 154 ERAEKGELLFGTiDtWLVWKLTGgkVHVTDYTNASRTMLFNIHTLDWDDELLELLDIPR--SMLPEVRPSSEVYGKTNPy 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 227 ---------------QAAAITGLAA----------GTpvvgGLFDVVSTA-------------LCAGLDDE--YTLNavm 266
Cdd:PRK00047 232 gffggevpiagiagdQQAALFGQLCfepgmakntyGT----GCFMLMNTGekavksengllttIAWGIDGKvvYALE--- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 267 GTWAVTSGITEGLRDneahpfvygryvneGQYIVHEASPTssgnlewltaqfgdisfDEINKLVDSlpkaTSDVFFLP-F 345
Cdd:PRK00047 305 GSIFVAGSAIQWLRD--------------GLKIISDASDS-----------------EALARKVED----NDGVYVVPaF 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 346 lygsnAGL-------DMTSGFYGMQALHTRAHLLQAVYEGVVFSHMTHLNRM-RERFTEVRSLRVTGGPAHSPVWMQMLA 417
Cdd:PRK00047 350 -----TGLgapywdsDARGAIFGLTRGTTKEHIIRATLESIAYQTRDVLDAMqADSGIRLKELRVDGGAVANNFLMQFQA 424
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 751394705 418 DVSGLPVELPQVEETGCFGAAIAALVGTGVYANFADAQQTLSYEmRTLMPDMNAhAAYQRKYYRYQILIEALQGF 492
Cdd:PRK00047 425 DILGVPVERPVVAETTALGAAYLAGLAVGFWKDLDELKEQWKID-RRFEPQMDE-EEREKLYAGWKKAVKRTLAW 497
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
37-205 |
9.67e-10 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 60.50 E-value: 9.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 37 VHTLSPQPGWAERDMAALWQHCATTLSRLLQRtGIRgeqIRGVGISAQGKGLFLLDKNDQPLGTAILSSDRRAMEIVKRW 116
Cdd:PRK10640 21 NNGLHSQDGFDTWDVDSLESAIRLGLNKVCEE-GIR---IDSIGIDTWGVDYVLLDKQGQRVGLPVSYRDSRTDGVMAQA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 117 QQDGIPQKLYP------LTRQTLWTghpaslLRWVKEHEPQRYAQIGCVMMGHDYLRWCLTGVKGCEESNISESNLYHMT 190
Cdd:PRK10640 97 QQQLGKRDIYRrsgiqfLPFNTLYQ------LRALTEQQPELIAQVAHALLIPDYFSYRLTGKMNWEYTNATTTQLVNIN 170
|
170
....*....|....*
gi 751394705 191 SGQYDPCLTQWLGIS 205
Cdd:PRK10640 171 SDDWDESLLAWSGAP 185
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
170-477 |
6.17e-09 |
|
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: 58.34 E-value: 6.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 170 LTG-VKGCEESNISESNLYHMTSGQYDPCLTQWLGISEIDAVLPPIVGSSQISGEITSQAAAITGLAAGTPVVGGLFD-- 246
Cdd:cd07776 196 LLGrYAPIDESDGSGMNLMDIRSRKWSPELLDAATAPDLKEKLGELVPSSTVAGGISSYFVERYGFSPDCLVVAFTGDnp 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 247 --VVSTALCAG-----LDDEYTLNAVMgtwavtsgiTEGLRDNEAHPFVYgrYVNEGQY---IVheaspTSSGNL--EWL 314
Cdd:cd07776 276 asLAGLGLEPGdvavsLGTSDTVFLVL---------DEPKPGPEGHVFAN--PVDPGSYmamLC-----YKNGSLarERV 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 315 TAQFGDISFDEINKLVDSLPKATSDVFFLPFLYG-----SNAGLDMTSGFYGMQALHTRAHLLQAVYEGVVFSHMTHLNR 389
Cdd:cd07776 340 RDRYAGGSWEKFNELLESTPPGNNGNLGLYFDEPeitppVPGGGRRFFGDDGVDAFFDPAVEVRAVVESQFLSMRLHAER 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 390 MRERfTEVRSLRVTGGPAHSPVWMQMLADVSGLPVELPQVEETGCFGAAIAALVGTGVYANFADAQQTLSY--EMRTLM- 466
Cdd:cd07776 420 LGSD-IPPTRILATGGASANKAILQVLADVFGAPVYTLDVANSAALGAALRAAHGLLCAGSGDFSPEFVVFsaEEPKLVa 498
|
330
....*....|..
gi 751394705 467 -PDMNAHAAYQR 477
Cdd:cd07776 499 ePDPEAAEVYDK 510
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
9-85 |
1.64e-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: 49.90 E-value: 1.64e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 751394705 9 LGIDCGGTYLKAGLYNSQGKEfdIERQSVHTLSPQPGwaerdmAALWQHCATTLSRLLQRTGIRGEQIRGVGISAQG 85
Cdd:COG1940 8 IGIDIGGTKIKAALVDLDGEV--LARERIPTPAGAGP------EAVLEAIAELIEELLAEAGISRGRILGIGIGVPG 76
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
9-85 |
6.17e-04 |
|
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family corresponds to a group of proteins including sugar kinases, transcriptional repressors, and yet uncharacterized open reading frames. ROK family sugar kinases phosphorylate a range of structurally distinct hexoses including the key carbon source D-glucose, various glucose epimers, and several acetylated hexosamines. The sugar kinases include N-acetyl-D-glucosamine kinase (NAGK; EC 2.7.1.59), polyphosphate glucokinase (PPGK; EC 2.7.1.63/EC 2.7.1.2), glucokinase (GLK; EC 2.7.1.2), fructokinase (FRK; EC 2.7.1.4), hexokinase (HK; EC 2.7.1.1), D-allose kinase (AlsK; EC 2.7.1.55), bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE; EC 3.2.1.183/EC 2.7.1.60), N-acetylmannosamine kinase (NanK; EC 2.7.1.60), beta-glucoside kinase (BglK; EC 2.7.1.85), and N-acetylglucosamine kinase (EC 2.7.1.59). The family also contains the repressor proteins, such as N-acetylglucosamine repressor (NagC), xylose repressor (XylR), cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and protein Mlc. ROK kinases harbor a conserved N-terminal ATP binding motif of sequence DxGxT, while ROK repressors possess a N-terminal extension that contains a canonical helix-turn-helix DNA binding motif. The ROK family proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466849 [Multi-domain] Cd Length: 239 Bit Score: 41.30 E-value: 6.17e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 751394705 9 LGIDCGGTYLKAGLYNSQGKEfdIERQSVHTLSPQPGwaerdmAALWQHCATTLSRLLQRTGIRgEQIRGVGISAQG 85
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEI--LARERVPTPAEEGP------EAVLDRIAELIEELLAEAGVR-ERILGIGIGVPG 68
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
9-85 |
2.26e-03 |
|
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: 39.85 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 9 LGIDCGGTYLKAGLYNSQGKEfdIERQSVHTLspqpgwaerdmaalwqhCATTLSRLLQRTG------IRGEQIRGVGIS 82
Cdd:cd24068 3 LGIDIGGTKIKYGLVDADGEI--LEKDSVPTP-----------------ASKGGDAILERLLeiiaelKEKYDIEGIGIS 63
|
...
gi 751394705 83 AQG 85
Cdd:cd24068 64 SAG 66
|
|
| ASKHA_NBD_HK |
cd24000 |
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) ... |
3-116 |
3.87e-03 |
|
nucleotide-binding domain (NBD) of the hexokinase (HK) domain family; Hexokinase (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). It can catalyze this reaction on glucose, fructose, sorbitol and glucosamine, and as such is the first step in a number of metabolic pathways. Hexokinase contains two structurally similar domains. Some members of the family have two copies of each of these domains. Hexokinases belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466850 [Multi-domain] Cd Length: 357 Bit Score: 39.57 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 751394705 3 EKETFwLGIDCGGTYLKAGLYNSQGKEFDIERQSVHTLSPQPgwAERDMAALWQHCATTLSRLLQRTGIRgeQIRGVGIS 82
Cdd:cd24000 41 ESGEF-LAIDLGGTNLRVALVSLDGKGIEVTISKKYEIPDEI--KTASAEEFFDFIADCIAEFLKENGLK--KPLPLGFT 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 751394705 83 AQ----------------GKGLFLLDKNDQPLGTAILSSDRRAMEIVKRW 116
Cdd:cd24000 116 FSfpleqtslndgkllswTKGFKIPGVEGKDVGELLNDALKKRGLPVKVV 165
|
|
| |
