|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
1-520 |
0e+00 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 1057.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 1 MSYLLALDAGTGSIRAVIFDLSGHQVAVGQAEWKHLSVENVPGSMEFDLTTNWLLACQCIRQALAAAHLQAADIQSIACC 80
Cdd:PRK10939 2 MSYLMALDAGTGSIRAVIFDLNGNQIAVGQAEWRHLAVPDVPGSMEFDLEKNWQLACQCIRQALQKAGIPASDIAAVSAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 81 SMREGIVLYDRNGEAIWACANVDARASREVSELKEIHDYqFESEVYDVSGQTLALSAMPRLLWLAHHRPDIYRQAATITM 160
Cdd:PRK10939 82 SMREGIVLYDRNGTEIWACANVDARASREVSELKELHNN-FEEEVYRCSGQTLALGALPRLLWLAHHRPDIYRQAHTITM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 161 ISDWLAAKLSGELAVDPSNAGTTGMLDLFSRDWRPALLDMAGLRADLLSPVKETGTPLGAVTDTAAQQCGLRAGTPVIMG 240
Cdd:PRK10939 161 ISDWIAYMLSGELAVDPSNAGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTAKAAAETGLRAGTPVVMG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 241 GGDVQLGCLGLGVVRAGQSAVLGGTFWQQVVNLPEVRTDPQMNIRINPHVIPGMAQAESISFFTGLTMRWFRDAFCAEEK 320
Cdd:PRK10939 241 GGDVQLGCLGLGVVRPGQTAVLGGTFWQQVVNLPAPVTDPNMNIRINPHVIPGMVQAESISFFTGLTMRWFRDAFCAEEK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 321 LVAERLGVDAYALLEEMASRVPAGSHGVMPIFSDAMHFKQWYHAAPSFINLSIDAEKCNKATLFRALEENAAIVSACNLA 400
Cdd:PRK10939 321 LLAERLGIDAYSLLEEMASRVPVGSHGIIPIFSDVMRFKSWYHAAPSFINLSIDPEKCNKATLFRALEENAAIVSACNLQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 401 QISRFSGVTFDSLVFAGGGSKGALWSQILSDVTGLPVRVPAVREATALGCAIAAGTGAGLYSDMASTGEKLVSWHRVFTP 480
Cdd:PRK10939 401 QIAAFSGVFPSSLVFAGGGSKGKLWSQILADVTGLPVKVPVVKEATALGCAIAAGVGAGIYSSLAETGERLVRWERTFEP 480
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 491006182 481 NPAHRELYQGMMEKWQSVYADQLGLVDSGLTTSMWQAPGL 520
Cdd:PRK10939 481 NPENHELYQEAKEKWQAVYADQLGLVDHGLTTSMWKAPGL 520
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
3-495 |
0e+00 |
|
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: 826.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 3 YLLALDAGTGSIRAVIFDLSGHQVAVGQAEWKHLSVENVPGSMEFDLTTNWLLACQCIRQALAAAHLQAADIQSIACCSM 82
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQREWRHKEVPDVPGSMDFDTEKNWKLICECIREALKKAGIAPKSIAAISTTSM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 83 REGIVLYDRNGEAIWACANVDARASREVSELKEIHDYqFESEVYDVSGQTLALSAMPRLLWLAHHRPDIYRQAATITMIS 162
Cdd:cd07775 81 REGIVLYDNEGEEIWACANVDARAAEEVSELKELYNT-LEEEVYRISGQTFALGAIPRLLWLKNNRPEIYRKAAKITMLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 163 DWLAAKLSGELAVDPSNAGTTGMLDLFSRDWRPALLDMAGLRADLLSPVKETGTPLGAVTDTAAQQCGLRAGTPVIMGGG 242
Cdd:cd07775 160 DWIAYKLSGELAVEPSNGSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKEAAEETGLKEGTPVVVGGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 243 DVQLGCLGLGVVRAGQSAVLGGTFWQQVVNLPEVRTDPQMNIRINPHVIPGMAQAESISFFTGLTMRWFRDAFCAEEKLV 322
Cdd:cd07775 240 DVQLGCLGLGVVRPGQTAVLGGSFWQQEVNTAAPVTDPAMNIRVNCHVIPDMWQAEGISFFPGLVMRWFRDAFCAEEKEI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 323 AERLGVDAYALLEEMASRVPAGSHGVMPIFSDAMHFKQWYHAAPSFINLSIDAEKCNKATLFRALEENAAIVSACNLAQI 402
Cdd:cd07775 320 AERLGIDAYDLLEEMAKDVPPGSYGIMPIFSDVMNYKNWRHAAPSFLNLDIDPEKCNKATFFRAIMENAAIVSAGNLERI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 403 SRFSGVTFDSLVFAGGGSKGALWSQILSDVTGLPVRVPAVREATALGCAIAAGTGAGLYSDMASTGEKLVSWHRVFTPNP 482
Cdd:cd07775 400 AEFSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKVPVVKEATALGAAIAAGVGAGIYSSLEEAVESLVKWEREYLPNP 479
|
490
....*....|...
gi 491006182 483 AHRELYQGMMEKW 495
Cdd:cd07775 480 ENHEVYQDLYEKW 492
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
3-459 |
7.45e-129 |
|
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: 383.11 E-value: 7.45e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 3 YLLALDAGTGSIRAVIFDLSGHQVAVGQAEWKHLSVENVPGSMEFDLTTNWLLACQCIRQALAAAHLQAADIQSIACCSM 82
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYPDAKEFDPEELWEKICEAIREALKKAGISPEDISAVSSTSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 83 REGIVLYDRNGEAIWACANVDARASREVSELkeihDYQFESEVYDVSGQ--TLALSAMpRLLWLAHHRPDIYRQAATITM 160
Cdd:cd07798 81 REGIVFLDKDGRELYAGPNIDARGVEEAAEI----DDEFGEEIYTTTGHwpTELFPAA-RLLWFKENRPEIFERIATVLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 161 ISDWLAAKLSGELAVDPSNAGTTGMLDLFSRDWRPALLDMAGLRADLLSPVKETGTPLGAVTDTAAQQCGLRAGTPVIMG 240
Cdd:cd07798 156 ISDWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAARELGLPEGTPVVVG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 241 GGDVQLGCLGLGVVRAGQSAVLGGTFW--QQVVNLPEVrtDPQMNIRINPHVIPGMAQAESISFFTGLTMRWFRDAFCAE 318
Cdd:cd07798 236 GADTQCALLGSGAIEPGDIGIVAGTTTpvQMVTDEPII--DPERRLWTGCHLVPGKWVLESNAGVTGLNYQWLKELLYGD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 319 EKlvaerlgvDAYALLEEMASRVPAGSHGVMPIF-SDAMHfkqwyHAAPSFINLSI------DAEKCNKATLFRALEENA 391
Cdd:cd07798 314 PE--------DSYEVLEEEASEIPPGANGVLAFLgPQIFD-----ARLSGLKNGGFlfptplSASELTRGDFARAILENI 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491006182 392 AIVSACNLAQISRFSGVTFDSLVFAGGGSKGALWSQILSDVTGLPVRVPAVREATALGCAIAAGTGAG 459
Cdd:cd07798 381 AFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLVPEGREASALGAAICAAVGAG 448
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
3-500 |
5.38e-126 |
|
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: 377.25 E-value: 5.38e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 3 YLLALDAGTGSIRAVIFDLSGHQVAVGQAEWKHLSVEnvPGSMEFDLTTNWLLACQCIRQALAAAHLQAADIQSIACCSM 82
Cdd:COG1070 2 YVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPH--PGWAEQDPEDWWEAVVEAIRELLAKAGVDPEEIAAIGVSGQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 83 REGIVLYDRNGEA-----IWAcanvDARASREVSELKEIHDyqfESEVYDVSGQTL-ALSAMPRLLWLAHHRPDIYRQAA 156
Cdd:COG1070 80 MHGLVLLDADGEPlrpaiLWN----DTRAAAEAAELREELG---EEALYEITGNPLhPGFTAPKLLWLKENEPEIFARIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 157 TITMISDWLAAKLSGELAVDPSNAGTTGMLDLFSRDWRPALLDMAGLRADLLSPVKETGTPLGAVTDTAAQQCGLRAGTP 236
Cdd:COG1070 153 KVLLPKDYLRYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPELVPPGEVAGTLTAEAAAETGLPAGTP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 237 VIMGGGDVQLGCLGLGVVRAGQSAVLGGT--FWQQVVnlPEVRTDPQMNIRINPHVIPGMAQAESISFFTGLTMRWFRDA 314
Cdd:COG1070 233 VVAGAGDNAAAALGAGAVEPGDAAVSLGTsgVVFVVS--DKPLPDPEGRVHTFCHAVPGRWLPMGATNNGGSALRWFRDL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 315 FCAEEklvaerlgVDAYALLEEMASRVPAGSHGVM--PIFS-------DAmhfkqwyHAAPSFINLSIDAekcNKATLFR 385
Cdd:COG1070 311 FADGE--------LDDYEELNALAAEVPPGADGLLflPYLSgertphwDP-------NARGAFFGLTLSH---TRAHLAR 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 386 ALEEnaAIvsACNLAQ---ISRFSGVTFDSLVFAGGGSKGALWSQILSDVTGLPVRVPAVREATALGCAIAAGTGAGLYS 462
Cdd:COG1070 373 AVLE--GV--AFALRDgleALEEAGVKIDRIRATGGGARSPLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYD 448
|
490 500 510
....*....|....*....|....*....|....*...
gi 491006182 463 DMASTGEKLVSWHRVFTPNPAHRELYQGMMEKWQSVYA 500
Cdd:COG1070 449 DLEEAAAAMVRVGETIEPDPENVAAYDELYERYRELYP 486
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
3-488 |
1.67e-110 |
|
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: 335.64 E-value: 1.67e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 3 YLLALDAGTGSIRAVIFDLSGHQVAVGQAEWKHLSVEnvPGSMEFDLTTNWLLACQCIRQALAAAHLQAADIQSIACCSM 82
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPE--PGWVEQDPDDWWDALCEALKEAVAKAGVDPEDIAAIGLTSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 83 REGIVLYDRNGEAIwacanvdarasrevselkeihdyqfesevydvsgqtlalsaMPRLLWLahhrpDiyRQAATITMIS 162
Cdd:cd07779 79 RSTFVPVDEDGRPL-----------------------------------------RPAISWQ-----D--KRTAKFLTVQ 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 163 DWLAAKLSGELAVDPSNAGTTGMLDLFSRDWRPALLDMAGLRADLLSPVKETGTPLGAVTDTAAQQCGLRAGTPVIMGGG 242
Cdd:cd07779 111 DYLLYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKLPELVPPGTVIGTLTKEAAEETGLPEGTPVVAGGG 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 243 DVQLGCLGLGVVRAGQSAVLGGTFWQQVVNLPEVRTDPQMNIRINPHVIPGMAQAESISFFTGLTMRWFRDAFCAEEKLV 322
Cdd:cd07779 191 DQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPGKWVLEGSINTGGSAVRWFRDEFGQDEVAE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 323 AErLGVDAYALLEEMASRVPAGSHGVM--PIFSDAMhFKQWYHAAP-SFINLSIDAekcNKATLFRALEENAAIVSACNL 399
Cdd:cd07779 271 KE-LGVSPYELLNEEAAKSPPGSDGLLflPYLAGAG-TPYWNPEARgAFIGLTLSH---TRAHLARAILEGIAFELRDNL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 400 AQISRfSGVTFDSLVFAGGGSKGALWSQILSDVTGLPVRVPAVREATALGCAIAAGTGAGLYSDMASTGEKLVSWHRVFT 479
Cdd:cd07779 346 EAMEK-AGVPIEEIRVSGGGSKSDLWNQIIADVFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKAMVRVTDTFE 424
|
....*....
gi 491006182 480 PNPAHRELY 488
Cdd:cd07779 425 PDPENVAIY 433
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
3-454 |
2.66e-99 |
|
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: 305.26 E-value: 2.66e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 3 YLLALDAGTGSIRAVIFDLSGHQVAVGQAEWKHLSVEnvPGSMEFDLTTNWLLACQCIRQALAAAHLQAADIQSIACCSM 82
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQ--PGWAEQDPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 83 REGIVLYDRNGEAIwacanvdarasrevselkeihdyqfesevydvsgqtlalsaMPRLLWLaHHRpdiyrqaATITMIS 162
Cdd:cd00366 79 MPGVVLVDADGNPL-----------------------------------------RPAIIWL-DRR-------AKFLQPN 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 163 DWLAAKLSGELAVDPSNAGTTGMLDLFSRDWRPALLDMAGLRADLLSPVKETGTPLGAVTDTAAQQCGLRAGTPVIMGGG 242
Cdd:cd00366 110 DYIVFRLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPPIVESGEVVGRVTPEAAEETGLPAGTPVVAGGG 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 243 DVQLGCLGLGVVRAGQSAVLGGTFWQQVVNLPEVRtDPQMNIRINPHVIPGMAQAESISFFTGLTMRWFRDAFCAEEKLV 322
Cdd:cd00366 190 DTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEPV-PPDPRLLNRCHVVPGLWLLEGAINTGGASLRWFRDEFGEEEDSD 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 323 AERLGvdayalLEEMASRVPAGSHGVM--PIFSDAMHFKQWYHAAPSFINLSIDaekCNKATLFRALEENAAIVSACNLA 400
Cdd:cd00366 269 AEYEG------LDELAAEVPPGSDGLIflPYLSGERSPIWDPAARGVFFGLTLS---HTRAHLIRAVLEGVAYALRDNLE 339
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 491006182 401 QISRfSGVTFDSLVFAGGGSKGALWSQILSDVTGLPVRVPAVREATALGCAIAA 454
Cdd:cd00366 340 ILEE-LGVKIKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVAEGAALGAAILA 392
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
3-495 |
2.07e-98 |
|
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: 305.98 E-value: 2.07e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 3 YLLALDAGTGSIRAVIFDLSGHQVAVGQAEWKHLSVEnvPGSMEFDLTTNWLLACQCIRQALAAAHLQAADIQSIACCSM 82
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPK--PGWAEQDPEDWWDAVCRATRALLEKSGIDPSDIAAIAFSGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 83 REGIVLYDRNGEA-----IWAcanvDARASREVSELKEIHDYqfESEVYDVSGQTL-ALSAMPRLLWLAHHRPDIYRQAA 156
Cdd:cd07805 79 MQGVVPVDKDGNPlrnaiIWS----DTRAAEEAEEIAGGLGG--IEGYRLGGGNPPsGKDPLAKILWLKENEPEIYAKTH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 157 TITMISDWLAAKLSGELAVDPSNAGTTGMLDLFSRDWRPALLDMAGLRADLLSPVKETGTPLGAVTDTAAQQCGLRAGTP 236
Cdd:cd07805 153 KFLDAKDYLNFRLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPEAAAELGLPAGTP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 237 VIMGGGDVQLGCLGLGVVRAGQSAV-LGGTFWqQVVNLPEVRTDPQMNIRINPHVIPGM--AQAEsisFFT-GLTMRWFR 312
Cdd:cd07805 233 VVGGGGDAAAAALGAGAVEEGDAHIyLGTSGW-VAAHVPKPKTDPDHGIFTLASADPGRylLAAE---QETaGGALEWAR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 313 DAFCAEEKlvaerLGVDAYALLEEMASRVPAGSHGVM----------PIFSDamhfkqwyHAAPSFINLSIDAekcNKAT 382
Cdd:cd07805 309 DNLGGDED-----LGADDYELLDELAAEAPPGSNGLLflpwlngersPVEDP--------NARGAFIGLSLEH---TRAD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 383 LFRALEENAAIVSACNLAQISRFsGVTFDSLVFAGGGSKGALWSQILSDVTGLPVRVPAV-REATALGCAIAAGTGAGLY 461
Cdd:cd07805 373 LARAVLEGVAFNLRWLLEALEKL-TRKIDELRLVGGGARSDLWCQILADVLGRPVEVPENpQEAGALGAALLAAVGLGLL 451
|
490 500 510
....*....|....*....|....*....|....
gi 491006182 462 SDMASTGeKLVSWHRVFTPNPAHRELYQGMMEKW 495
Cdd:cd07805 452 KSFDEAK-ALVKVEKVFEPDPENRARYDRLYEVF 484
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
3-499 |
4.04e-95 |
|
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: 297.53 E-value: 4.04e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 3 YLLALDAGTGSIRAVIFDLSGHQVAVGQAEWKHLSVEnvPGSMEFDLTTNWLLACQCIRQALAAAHLQAADIQSIACCSM 82
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPK--PGWAEQDPEDWWQATKEALRELLAKAGISPSDIAAIGLTGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 83 REGIVLYDRNGEAI-----WAcanvDARASREVSELKEihdyQFESEVYDVSGQT-LALSAMPRLLWLAHHRPDIYRQAA 156
Cdd:cd07808 79 MHGLVLLDKNGRPLrpailWN----DQRSAAECEELEA----RLGDEILIITGNPpLPGFTLPKLLWLKENEPEIFARIR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 157 TITMISDWLAAKLSGELAVDPSNAGTTGMLDLFSRDWRPALLDMAGLRADLLSPVKETGTPLGAVTDTAAQQCGLRAGTP 236
Cdd:cd07808 151 KILLPKDYLRYRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILPPIVESTEIVGTLTPEAAEELGLPEGTP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 237 VIMGGGDVQLGCLGLGVVRAGQSAVLGGTFWQQVVNLPEVRTDPQMNIRINPHVIPGMAQAESISFFTGLTMRWFRDAFC 316
Cdd:cd07808 231 VVAGAGDNAAAALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGRLHTFPHAVPGKWYAMGVTLSAGLSLRWLRDLFG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 317 AEEklvaerlgvDAYALLEEMASRVPAGSHGVM----------PIFSdamhfkqwYHAAPSFINLSIDaekCNKATLFRA 386
Cdd:cd07808 311 PDR---------ESFDELDAEAAKVPPGSEGLLflpylsgertPYWD--------PNARGSFFGLSLS---HTRAHLARA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 387 LEEnaAIvsACNLAQISRF---SGVTFDSLVFAGGGSKGALWSQILSDVTGLPVRVPAVREATALGCAIAAGTGAGLYSD 463
Cdd:cd07808 371 VLE--GV--AFSLRDSLEVlkeLGIKVKEIRLIGGGAKSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDD 446
|
490 500 510
....*....|....*....|....*....|....*.
gi 491006182 464 MASTGEKLVSWHRVFTPNPAHRELYQGMMEKWQSVY 499
Cdd:cd07808 447 LEEAAAACIKIEKTIEPDPERHEAYDELYARYRELY 482
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
3-459 |
2.91e-90 |
|
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: 283.67 E-value: 2.91e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 3 YLLALDAGTGSIRAVIFDLSGHQVAVGQAEWKHLSVEnvPGSMEFDLTTNWLLACQCIRQALAAAHLQAADIQSIACCSM 82
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPR--PGWAERDMDELWQATAEAIRELLEKSGVDPSDIAGVGVTGH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 83 REGIVLYDRNGEAIW-ACANVDARASREVSELKEIHDYQfesEVYDVSGQTL-ALSAMPRLLWLAHHRPDIYRQAATITM 160
Cdd:cd07802 79 GNGLYLVDKDGKPVRnAILSNDSRAADIVDRWEEDGTLE---KVYPLTGQPLwPGQPVALLRWLKENEPERYDRIRTVLF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 161 ISDWLAAKLSGELAVDPSNAGTtGMLDLFSRDWRPALLDMAGLRA--DLLSPVKETGTPLGAVTDTAAQQCGLRAGTPVI 238
Cdd:cd07802 156 CKDWIRYRLTGEISTDYTDAGS-SLLDLDTGEYDDELLDLLGIEElkDKLPPLVPSTEIAGRVTAEAAALTGLPEGTPVA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 239 MGGGDVQLGCLGLGVVRAGQSAVLGGTFW--QQVVNLPEVRTDPQMNIrinPHVIPGMAQAESISFFTGLTMRWFRDAFC 316
Cdd:cd07802 235 AGAFDVVASALGAGAVDEGQLCVILGTWSinEVVTDEPVVPDSVGSNS---LHADPGLYLIVEASPTSASNLDWFLDTLL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 317 AEEKlvaeRLGVDAYALLEEMASRVPAGSHGVMpifsdamhfkqwYH-----------AAPSFINLSIDAekcNKATLFR 385
Cdd:cd07802 312 GEEK----EAGGSDYDELDELIAAVPPGSSGVI------------FLpylygsganpnARGGFFGLTAWH---TRAHLLR 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491006182 386 ALEENAAIvsaCNLAQISRF-SGVTFDSLVFAGGGSKGALWSQILSDVTGLPVRVPAVREATALGCAIAAGTGAG 459
Cdd:cd07802 373 AVYEGIAF---SHRDHLERLlVARKPETIRLTGGGARSPVWAQIFADVLGLPVEVPDGEELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
3-459 |
4.23e-90 |
|
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: 283.32 E-value: 4.23e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 3 YLLALDAGTGSIRAVIFDLSGHQVAVGQAE--WKHLSvenvPGSMEFDLTTNWLLACQCIRQALAAAHLQaaDIQSIACC 80
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASREtpLIHPG----PGWAELDPEELWEAVKEAIREAAAQAGPD--PIAAISVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 81 SMREGIVLYDRNGEAIWAC-ANVDARASREVSELKEIHDyqfESEVYDVSGQTLalSAM---PRLLWLAHHRPDIYRQAA 156
Cdd:cd07773 75 SQGESGVPVDRDGEPLGPAiVWFDPRGKEEAEELAERIG---AEELYRITGLPP--SPMyslAKLLWLREHEPEIFAKAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 157 TITMISDWLAAKLSGELAVDPSNAGTTGMLDLFSRDWRPALLDMAGLRADLLSPVKETGTPLGAVTDTAAQQCGLRAGTP 236
Cdd:cd07773 150 KWLSVADYIAYRLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLLPELVPSGTVIGTVTPEAAEELGLPAGTP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 237 VIMGGGDVQLGCLGLGVVRAGQSAVLGGTFWQQVVNLPEVRTDPQMNIRIN---PHVIPGMAQAeSISFFTGLTMRWFRD 313
Cdd:cd07773 230 VVVGGHDHLCAALGAGVIEPGDVLDSTGTAEALLAVVDEPPLDEMLAEGGLsygHHVPGGYYYL-AGSLPGGALLEWFRD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 314 AFCAEEklvaerlgvDAYALLEEMASRVPAGSHGVMPIFSDAMHFKQWY--HAAPSFINLSIDaekCNKATLFRALEENA 391
Cdd:cd07773 309 LFGGDE---------SDLAAADELAEAAPPGPTGLLFLPHLSGSGTPDFdpDARGAFLGLTLG---TTRADLLRAILEGL 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491006182 392 AIVSACNLAQISRFsGVTFDSLVFAGGGSKGALWSQILSDVTGLPVRVPAVREATALGCAIAAGTGAG 459
Cdd:cd07773 377 AFELRLNLEALEKA-GIPIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVPEATALGAALLAGVGAG 443
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
3-459 |
8.45e-86 |
|
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: 272.48 E-value: 8.45e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 3 YLLALDAGTGSIRAVIFDLSGHQVAVGQAEwkHLSVENVPGSMEFDLTTNWLLACQCIRQALAAAHLQAADIQSIACCSM 82
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIE--HDLLTPKPGWAEHDPEVWWGAVCEIIRELLAKAGISPKEIAAIGVSGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 83 REGIVLYDRNGEA-----IWAcanvDARASREVSELKEIHDyqfESEVYDVSGQTLAL-SAMPRLLWLAHHRPDIYRQAA 156
Cdd:cd07804 79 VPALVPVDENGKPlrpaiLYG----DRRATEEIEWLNENIG---EDRIFEITGNPLDSqSVGPKLLWIKRNEPEVFKKTR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 157 TITMISDWLAAKLSGELAVDPSNAG-TTGMLDLFSRDWRPALLDMAGLRADLLSPVKETGTPLGAVTDTAAQQCGLRAGT 235
Cdd:cd07804 152 KFLGAYDYIVYKLTGEYVIDYSSAGnEGGLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTKEAAEETGLAEGT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 236 PVIMGGGDVQLGCLGLGVVRAGQSAV-LGGT-FWQQVvnLPEVRTDPQMniRINPHVIPGMAQAESISFFTGLTMRWFRD 313
Cdd:cd07804 232 PVVAGTVDAAASALSAGVVEPGDLLLmLGTAgDIGVV--TDKLPTDPRL--WLDYHDIPGTYVLNGGMATSGSLLRWFRD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 314 AFCAEEKLVAERLGVDAYALLEEMASRVPAGSHG--VMPIFS-------DAmhfkqwyHAAPSFINLSIDAekcNKATLF 384
Cdd:cd07804 308 EFAGEEVEAEKSGGDSAYDLLDEEAEKIPPGSDGliVLPYFMgertpiwDP-------DARGVIFGLTLSH---TRAHLY 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491006182 385 RALEENAAIVSACNLAQISRfSGVTFDSLVFAGGGSKGALWSQILSDVTGLPVRVPAVREATALGCAIAAGTGAG 459
Cdd:cd07804 378 RALLEGVAYGLRHHLEVIRE-AGLPIKRLVAVGGGAKSPLWRQIVADVTGVPQEYVKDTVGASLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
3-499 |
2.37e-81 |
|
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: 261.72 E-value: 2.37e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 3 YLLALDAGTGSIRAVIFDLSGHQVAVGQAEWKHLSVEnvPGSMEFDLTTNWLLACQCIRQALAAAHLQaaDIQSIACCSM 82
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPE--PGWAEQDPEEILEAVLEALKEVLAKLGGG--EVDAIGFSSA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 83 REGIVLYDRNGEA-----IWAcanvDARASREVSELKEIHDyqfESEVYDVSGQTL-ALSAMPRLLWLAHHRPDIYRQAA 156
Cdd:cd07770 77 MHSLLGVDEDGEPltpviTWA----DTRAAEEAERLRKEGD---GSELYRRTGCPIhPMYPLAKLLWLKEERPELFAKAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 157 TITMISDWLAAKLSGELAVDPSNAGTTGMLDLFSRDWRPALLDMAGLRADLLSPVKETGTPLGAVTDTAAQQCGLRAGTP 236
Cdd:cd07770 150 KFVSIKEYLLYRLTGELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQLPELVDPTEVLPGLKPEFAERLGLLAGTP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 237 VIMGGGDvqlGCL---GLGVVRAGQSAVLGGTfwqqvVNLPEVRTDPQMNI---RINP-HVIPGMAQAESisfftGLTMR 309
Cdd:cd07770 230 VVLGASD---GALanlGSGALDPGRAALTVGTsgairVVSDRPVLDPPGRLwcyRLDEnRWLVGGAINNG-----GNVLD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 310 WFRDAFCaeeklvaerLGVDAYALLEEMASRVPAGSHGVM----------PIFSDamhfkqwyHAAPSFINLSIDAekcN 379
Cdd:cd07770 302 WLRDTLL---------LSGDDYEELDKLAEAVPPGSHGLIflpylageraPGWNP--------DARGAFFGLTLNH---T 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 380 KATLFRALEEnaAIvsACNLAQIS---RFSGVTFDSLVFAGGGSKGALWSQILSDVTGLPVRVPAVREATALGCAIAAGT 456
Cdd:cd07770 362 RADILRAVLE--GV--AFNLKSIYealEELAGPVKEIRASGGFLRSPLWLQILADVLGRPVLVPEEEEASALGAALLALE 437
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 491006182 457 GAGLYSDMAStgEKLVSWHRVFTPNPAHRELYQGMMEKWQSVY 499
Cdd:cd07770 438 ALGLISSLEA--DELVKIGKVVEPDPENHAIYAELYERFKKLY 478
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
3-504 |
1.35e-67 |
|
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: 226.26 E-value: 1.35e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 3 YLLALDAGTGSIRAVIFDL-SGHQVAVGQAEWKHLSVENVPGSMEFDlTTNWLLA-CQCIRQALAAAHLQAADIQSIA-- 78
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDLaDGEELASAVVPYPTGYIPPRPGWAEQN-PADYWEAlEEAVRGALAEAGVDPEDVVGIGvd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 79 --CCSMregiVLYDRNGEAIwacANV----DARASREVSELKEI-HDYQFESEVY---DVSGQTLalsaMPRLLWLAHHR 148
Cdd:cd07781 80 ttSSTV----VPVDEDGNPL---APAilwmDHRAQEEAAEINETaHPALEYYLAYyggVYSSEWM----WPKALWLKRNA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 149 PDIYRQAATITMISDWLAAKLSGELAVDPSNAGTTGMLD----LFSRDWRPAL-LDMAGLRADLLSPVKETGTPLGAVTD 223
Cdd:cd07781 149 PEVYDAAYTIVEACDWINARLTGRWVRSRCAAGHKWMYNewggGPPREFLAALdPGLLKLREKLPGEVVPVGEPAGTLTA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 224 TAAQQCGLRAGTPVIMGGGDVQLGCLGLGVVRAGQSAVLGGTFWQQVVNLPEVRTDPQMNiriNPH---VIPGMAQAES- 299
Cdd:cd07781 229 EAAERLGLPAGIPVAQGGIDAHMGAIGAGVVEPGTLALIMGTSTCHLMVSPKPVDIPGIC---GPVpdaVVPGLYGLEAg 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 300 -ISffTGLTMRWFRDAFCAEeklvAERLGVDAYALLEEMASRVPAGSHGVM---------PIFSDAmhfkqwyHAAPSFI 369
Cdd:cd07781 306 qSA--VGDIFAWFVRLFVPP----AEERGDSIYALLSEEAAKLPPGESGLValdwfngnrTPLVDP-------RLRGAIV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 370 NLSIDAEkcnKATLFRALEENAAIVSACNLAQISRfSGVTFDSLVFAGGGS-KGALWSQILSDVTGLPVRVPAVREATAL 448
Cdd:cd07781 373 GLTLGTT---PAHIYRALLEATAFGTRAIIERFEE-AGVPVNRVVACGGIAeKNPLWMQIYADVLGRPIKVPKSDQAPAL 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 491006182 449 GCAIAAGTGAGLYSDMASTGEKLVSWHRVFTPNPAHRELYQGMMEKWQSVYaDQLG 504
Cdd:cd07781 449 GAAILAAVAAGVYADIEEAADAMVRVDRVYEPDPENHAVYEELYALYKELY-DALG 503
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
3-459 |
2.28e-61 |
|
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: 208.17 E-value: 2.28e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 3 YLLALDAGTGSIRAVIFDLSGHQV-AVGQAEWKHLSVEnvPGSMEFDLTTNWLLACQCIRQALAAAHLQAADIQSIACCS 81
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDAETGRVvASGSAPHENILID--PGWAEQDPEDWWDALQAAFAQLLKDAGAELRDVAAIGISG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 82 MREGIVLYDRNGEAI-----WaCanvDARASREVSELKEIHDYQFESEVYDVSGQtlALSAmPRLLWLAHHRPDIYRQAA 156
Cdd:cd07809 79 QMHGLVALDADGKVLrpaklW-C---DTRTAPEAEELTEALGGKKCLLVGLNIPA--RFTA-SKLLWLKENEPEHYARIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 157 TITMISDWLAAKLSGELAVDPSNAGTTGMLDLFSRDWRPALL---DMAGLRADLLSPVKETGTPLGAVTDTAAQQCGLRA 233
Cdd:cd07809 152 KILLPHDYLNWKLTGEKVTGLGDASGTFPIDPRTRDYDAELLaaiDPSRDLRDLLPEVLPAGEVAGRLTPEGAEELGLPA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 234 GTPVIMGGGDVQLGCLGLGVVRAGQSAVLGGTfwQQVVN--LPEVRTDPQMniRINP--HVIPGMAQAESisfFTGLTMR 309
Cdd:cd07809 232 GIPVAPGEGDNMTGALGTGVVNPGTVAVSLGT--SGTAYgvSDKPVSDPHG--RVATfcDSTGGMLPLIN---TTNCLTA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 310 WFrdafcaeeKLVAERLGVDaYALLEEMASRVPAGSHGVMPI-FSDAMHFKQWYHAAPSFINLsiDAEKCNKATLFRALE 388
Cdd:cd07809 305 WT--------ELFRELLGVS-YEELDELAAQAPPGAGGLLLLpFLNGERTPNLPHGRASLVGL--TLSNFTRANLARAAL 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491006182 389 ENAaivsACNLA---QISRFSGVTFDSLVFAGGGSKGALWSQILSDVTGLPVRVPAVREATALGCAIAAGTGAG 459
Cdd:cd07809 374 EGA----TFGLRyglDILRELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVVPETGEGGALGAALQAAWGAG 443
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
3-459 |
2.53e-61 |
|
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: 208.25 E-value: 2.53e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 3 YLLALDAGTGSIRAVIFDLSGHQVAVGQAEWKHLSVEnvPGSMEFDLTTNWLLACQCIRQALAAAHLQAADIQSIACCSM 82
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQ--PGWAEQDMNETWQAVVATIREVVAKLDVLPDRVAAIGVTGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 83 REGIVLYDRNGE-----AIWAcanvDARASREVSELKEihDYQFESeVYDVSGQTLALSAM-PRLLWLAHHRPDIYRQAA 156
Cdd:cd24121 79 GDGTWLVDEDGRpvrdaILWL----DGRAADIVERWQA--DGIAEA-VFEITGTGLFPGSQaAQLAWLKENEPERLERAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 157 TITMISDWLAAKLSGELAVDPSNAGTTgMLDLFSRDWRPALLDMAGL--RADLLSPVKETGTPLGAVTDTAAQQCGLRAG 234
Cdd:cd24121 152 TALHCKDWLFYKLTGEIATDPSDASLT-FLDFRTRQYDDEVLDLLGLeeLRHLLPPIRPGTEVIGPLTPEAAAATGLPAG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 235 TPVIMGGGDVQLGCLGLGVVRAGQ-SAVLGGTFWQQVVnLPEVRTDPQMNIRINPHVIPG--------MAQAESIsfftg 305
Cdd:cd24121 231 TPVVLGPFDVVATALGSGAIEPGDaCSILGTTGVHEVV-VDEPDLEPEGVGYTICLGVPGrwlramanMAGTPNL----- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 306 ltmRWFRDAFCAEEKLVAERLGVDAYALLEEMASRVPAGSHGVM--PIFSD----AMHFKQwyHAAPSFINLSIDaekCN 379
Cdd:cd24121 305 ---DWFLRELGEVLKEGAEPAGSDLFQDLEELAASSPPGAEGVLyhPYLSPagerAPFVNP--NARAQFTGLSLE---HT 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 380 KATLFRALEENAAIVSACNLAQISRFSGvtfdSLVFAGGGSKGALWSQILSDVTGLPVRVPAVREATALGCAIAAGTGAG 459
Cdd:cd24121 377 RADLLRAVYEGVALAMRDCYEHMGEDPG----ELRLSGGGARSDTWCQILADALGVPVRVPAGEEFGARGAAMNAAVALG 452
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
3-458 |
1.07e-55 |
|
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: 192.82 E-value: 1.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 3 YLLALDAGTGSIRAVIFDLSGHQVAVGQAEWKHLSveNVPGSMEFDLTTNWLLACQCIRQALAAAHLQaaDIQSIACCSM 82
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSR--PGPGWVEQDPEDWWEALRSLLRELPAELRPR--RVVAIAVDGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 83 REGIVLYDRNGEAIwacANV----DARASREVSELKEIHDYQFESEVYDVSGQtlalSAMPRLLWLAHHRPDIYRQAATI 158
Cdd:cd07783 77 SGTLVLVDREGEPL---RPAimynDARAVAEAEELAEAAGAVAPRTGLAVSPS----SSLAKLLWLKRHEPEVLAKTAKF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 159 TMISDWLAAKLSGELAV-DPSNAGTTGmLDLFSRDWRPALLDMAGLRADLLSPVKETGTPLGAVTDTAAQQCGLRAGTPV 237
Cdd:cd07783 150 LHQADWLAGRLTGDRGVtDYNNALKLG-YDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAEAAEELGLPAGTPV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 238 IMGGGDVQLGCLGLGVVRAGQ-SAVLGGTFwqqVVNL--PEVRTDPQMNIRINPHV----IPGMAqaesiSFFTGLTMRW 310
Cdd:cd07783 229 VAGTTDSIAAFLASGAVRPGDaVTSLGTTL---VLKLlsDKRVPDPGGGVYSHRHGdgywLVGGA-----SNTGGAVLRW 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 311 FrdAFCAEEKLVAERL------GVDAYALLeEMASRVPagshgvmpiFSDAmhfkqwyHAAPSFINLSIDAEKcnkatLF 384
Cdd:cd07783 301 F--FSDDELAELSAQAdppgpsGLIYYPLP-LRGERFP---------FWDP-------DARGFLLPRPHDRAE-----FL 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491006182 385 RALEENAAIVSACNLAQISRFSGVTFDSLVFAGGGSKGALWSQILSDVTGLPVRVPAvREATALGCAIAAGTGA 458
Cdd:cd07783 357 RALLEGIAFIERLGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAE-EEEAALGAALLAAAGL 429
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
1-491 |
1.35e-50 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 180.22 E-value: 1.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 1 MSYLLALDAGTGSIRAVIFDLSGHQVAVG-QAEWKHLSVENvPGSMEFDLTTNWLLACQCIRQALAAAHLQaaDIQSIAC 79
Cdd:PRK10331 1 QDVILVLDCGATNVRAIAVDRQGKIVARAsTPNASDIAAEN-SDWHQWSLDAILQRFADCCRQINSELTEC--HIRGITV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 80 CSMREGIVLYDRNGEAI-----WACAnvdarasREVSELKEIHDYQFESEVYDVSG-QTLALSAMPRLLWLAHHRPDIYR 153
Cdd:PRK10331 78 TTFGVDGALVDKQGNLLypiisWKCP-------RTAAVMENIERYISAQQLQQISGvGAFSFNTLYKLVWLKENHPQLLE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 154 QAATITMISDWLAAKLSGELAVDPSNAGTTGMLDLFSRDWRPALLDMAGLRADLLSPVKETGTPLGAVTDTAAQQCGLRA 233
Cdd:PRK10331 151 QAHAWLFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGLSRRLFPRLVEAGEQIGTLQPSAAALLGLPV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 234 GTPVIMGGGDVQLGCLGLGvvrAGQS-AVLGGTFWQQVVnlpeVRTdPQMNIRINPHVIPGMAQAESIS--FFTGL---- 306
Cdd:PRK10331 231 GIPVISAGHDTQFALFGSG---AGQNqPVLSSGTWEILM----VRS-AQVDTSLLSQYAGSTCELDSQSglYNPGMqwla 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 307 --TMRWFRDAFCAEEklvaerlgvDAYALLEEMASRVPAGSHGV--MPIFSDAMHfkqwyhaaPSFINLSIDAekcNKAT 382
Cdd:PRK10331 303 sgVLEWVRKLFWTAE---------TPYQTMIEEARAIPPGADGVkmQCDLLACQN--------AGWQGVTLNT---TRGH 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 383 LFRALEENAAIVSACNLAQISRFSGVTFDSLVFAGGGSKGALWSQILSDVTGLPVRVPAVREATALGCAIAAGTGAGLYS 462
Cdd:PRK10331 363 FYRAALEGLTAQLKRNLQVLEKIGHFKASELLLVGGGSRNALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFS 442
|
490 500
....*....|....*....|....*....
gi 491006182 463 DMASTGEKLVSWHRVFTPNpAHRELYQGM 491
Cdd:PRK10331 443 SPEQARAQMKYQYRYFYPQ-TEPEFIEEV 470
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
3-250 |
1.87e-45 |
|
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: 159.81 E-value: 1.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 3 YLLALDAGTGSIRAVIFDLSGHQVAVGQAEWKHLSVEnvPGSMEFDLttNWLLAC--QCIRQALAAAHLQAADIQSIACC 80
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPH--PGWAEQDP--DEIWQAvaQCIAKTLSQLGISLKQIKGIGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 81 SMREGIVLYDRNGE----AI-WACAnvdaRASREVSELKEIHDYQFeseVYDVSGQTL-ALSAMPRLLWLAHHRPDIYRQ 154
Cdd:pfam00370 77 NQGHGTVLLDKNDKplynAIlWKDR----RTAEIVENLKEEGNNQK---LYEITGLPIwPGFTLSKLRWIKENEPEVFEK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 155 AATITMISDWLAAKLSGELAVDPSNAGTTGMLDLFSRDWRPALLDMAGLRADLLSPVKETGTPLGAVTDTAAQQCGLRAG 234
Cdd:pfam00370 150 IHKFLTIHDYLRWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMWGLDEG 229
|
250
....*....|....*.
gi 491006182 235 TPVIMGGGDVQLGCLG 250
Cdd:pfam00370 230 VPVVGGGGDQQAAAFG 245
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
1-502 |
3.89e-38 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 146.80 E-value: 3.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 1 MSYLLALDAGTGSIRAVIFDLS-GHQVAVGQAEWKHLsvenVPGsMEFDLTTNWLL---------ACQCIRQALAAAHLQ 70
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDAAdGEELASAVHPYPRW----VIG-LYLPPPPDQARqhpldyleaLEAAVREALAQAGVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 71 AADIQSIA----CCSMregiVLYDRNGEAI-----WAC---ANV----DARASREVSELKEI-----HDY-QFE-----S 123
Cdd:COG1069 76 PADVVGIGvdatGCTP----VPVDADGTPLallpeFAEnphAMVilwkDHTAQEEAERINELakargEDYlRYVggiisS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 124 EVYdvsgqtlalsaMPRLLWLAHHRPDIYRQAATITMISDWLAAKLSGELAvdpSNAGTTGMLDLFSRDWR--P------ 195
Cdd:COG1069 152 EWF-----------WPKILHLLREDPEVYEAADSFVELCDWITWQLTGSLK---RSRCTAGHKALWHAHEGgyPseeffa 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 196 AL-LDMAGLRADLLSPVKETGTPLGAVTDTAAQQCGLRAGTPVIMGGGDVQLGCLGLGVVRAGQSAVLGGTFWQQVVNLP 274
Cdd:COG1069 218 ALdPLLDGLADRLGTEIYPLGEPAGTLTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGGVEPGTLVKVMGTSTCHMLVSP 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 275 EVRTDPQMNIRINPHVIPGM-----AQaesiSFFtGLTMRWFRDAFCAEEKLV--AERLGVDAYALLEEMASRVPAGSHG 347
Cdd:COG1069 298 EERFVPGICGQVDGSIVPGMwgyeaGQ----SAV-GDIFAWFVRLLVPPLEYEkeAEERGISLHPLLTEEAAKLPPGESG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 348 --VMP-------IFSDAmHFKqwyhAAPSFINLSIDAEKcnkatLFRALEEnaAIvsACNLAQI-SRF--SGVTFDSLVF 415
Cdd:COG1069 373 lhALDwfngnrsPLADQ-RLK----GVILGLTLGTDAED-----IYRALVE--AT--AFGTRAIiERFeeEGVPIDEIIA 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 416 AGGGS-KGALWSQILSDVTGLPVRVPAVREATALGCAIAAGTGAGLYSDMASTGEKLVS-WHRVFTPNPAHRELYQGMME 493
Cdd:COG1069 439 CGGIAtKNPLVMQIYADVTGRPIKVAASEQACALGAAMFAAVAAGAYPDVEEAMAAMGSgFDKVYTPDPENVAVYDALYA 518
|
....*....
gi 491006182 494 KWQSVYADQ 502
Cdd:COG1069 519 EYLQLHDYF 527
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
3-496 |
5.73e-33 |
|
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: 131.43 E-value: 5.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 3 YLLALDAGTGSIRAVIFDLSGHQVAVGQAEwkHLSVENVPGSMEFDLTTNWLLACQCIRQALAAAHLQAADIQSIACCSM 82
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKE--HEQIYPQPGWVEHDPEEIWENTLEVIREALAKAGISASDIAAIGITNQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 83 REGIVLYDRN-GEAIwacANV----DARASREVSELKEihdYQFESEVYDVSGqtLALSAM---PRLLWLAHHRPDIyRQ 154
Cdd:cd07769 79 RETTVVWDKKtGKPL---YNAivwqDRRTADICEELKA---KGLEERIREKTG--LPLDPYfsaTKIKWILDNVPGA-RE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 155 AA--------TItmisD-WLAAKLSG--ELAVDPSNAGTTGMLDLFSRDWRPALLDMAGLRADLLSPVKETGTPLGAVTD 223
Cdd:cd07769 150 RAergellfgTI----DtWLIWKLTGgkVHVTDVTNASRTMLFNIHTLEWDDELLELFGIPRSMLPEVRPSSEVFGYTDP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 224 taaqqCGLRAGTPV--IMggGDVQLGCLGLGVVRAGQSAVLGGT--FWqqVVNLPEVRTDPQMNI------RINPHVIPG 293
Cdd:cd07769 226 -----EGLGAGIPIagIL--GDQQAALFGQGCFEPGMAKNTYGTgcFL--LMNTGEKPVPSKNGLlttiawQIGGKVTYA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 294 MaqaESISFFTGLTMRWFRDafcaeeklvaeRLG-VDAYALLEEMASRVPaGSHGVM--PIFSD--AMHFKQwyHAAPSF 368
Cdd:cd07769 297 L---EGSIFIAGAAIQWLRD-----------NLGlIEDAAETEELARSVE-DNGGVYfvPAFSGlgAPYWDP--DARGAI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 369 INLSIDAekcNKATLFRALEENAAIVSACNLAQISRFSGVTFDSLVFAGGGSKGALWSQILSDVTGLPVRVPAVREATAL 448
Cdd:cd07769 360 VGLTRGT---TKAHIVRAALESIAYQTRDVLEAMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPVVRPKVAETTAL 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 491006182 449 GCAIAAGTGAGLYSDMASTGEKLVSWhRVFTPN--PAHRE-LYQGmmekWQ 496
Cdd:cd07769 437 GAAYLAGLAVGFWKDLDELASLWQVD-KRFEPSmdEEERErLYRG----WK 482
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
3-454 |
5.66e-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: 116.17 E-value: 5.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 3 YLLALDAGTGSIRAVIFDL-SGHQVAVGQAEWKHLSVENVPGSMEFDLTTNWLLACQCIRQALAAAHLqaaDIQSIA-CC 80
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDLeSGRILESVSRPTPAPISSDDPGRSEQDPEKILEAVRNLIDELPREYLS---DVTGIGiTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 81 SMrEGIVLYDRNGEAI-----WAcanvDARASREvsELKEIHDYQFESEvyDVSGQTLALS-AMPRLLWLAHHRPDIYRq 154
Cdd:cd07777 78 QM-HGIVLWDEDGNPVsplitWQ----DQRCSEE--FLGGLSTYGEELL--PKSGMRLKPGyGLATLFWLLRNGPLPSK- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 155 AATITMISDWLAAKLSG--ELAVDPSNAGTTGMLDLFSRDWRPALLDMAGLRADLLSPVKETGTPLGAVTdtaaqqCGLR 232
Cdd:cd07777 148 ADRAGTIGDYIVARLTGlpKPVMHPTNAASWGLFDLETGTWNKDLLEALGLPVILLPEIVPSGEIVGTLS------SALP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 233 AGTPVIMGGGDVQLGCLGLGVVRAGqSAVLG-GTFWQQVVNLPEVRTDPQMNIRinP-------HVIPGMAQAESISFFT 304
Cdd:cd07777 222 KGIPVYVALGDNQASVLGSGLNEEN-DAVLNiGTGAQLSFLTPKFELSGSVEIR--PffdgrylLVAASLPGGRALAVLV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 305 GLTMRWFRDAFCAEEKlvaerlgVDAYALLEEMASRVPAGSHGVMP-IFSDAMHFKQwyHAAPSFI---NLSIDAekcnk 380
Cdd:cd07777 299 DFLREWLRELGGSLSD-------DEIWEKLDELAESEESSDLSVDPtFFGERHDPEG--RGSITNIgesNFTLGN----- 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491006182 381 atLFRALEENaaIVSA-CNLAQISRFSGVTFDSLVFAGGGS-KGALWSQILSDVTGLPVRVPAVREATALGCAIAA 454
Cdd:cd07777 365 --LFRALCRG--IAENlHEMLPRLDLDLSGIERIVGSGGALrKNPVLRRIIEKRFGLPVVLSEGSEEAAVGAALLA 436
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
3-496 |
7.92e-28 |
|
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: 116.51 E-value: 7.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 3 YLLALDAGTGSIRAVIFDLSGHqvAVGQAEWKHLSVENVPGSMEFDLTTNWLLACQCIRQALAAAHLQAADIQSIACCSM 82
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGK--IIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKNAGLTPEDIAAIGISTQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 83 REGIVLYDR-NGEAI-----WAcanvDARASREVSE------LKEIHdyQFESEVYDVSGQTLALSAM----------PR 140
Cdd:cd07793 79 RNTFLTWDKkTGKPLhnfitWQ----DLRAAELCESwnrsllLKALR--GGSKFLHFLTRNKRFLAASvlkfstahvsIR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 141 LLWLAHHRPDIYRQAATITM----ISDWLAAKLSG--ELAVDPSNAGTTGMLDLFSRDWRPALLDMAGLRADLLSPVKET 214
Cdd:cd07793 153 LLWILQNNPELKEAAEKGELlfgtIDTWLLWKLTGgkVHATDYSNASATGLFDPFTLEWSPILLSLFGIPSSILPEVKDT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 215 GTPLGaVTDtaaqqcglragtPVIMGG--------GDVQLGCLGLGVVRAGQSAV-LG-GTFWqqvvnlpevrtdpQMNI 284
Cdd:cd07793 233 SGDFG-STD------------PSIFGAeipitavvADQQAALFGECCFDKGDVKItMGtGTFI-------------DINT 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 285 RINPHV-IPGMAQ-------------AESISFFTGLTMRWFRDAfcaeeklvaerLGVDAYALLEEMASRVPAgSHGV-- 348
Cdd:cd07793 287 GSKPHAsVKGLYPlvgwkiggeitylAEGNASDTGTVIDWAKSI-----------GLFDDPSETEDIAESVED-TNGVyf 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 349 MPIFSD--AMHFKqwYHAAPSFINLSIDAekcNKATLFRALEENAAIVSACNLAQISRFSGVTFDSLVFAGGGSKGALWS 426
Cdd:cd07793 355 VPAFSGlqAPYND--PTACAGFIGLTPST---TKAHLVRAILESIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFIL 429
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 427 QILSDVTGLPVRVPAVREATALGCAIAAGTGAGLYSDMAStGEKLVSWHRVFTPNPAhRELYQGMMEKWQ 496
Cdd:cd07793 430 QLIADLLGKPVERPKNTEMSALGAAFLAGLASGIWKSKEE-LKKLRKIEKIFEPKMD-NEKREELYKNWK 497
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
1-496 |
3.54e-26 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 111.60 E-value: 3.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 1 MSYLLALDAGTGSIRAVIFDLSGHQVAVGQAEwkHLSVENVPGSMEFDLTTNWLLACQCIRQAL--AAAHLQAADIQSIA 78
Cdd:PTZ00294 1 MKYIGSIDQGTTSTRFIIFDEKGNVVSSHQIP--HEQITPHPGWLEHDPEEILRNVYKCMNEAIkkLREKGPSFKIKAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 79 CCSMREGIVLYDRN-GE----AI-WacanVDARASREVSELKEihDYQFESEVYDVSGQTLA--LSAMpRLLWLAHHRP- 149
Cdd:PTZ00294 79 ITNQRETVVAWDKVtGKplynAIvW----LDTRTYDIVNELTK--KYGGSNFFQKITGLPIStyFSAF-KIRWMLENVPa 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 150 ---DIYRQAATITMISDWLAAKLSGELA--VDPSNAGTTGMLDLFSRDWRPALLDMAGLRADLLSPVKETGTPLGAVTdt 224
Cdd:PTZ00294 152 vkdAVKEGTLLFGTIDTWLIWNLTGGKShvTDVTNASRTFLMNIKTLKWDEELLNKFGIPKETLPEIKSSSENFGTIS-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 225 aAQQCGLRAGTPvIMGG-GDVQLGCLGLGVVRAGQSAVLGGTFWQQVVNlpeVRTDPQMN---------IRINPHVIPGM 294
Cdd:PTZ00294 230 -GEAVPLLEGVP-ITGCiGDQQAALIGHGCFEKGDAKNTYGTGCFLLMN---TGTEIVFSkhgllttvcYQLGPNGPTVY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 295 AQAESISfFTGLTMRWFRDafcaeeklvaeRLG-VDAYALLEEMASRVPaGSHGV--MPIFSdAMHFKQW-YHAAPSFIN 370
Cdd:PTZ00294 305 ALEGSIA-VAGAGVEWLRD-----------NMGlISHPSEIEKLARSVK-DTGGVvfVPAFS-GLFAPYWrPDARGTIVG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 371 LSIdaeKCNKATLFRALEEnaAIVSACN--LAQISRFSGVTFDSLVFAGGGSKGALWSQILSDVTGLPVRVPAVREATAL 448
Cdd:PTZ00294 371 MTL---KTTRAHIVRAALE--AIALQTNdvIESMEKDAGIELNSLRVDGGLTKNKLLMQFQADILGKDIVVPEMAETTAL 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 491006182 449 GCAIAAGTGAGLYSDMASTGEKLVSWHRVFTPNPAHRElYQGMMEKWQ 496
Cdd:PTZ00294 446 GAALLAGLAVGVWKSLEEVKKLIRRSNSTFSPQMSAEE-RKAIYKEWN 492
|
|
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
3-473 |
6.16e-26 |
|
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: 110.70 E-value: 6.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 3 YLLALDAGTGSIRAVIFDLSGhqvavgqaewKHLSVENVpgsMEFD---------LTTNWLLACQCIRQALAAAHLQAAD 73
Cdd:cd07771 1 NYLAVDLGASSGRVILGSLDG----------GKLELEEI---HRFPnrpveinghLYWDIDRLFDEIKEGLKKAAEQGGD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 74 IQSIACCSMreGI--VLYDRNGEAIwacANV----DARASREVSELKEIHDyqfESEVYDVSG-QTLALSAMPRLLWLAH 146
Cdd:cd07771 68 IDSIGIDTW--GVdfGLLDKNGELL---GNPvhyrDPRTEGMMEELFEKIS---KEELYERTGiQFQPINTLYQLYALKK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 147 HRPDIYRQAATITMISDWLAAKLSGELAVDPSNAGTTGMLDLFSRDWRPALLDMAGLRADLLSPVKETGTPLGAVTDTAA 226
Cdd:cd07771 140 EGPELLERADKLLMLPDLLNYLLTGEKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLKPEVA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 227 QQCGLrAGTPVIMGGG-DVqlgclglgvvragQSAVLG-------------GTfWQQV-VNLPE-VRTDPQMNIRI-NPH 289
Cdd:cd07771 220 EELGL-KGIPVIAVAShDT-------------ASAVAAvpaededaafissGT-WSLIgVELDEpVITEEAFEAGFtNEG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 290 VIPGmaqaeSISFFTGLTMRWFRDAfCAEEklVAERLGVDAYALLEEMASRVPAGSHgvmPIFSDamhfkqwyhaAPSFI 369
Cdd:cd07771 285 GADG-----TIRLLKNITGLWLLQE-CRRE--WEEEGKDYSYDELVALAEEAPPFGA---FIDPD----------DPRFL 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 370 NLS--IDA--EKC---------NKATLFRALEENAAIVSACNLAQISRFSGVTFDSLVFAGGGSKGALWSQILSDVTGLP 436
Cdd:cd07771 344 NPGdmPEAirAYCretgqpvpeSPGEIARCIYESLALKYAKTIEELEELTGKRIDRIHIVGGGSRNALLCQLTADATGLP 423
|
490 500 510
....*....|....*....|....*....|....*...
gi 491006182 437 VRV-PAvrEATALGCAIAAGTGAGLYSDMAStGEKLVS 473
Cdd:cd07771 424 VIAgPV--EATAIGNLLVQLIALGEIKSLEE-GRELVR 458
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
3-482 |
1.67e-25 |
|
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: 110.02 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 3 YLLALDAGTGSIRAVIFDLS-GHQVAVGQAEWKHLSVenvPGSMEFDL--TTNWLLACQCIRQALAAAHLQAADIQSI-- 77
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDLYaGLEMAQEPVPYYQDSS---KKSWKFWQksTEIIKALQKCVQKLNIREGVDAYEVKGCgv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 78 -ACCSM----REG---IVLYDRNGEAiWACANVDARASREVSELKEIHDYQFESEVydvSGQTLALSAMPRLLWLAHHRP 149
Cdd:cd07768 78 dATCSLaifdREGtplMALIPYPNED-NVIFWMDHSAVNEAQWINMQCPQQLLDYL---GGKISPEMGVPKLKYFLDEYS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 150 DIYRQAATITMISDWLAAKLSGELAVDPSNAGTTGMLDLFSRDWRPALLDMAGLR------ADLLSPVKETGTPLGAVTD 223
Cdd:cd07768 154 HLRDKHFHIFDLHDYIAYELTRLYEWNICGLLGKENLDGEESGWSSSFFKNIDPRlehlttTKNLPSNVPIGTTSGVALP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 224 TAAQQCGLRAGTPVIMGGGDVQLGCLGLGVVRA-GQSAVLGGTFWQQVVNLPEVRTDPQMNIRINPHVIPGMAQAESISF 302
Cdd:cd07768 234 EMAEKMGLHPGTAVVVSCIDAHASWFAVASPHLeTSLFMIAGTSSCHMYGTTISDRIPGVWGPFDTIIDPDYSVYEAGQS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 303 FTGLTMRWF-RDAFCAEEKLVAERLGVDAYALLEEMASRVPAGshgvmPIFSDAMHFKQWYH------AAP----SFINL 371
Cdd:cd07768 314 ATGKLIEHLfESHPCARKFDEALKKGADIYQVLEQTIRQIEKN-----NGLSIHILTLDMFFgnrsefADPrlkgSFIGE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 372 SIDAEKCNKATLFRALEENAA-----IVSACNLaqisrfSGVTFDSLVFAGGGSKGALWSQILSDVTGLPVRVPAVREAT 446
Cdd:cd07768 389 SLDTSMLNLTYKYIAILEALAfgtrlIIDTFQN------EGIHIKELRASGGQAKNERLLQLIALVTNVAIIKPKENMMG 462
|
490 500 510
....*....|....*....|....*....|....*....
gi 491006182 447 ALGCAIAAGTGAGLYSDMASTGEKLVSWHRV---FTPNP 482
Cdd:cd07768 463 ILGAAVLAKVAAGKKQLADSITEADISNDRKsetFEPLA 501
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
3-489 |
7.60e-25 |
|
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: 108.01 E-value: 7.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 3 YLLALDAGTGSIRAVIFDLSGHQVAVGQAE---WKHL------SVENVpgsmefdlttnWLLACQCIRQALAAAHLQAAD 73
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPittWNPKpdfyeqSSEDI-----------WQAVCEAVKEVLEGAGVDPEQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 74 IQSI---ACCSMregiVLYDRNGEAI--------------WAcanvDARASREVSELKEIHdyqfeSEVYDVSGQTLALS 136
Cdd:cd07782 70 VKGIgfdATCSL----VVLDAEGKPVsvspsgddernvilWM----DHRAVEEAERINATG-----HEVLKYVGGKISPE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 137 -AMPRLLWLAHHRPDIYRQAATITMISDWLAAKLSGELA-----------VDPSNAGTTGmldlfsrdWRPALLDMAGLr 204
Cdd:cd07782 137 mEPPKLLWLKENLPETWAKAGHFFDLPDFLTWKATGSLTrslcslvckwtYLAHEGSEGG--------WDDDFFKEIGL- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 205 ADLL--------SPVKETGTPLG-AVTDTAAQQCGLRAGTPVIMG------GGdvqLGCLGLGVVRAGQS--------AV 261
Cdd:cd07782 208 EDLVednfakigSVVLPPGEPVGgGLTAEAAKELGLPEGTPVGVSlidahaGG---LGTLGADVGGLPCEadpltrrlAL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 262 LGGTfwqqvvnlpevrTDPQMNIRINPHVIPGMaqaesisfftgltmrW--FRDA-----FCAE------EKLV------ 322
Cdd:cd07782 285 ICGT------------SSCHMAVSPEPVFVPGV---------------WgpYYSAmlpglWLNEggqsatGALLdhiiet 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 323 ----------AERLGVDAYALLEEMASRVPAGSHGVMPIFSDAMHFKQWYH------AAPSF----INLSIDAEKCNKAT 382
Cdd:cd07782 338 hpaypelkeeAKAAGKSIYEYLNERLEQLAEEKGLPLAYLTRDLHVLPDFHgnrsplADPTLrgmiSGLTLDTSLDDLAL 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 383 LFRALEENAA-----IVSACNLAqisrfsGVTFDSLVFAGGGSKGALWSQILSDVTGLPVRVPAVREATALGCAIAAGTG 457
Cdd:cd07782 418 LYLATLQALAygtrhIIEAMNAA------GHKIDTIFMCGGLSKNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVA 491
|
570 580 590
....*....|....*....|....*....|..
gi 491006182 458 AGLYSDMASTGEKLVSWHRVFTPNPAHRELYQ 489
Cdd:cd07782 492 SGDFPSLWDAMAAMSGPGKVVEPNEELKKYHD 523
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
3-496 |
4.92e-24 |
|
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: 105.27 E-value: 4.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 3 YLLALDAGTGSIRAVIFDLSGHQVAVGQAEWKHLSVEnvPGSMEFDLTTNWLLACQCIRQALAAAHLQAADIQSIACCSM 82
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPK--PGWVEHDPEEIWESQLAVAREALAKAGIRASDIAAIGITNQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 83 REGIVLYDRN-GEAI-----WAcanvDARASREVSELKEIhdyQFESEVYDVSGqtLAL----SAmPRLLWLAHHRPDIY 152
Cdd:cd07786 79 RETTVVWDREtGKPVynaivWQ----DRRTADICEELKAE---GHEEMIREKTG--LVLdpyfSA-TKIRWILDNVPGAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 153 RQAA-------TItmisD-WLAAKLSGEL--AVDPSNAGTTGMLDLFSRDWRPALLDMAGLRADLLSPVKETGTPLGaVT 222
Cdd:cd07786 149 ERAErgelafgTI----DsWLIWKLTGGKvhATDVTNASRTMLFNIHTLEWDDELLELFGIPASMLPEVKPSSEVFG-YT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 223 DTAaqqcGLRAGTPvIMG-GGDVQL-----GCLGLGVVRA--GQSAVLggtfwqqVVNLPEVRTDPQMN------IRINP 288
Cdd:cd07786 224 DPD----LLGAEIP-IAGiAGDQQAalfgqACFEPGMAKNtyGTGCFM-------LMNTGEKPVRSKNGllttiaWQLGG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 289 HVipGMAQAESIsFFTGLTMRWFRDafcaeeklvaeRLG-VDAYALLEEMASRVPaGSHGVM--PIFSD--AMHFKQwyH 363
Cdd:cd07786 292 KV--TYALEGSI-FIAGAAVQWLRD-----------GLGlIESAAETEALARSVP-DNGGVYfvPAFTGlgAPYWDP--D 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 364 AAPSFINLSIDAekcNKATLFRALEENAAIVSACNLAQISRFSGVTFDSLVFAGGGSKGALWSQILSDVTGLPVRVPAVR 443
Cdd:cd07786 355 ARGAIFGLTRGT---TRAHIARAALESIAYQTRDLLEAMEADSGIPLKELRVDGGASANDFLMQFQADILGVPVERPKVT 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 491006182 444 EATALGCAIAAGTGAGLYSDMASTgEKLVSWHRVFTPN--PAHRE-LYQGmmekWQ 496
Cdd:cd07786 432 ETTALGAAYLAGLAVGLWKSLDEL-AKLWQVDRRFEPSmsEEEREaLYAG----WK 482
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
139-435 |
7.99e-23 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 101.58 E-value: 7.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 139 PRLLWLAHHRPDIYRQAATITMISDWLAAKLSGELAVDPSNAGTTGMLDLFSRDWRPALLDMAGLRADLLSPVKETGTPL 218
Cdd:PRK15027 130 PKLLWVQRHEPEIFRQIDKVLLPKDYLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEIT 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 219 GAVTDTAAQQCGLRAgTPVIMGGGDVQLGCLGLGVVRAGQSAVLGGTFWQQVVNLPEVRTDPQMNIRINPHVIPGMAQAE 298
Cdd:PRK15027 210 GALLPEVAKAWGMAT-VPVVAGGGDNAAGAVGVGMVDANQAMLSLGTSGVYFAVSEGFLSKPESAVHSFCHALPQRWHLM 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 299 SISFFTGLTMRWfrdafcaeeklVAERLGVDAYALLEEMASRV--PAGSHGVMPIFSDAMHFKQWYHAAPSFINLSidaE 376
Cdd:PRK15027 289 SVMLSAASCLDW-----------AAKLTGLSNVPALIAAAQQAdeSAEPVWFLPYLSGERTPHNNPQAKGVFFGLT---H 354
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491006182 377 KCNKATLFRALEENAA--------IVSACnlaqisrfsGVTFDSLVFAGGGSKGALWSQILSDVTGL 435
Cdd:PRK15027 355 QHGPNELARAVLEGVGyaladgmdVVHAC---------GIKPQSVTLIGGGARSEYWRQMLADISGQ 412
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
3-495 |
8.51e-23 |
|
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: 101.45 E-value: 8.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 3 YLLALDAGTGSIRAVIFDLSGHQVAVGQAEWKHLSVEnvPGSMEFD----LTTnwllACQCIRQALAAAHLQAADIQSIA 78
Cdd:cd07792 2 LVGAIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPK--PGWVEHDpmeiLES----VYECIEEAVEKLKALGISPSDIK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 79 C---CSMREGIVLYDRN-GE----AI-WacanVDARASREVSELKEIHDyQFESEVYDVSGQTLA--LSAMpRLLWLAHH 147
Cdd:cd07792 76 AigiTNQRETTVVWDKStGKplynAIvW----LDTRTSDTVEELSAKTP-GGKDHFRKKTGLPIStyFSAV-KLRWLLDN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 148 RPDIyRQAAT-----ITMISDWLAAKLSGEL-----AVDPSNAGTTGMLDLFSRDWRPALLDMAGLRADLLSPVKETGTP 217
Cdd:cd07792 150 VPEV-KKAVDdgrllFGTVDSWLIWNLTGGKnggvhVTDVTNASRTMLMNLRTLQWDPELCEFFGIPMSILPEIRSSSEV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 218 LGAVTDTAAqqcglrAGTPvIMGG-GDVQLGCLGLGVVRAGQSAVLGGT--FWqqVVNlpeVRTDPQMN---------IR 285
Cdd:cd07792 229 YGKIASGPL------AGVP-ISGClGDQQAALVGQGCFKPGEAKNTYGTgcFL--LYN---TGEEPVFSkhgllttvaYK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 286 INPHVIPGMAQAESISfFTGLTMRWFRDafcaeeklvaeRLG-VDAYALLEEMASRVPaGSHGV--MPIFSD--AMHFKQ 360
Cdd:cd07792 297 LGPDAPPVYALEGSIA-IAGAAVQWLRD-----------NLGiISSASEVETLAASVP-DTGGVyfVPAFSGlfAPYWRP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 361 wyHAAPSFINLSidaEKCNKATLFRALEENAAIVSACNLAQISRFSGVTFDSLVFAGGGSKGALWSQILSDVTGLPVRVP 440
Cdd:cd07792 364 --DARGTIVGLT---QFTTKAHIARAALEAVCFQTREILDAMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERP 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 491006182 441 AVREATALGCAIAAGTGAGLYSDMASTGEKLVSWHRVFTPN--PAHRELyqgMMEKW 495
Cdd:cd07792 439 SMVETTALGAAIAAGLAVGVWKSLDELKSLNEGGRTVFEPQisEEERER---RYKRW 492
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
1-504 |
2.61e-22 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 100.31 E-value: 2.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 1 MSYLLALDAGTGSIRAVIFDLS-GHQVAVGQAEWKHLSVENVPgsmefDLTTNWLLAC---------QCIRQALAAAHLQ 70
Cdd:PRK04123 2 MAYVIGLDFGTDSVRALLVDCAtGEELATAVVEYPHWVKGRYL-----DLPPNQALQHpldyiesleAAIPAVLKEAGVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 71 AADIQSIAC----CSM----REGIVLYDRNGEA--------IWAcanvDARASREVSELKEI-HDYQFE----------- 122
Cdd:PRK04123 77 PAAVVGIGVdftgSTPapvdADGTPLALLPEFAenphamvkLWK----DHTAQEEAEEINRLaHERGEAdlsryiggiys 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 123 SEVYdvsgqtlalsaMPRLLWLAHHRPDIYRQAATITMISDWLAAKLSGElaVDPS----NAGTTGMLDLFSRDW----- 193
Cdd:PRK04123 153 SEWF-----------WAKILHVLREDPAVYEAAASWVEACDWVVALLTGT--TDPQdivrSRCAAGHKALWHESWgglps 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 194 -------RPALLDmaGLRADLLSPVKETGTPLGAVTDTAAQQCGLRAGTPVIMGGGDVQLGCLGLGVvRAGQ-SAVLGgT 265
Cdd:PRK04123 220 adffdalDPLLAR--GLRDKLFTETWTAGEPAGTLTAEWAQRLGLPEGVAVSVGAFDAHMGAVGAGA-EPGTlVKVMG-T 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 266 FWQQVVNLPEVRTDPQMNIRINPHVIPGMAQAESISFFTGLTMRWFRD-AFCAEEKLVAERLGVDAYALLEEMASRVPAG 344
Cdd:PRK04123 296 STCDILLADKQRAVPGICGQVDGSIVPGLIGYEAGQSAVGDIFAWFARlLVPPEYKDEAEARGKQLLELLTEAAAKQPPG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 345 SHGVM---------PIFSDAmHFKqwyhAAPSFINLSIDAEkcnkaTLFRALEENAA-----IvsacnlaqISRF--SGV 408
Cdd:PRK04123 376 EHGLValdwfngrrTPLADQ-RLK----GVITGLTLGTDAP-----DIYRALIEATAfgtraI--------MECFedQGV 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 409 TFDSLVFAGG-GSKGALWSQILSDVTGLPVRVPAVREATALGCAIAAGTGAGLYSDMASTGEKLVSWH-RVFTPNPAHRE 486
Cdd:PRK04123 438 PVEEVIAAGGiARKNPVLMQIYADVLNRPIQVVASDQCPALGAAIFAAVAAGAYPDIPEAQQAMASPVeKTYQPDPENVA 517
|
570
....*....|....*...
gi 491006182 487 LYQGMMEKWQSVYaDQLG 504
Cdd:PRK04123 518 RYEQLYQEYKQLH-DYFG 534
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
3-486 |
1.29e-19 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 91.68 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 3 YLLALDAGTGSIRAVIFDLSGHQVAVGQAEWKHLSVEnvPGSMEFDLTTNWLLACQCIRQALAAAHLQAADIQS----IA 78
Cdd:PLN02295 1 FVGAIDQGTTSTRFIIYDRDARPVASHQVEFTQIYPQ--AGWVEHDPMEILESVLTCIAKALEKAAAKGHNVDSglkaIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 79 CCSMREGIVLYDRN-GEAIW-ACANVDARASREVSELkeihdyqfESEVYDVSGQTLALSAMP--------RLLWLAHH- 147
Cdd:PLN02295 79 ITNQRETTVAWSKStGRPLYnAIVWMDSRTSSICRRL--------EKELSGGRKHFVETCGLPistyfsatKLLWLLENv 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 148 ---RPDIYRQAATITMISDWLAAKLSGELA-----VDPSNAGTTGMLDLFSRDWRPALLDMAGLRADLLSPVKETGTPLG 219
Cdd:PLN02295 151 davKEAVKSGDALFGTIDSWLIWNLTGGASggvhvTDVTNASRTMLMNLKTLDWDKPTLEALGIPAEILPKIVSNSEVIG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 220 AVTDTaaqqcGLRAGTPVIMGGGDVQLGCLGLGVvRAGQSAVLGGTFWQQVVNLPEVRTDPQ------MNIRINPHVIPG 293
Cdd:PLN02295 231 TIAKG-----WPLAGVPIAGCLGDQHAAMLGQRC-RPGEAKSTYGTGCFILLNTGEEVVPSKhgllttVAYKLGPDAPTN 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 294 MAQAESISFfTGLTMRWFRDafcaeeklvaeRLGV-DAYALLEEMASRVPAgSHGV--MPIFSDAmhFKQWYHAapsfin 370
Cdd:PLN02295 305 YALEGSVAI-AGAAVQWLRD-----------NLGIiKSASEIEALAATVDD-TGGVyfVPAFSGL--FAPRWRD------ 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 371 lsiDAEKC--------NKATLFRALEENAA-----IVSACNLAQISRFSGVTFDSLVFAGGGSKGALWSQILSDVTGLPV 437
Cdd:PLN02295 364 ---DARGVcvgitrftNKAHIARAVLESMCfqvkdVLDAMRKDAGEEKSHKGLFLLRVDGGATANNLLMQIQADLLGSPV 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 491006182 438 RVPAVREATALGCAIAAGTGAGLYSDMASTGEKLVSWHRVFTP--NPAHRE 486
Cdd:PLN02295 441 VRPADIETTALGAAYAAGLAVGLWTEEEIFASEKWKNTTTFRPklDEEERA 491
|
|
| ASKHA_NBD_FGGY_SpXK-like |
cd07776 |
nucleotide-binding domain (NBD) of Homo sapiens xylulose kinase (XK) and similar proteins; XK ... |
144-494 |
3.78e-17 |
|
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: 84.15 E-value: 3.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 144 LAHHRPDIYRQAATITMISDWLAAKLSGELA-VDPSNAGTTGMLDLFSRDWRPALLDMA---GLRaDLLSPVKETGTPLG 219
Cdd:cd07776 171 IAQTDPEAYENTERISLVSSFLASLLLGRYApIDESDGSGMNLMDIRSRKWSPELLDAAtapDLK-EKLGELVPSSTVAG 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 220 AVTDTAAQQCGLRAGTPVIMGGGDVQLGCLGLGVvRAGQSAVLGGT----FwqqvVNLPEVRTDPQMNIRINPhVIPGma 295
Cdd:cd07776 250 GISSYFVERYGFSPDCLVVAFTGDNPASLAGLGL-EPGDVAVSLGTsdtvF----LVLDEPKPGPEGHVFANP-VDPG-- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 296 qaesiSFFT-------GLTMRWFRDAFCAEEklvaerlgvdaYALLEEMASRVPAGSHGVMPIFSD-------AMHFKQW 361
Cdd:cd07776 322 -----SYMAmlcykngSLARERVRDRYAGGS-----------WEKFNELLESTPPGNNGNLGLYFDepeitppVPGGGRR 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 362 YHAAPSFINLSIDAEKCnkatlfRALEENAAIVSACNLAQISrfSGVTFDSLVFAGGGS--KGALwsQILSDVTGLPVRV 439
Cdd:cd07776 386 FFGDDGVDAFFDPAVEV------RAVVESQFLSMRLHAERLG--SDIPPTRILATGGASanKAIL--QVLADVFGAPVYT 455
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491006182 440 PAVREATALGCAIAAGTgaGLYSDMASTGEKLVSW------HRVFTPNPAHRELYQGMMEK 494
Cdd:cd07776 456 LDVANSAALGAALRAAH--GLLCAGSGDFSPEFVVfsaeepKLVAEPDPEAAEVYDKLLER 514
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
290-458 |
9.67e-14 |
|
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: 70.05 E-value: 9.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 290 VIPGMAQAESISFFTGLTMRWFRDAFCAEEKLVAERlGVDAYALLEEMASRVPAGSHGVMPIFSdAMHFKQWYHAAP-SF 368
Cdd:pfam02782 33 MLPGYWGLEGGQSAAGSLLAWLLQFHGLREELRDAG-NVESLAELAALAAVAPAGGLLFYPDFS-GNRAPGADPGARgSI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 369 INLSIDAEKCNkatLFRALEENAAIVSACNLAQISRFSGVTFDSLVFAGGGSKGALWSQILSDVTGLPVRVPAVREATAL 448
Cdd:pfam02782 111 TGLSSPTTLAH---LYRAILESLALQLRQILEALTKQEGHPIDTIHVSGGGSRNPLLLQLLADALGLPVVVPGPDEATAL 187
|
170
....*....|
gi 491006182 449 GCAIAAGTGA 458
Cdd:pfam02782 188 GAALLAAVAA 197
|
|
| glpK |
PRK00047 |
glycerol kinase GlpK; |
3-496 |
3.31e-13 |
|
glycerol kinase GlpK;
Pssm-ID: 234594 [Multi-domain] Cd Length: 498 Bit Score: 71.78 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 3 YLLALDAGTGSIRAVIFDLSGHQVAVGQAEWKHLSVEnvPGSMEFDLTTNWLLACQCIRQALAAAHLQAADIQSIACCSM 82
Cdd:PRK00047 6 YILALDQGTTSSRAIIFDHDGNIVSVAQKEFTQIFPQ--PGWVEHDPNEIWASQLSVIAEALAKAGISPDQIAAIGITNQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 83 REGIVLYDRN-GE----AI-WACanvdARASREVSELKEIhdyQFESEVYDVSGQTLA--LSAmPRLLWLAHHRPDIyRQ 154
Cdd:PRK00047 84 RETTVVWDKEtGRpiynAIvWQD----RRTADICEELKRD---GYEDYIREKTGLVIDpyFSG-TKIKWILDNVEGA-RE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 155 AA--------TItmisD-WLAAKLSGEL--AVDPSNAGTTGMLDLFSRDWRPALLDMAGLRADLLSPVKETGTPLGAVTD 223
Cdd:PRK00047 155 RAekgellfgTI----DtWLVWKLTGGKvhVTDYTNASRTMLFNIHTLDWDDELLELLDIPRSMLPEVRPSSEVYGKTNP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 224 taaqqcGLRAGTPV-IMG-GGDVQLGCLGLGVVRAGQSAVLGGTFWQQVVNLPE--VRTDPQM--NIRINPHVIPGMAQA 297
Cdd:PRK00047 231 ------YGFFGGEVpIAGiAGDQQAALFGQLCFEPGMAKNTYGTGCFMLMNTGEkaVKSENGLltTIAWGIDGKVVYALE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 298 ESIsFFTGLTMRWFRDafcaEEKLVAerlgvDAyALLEEMASRVPAgshgvmpifSDAMHFkqwyhaAPSFINLSI---D 374
Cdd:PRK00047 305 GSI-FVAGSAIQWLRD----GLKIIS-----DA-SDSEALARKVED---------NDGVYV------VPAFTGLGApywD 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 375 AEK----------CNKATLFRALEENAAIVSACNLAQISRFSGVTFDSLVFAGGGSKGALWSQILSDVTGLPVRVPAVRE 444
Cdd:PRK00047 359 SDArgaifgltrgTTKEHIIRATLESIAYQTRDVLDAMQADSGIRLKELRVDGGAVANNFLMQFQADILGVPVERPVVAE 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 491006182 445 ATALGCAIAAGTGAGLYSDMASTGEKlvsWH--RVFTP--NPAHRE-LYQGmmekWQ 496
Cdd:PRK00047 439 TTALGAAYLAGLAVGFWKDLDELKEQ---WKidRRFEPqmDEEEREkLYAG----WK 488
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
87-219 |
4.46e-09 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 58.58 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 87 VLYDRNGEAIWAcaNVDARASREVSELKEIHDYQFESEVYDVSG-QTLALSAMPRLLWLAHHRPDIYRQAATITMISDWL 165
Cdd:PRK10640 69 VLLDKQGQRVGL--PVSYRDSRTDGVMAQAQQQLGKRDIYRRSGiQFLPFNTLYQLRALTEQQPELIAQVAHALLIPDYF 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 491006182 166 AAKLSGELAVDPSNAGTTGMLDLFSRDWRPALLDMAGLRADLLSPVKETGTPLG 219
Cdd:PRK10640 147 SYRLTGKMNWEYTNATTTQLVNINSDDWDESLLAWSGAPKAWFGRPTHPGNVIG 200
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
141-243 |
2.57e-08 |
|
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: 56.11 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 141 LLWLAHHRPDIYRQAATITMISDWLAAKLSGELAVDPSNAGT-TGMLDLFSRDWRPALLDMAGLRadLLSPVKETGTPLG 219
Cdd:cd07772 129 LYWLKREKPELFARAKTILPLPQYWAWRLTGKAASEITSLGChTDLWDFEKNEYSSLVKKEGWDK--LFPPLRKAWEVLG 206
|
90 100
....*....|....*....|....
gi 491006182 220 AVTDTAAQQCGLRAGTPVIMGGGD 243
Cdd:cd07772 207 PLRPDLARRTGLPKDIPVGCGIHD 230
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
4-241 |
2.05e-03 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Saccharomyces cerevisiae protein MPA43. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466797 [Multi-domain] Cd Length: 544 Bit Score: 40.85 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 4 LLALDAGTGSIRAVIFDLSGHQVAVGQAEWKHLSVENVPGSMEFDLTTNWLLACQCIRQALAAAHLQAADIQSI-ACCSM 82
Cdd:cd07778 2 GIGIDVGSTSVRIGIFDYHGTLLATSERPISYKQDPKDLWFVTQSSTEIWKAIKTALKELIEELSDYIVSGIGVsATCSM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 83 ----RE----------GIVLYDRNGEAI--WacanVDARASREVSELKEIHDyqfESEVYDVSGQTLALSAMPRLLWLAH 146
Cdd:cd07778 82 vvmqRDsdtsylvpynVIHEKSNPDQDIifW----MDHRASEETQWLNNILP---DDILDYLGGGFIPEMAIPKLKYLID 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491006182 147 HRPDIYRQAATITMISDWLAAKLSGELA---VDPSNA-GTTGM----------LDLFSRDWRPALLDMAGLRADLLSPVK 212
Cdd:cd07778 155 LIKEDTFKKLEVFDLHDWISYMLATNLGhsnIVPVNApPSIGIgidgslkgwsKDFYSKLKISTKVCNVGNTFKEAPPLP 234
|
250 260
....*....|....*....|....*....
gi 491006182 213 ETGTPLGAVTDTAAQQCGLRaGTPVIMGG 241
Cdd:cd07778 235 YAGIPIGKVNVILASYLGID-KSTVVGHG 262
|
|
| |
