|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
1-550 |
0e+00 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 941.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 1 MAIAIGLDFGSDSVRALAVDCATGDEIATSVEWYPRWQEGRYCDGPNNQFRHHPRDYMESMEAALKAVLAQlSAAQRANV 80
Cdd:PRK04123 2 MAYVIGLDFGTDSVRALLVDCATGEELATAVVEYPHWVKGRYLDLPPNQALQHPLDYIESLEAAIPAVLKE-AGVDPAAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 81 VGIGVDSTGSTPAPIDADGNVLALRPEFAENPNAMFVLWKDHTAVEEADEITRLCHKPGKVDYSRYIGGIYSSEWFWAKI 160
Cdd:PRK04123 81 VGIGVDFTGSTPAPVDADGTPLALLPEFAENPHAMVKLWKDHTAQEEAEEINRLAHERGEADLSRYIGGIYSSEWFWAKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 161 LHVTRQDSAVAQAAVSWIELCDWVPALLSGTTRPQDIRRGRCSAGHKTLWHESWGGLPPASFFDELDPCINRHLRYPLFS 240
Cdd:PRK04123 161 LHVLREDPAVYEAAASWVEACDWVVALLTGTTDPQDIVRSRCAAGHKALWHESWGGLPSADFFDALDPLLARGLRDKLFT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 241 ETFTADLPVGTLCAEWAQRLGLPESVVISGGAFDCHMGAVGAGAQPNTLVKVIGTSTCDILIADKQsvgdRAVKGICGQV 320
Cdd:PRK04123 241 ETWTAGEPAGTLTAEWAQRLGLPEGVAVSVGAFDAHMGAVGAGAEPGTLVKVMGTSTCDILLADKQ----RAVPGICGQV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 321 DGSVVPNFIGLEAGQSAFGDIYAWFSRVLSwpleqlaaqHPELKTQINASQKQLLPALTDAWAKNPSLDHLPVVLDWFNG 400
Cdd:PRK04123 317 DGSIVPGLIGYEAGQSAVGDIFAWFARLLV---------PPEYKDEAEARGKQLLELLTEAAAKQPPGEHGLVALDWFNG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 401 RRTPNANQRLKGVITDLNLATDAPALFGGLVASTAFGARAIQECFTDQGIAVNNVMALGGIARKNQVIMQVCCDVLNRPL 480
Cdd:PRK04123 388 RRTPLADQRLKGVITGLTLGTDAPDIYRALIEATAFGTRAIMECFEDQGVPVEEVIAAGGIARKNPVLMQIYADVLNRPI 467
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 481 QIVASDQCCALGAAIFAAVAAKVHADIPAAQQSMASAVERTLRPRPEQAQRLEQLYRRYQQWalsAEQHY 550
Cdd:PRK04123 468 QVVASDQCPALGAAIFAAVAAGAYPDIPEAQQAMASPVEKTYQPDPENVARYEQLYQEYKQL---HDYFG 534
|
|
| L-ribulokinase |
TIGR01234 |
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely ... |
2-549 |
0e+00 |
|
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely related protein subfamily outside the scope of this model includes ribitol kinase from E. coli. [Energy metabolism, Sugars]
Pssm-ID: 130301 [Multi-domain] Cd Length: 536 Bit Score: 819.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 2 AIAIGLDFGSDSVRALAVDCATGDEIATSVEWYPRWQEGRYCDG-----PNNQFRHHPRDYMESMEAALKAVLAQLSAAQ 76
Cdd:TIGR01234 1 AYAIGVDFGTLSGRALAVDVATGEEIATAVEWYRHWVKGQFLPKtgaklPNDQALQHPADYIEVLEAAIPTVLAELGVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 77 rANVVGIGVDSTGSTPAPIDADGNVLALRPEFAENPNAMFVLWKDHTAVEEADEITRLCHKPGKVDYSRYiGGIYSSEWF 156
Cdd:TIGR01234 81 -ADVVGIGVDFTACTPAPIDSDGNPLCLLPEFAENPHAYFKLWKHHAAQEEADRINRLAHAPGEVDLSRY-GGIISSEWF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 157 WAKILHVTRQDSAVAQAAVSWIELCDWVPALLSGttrpqDIRRGRCSAGHKTLWHESWGgLPPASFFDELDPCINRHLRY 236
Cdd:TIGR01234 159 WAKILQITEEDPAIYQAADRWIELADWIVAQLSG-----DIRRGRCTAGYKALWHESWG-YPSASFFDELNPILNRHLPD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 237 PLFSETFTADLPVGTLCAEWAQRLGLPESVVISGGAFDCHMGAVGAG-AQPNTLVKVIGTSTCDILIADKQsvgdRAVKG 315
Cdd:TIGR01234 233 KLFTDIWTAGEPAGTLTPEWAQRTGLPEGVVVAVGNFDAHVGAVAAGiAQPGALVKIMGTSTCHVLIGDKQ----RAVPG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 316 ICGQVDGSVVPNFIGLEAGQSAFGDIYAWFSRVLswpleqlaaQHPELKTQINASQKQLLPALTDAWAKNPSLDHLPVVL 395
Cdd:TIGR01234 309 MCGVVDGGIVPGFIGYEAGQSAVGDIFAWFGKVC---------VPPELKTEANASQKQLHEALSEAAAKQPSGEHGLVAL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 396 DWFNGRRTPNANQRLKGVITDLNLATDAPALFGGLVASTAFGARAIQECFTDQGIAVNNVMALGGIARKNQVIMQVCCDV 475
Cdd:TIGR01234 380 DWFNGNRSPLVDQRLKGVITGLTLATDAPLLYRALIEATAFGTRMIMETFTDSGVPVEELMAAGGIARKNPVIMQIYADV 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 340763515 476 LNRPLQIVASDQCCALGAAIFAAVAAKVHADIPAAQQSMASAVERTLRPRPEQAQRLEQLYRRYQQWALSAEQH 549
Cdd:TIGR01234 460 TNRPLQIVASDQAPALGAAIFAAVAAGVYADIPSAQAKMGSAVEKTLTPCSENAQRYEQLYARYQELAMSFGQY 533
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
1-550 |
0e+00 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 817.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 1 MAIAIGLDFGSDSVRALAVDCATGDEIATSVEWYPRWQEGRYCDGPNNQFRHHPRDYMESMEAALKAVLAQlSAAQRANV 80
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDAADGEELASAVHPYPRWVIGLYLPPPPDQARQHPLDYLEALEAAVREALAQ-AGVDPADV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 81 VGIGVDSTGSTPAPIDADGNVLALRPEFAENPNAMFVLWKDHTAVEEADEITRLCHKpGKVDYSRYIGGIYSSEWFWAKI 160
Cdd:COG1069 80 VGIGVDATGCTPVPVDADGTPLALLPEFAENPHAMVILWKDHTAQEEAERINELAKA-RGEDYLRYVGGIISSEWFWPKI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 161 LHVTRQDSAVAQAAVSWIELCDWVPALLSGttrpqDIRRGRCSAGHKTLWHESWGGLPPASFFDELDPCINrHLRYPLFS 240
Cdd:COG1069 159 LHLLREDPEVYEAADSFVELCDWITWQLTG-----SLKRSRCTAGHKALWHAHEGGYPSEEFFAALDPLLD-GLADRLGT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 241 ETFTADLPVGTLCAEWAQRLGLPESVVISGGAFDCHMGAVGAGA-QPNTLVKVIGTSTCDILIADKQsvgdRAVKGICGQ 319
Cdd:COG1069 233 EIYPLGEPAGTLTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGGvEPGTLVKVMGTSTCHMLVSPEE----RFVPGICGQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 320 VDGSVVPNFIGLEAGQSAFGDIYAWFSRVLSWPLEqlaaqhpeLKTQINASQKQLLPALTDAWAKNPSLDHLPVVLDWFN 399
Cdd:COG1069 309 VDGSIVPGMWGYEAGQSAVGDIFAWFVRLLVPPLE--------YEKEAEERGISLHPLLTEEAAKLPPGESGLHALDWFN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 400 GRRTPNANQRLKGVITDLNLATDAPALFGGLVASTAFGARAIQECFTDQGIAVNNVMALGGIARKNQVIMQVCCDVLNRP 479
Cdd:COG1069 381 GNRSPLADQRLKGVILGLTLGTDAEDIYRALVEATAFGTRAIIERFEEEGVPIDEIIACGGIATKNPLVMQIYADVTGRP 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 340763515 480 LQIVASDQCCALGAAIFAAVAAKVHADIPAAQQSMASAVERTLRPRPEQAQRLEQLYRRYQQWALSAEQHY 550
Cdd:COG1069 461 IKVAASEQACALGAAMFAAVAAGAYPDVEEAMAAMGSGFDKVYTPDPENVAVYDALYAEYLQLHDYFGRGR 531
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
3-541 |
0e+00 |
|
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: 636.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 3 IAIGLDFGSDSVRALAVDCATGDEIATSVEWYPRWqegrYCDGPNNQFRHHPRDYMESMEAALKAVLAQlSAAQRANVVG 82
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDLADGEELASAVVPYPTG----YIPPRPGWAEQNPADYWEALEEAVRGALAE-AGVDPEDVVG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 83 IGVDSTGSTPAPIDADGNvlalrpefaenPNAMFVLWKDHTAVEEADEITRLCHKPGKVDYSRYiGGIYSSEWFWAKILH 162
Cdd:cd07781 76 IGVDTTSSTVVPVDEDGN-----------PLAPAILWMDHRAQEEAAEINETAHPALEYYLAYY-GGVYSSEWMWPKALW 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 163 VTRQDSAVAQAAVSWIELCDWVPALLSGTtrpqdIRRGRCSAGHKTLWHEsWGGLPPASFFDELDPCINRhLRYPLFSET 242
Cdd:cd07781 144 LKRNAPEVYDAAYTIVEACDWINARLTGR-----WVRSRCAAGHKWMYNE-WGGGPPREFLAALDPGLLK-LREKLPGEV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 243 FTADLPVGTLCAEWAQRLGLPESVVISGGAFDCHMGAVGAGA-QPNTLVKVIGTSTCDILIADKQSvgdrAVKGICGQVD 321
Cdd:cd07781 217 VPVGEPAGTLTAEAAERLGLPAGIPVAQGGIDAHMGAIGAGVvEPGTLALIMGTSTCHLMVSPKPV----DIPGICGPVP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 322 GSVVPNFIGLEAGQSAFGDIYAWFSRVLSWPLEQLAaqhpelktqinasqKQLLPALTDAWAKNPSLDHLPVVLDWFNGR 401
Cdd:cd07781 293 DAVVPGLYGLEAGQSAVGDIFAWFVRLFVPPAEERG--------------DSIYALLSEEAAKLPPGESGLVALDWFNGN 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 402 RTPNANQRLKGVITDLNLATDAPALFGGLVASTAFGARAIQECFTDQGIAVNNVMALGGIARKNQVIMQVCCDVLNRPLQ 481
Cdd:cd07781 359 RTPLVDPRLRGAIVGLTLGTTPAHIYRALLEATAFGTRAIIERFEEAGVPVNRVVACGGIAEKNPLWMQIYADVLGRPIK 438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 482 IVASDQCCALGAAIFAAVAAKVHADIPAAQQSMASaVERTLRPRPEQAQRLEQLYRRYQQ 541
Cdd:cd07781 439 VPKSDQAPALGAAILAAVAAGVYADIEEAADAMVR-VDRVYEPDPENHAVYEELYALYKE 497
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
5-541 |
5.06e-62 |
|
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: 213.26 E-value: 5.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 5 IGLDFGSDSVRALAVDCATGDEIATSVEWYPRWQEGRycdgpNNQFRHHPRDYMESMEAALKAVLAQlSAAQRANVVGIG 84
Cdd:cd07768 3 IGVDVGTSSARAGVYDLYAGLEMAQEPVPYYQDSSKK-----SWKFWQKSTEIIKALQKCVQKLNIR-EGVDAYEVKGCG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 85 VDSTGSTpAPIDADGNVLALRPEFaeNPNAMFVLWKDHTAVEEADEITRLCHKPGKvdysRYIGGIYSSEWFWAKILHVT 164
Cdd:cd07768 77 VDATCSL-AIFDREGTPLMALIPY--PNEDNVIFWMDHSAVNEAQWINMQCPQQLL----DYLGGKISPEMGVPKLKYFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 165 RQDSAVAQAAVSWIELCDWVPALLSGttrpqDIRRGRCSAGHKTLWHESWGGlPPASFFDELDPCINRHLRYPLFSETFT 244
Cdd:cd07768 150 DEYSHLRDKHFHIFDLHDYIAYELTR-----LYEWNICGLLGKENLDGEESG-WSSSFFKNIDPRLEHLTTTKNLPSNVP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 245 ADLPVGTLCAEWAQRLGLPESVVISGGAFDCHMG--AVGAGAQPNTLVKVIGTSTCDILIADKQsvgdRAVKGICGQVDG 322
Cdd:cd07768 224 IGTTSGVALPEMAEKMGLHPGTAVVVSCIDAHASwfAVASPHLETSLFMIAGTSSCHMYGTTIS----DRIPGVWGPFDT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 323 SVVPNFIGLEAGQSAFGDIYAWFSRvlswpleqlaaQHPELKTQINASQK-----QLLPALTDAWAKNPSLDHLPVVLDW 397
Cdd:cd07768 300 IIDPDYSVYEAGQSATGKLIEHLFE-----------SHPCARKFDEALKKgadiyQVLEQTIRQIEKNNGLSIHILTLDM 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 398 FNGRRTPNANQRLKGVITDLNLAT---DAPALFGGLVASTAFGARAIQECFTDQGIAVNNVMALGGIArKNQVIMQVCCD 474
Cdd:cd07768 369 FFGNRSEFADPRLKGSFIGESLDTsmlNLTYKYIAILEALAFGTRLIIDTFQNEGIHIKELRASGGQA-KNERLLQLIAL 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 340763515 475 VLNRPLQIVASDQCCALGAA--IFAAVAAKVHAD-IPAAQQSMaSAVERTLRPRP-EQAQRLEQLYRRYQQ 541
Cdd:cd07768 448 VTNVAIIKPKENMMGILGAAvlAKVAAGKKQLADsITEADISN-DRKSETFEPLAyRLGADYILLYKLLCV 517
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
5-541 |
2.08e-49 |
|
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: 178.10 E-value: 2.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 5 IGLDFGSDSVRALAVDcATGDEIAT-SVEW-----YPRWQEgrycdgpnnqfrHHPRDYMESMEAALKAVLAQlSAAQRA 78
Cdd:COG1070 4 LGIDIGTTSVKAVLFD-ADGEVVASaSAEYplsspHPGWAE------------QDPEDWWEAVVEAIRELLAK-AGVDPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 79 NVVGIGVDSTGSTPAPIDADGNVLalRPefaenpnamFVLWKDHTAVEEADEITRlchKPGKVDYSRYIGGIYSSEWFWA 158
Cdd:COG1070 70 EIAAIGVSGQMHGLVLLDADGEPL--RP---------AILWNDTRAAAEAAELRE---ELGEEALYEITGNPLHPGFTAP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 159 KILHVTRQDSAVAQAAVSWIELCDWV-----------PALLSGTTrPQDIRRGRcsaghktlWHESWgglppasfFDELD 227
Cdd:COG1070 136 KLLWLKENEPEIFARIAKVLLPKDYLryrltgefvtdYSDASGTG-LLDVRTRD--------WSDEL--------LEALG 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 228 pcinrhLRYPLFSETFTADLPVGTLCAEWAQRLGLPESVVISGGAFDCHMGAVGAGA-QPNTLVKVIGTSTCDILIADKQ 306
Cdd:COG1070 199 ------IDRELLPELVPPGEVAGTLTAEAAAETGLPAGTPVVAGAGDNAAAALGAGAvEPGDAAVSLGTSGVVFVVSDKP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 307 SVGDR-AVKGICGQVDGSVVPnfiglEAGQSAFGDIYAWFSRvlswpleqlaaqhpelktQINASQKQLLPALTDAWAKN 385
Cdd:COG1070 273 LPDPEgRVHTFCHAVPGRWLP-----MGATNNGGSALRWFRD------------------LFADGELDDYEELNALAAEV 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 386 PSLDHLPVVLDWFNGRRTPNANQRLKGVITDLNLATDAPALFGGLVASTAFGARAIQECFTDQGIAVNNVMALGGIARkN 465
Cdd:COG1070 330 PPGADGLLFLPYLSGERTPHWDPNARGAFFGLTLSHTRAHLARAVLEGVAFALRDGLEALEEAGVKIDRIRATGGGAR-S 408
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 340763515 466 QVIMQVCCDVLNRPLQIVASDQCCALGAAIFAAVAAKVHADIPAAQQSMAsAVERTLRPRPEQAQRLEQLYRRYQQ 541
Cdd:COG1070 409 PLWRQILADVLGRPVEVPEAEEGGALGAALLAAVGLGLYDDLEEAAAAMV-RVGETIEPDPENVAAYDELYERYRE 483
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
5-540 |
2.84e-40 |
|
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: 153.84 E-value: 2.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 5 IGLDFGSDSVRALAVDCaTGDEIATSVEwyprwqegrycdgpNNQFRHHPRDYME--SME------AALKAVLAQlSAAQ 76
Cdd:cd07782 3 IGVDVGTGSARAGLFDL-DGRLLATASQ--------------PITTWNPKPDFYEqsSEDiwqavcEAVKEVLEG-AGVD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 77 RANVVGIGVDSTGSTPApIDADGNVLALRPEfaENPNAMFVLWKDHTAVEEADEITRLCHKPgkvdySRYIGGIYSSEWF 156
Cdd:cd07782 67 PEQVKGIGFDATCSLVV-LDAEGKPVSVSPS--GDDERNVILWMDHRAVEEAERINATGHEV-----LKYVGGKISPEME 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 157 WAKILHVTRQDSAVAQAAVSWIELCDWvpalLS-----GTTRPQdirrgrCSAGHKtlwhesWGGLPP--------ASFF 223
Cdd:cd07782 139 PPKLLWLKENLPETWAKAGHFFDLPDF----LTwkatgSLTRSL------CSLVCK------WTYLAHegseggwdDDFF 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 224 DELDPCINRHLRYPLFSETFTADLPV--GTLCAEWAQRLGLPESVVISGGAFDCHMGAVG-AGAQ-----------PNTL 289
Cdd:cd07782 203 KEIGLEDLVEDNFAKIGSVVLPPGEPvgGGLTAEAAKELGLPEGTPVGVSLIDAHAGGLGtLGADvgglpceadplTRRL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 290 VKVIGTSTCDILIADKQsvgdRAVKGICGQVDGSVVPNFIGLEAGQSAFGdiyAWFSRVL-SWPleqlaaQHPELKTQIN 368
Cdd:cd07782 283 ALICGTSSCHMAVSPEP----VFVPGVWGPYYSAMLPGLWLNEGGQSATG---ALLDHIIeTHP------AYPELKEEAK 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 369 ASQK---QLLPALTD--AWAKNPSLDHLPV---VLDWFNGRRTPNANQRLKGVITDLNLATDAPAL----FGGLVAsTAF 436
Cdd:cd07782 350 AAGKsiyEYLNERLEqlAEEKGLPLAYLTRdlhVLPDFHGNRSPLADPTLRGMISGLTLDTSLDDLallyLATLQA-LAY 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 437 GARAIQECFTDQGIAVNNVMALGGIArKNQVIMQVCCDVLNRPLQIVASDQCCALGAAIFAAVAAKVHADIPAAQQSMaS 516
Cdd:cd07782 429 GTRHIIEAMNAAGHKIDTIFMCGGLS-KNPLFVQLHADVTGCPVVLPKEPEAVLLGAAILGAVASGDFPSLWDAMAAM-S 506
|
570 580
....*....|....*....|....
gi 340763515 517 AVERTLRPRPEQAQRLEqlyRRYQ 540
Cdd:cd07782 507 GPGKVVEPNEELKKYHD---RKYE 527
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
5-492 |
5.97e-40 |
|
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: 150.82 E-value: 5.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 5 IGLDFGSDSVRALAVDcATGDEIATSVEWYPrwqegrYCDGPNNQFRHHPRDYMESMEAALKAVLAQLSAAQranVVGIG 84
Cdd:cd07773 3 LGIDIGTTNVKAVLFD-EDGRILASASRETP------LIHPGPGWAELDPEELWEAVKEAIREAAAQAGPDP---IAAIS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 85 VDSTGSTPAPIDADGNVLAlrpefaenpNAMfvLWKDHTAVEEADEITrlcHKPGKVDYSRYIGGIYSSEWFWAKILHVT 164
Cdd:cd07773 73 VSSQGESGVPVDRDGEPLG---------PAI--VWFDPRGKEEAEELA---ERIGAEELYRITGLPPSPMYSLAKLLWLR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 165 RQDSAVAQAAVSWIELCDWVPALLSG---TTRPQ-------DIRRGRcsaghktlWHE---SWGGLPPAsffdeldpcin 231
Cdd:cd07773 139 EHEPEIFAKAAKWLSVADYIAYRLTGepvTDYSLasrtmlfDIRKRT--------WSEellEAAGIDAS----------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 232 rhlrypLFSETFTADLPVGTLCAEWAQRLGLPESVVISGGAFDCHMGAVGAGA-QPNTLVKVIGTSTCDILIADKQSVGD 310
Cdd:cd07773 200 ------LLPELVPSGTVIGTVTPEAAEELGLPAGTPVVVGGHDHLCAALGAGViEPGDVLDSTGTAEALLAVVDEPPLDE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 311 RAVKGICgQVDGSVVPNFIGLEAGQSAfGDIYAWFSRVLSWPLEQLAAQHPELktqinasqkqllpaltdawAKNPSLDH 390
Cdd:cd07773 274 MLAEGGL-SYGHHVPGGYYYLAGSLPG-GALLEWFRDLFGGDESDLAAADELA-------------------EAAPPGPT 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 391 LPVVLDWFNGRRTPNANQRLKGVITDLNLATDAPALFGGLVASTAFGARAIQECFTDQGIAVNNVMALGGIARkNQVIMQ 470
Cdd:cd07773 333 GLLFLPHLSGSGTPDFDPDARGAFLGLTLGTTRADLLRAILEGLAFELRLNLEALEKAGIPIDEIRAVGGGAR-SPLWLQ 411
|
490 500
....*....|....*....|..
gi 340763515 471 VCCDVLNRPLQIVASDQCCALG 492
Cdd:cd07773 412 LKADILGRPIEVPEVPEATALG 433
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
3-486 |
3.94e-35 |
|
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: 136.97 E-value: 3.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 3 IAIGLDFGSDSVRALAVDcATGDEIATSVEWYPrwqEGRYCDGPNNQfrhHPRDYMESMEAALKAVLAQLSAAQranVVG 82
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVD-EDGTVLASASEPYP---TSRPGPGWVEQ---DPEDWWEALRSLLRELPAELRPRR---VVA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 83 IGVDSTGSTPAPIDADGNVLAlrpefaenpNAMfvLWKDHTAVEEADEITRLchkpGKVDYSRYiGGIYSSEWFWAKILH 162
Cdd:cd07783 71 IAVDGTSGTLVLVDREGEPLR---------PAI--MYNDARAVAEAEELAEA----AGAVAPRT-GLAVSPSSSLAKLLW 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 163 VTRQDSAVAQAAVSWIELCDWVPALLSGTTRPQDirrgrCSAGHKTLW---HESWgglpPASFFDELdpcINRHLRYPLF 239
Cdd:cd07783 135 LKRHEPEVLAKTAKFLHQADWLAGRLTGDRGVTD-----YNNALKLGYdpeTGRW----PSWLLALL---GIPPDLLPRV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 240 SETFTadlPVGTLCAEWAQRLGLPESVVISGGAFDCHMGAVGAGA-QPNTLVKVIGTSTC-----DILIADKQSvgdrav 313
Cdd:cd07783 203 VAPGT---VIGTLTAEAAEELGLPAGTPVVAGTTDSIAAFLASGAvRPGDAVTSLGTTLVlkllsDKRVPDPGG------ 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 314 kGIcgqvdgSVVPNFIGL---EAGQSAFGDIYAWFSRvlSWPLEQLAAQ-HPELKTqinasqkqllpaltdawaknpSLD 389
Cdd:cd07783 274 -GV------YSHRHGDGYwlvGGASNTGGAVLRWFFS--DDELAELSAQaDPPGPS---------------------GLI 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 390 HLPVVLdwfNGRRTPNANQRLKGVItdLNLATDAPALFGGLVASTAFGARAIQECFTDQG-IAVNNVMALGGIARkNQVI 468
Cdd:cd07783 324 YYPLPL---RGERFPFWDPDARGFL--LPRPHDRAEFLRALLEGIAFIERLGYERLEELGaPPVEEVRTAGGGAR-NDLW 397
|
490
....*....|....*...
gi 340763515 469 MQVCCDVLNRPLQIVASD 486
Cdd:cd07783 398 NQIRADVLGVPVVIAEEE 415
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
5-492 |
7.60e-33 |
|
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: 129.99 E-value: 7.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 5 IGLDFGSDSVRALAVDcATGDEIATSVEWY------PRWQEgrycdgpnnqfrHHPRDYMESMEAALKAVLAQlSAAQRA 78
Cdd:cd00366 3 LGIDIGTTSVKAALFD-EDGNLVASASREYpliypqPGWAE------------QDPEDWWQAVVEAIREVLAK-AGIDPS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 79 NVVGIGVDSTGSTPAPIDADGNVLalRPefaenpnamFVLWKD--HTAVEEADEIT-RLCHKPGkVDYSryiggiYSSEW 155
Cdd:cd00366 69 DIAAIGISGQMPGVVLVDADGNPL--RP---------AIIWLDrrAKFLQPNDYIVfRLTGEFA-IDYS------NASGT 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 156 FWakiLHVTRQDsavaqaavsWI-ELCDWVpallsgttrpqdirrgrcsaghktlwheswgGLPPASFFDELDPCinrhl 234
Cdd:cd00366 131 GL---YDIKTGD---------WSeELLDAL-------------------------------GIPREKLPPIVESG----- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 235 ryplfsETftadlpVGTLCAEWAQRLGLPESVVISGGAFDCHMGAVGAGA-QPNTLVKVIGTSTCDILIADKQSVGDRAV 313
Cdd:cd00366 163 ------EV------VGRVTPEAAEETGLPAGTPVVAGGGDTAAAALGAGVvEPGDAVDSTGTSSVLSVCTDEPVPPDPRL 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 314 KGICgqvdgSVVPNFIGLEAGQSAFGDIYAWFSRVLsWPLEQLAAQHPELKTQInasqkqllpaltdawAKNPSLDHLPV 393
Cdd:cd00366 231 LNRC-----HVVPGLWLLEGAINTGGASLRWFRDEF-GEEEDSDAEYEGLDELA---------------AEVPPGSDGLI 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 394 VLDWFNGRRTPNANQRLKGVITDLNLATDAPALFGGLVASTAFGARAIQECFTDQGIAVNNVMALGGIArKNQVIMQVCC 473
Cdd:cd00366 290 FLPYLSGERSPIWDPAARGVFFGLTLSHTRAHLIRAVLEGVAYALRDNLEILEELGVKIKEIRVTGGGA-KSRLWNQIKA 368
|
490
....*....|....*....
gi 340763515 474 DVLNRPLQIVASDQCCALG 492
Cdd:cd00366 369 DVLGVPVVVPEVAEGAALG 387
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
289-495 |
1.47e-32 |
|
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: 123.59 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 289 LVKVIGTSTCDILIADKQsvgDRAVKGICGQVDGSVVPNFIGLEAGQSAFGDIYAWFSRvlswpleqlaaQHPELKTQIN 368
Cdd:pfam02782 1 LAISAGTSSFVLVETPEP---VLSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQ-----------FHGLREELRD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 369 ASQKQLLPALTDAWAKNPSLdhLPVVLDWFNGRRTPNANQRLKGVITDLNLATDAPALFGGLVASTAFGARAIQECFTDQ 448
Cdd:pfam02782 67 AGNVESLAELAALAAVAPAG--GLLFYPDFSGNRAPGADPGARGSITGLSSPTTLAHLYRAILESLALQLRQILEALTKQ 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 340763515 449 -GIAVNNVMALGGIARkNQVIMQVCCDVLNRPLQIVASDQCCALGAAI 495
Cdd:pfam02782 145 eGHPIDTIHVSGGGSR-NPLLLQLLADALGLPVVVPGPDEATALGAAL 191
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
5-492 |
2.25e-29 |
|
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: 121.09 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 5 IGLDFGSDSVRALAVDcATGDEIATSVEWY------PRWQEgrycdgpnnqfrHHPRDYMESMEAALKAVLAQlSAAQRA 78
Cdd:cd07804 3 LGIDIGTTGTKGVLVD-EDGKVLASASIEHdlltpkPGWAE------------HDPEVWWGAVCEIIRELLAK-AGISPK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 79 NVVGIGVdsTGSTPA--PIDADGNvlALRPefaenpnAMfvLWKDHTAVEEADEITRLCHKpgkvDYSRYIGGIYSSEWF 156
Cdd:cd07804 69 EIAAIGV--SGLVPAlvPVDENGK--PLRP-------AI--LYGDRRATEEIEWLNENIGE----DRIFEITGNPLDSQS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 157 WA-KILHVTRQDSAVAQAAVSWIELCDWVPALLSGTtRPQDIRRGRCSAGHKTLWHESWGglppASFFDELdpcinrHLR 235
Cdd:cd07804 132 VGpKLLWIKRNEPEVFKKTRKFLGAYDYIVYKLTGE-YVIDYSSAGNEGGLFDIRKRTWD----EELLEAL------GID 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 236 YPLFSETFTADLPVGTLCAEWAQRLGLPESV-VISGGAfDCHMGAVGAGA-QPNTLVKVIGTSTCDILIADKqSVGDRAV 313
Cdd:cd07804 201 PDLLPELVPSTEIVGEVTKEAAEETGLAEGTpVVAGTV-DAAASALSAGVvEPGDLLLMLGTAGDIGVVTDK-LPTDPRL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 314 kgicgQVDGSVVPNFIGLEAGQSAFGDIYAWFsrvlswpLEQLAAQHPELKTQINASQKQLLpaltDAWAKN--PSLDHL 391
Cdd:cd07804 279 -----WLDYHDIPGTYVLNGGMATSGSLLRWF-------RDEFAGEEVEAEKSGGDSAYDLL----DEEAEKipPGSDGL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 392 pVVLDWFNGRRTPNANQRLKGVITDLNLATDAPALFGGLVASTAFGARAIQECFTDQGIAVNNVMALGGIArKNQVIMQV 471
Cdd:cd07804 343 -IVLPYFMGERTPIWDPDARGVIFGLTLSHTRAHLYRALLEGVAYGLRHHLEVIREAGLPIKRLVAVGGGA-KSPLWRQI 420
|
490 500
....*....|....*....|.
gi 340763515 472 CCDVLNRPLQIVASDQCCALG 492
Cdd:cd07804 421 VADVTGVPQEYVKDTVGASLG 441
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
5-542 |
5.27e-29 |
|
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: 120.34 E-value: 5.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 5 IGLDFGSDSVRALAVDcATGDEIATSVEWY------PRWQEgrycdgpnnqfrHHPRDYMESMEAALKAVLAQlSAAQRA 78
Cdd:cd07808 3 LGIDLGTSSVKAVLVD-EDGRVLASASAEYptsspkPGWAE------------QDPEDWWQATKEALRELLAK-AGISPS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 79 NVVGIGVDSTGSTPAPIDADGNVLalRPefaenpnAMfvLWKDHTAVEEADEITRlchKPGKVDYSRyIGGIYSSEWFWA 158
Cdd:cd07808 69 DIAAIGLTGQMHGLVLLDKNGRPL--RP-------AI--LWNDQRSAAECEELEA---RLGDEILII-TGNPPLPGFTLP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 159 KILHVTRQDSAVAqAAVSWIELC-DWVPALLSGT--TRPQDirrgrcSAGhkTLW----HESW-------GGLPPASFfd 224
Cdd:cd07808 134 KLLWLKENEPEIF-ARIRKILLPkDYLRYRLTGElaTDPSD------ASG--TLLfdveKREWseelleaLGLDPSIL-- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 225 eldPcinrhlryPLFSETFTadlpVGTLCAEWAQRLGLPESVVISGGAFDCHMGAVGAGA-QPNTLVKVIGTSTCDILIA 303
Cdd:cd07808 203 ---P--------PIVESTEI----VGTLTPEAAEELGLPEGTPVVAGAGDNAAAALGAGVvEPGDALISLGTSGVVFAPT 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 304 DK-QSVGDRAVKGICgqvdgSVVPN-FIGLEAGQSAfGDIYAWFSRVLswpleqlaAQHPELKTQINASQKQL------- 374
Cdd:cd07808 268 DKpVPDPKGRLHTFP-----HAVPGkWYAMGVTLSA-GLSLRWLRDLF--------GPDRESFDELDAEAAKVppgsegl 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 375 --LPALtdawaknpsldhlpvvldwfNGRRTPNANQRLKGVITDLNLATDAPALFGGLVASTAFGARAIQECFTDQGIAV 452
Cdd:cd07808 334 lfLPYL--------------------SGERTPYWDPNARGSFFGLSLSHTRAHLARAVLEGVAFSLRDSLEVLKELGIKV 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 453 NNVMALGGIArKNQVIMQVCCDVLNRPLQIVASDQCCALGAAIFAAVAAKVHADIPAAQQsMASAVERTLRPRPEQAQRL 532
Cdd:cd07808 394 KEIRLIGGGA-KSPLWRQILADVLGVPVVVPAEEEGSAYGAALLAAVGAGVFDDLEEAAA-ACIKIEKTIEPDPERHEAY 471
|
570
....*....|
gi 340763515 533 EQLYRRYQQW 542
Cdd:cd07808 472 DELYARYREL 481
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
5-539 |
3.30e-28 |
|
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: 118.01 E-value: 3.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 5 IGLDFGSDSVRALAVDcATGDEIATSVEWYPRWQEGrycDGPNNQfrhHPRDYMESMEAALKAVLAQlSAAQRANVVGIG 84
Cdd:cd07805 3 LAIDLGTSGVKAALVD-LDGELVASAFAPYPTYYPK---PGWAEQ---DPEDWWDAVCRATRALLEK-SGIDPSDIAAIA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 85 VDSTGSTPAPIDADGNVLAlrpefaenpNAMfvLWKDHTAVEEADEItrLCHKPGKVDYSRYIGGIYSSEWFWAKILHVT 164
Cdd:cd07805 75 FSGQMQGVVPVDKDGNPLR---------NAI--IWSDTRAAEEAEEI--AGGLGGIEGYRLGGGNPPSGKDPLAKILWLK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 165 RQDSAVAQAAVSWIELCDWVPALLSG----------TTRPQDIRRGRcsaghktlWHESW---GGLPPAsffdeldpcin 231
Cdd:cd07805 142 ENEPEIYAKTHKFLDAKDYLNFRLTGraatdpstasTTGLMDLRKRR--------WSEELlraAGIDPD----------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 232 rhlrypLFSETFTADLPVGTLCAEWAQRLGLPESVVISGGAFDCHMGAVGAGA-QPNTLVKVIGTSTCDILIADKQSVG- 309
Cdd:cd07805 203 ------KLPELVPSTEVVGELTPEAAAELGLPAGTPVVGGGGDAAAAALGAGAvEEGDAHIYLGTSGWVAAHVPKPKTDp 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 310 DRAVKGICGQVDGSVvpNFIGleAGQSAfGDIYAWFSRVLSWP----------LEQLAAQHPelktqinASQKQLLpalt 379
Cdd:cd07805 277 DHGIFTLASADPGRY--LLAA--EQETA-GGALEWARDNLGGDedlgaddyelLDELAAEAP-------PGSNGLL---- 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 380 dawaknpsldHLPvvldWFNGRRTPNANQRLKGVITDLNLATD----APALFGGLvastAFGARAIQECFTDQGIAVNNV 455
Cdd:cd07805 341 ----------FLP----WLNGERSPVEDPNARGAFIGLSLEHTradlARAVLEGV----AFNLRWLLEALEKLTRKIDEL 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 456 MALGGIARkNQVIMQVCCDVLNRPLQIVASDQ--------CCA---LGaaifaavAAKVHADIPAAQQsmasaVERTLRP 524
Cdd:cd07805 403 RLVGGGAR-SDLWCQILADVLGRPVEVPENPQeagalgaaLLAavgLG-------LLKSFDEAKALVK-----VEKVFEP 469
|
570
....*....|....*
gi 340763515 525 RPEQAQRLEQLYRRY 539
Cdd:cd07805 470 DPENRARYDRLYEVF 484
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
5-531 |
3.74e-27 |
|
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: 114.15 E-value: 3.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 5 IGLDFGSDSVRALAVDcATGDEIATSVEWYPR------WQEgrycdgpnnqfrHHPRDYMESMEAALKAVLAQlSAAQRA 78
Cdd:cd07779 3 LGIDVGTTSTRAIIFD-LDGNIVASGYREYPPyypepgWVE------------QDPDDWWDALCEALKEAVAK-AGVDPE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 79 NVVGIGVDSTGSTPAPIDADGNvlALRPefaenpnamFVLWKDhtaveeadeiTRlchkpgkvdySRYIGGIysSEWFwa 158
Cdd:cd07779 69 DIAAIGLTSQRSTFVPVDEDGR--PLRP---------AISWQD----------KR----------TAKFLTV--QDYL-- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 159 kILHVTRQdsavaqaavswiELCDWVPALLSGttrPQDIRRGRCSAGHktlwhESWGGLPPASFFDELDPCInrhlrypl 238
Cdd:cd07779 114 -LYRLTGE------------FVTDTTSASRTG---LPDIRTRDWSDDL-----LDAFGIDRDKLPELVPPGT-------- 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 239 fsetftadlPVGTLCAEWAQRLGLPESV-VISGGAfD--ChmGAVGAGA-QPNTLVKVIGTSTCDILIADKqSVGDRAVK 314
Cdd:cd07779 165 ---------VIGTLTKEAAEETGLPEGTpVVAGGG-DqqC--AALGAGVlEPGTASLSLGTAAVVIAVSDK-PVEDPERR 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 315 GICGqvdGSVVPNFIGLEAGQSAFGDIYAWFSRVLSWPLEQLAAQHPELKTQINASqkqllpaltdAWAKNPSLDHLpVV 394
Cdd:cd07779 232 IPCN---PSAVPGKWVLEGSINTGGSAVRWFRDEFGQDEVAEKELGVSPYELLNEE----------AAKSPPGSDGL-LF 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 395 LDWFNGRRTPNANQRLKGVITDLNLATDAPALFGGLVASTAFGARAIQECFTDQGIAVNNVMALGGIArKNQVIMQVCCD 474
Cdd:cd07779 298 LPYLAGAGTPYWNPEARGAFIGLTLSHTRAHLARAILEGIAFELRDNLEAMEKAGVPIEEIRVSGGGS-KSDLWNQIIAD 376
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 340763515 475 VLNRPLQIVASDQCCALGAAIFAAVAAKVHADIPAAQQSMaSAVERTLRPRPEQAQR 531
Cdd:cd07779 377 VFGRPVERPETSEATALGAAILAAVGAGIYPDFEEAVKAM-VRVTDTFEPDPENVAI 432
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
5-492 |
2.24e-23 |
|
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: 103.01 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 5 IGLDFGSDSVRALAVDCATGDEIATSveWYPrWQEGRYCDGPNNQfrhHPRDYMESMEAALKAVLAQLSaAQRANVVGIG 84
Cdd:cd07809 3 LGIDLGTQSIKAVLIDAETGRVVASG--SAP-HENILIDPGWAEQ---DPEDWWDALQAAFAQLLKDAG-AELRDVAAIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 85 VDSTGSTPAPIDADGNVlaLRPefaenpnamFVLWKDHTAVEEADEITRLCHKPGKVDYSRYIGGIYSSewfwAKILHVT 164
Cdd:cd07809 76 ISGQMHGLVALDADGKV--LRP---------AKLWCDTRTAPEAEELTEALGGKKCLLVGLNIPARFTA----SKLLWLK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 165 RQDSAVAqAAVSWIEL-CDWVPALLSGTTRpqdIRRGRCSAghkTLW----HESWGGLPPASFFDELDPCInrhlrypLF 239
Cdd:cd07809 141 ENEPEHY-ARIAKILLpHDYLNWKLTGEKV---TGLGDASG---TFPidprTRDYDAELLAAIDPSRDLRD-------LL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 240 SETFTADLPVGTLCAEWAQRLGLPESVVISGGAFDCHMGAVGAGA-QPNTLVKVIGTSTCDILIADKQSVGDR-AVKGIC 317
Cdd:cd07809 207 PEVLPAGEVAGRLTPEGAEELGLPAGIPVAPGEGDNMTGALGTGVvNPGTVAVSLGTSGTAYGVSDKPVSDPHgRVATFC 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 318 GqVDGSVVPNFIGLeagqsafGDIYAW---FSRVLSWP---LEQLAAQHPelktqinasqkqllpaltdawAKNPSLdhl 391
Cdd:cd07809 287 D-STGGMLPLINTT-------NCLTAWtelFRELLGVSyeeLDELAAQAP---------------------PGAGGL--- 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 392 pVVLDWFNGRRTPNaNQRLKGVITDLNLATDAPALFgglvastafgARAIQE-----------CFTDQGIAVNNVMALGG 460
Cdd:cd07809 335 -LLLPFLNGERTPN-LPHGRASLVGLTLSNFTRANL----------ARAALEgatfglrygldILRELGVEIDEIRLIGG 402
|
490 500 510
....*....|....*....|....*....|..
gi 340763515 461 IArKNQVIMQVCCDVLNRPLQIVASDQCCALG 492
Cdd:cd07809 403 GS-KSPVWRQILADVFGVPVVVPETGEGGALG 433
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
5-475 |
2.75e-22 |
|
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: 100.56 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 5 IGLDFGSDSVRALAVDcATGDEIATSVEWYPRWQEgrycdgPNNQFRH--HPRDYMESMEAALKAVLAQLSAAQranVVG 82
Cdd:cd07778 3 IGIDVGSTSVRIGIFD-YHGTLLATSERPISYKQD------PKDLWFVtqSSTEIWKAIKTALKELIEELSDYI---VSG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 83 IGVDSTGSTPA--PIDADGNVLALRPEFAE-NPNAMFVLWKDHTAVEEADEITRLChkpgKVDYSRYIGGIYSSEWFWAK 159
Cdd:cd07778 73 IGVSATCSMVVmqRDSDTSYLVPYNVIHEKsNPDQDIIFWMDHRASEETQWLNNIL----PDDILDYLGGGFIPEMAIPK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 160 ILHVTRQDSAVAQAAVSWIELCDWVPALLS-----GTTRPQDIRRGRCSAGHKTL--WHES---WGGLPPASFFDELDPc 229
Cdd:cd07778 149 LKYLIDLIKEDTFKKLEVFDLHDWISYMLAtnlghSNIVPVNAPPSIGIGIDGSLkgWSKDfysKLKISTKVCNVGNTF- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 230 iNRHLRYPLFSetftadLPVGTLCAEWAQRLGLPESVVISGGAFDCHMGAVG----AGAQPNTLVKVIGTSTCDILIAdk 305
Cdd:cd07778 228 -KEAPPLPYAG------IPIGKVNVILASYLGIDKSTVVGHGCIDCYAGWFStfaaAKTLDTTLFMVAGTSTCFLYAT-- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 306 QSVGDRAVKGICGQVDgSVVPNFIGLEAGQSAFGdiyawfsrVLswpLEQLAAQHPELKTQI--NASQKQLLPALTDAWA 383
Cdd:cd07778 299 SSSQVGPIPGIWGPFD-QLLKNYSVYEGGQSATG--------KL---IEKLFNSHPAIIELLksDANFFETVEEKIDKYE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 384 K--NPSLDHLpvVLDWF-----NGRRTPNANQRLKGVITDlnlATDAPALFgGLVAS-------TAFGARAIQECFTDQG 449
Cdd:cd07778 367 RllGQSIHYL--TRHMFfygdyLGNRTPYNDPNMSGSFIG---ESTDSSLT-DLVLKyililefLAFQTKLIIDNFQKEK 440
|
490 500 510
....*....|....*....|....*....|
gi 340763515 450 IAVNNVMALGGIArKN----QVIMQVCCDV 475
Cdd:cd07778 441 IIIQKVVISGSQA-KNarllQLLSTVLSKI 469
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
5-541 |
5.64e-22 |
|
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: 99.17 E-value: 5.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 5 IGLDFGSDSVRALAVDcATGDEIATSVEWYP------RWQEgrycdgpnnqfrHHPRDYMESMEAALKAVLAQLsaaQRA 78
Cdd:cd07770 3 LGIDIGTTSTKAVLFD-EDGRVVASSSAEYPlirpepGWAE------------QDPEEILEAVLEALKEVLAKL---GGG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 79 NVVGIGVDSTGSTPAPIDADGNVLAlrpefaenpNAMfvLWKDHTAVEEADEITRlcHKPGKVDYSRyiGG--IYSSEWF 156
Cdd:cd07770 67 EVDAIGFSSAMHSLLGVDEDGEPLT---------PVI--TWADTRAAEEAERLRK--EGDGSELYRR--TGcpIHPMYPL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 157 wAKILHVTRQDSAVAQAAVSWIELCDWV-----------PALLSGTtrpQ--DIRRGRcsaghktlWHE---SWGGLPPA 220
Cdd:cd07770 132 -AKLLWLKEERPELFAKAAKFVSIKEYLlyrltgelvtdYSTASGT---GllNIHTLD--------WDEealELLGIDEE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 221 SFfDELDPCinrhlryplfsetftaDLPVGTLCAEWAQRLGLPESVVISGGAFDchmGA---VGAGA-QPNTLVKVIGTS 296
Cdd:cd07770 200 QL-PELVDP----------------TEVLPGLKPEFAERLGLLAGTPVVLGASD---GAlanLGSGAlDPGRAALTVGTS 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 297 -----TCDILIADKQsvgdravKGI-CGQVDGSVVpnFIGleagqSAF---GDIYAWFsrvlswpLEQLAAQHPElktqi 367
Cdd:cd07770 260 gairvVSDRPVLDPP-------GRLwCYRLDENRW--LVG-----GAInngGNVLDWL-------RDTLLLSGDD----- 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 368 nasqkqllPALTDAWA-KNPSLDHLPVVLDWFNGRRTPNANQRLKGVITDLNLATDAPALFGGLVASTAFGARAIQECFT 446
Cdd:cd07770 314 --------YEELDKLAeAVPPGSHGLIFLPYLAGERAPGWNPDARGAFFGLTLNHTRADILRAVLEGVAFNLKSIYEALE 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 447 DQGIAVNNVMALGGIARkNQVIMQVCCDVLNRPLQIVASDQCCALGAAIFAAVAAKVHADIPAAQqsmASAVERTLRPRP 526
Cdd:cd07770 386 ELAGPVKEIRASGGFLR-SPLWLQILADVLGRPVLVPEEEEASALGAALLALEALGLISSLEADE---LVKIGKVVEPDP 461
|
570
....*....|....*
gi 340763515 527 EQAQRLEQLYRRYQQ 541
Cdd:cd07770 462 ENHAIYAELYERFKK 476
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
5-492 |
1.55e-16 |
|
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: 82.21 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 5 IGLDFGSDSVRALAVDcATGDEIATSvewyprwqeGRYCDGPNNQFRHHPRDyMESMEAALKAVLAQLSAAQR---ANVV 81
Cdd:cd07802 3 LGIDNGTTNVKAVLFD-LDGREIAVA---------SRPTPVISPRPGWAERD-MDELWQATAEAIRELLEKSGvdpSDIA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 82 GIGVDSTGSTPAPIDADGNvlALRpefaenpNAmfVLWKDHTAVEEADEITRlchkpgkvdysryiGGIYssewfwAKIL 161
Cdd:cd07802 72 GVGVTGHGNGLYLVDKDGK--PVR-------NA--ILSNDSRAADIVDRWEE--------------DGTL------EKVY 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 162 HVTRQD----SAVAQ------------AAVSWIELC-DWVPALLSG---------TTRPQDIRRGRCSaghktlwHE--S 213
Cdd:cd07802 121 PLTGQPlwpgQPVALlrwlkeneperyDRIRTVLFCkDWIRYRLTGeistdytdaGSSLLDLDTGEYD-------DEllD 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 214 WGGLPPAsffdeldpcinrhlrYPLFSETFTADLPVGTLCAEWAQRLGLPESVVISGGAFDCHMGAVGAGA-QPNTLVKV 292
Cdd:cd07802 194 LLGIEEL---------------KDKLPPLVPSTEIAGRVTAEAAALTGLPEGTPVAAGAFDVVASALGAGAvDEGQLCVI 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 293 IGTSTCDILIADKQSVGDRAVKGICGQVDGSvvpnFIGLEAGQSAfgdiyawfSRVLSWPLEQLAAqhpelktQINASQK 372
Cdd:cd07802 259 LGTWSINEVVTDEPVVPDSVGSNSLHADPGL----YLIVEASPTS--------ASNLDWFLDTLLG-------EEKEAGG 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 373 QLLPALTDAWAKNPSLDHLPVVLDWFNGrrtPNANQRLKGVITDLNLATDAPALFGGLVASTAFGARAIQEcFTDQGIAV 452
Cdd:cd07802 320 SDYDELDELIAAVPPGSSGVIFLPYLYG---SGANPNARGGFFGLTAWHTRAHLLRAVYEGIAFSHRDHLE-RLLVARKP 395
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 340763515 453 NNVMALGGIARkNQVIMQVCCDVLNRPLQIVASDQCCALG 492
Cdd:cd07802 396 ETIRLTGGGAR-SPVWAQIFADVLGLPVEVPDGEELGALG 434
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
5-492 |
1.86e-15 |
|
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: 78.80 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 5 IGLDFGSDSVRALAVDCATGDEIATSVEW-------YPrwqEGRYCDgpnnqfrhhPRDYMESMEAALKAVLAQlSAAQR 77
Cdd:cd07798 3 LVIDIGTGGGRCALVDSEGKIVAIAYREWeyytdddYP---DAKEFD---------PEELWEKICEAIREALKK-AGISP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 78 ANVVGIGVDSTGSTPAPIDADGNVL-ALrpefaenPNamfvlwKDHTAVEEADEITRlchKPGKVDYSryIGGIYSSEWF 156
Cdd:cd07798 70 EDISAVSSTSQREGIVFLDKDGRELyAG-------PN------IDARGVEEAAEIDD---EFGEEIYT--TTGHWPTELF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 157 -WAKILHVTRQDSAVAQAAVSWIELCDWVPALLSGT----------TRPQDIRRGRcsaghktlWHESWgglppasfFDE 225
Cdd:cd07798 132 pAARLLWFKENRPEIFERIATVLSISDWIGYRLTGElvsepsqaseTQLFDIKKRE--------WSQEL--------LEA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 226 LDpcinrhLRYPLFSETFTADLPVGTLCAEWAQRLGLPESV-VISGGAfDCHMGAVGAGAQ-PNTLVKVIGTST-----C 298
Cdd:cd07798 196 LG------LPPEILPEIVPSGTVLGTVSEEAARELGLPEGTpVVVGGA-DTQCALLGSGAIePGDIGIVAGTTTpvqmvT 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 299 DILIADKQ--------SVGDRAVkgicgqvdgsvvpnfigLEAGQSAFGDIYAWFSRVLSWP-------LEQLAAQHPEL 363
Cdd:cd07798 269 DEPIIDPErrlwtgchLVPGKWV-----------------LESNAGVTGLNYQWLKELLYGDpedsyevLEEEASEIPPG 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 364 KTQINASqkqLLPALTDAwAKNPSLDHLPVVldwfngrRTPNANQRLkgvitdlnlatDAPALFGGLVASTAFGARA-IQ 442
Cdd:cd07798 332 ANGVLAF---LGPQIFDA-RLSGLKNGGFLF-------PTPLSASEL-----------TRGDFARAILENIAFAIRAnLE 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 340763515 443 ECFTDQGIAVNNVMALGGIARkNQVIMQVCCDVLNRPLQIVASDQCCALG 492
Cdd:cd07798 390 QLEEVSGREIPYIILCGGGSR-SALLCQILADVLGKPVLVPEGREASALG 438
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
5-541 |
3.31e-09 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 59.21 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 5 IGLDFGSDSVRALAVDcATGDEIATSVEW------YPRWQEgrycdgpnnqfrHHPRDYMESMEAALKAvLAQLSAAQRA 78
Cdd:PRK15027 3 IGIDLGTSGVKVILLN-EQGEVVASQTEKltvsrpHPLWSE------------QDPEQWWQATDRAMKA-LGDQHSLQDV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 79 NVVGIGVDSTGSTPapIDADGNVLalRPEfaenpnamfVLWKDHTAVEEADEITRlchkpgKVDYSRYIGGIYSSEWFWA 158
Cdd:PRK15027 69 KALGIAGQMHGATL--LDAQQRVL--RPA---------ILWNDGRCAQECALLEA------RVPQSRVITGNLMMPGFTA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 159 -KILHVTRQDSAVAQAAVSwielcdwvpALLsgttrPQDIRRGRCSAGHKTLWHES----WGGLPPASFFDE-LDPCinr 232
Cdd:PRK15027 130 pKLLWVQRHEPEIFRQIDK---------VLL-----PKDYLRLRMTGEFASDMSDAagtmWLDVAKRDWSDVmLQAC--- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 233 HLRYPLFSETFTADLPVGTLCAEWAQRLGLPESVVISGGAfDCHMGAVGAG-AQPNTLVKVIGTSTCDILIADK-QSVGD 310
Cdd:PRK15027 193 HLSRDQMPALYEGSEITGALLPEVAKAWGMATVPVVAGGG-DNAAGAVGVGmVDANQAMLSLGTSGVYFAVSEGfLSKPE 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 311 RAVKGICGQVDGSVVPNFIGLEAgqsafgdiyawfSRVLSWpleqlAAQHPELKTqinasqkqlLPALTDAwAKNPSLDH 390
Cdd:PRK15027 272 SAVHSFCHALPQRWHLMSVMLSA------------ASCLDW-----AAKLTGLSN---------VPALIAA-AQQADESA 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 391 LPV-VLDWFNGRRTPNANQRLKGVITDLNL----ATDAPALFGGLVASTAFGARAIQECftdqGIAVNNVMALGGIARkN 465
Cdd:PRK15027 325 EPVwFLPYLSGERTPHNNPQAKGVFFGLTHqhgpNELARAVLEGVGYALADGMDVVHAC----GIKPQSVTLIGGGAR-S 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 466 QVIMQVCCDVLNRPLQI-VASDQCCALGAAIFAAVAakVHADIPAAQQSMASAVERTLRPRPEQ----AQRLEQLYRRYQ 540
Cdd:PRK15027 400 EYWRQMLADISGQQLDYrTGGDVGPALGAARLAQIA--ANPEKSLIELLPQLPLEQSHLPDAQRyaayQPRRETFRRLYQ 477
|
.
gi 340763515 541 Q 541
Cdd:PRK15027 478 Q 478
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
3-281 |
2.97e-08 |
|
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: 54.65 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 3 IAIGLDFGSDSVRALAVDcATGDEIATSVEWY------PRWQEgrycdgpnnqfrHHPRDYMESMEAALKAVLAQLSAAQ 76
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFN-EQGKIIAVAQLENpqitphPGWAE------------QDPDEIWQAVAQCIAKTLSQLGISL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 77 RaNVVGIGVDSTGSTPAPIDADGNVLAlrpefaenpNAmfVLWKDHTAVEEADEITRlchkPGKVDYSRYIGGIYSSEWF 156
Cdd:pfam00370 68 K-QIKGIGISNQGHGTVLLDKNDKPLY---------NA--ILWKDRRTAEIVENLKE----EGNNQKLYEITGLPIWPGF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 157 WAKILH-VTRQDSAVAQAAVSWIELCDWVPALLSG--TTRPQDIRRgrcsaghkTLWheswgglppasfFD----ELDPC 229
Cdd:pfam00370 132 TLSKLRwIKENEPEVFEKIHKFLTIHDYLRWRLTGvfVTDHTNASR--------SMM------------FNihklDWDPE 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 340763515 230 INRHLRYP--LFSETFTADLPVGTLCAEWAQRLGLPESVVISGGAFDCHMGAVG 281
Cdd:pfam00370 192 LLAALGIPrdHLPPLVESSEIYGELNPELAAMWGLDEGVPVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
5-495 |
2.23e-05 |
|
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: 47.23 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 5 IGLDFGSDSVRALAVDcATGDEIATSVEwyprwqegrycdgPNNQFRHHPRDYMESMEA-------ALKAVLAQLSAAQR 77
Cdd:cd24121 3 IGIDAGTSVVKAVAFD-LDGRELAVAAR-------------RNAVLYPQPGWAEQDMNEtwqavvaTIREVVAKLDVLPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 78 AnVVGIGVDSTGSTPAPIDADGNvlALRPEfaenpnamfVLWKDHTAveeADEITRLCHKPGKVDYSRYIGGIYSSEWFW 157
Cdd:cd24121 69 R-VAAIGVTGQGDGTWLVDEDGR--PVRDA---------ILWLDGRA---ADIVERWQADGIAEAVFEITGTGLFPGSQA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 158 AKILHVTRQDSAVAQAAvSWIELC-DWVPALLSG--TTRPQDirrgrcsAGHktlwheSWGGLPPASFFDELDPCINRHL 234
Cdd:cd24121 134 AQLAWLKENEPERLERA-RTALHCkDWLFYKLTGeiATDPSD-------ASL------TFLDFRTRQYDDEVLDLLGLEE 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 235 RYPLFSETFTADLPVGTLCAEWAQRLGLPESVVISGGAFDCHMGAVGAGA-QPNTLVKVIGTSTCDILIADKQSVGDRAV 313
Cdd:cd24121 200 LRHLLPPIRPGTEVIGPLTPEAAAATGLPAGTPVVLGPFDVVATALGSGAiEPGDACSILGTTGVHEVVVDEPDLEPEGV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 314 KG-ICGQVDGSVVpnfigleagqSAFGDIYAwfSRVLSWPLEQLAAQhpeLKTQINASQKQLLPALtDAWAKN--PSLD- 389
Cdd:cd24121 280 GYtICLGVPGRWL----------RAMANMAG--TPNLDWFLRELGEV---LKEGAEPAGSDLFQDL-EELAASspPGAEg 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 390 --HLPVVLDwfNGRRTPNANQRLKGVITDLNLATDAPALFGGLVASTAFGARaiqECFTDQGIAVNNVMALGGIARKNQV 467
Cdd:cd24121 344 vlYHPYLSP--AGERAPFVNPNARAQFTGLSLEHTRADLLRAVYEGVALAMR---DCYEHMGEDPGELRLSGGGARSDTW 418
|
490 500
....*....|....*....|....*...
gi 340763515 468 iMQVCCDVLNRPLQIVASDQCCALGAAI 495
Cdd:cd24121 419 -CQILADALGVPVRVPAGEEFGARGAAM 445
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
238-520 |
3.61e-04 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 43.09 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 238 LFSETFTADLPVGTLCAEWAQRLGLPESV-VISGGaFDCHMGAVGAGAQPNTlvKVIGTSTCDILIADKQsvgdravkgi 316
Cdd:PRK10331 204 LFPRLVEAGEQIGTLQPSAAALLGLPVGIpVISAG-HDTQFALFGSGAGQNQ--PVLSSGTWEILMVRSA---------- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 317 cgQVDGSVVPNFIG----LEAGQSAFGDIYAWF-SRVLSWpleqlaaqhpelktqinasQKQLLPALTDAWaknPSLDHl 391
Cdd:PRK10331 271 --QVDTSLLSQYAGstceLDSQSGLYNPGMQWLaSGVLEW-------------------VRKLFWTAETPY---QTMIE- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 392 pvvldwfNGRRTPNANQrlkGVITDLNLATDAPALFGGLVASTAFG--ARAIQECFTDQ------------GIAVNNVMA 457
Cdd:PRK10331 326 -------EARAIPPGAD---GVKMQCDLLACQNAGWQGVTLNTTRGhfYRAALEGLTAQlkrnlqvlekigHFKASELLL 395
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 340763515 458 LGGIARkNQVIMQVCCDVLNRPLQIVASDQCCALGAAIFAAVAAKVHADIPAAQQSMASAVER 520
Cdd:PRK10331 396 VGGGSR-NALWNQIKANMLDIPIKVLDDAETTVAGAAMFGWYGVGEFSSPEQARAQMKYQYRY 457
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
417-539 |
5.75e-04 |
|
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: 42.70 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 417 LNLATDAP-----ALFGGLVASTAFGARA----IQECFtdqGIAVNNVMALGGiARKNQVIMQVCCDVLNRPLQIVASDQ 487
Cdd:cd07775 366 LNLDIDPEkcnkaTFFRAIMENAAIVSAGnlerIAEFS---GIFPDSLVFAGG-ASKGKLWCQILADVLGLPVKVPVVKE 441
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 340763515 488 CCALGAAIFAAVAAKVHADIPAAQQSMASaVERTLRPRPEQAQRLEQLYRRY 539
Cdd:cd07775 442 ATALGAAIAAGVGAGIYSSLEEAVESLVK-WEREYLPNPENHEVYQDLYEKW 492
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
3-85 |
7.38e-04 |
|
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: 42.21 E-value: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 3 IAIGLDFGSDSVRALAVDCATGDEIATSVEWYPRWQEGRYCdgpnnqfRHHPRDyMESMEAALKAVLAQLSAAQRANVVG 82
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDLESGRILESVSRPTPAPISSDDP-------GRSEQD-PEKILEAVRNLIDELPREYLSDVTG 72
|
...
gi 340763515 83 IGV 85
Cdd:cd07777 73 IGI 75
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-102 |
2.96e-03 |
|
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];
Pssm-ID: 441543 [Multi-domain] Cd Length: 306 Bit Score: 39.88 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 340763515 1 MAIAIGLDFGSDSVRALAVDcATGDEIATSVEWYPRWQEgrycdgpnnqfrhhPRDYMESMEAALKAVLAQLSaAQRANV 80
Cdd:COG1940 4 AGYVIGIDIGGTKIKAALVD-LDGEVLARERIPTPAGAG--------------PEAVLEAIAELIEELLAEAG-ISRGRI 67
|
90 100
....*....|....*....|..
gi 340763515 81 VGIGVdstgSTPAPIDADGNVL 102
Cdd:COG1940 68 LGIGI----GVPGPVDPETGVV 85
|
|
| |
