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Conserved domains on  [gi|12698097|dbj|BAB21875|]
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hypothetical protein [Macaca fascicularis]

Protein Classification

shikimate kinase( domain architecture ID 10087470)

shikimate kinase catalyzes the specific phosphorylation of the 3-hydroxylgroup of shikimic acid using ATP as a cosubstrate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thr-synth_2 cd01560
Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of ...
 230-733 0e+00

Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of O-phosphohomoserine into threonine and inorganic phosphate is pyridoxal 5'-phosphate dependent. The Thr-synth_1 CD includes members from higher plants, cyanobacteria, archaebacteria and eubacterial groups. This CD, Thr-synth_2, includes enzymes from fungi and eubacterial groups, as well as, metazoan threonine synthase-like proteins.


:

Pssm-ID: 107203 [Multi-domain]  Cd Length: 460  Bit Score: 594.99  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 230 TFISTRHVWPKdceqkVSakfFSEAVIEGLASDGGLFVPAkEFPKLSCGEWKSLVGATYIERAQILLERCIhPADIPAAR 309
Cdd:cd01560   1 KYVSTRGGNPG-----VS---FSEALLSGLAPDGGLYVPE-ELPKLSAEEIASWSGLSYQELAFEVLSLFI-GDEIPEDD 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 310 LGEMIETAYGEnFACSKIAPVRHLSGNQFILELFHGPTGSFKDLSLQLMPHIFAHCIPP-SCNYMILVATSGDTGSAVLN 388
Cdd:cd01560  71 LKSLIDRAYSF-FRHPDIAPLVQLGDNLYVLELFHGPTLAFKDMALQFLGRLLEYFLKRrNERITILVATSGDTGSAAIE 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 389 GFSrlnknDKQRIAVVTFFPENGVSDFQKAQIIGSQRENGWAVGVESDFDFCQTAIKRIFNDSDFTgfltveYGTILSSA 468
Cdd:cd01560 150 GFR-----GKPNVDVVVLYPKGGVSPIQELQMTTLPADNVHVVAVEGDFDDCQSLVKALFADEDFN------KKLKLSSA 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 469 NSINWGRLLPQVVYHASAYLDLVSQGFisfGSPVDVCIPTGNFGNILAAVYAKMMGIPIRKFICASNQNRVLTDFIKTGH 548
Cdd:cd01560 219 NSINWARILAQIVYYFYAYLQLLKRGE---GEKVEFSVPTGNFGNILAGYYAKKMGLPIKKLIVATNENDVLRRFFKTGR 295

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 549 YDLRErKLAQTFSPSIDILKSSNLERHLHLMANKDGQLMTELFNQLESQHHFQIEKVLVEKLQQDFVADWCSEGECLAAI 628
Cdd:cd01560 296 YDRRE-SLKQTLSPAMDILKSSNFERLLFLLAGRDRTKVKMLMEEFEATGFLSLPKEELKKLREDFSSGSVSDEETLETI 374

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 629 NSTYNTSGYILDPHTAVAKVVADRVQDK-TCPVIVSSTAHYSKFAPAIMQALKIKEInetsssqlyllgsynALPPLHEA 707
Cdd:cd01560 375 REVYEETGYLIDPHTAVGVRAAERVRKSpGTPGVVLSTAHPAKFPEAVKEALGEEPV---------------ELPEELEG 439

                       490       500
                ....*....|....*....|....*.
gi 12698097 708 LLERTKQQEKMEyqvcaADMNVLKSH 733
Cdd:cd01560 440 LEDLEKRHEDLL-----ADKELLKSH 460
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 57-211 4.32e-41

Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.


:

Pssm-ID: 238260 [Multi-domain]  Cd Length: 154  Bit Score: 147.32  E-value: 4.32e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097  57 NIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSAS-GSVISLTGSN 135
Cdd:cd00464   1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLDELI-EQRAGMSIPEIFAEEGEEGFRELEREVLLLLLTKeNAVIATGGGA 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12698097 136 PMHDASMWHLKKNGVIVYLDVPLLDLIHRLKLMKIDRIVGRNSGTSMKDLLKFRRQYYKKWYDARVFCEsGASPEE 211
Cdd:cd00464  80 VLREENRRLLLENGIVVWLDASPEELLERLARDKTRPLLQDEDPERLRELLEEREPLYREVADLTIDTD-ELSPEE 154
 
Name Accession Description Interval E-value
Thr-synth_2 cd01560
Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of ...
 230-733 0e+00

Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of O-phosphohomoserine into threonine and inorganic phosphate is pyridoxal 5'-phosphate dependent. The Thr-synth_1 CD includes members from higher plants, cyanobacteria, archaebacteria and eubacterial groups. This CD, Thr-synth_2, includes enzymes from fungi and eubacterial groups, as well as, metazoan threonine synthase-like proteins.


Pssm-ID: 107203 [Multi-domain]  Cd Length: 460  Bit Score: 594.99  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 230 TFISTRHVWPKdceqkVSakfFSEAVIEGLASDGGLFVPAkEFPKLSCGEWKSLVGATYIERAQILLERCIhPADIPAAR 309
Cdd:cd01560   1 KYVSTRGGNPG-----VS---FSEALLSGLAPDGGLYVPE-ELPKLSAEEIASWSGLSYQELAFEVLSLFI-GDEIPEDD 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 310 LGEMIETAYGEnFACSKIAPVRHLSGNQFILELFHGPTGSFKDLSLQLMPHIFAHCIPP-SCNYMILVATSGDTGSAVLN 388
Cdd:cd01560  71 LKSLIDRAYSF-FRHPDIAPLVQLGDNLYVLELFHGPTLAFKDMALQFLGRLLEYFLKRrNERITILVATSGDTGSAAIE 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 389 GFSrlnknDKQRIAVVTFFPENGVSDFQKAQIIGSQRENGWAVGVESDFDFCQTAIKRIFNDSDFTgfltveYGTILSSA 468
Cdd:cd01560 150 GFR-----GKPNVDVVVLYPKGGVSPIQELQMTTLPADNVHVVAVEGDFDDCQSLVKALFADEDFN------KKLKLSSA 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 469 NSINWGRLLPQVVYHASAYLDLVSQGFisfGSPVDVCIPTGNFGNILAAVYAKMMGIPIRKFICASNQNRVLTDFIKTGH 548
Cdd:cd01560 219 NSINWARILAQIVYYFYAYLQLLKRGE---GEKVEFSVPTGNFGNILAGYYAKKMGLPIKKLIVATNENDVLRRFFKTGR 295

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 549 YDLRErKLAQTFSPSIDILKSSNLERHLHLMANKDGQLMTELFNQLESQHHFQIEKVLVEKLQQDFVADWCSEGECLAAI 628
Cdd:cd01560 296 YDRRE-SLKQTLSPAMDILKSSNFERLLFLLAGRDRTKVKMLMEEFEATGFLSLPKEELKKLREDFSSGSVSDEETLETI 374

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 629 NSTYNTSGYILDPHTAVAKVVADRVQDK-TCPVIVSSTAHYSKFAPAIMQALKIKEInetsssqlyllgsynALPPLHEA 707
Cdd:cd01560 375 REVYEETGYLIDPHTAVGVRAAERVRKSpGTPGVVLSTAHPAKFPEAVKEALGEEPV---------------ELPEELEG 439

                       490       500
                ....*....|....*....|....*.
gi 12698097 708 LLERTKQQEKMEyqvcaADMNVLKSH 733
Cdd:cd01560 440 LEDLEKRHEDLL-----ADKELLKSH 460
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 251-682 1.48e-66

Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the Pathway/BioSystem: Threonine biosynthesis


Pssm-ID: 440264 [Multi-domain]  Cd Length: 394  Bit Score: 225.46  E-value: 1.48e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 251 FSEAVIEGLASDGGLfVPAkEFPKLSCGEWKSLVG-ATYIEraqiLLercihPADIPAARLgemietAYGENFA----CS 325
Cdd:COG0498  11 FSDALLYLCPDCGGL-LPD-SYPALSREDLASRRGlWRYRE----LL-----PFDDEEKAV------SLGEGGTplvkAP 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 326 KIApvRHLSGNQFILELFHGPTGSFKDLSLQLMPHIFAHcippSCNYMILVATSGdTGSAVLNGFSrlnknDKQRIAVVT 405
Cdd:COG0498  74 RLA--DELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALE----RGAKTIVCASSG-NGSAALAAYA-----ARAGIEVFV 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 406 FFPENGVSDFQKAQII--GSQrengwAVGVESDFDFCQTAIKRIFNDSDFtgfltveygtilSSANSINWGRLLPQVVYH 483
Cdd:COG0498 142 FVPEGKVSPGQLAQMLtyGAH-----VIAVDGNFDDAQRLVKELAADEGL------------YAVNSINPARLEGQKTYA 204

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 484 ASAYLDLVSqgfisfgSPVDVCIPTGNFGNILAAVYAKMM----GIPIR--KFI--CASNQNRVLTDFiKTGHyDLRERK 555
Cdd:COG0498 205 FEIAEQLGR-------VPDWVVVPTGNGGNILAGYKAFKElkelGLIDRlpRLIavQATGCNPILTAF-ETGR-DEYEPE 275

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 556 LAQTFSPSIDILKSSNLERHLHLMANKDGqlmtelfnqlesqhhfqiekvlveklqqdfVADWCSEGECLAAINSTYNTS 635
Cdd:COG0498 276 RPETIAPSMDIGNPSNGERALFALRESGG------------------------------TAVAVSDEEILEAIRLLARRE 325

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|..
gi 12698097 636 GYILDPHTAVA-----KVVADRVQDKTCPVIVSSTAHYSKFAPAIMQALKIK 682
Cdd:COG0498 326 GIFVEPATAVAvaglrKLREEGEIDPDEPVVVLSTGHGLKFPDAVREALGGE 377
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 57-211 4.32e-41

Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.


Pssm-ID: 238260 [Multi-domain]  Cd Length: 154  Bit Score: 147.32  E-value: 4.32e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097  57 NIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSAS-GSVISLTGSN 135
Cdd:cd00464   1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLDELI-EQRAGMSIPEIFAEEGEEGFRELEREVLLLLLTKeNAVIATGGGA 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12698097 136 PMHDASMWHLKKNGVIVYLDVPLLDLIHRLKLMKIDRIVGRNSGTSMKDLLKFRRQYYKKWYDARVFCEsGASPEE 211
Cdd:cd00464  80 VLREENRRLLLENGIVVWLDASPEELLERLARDKTRPLLQDEDPERLRELLEEREPLYREVADLTIDTD-ELSPEE 154
SKI pfam01202
Shikimate kinase;
64-221 2.13e-40

Shikimate kinase;


Pssm-ID: 426122 [Multi-domain]  Cd Length: 159  Bit Score: 145.42  E-value: 2.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097    64 PGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSAS-GSVISLTGSNPMHDASM 142
Cdd:pfam01202   1 MGAGKSTIGRLLAKALGLPFIDTDEEI-EKRTGMSIAEIFEEEGEEGFRRLESEVLKELLAEhGLVIATGGGAVLSEENR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   143 WHLKKNGVIVYLDVPLLDLIHRLKlMKIDRIV--GRNSGTSMKDLLKFRRQY-YKKwYDARVFCESGASPEEVADKVLNA 219
Cdd:pfam01202  80 DLLKERGIVIYLDAPLEVLLERLK-RDKTRPLlqNKDPEEELLELLFEERDPlYEE-AADIVIDTDESSPEEVATEILEA 157


                  ..
gi 12698097   220 IK 221
Cdd:pfam01202 158 LE 159
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
 289-670 5.47e-37

threonine synthase; Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 272986 [Multi-domain]  Cd Length: 327  Bit Score: 141.37  E-value: 5.47e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   289 IERAQILLErcihPADIPAARLGEMIEtaygENFACSKIaPVRHLSGNQFILELFHGPTGSFKDLSLQLMphiFAHcIPP 368
Cdd:TIGR00260   1 VWRYREFLP----VTEKDLVDLGEGVT----PLFRAPAL-AANVGIKNLYVKELGHNPTLSFKDRGMAVA---LTK-ALE 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   369 SCNYMILVATSGDTGSAVLNGFSRLNKNdkqriaVVTFFPENGVSDFQKAQIIGsqrENGWAVGVESDFDFCQTAIKRIF 448
Cdd:TIGR00260  68 LGNDTVLCASTGNTGAAAAAYAGKAGLK------VVVLYPAGKISLGKLAQALG---YNAEVVAIDGNFDDAQRLVKQLF 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   449 NDSdftgfltveYGTILSSANSInWGRLLPQvVYHASAYLDLVSQgfisfGSPVDVCIP---TGNFGNILAAVYAKMMG- 524
Cdd:TIGR00260 139 EDK---------PALGLNSANSI-PYRLEGQ-KTYAFEAVEQLGW-----EAPDKVVVPvpnSGNFGAIWKGFKEKKMLg 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   525 ---IPIRKFICASNQNRVLTDFIKTGHYDLRERKlaQTFSPSIDILKSSNLERHLHLMANKDGQlMTELfnqlesqhhfq 601
Cdd:TIGR00260 203 ldsLPVKRGIQAEGAADIVRAFLEGGQWEPIETP--ETLSTAMDIGNPANWPRALEAFRRSNGY-AEDL----------- 268

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12698097   602 iekvlveklqqdfvadwcSEGECLAAINSTYNTSGYILDPHTAVAKVVADRVQDKTcpvivssTAHYSK 670
Cdd:TIGR00260 269 ------------------SDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVEKG-------TADPAE 312
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
 58-222 4.37e-35

Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440467 [Multi-domain]  Cd Length: 165  Bit Score: 130.63  E-value: 4.37e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097  58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSA-SGSVISLTGSNP 136
Cdd:COG0703   1 IVLIGMMGAGKSTVGRLLAKRLGLPFVDTDAEI-EERAGMSIPEIFAEEGEAGFRELEREVLAELLEeENAVIATGGGAV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 137 MHDASMWHLKKNGVIVYLDVPLLDLIHRLKLMKiDR--IVGRNSGTSMKDLLKFRRQYYKKWYDARVFCeSGASPEEVAD 214
Cdd:COG0703  80 LSPENRELLKEHGTVVYLDASPETLLERLRRDD-NRplLQGEDPRERLEELLAEREPLYREVADITVDT-DGRSPEEVVD 157


                ....*...
gi 12698097 215 KVLNAIKR 222
Cdd:COG0703 158 EILEALEE 165
aroK PRK00131
shikimate kinase; Reviewed
 56-223 1.47e-32

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 123.76  E-value: 1.47e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   56 KNIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEgKAVLNF--SASGSVISLTG 133
Cdd:PRK00131   5 PNIVLIGFMGAGKSTIGRLLAKRLGYDFIDTDHLI-EARAGKSIPEIFEEEGEAAFRELE-EEVLAEllARHNLVISTGG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097  134 SNPMHDASMWHLKKNGVIVYLDVPLLDLIHRLKlMKIDR--IVGRNSGTSMKDLLKFRRQYYKKWYDARVFCEsGASPEE 211
Cdd:PRK00131  83 GAVLREENRALLRERGTVVYLDASFEELLRRLR-RDRNRplLQTNDPKEKLRDLYEERDPLYEEVADITVETD-GRSPEE 160

                        170
                 ....*....|..
gi 12698097  212 VADKVLNAIKRY 223
Cdd:PRK00131 161 VVNEILEKLEAA 172
Thr_synth_N pfam14821
Threonine synthase N terminus; This domain is found at the N-terminus of many threonine ...
 231-318 1.33e-16

Threonine synthase N terminus; This domain is found at the N-terminus of many threonine synthase enzymes.


Pssm-ID: 464335 [Multi-domain]  Cd Length: 79  Bit Score: 75.15  E-value: 1.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   231 FISTRhvwpkDCEQKVSakfFSEAVIEGLASDGGLFVPAkEFPKLSCGEWKSLVGATYIERAQILLERCIhPADIPAARL 310
Cdd:pfam14821   2 YISTR-----GGAPPLS---FEDALLKGLAPDGGLYVPE-EIPQLSAEELASWRGLSYQELAFEVLSLFI-GDDIPEEDL 71


                  ....*...
gi 12698097   311 GEMIETAY 318
Cdd:pfam14821  72 KALIERAY 79
PLN02569 PLN02569
threonine synthase
 346-672 5.73e-12

threonine synthase


Pssm-ID: 178182 [Multi-domain]  Cd Length: 484  Bit Score: 68.69  E-value: 5.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097  346 PTGSFKDLSLQL------------MPHIFAHCippscnymilvATSGDTGSAVLNGFSRLNkndkqrIAVVTFFPENGVS 413
Cdd:PLN02569 161 HTGSFKDLGMTVlvsqvnrlrkmaKPVVGVGC-----------ASTGDTSAALSAYCAAAG------IPSIVFLPADKIS 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097  414 DFQKAQIIGsqreNGWAV-GVESDFDFCQTAIKRIfndsdftgflTVEYGTILssANSINWGRLLPQvvyhASAYLDLVS 492
Cdd:PLN02569 224 IAQLVQPIA----NGALVlSIDTDFDGCMRLIREV----------TAELPIYL--ANSLNSLRLEGQ----KTAAIEILQ 283

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097  493 QgfisFGSPVD--VCIPTGNFGNILAAVYA----KMMGI--PIRKFICASNQN-RVLTDFIKTGHYDLRERKLAQTFSPS 563
Cdd:PLN02569 284 Q----FDWEVPdwVIVPGGNLGNIYAFYKGfkmcKELGLvdRLPRLVCAQAANaNPLYRAYKSGWEEFKPVKANPTFASA 359

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097  564 IDILKSSNLERHLHLMANKDGqlmtelfnqlesqhhfqiekvLVEKLQQDFVADWCSEGEclaainstynTSGYILDPHT 643
Cdd:PLN02569 360 IQIGDPVSIDRAVYALKESNG---------------------IVEEATEEELMDAQAEAD----------KTGMFLCPHT 408

                        330       340       350
                 ....*....|....*....|....*....|....
gi 12698097  644 AVA-----KVVADRVQDKTCPVIVSSTAHYSKFA 672
Cdd:PLN02569 409 GVAlaalkKLRASGVIGPTDRTVVVSTAHGLKFT 442
therm_gnt_kin TIGR01313
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of ...
 58-88 3.06e-03

carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of proteins that includes thermoresistant and thermosensitve isozymes of gluconate kinase (gluconokinase) in E. coli and other related proteins; members of this family are often named by similarity to the thermostable isozyme. These proteins show homology to shikimate kinases and adenylate kinases but not to gluconate kinases from the FGGY family of carbohydrate kinases.


Pssm-ID: 273551  Cd Length: 163  Bit Score: 38.92  E-value: 3.06e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 12698097    58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVDD 88
Cdd:TIGR01313   1 FVLMGVAGSGKSTIASALAHRLGAKFIEGDD 31
BREX_3_BrxF NF033453
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino ...
 58-110 4.38e-03

BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino acids in length includes BrxF from type 3 BREX (bacteriophage exclusion) systems. Most members have the P-loop motif GxxGxGKT, but the region is surprisingly poorly conserved in a sizable fraction of otherwise strongly similar proteins.


Pssm-ID: 468038  Cd Length: 149  Bit Score: 38.24  E-value: 4.38e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 12698097   58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVdddilektwNMSVSEKLQDVGNEQ 110
Cdd:NF033453  19 ILLVGPPGSGKTALLRELAAKRGAPVINV---------NLELSRRLLELPEKQ 62
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 56-88 4.55e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 38.51  E-value: 4.55e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 12698097     56 KNIILMGPPGAGKTTVGRIIGQKL-----GCCVIDVDD 88
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELgppggGVIYIDGED 40
 
Name Accession Description Interval E-value
Thr-synth_2 cd01560
Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of ...
 230-733 0e+00

Threonine synthase catalyzes the final step of threonine biosynthesis. The conversion of O-phosphohomoserine into threonine and inorganic phosphate is pyridoxal 5'-phosphate dependent. The Thr-synth_1 CD includes members from higher plants, cyanobacteria, archaebacteria and eubacterial groups. This CD, Thr-synth_2, includes enzymes from fungi and eubacterial groups, as well as, metazoan threonine synthase-like proteins.


Pssm-ID: 107203 [Multi-domain]  Cd Length: 460  Bit Score: 594.99  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 230 TFISTRHVWPKdceqkVSakfFSEAVIEGLASDGGLFVPAkEFPKLSCGEWKSLVGATYIERAQILLERCIhPADIPAAR 309
Cdd:cd01560   1 KYVSTRGGNPG-----VS---FSEALLSGLAPDGGLYVPE-ELPKLSAEEIASWSGLSYQELAFEVLSLFI-GDEIPEDD 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 310 LGEMIETAYGEnFACSKIAPVRHLSGNQFILELFHGPTGSFKDLSLQLMPHIFAHCIPP-SCNYMILVATSGDTGSAVLN 388
Cdd:cd01560  71 LKSLIDRAYSF-FRHPDIAPLVQLGDNLYVLELFHGPTLAFKDMALQFLGRLLEYFLKRrNERITILVATSGDTGSAAIE 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 389 GFSrlnknDKQRIAVVTFFPENGVSDFQKAQIIGSQRENGWAVGVESDFDFCQTAIKRIFNDSDFTgfltveYGTILSSA 468
Cdd:cd01560 150 GFR-----GKPNVDVVVLYPKGGVSPIQELQMTTLPADNVHVVAVEGDFDDCQSLVKALFADEDFN------KKLKLSSA 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 469 NSINWGRLLPQVVYHASAYLDLVSQGFisfGSPVDVCIPTGNFGNILAAVYAKMMGIPIRKFICASNQNRVLTDFIKTGH 548
Cdd:cd01560 219 NSINWARILAQIVYYFYAYLQLLKRGE---GEKVEFSVPTGNFGNILAGYYAKKMGLPIKKLIVATNENDVLRRFFKTGR 295

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 549 YDLRErKLAQTFSPSIDILKSSNLERHLHLMANKDGQLMTELFNQLESQHHFQIEKVLVEKLQQDFVADWCSEGECLAAI 628
Cdd:cd01560 296 YDRRE-SLKQTLSPAMDILKSSNFERLLFLLAGRDRTKVKMLMEEFEATGFLSLPKEELKKLREDFSSGSVSDEETLETI 374

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 629 NSTYNTSGYILDPHTAVAKVVADRVQDK-TCPVIVSSTAHYSKFAPAIMQALKIKEInetsssqlyllgsynALPPLHEA 707
Cdd:cd01560 375 REVYEETGYLIDPHTAVGVRAAERVRKSpGTPGVVLSTAHPAKFPEAVKEALGEEPV---------------ELPEELEG 439

                       490       500
                ....*....|....*....|....*.
gi 12698097 708 LLERTKQQEKMEyqvcaADMNVLKSH 733
Cdd:cd01560 440 LEDLEKRHEDLL-----ADKELLKSH 460
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 251-682 1.48e-66

Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the Pathway/BioSystem: Threonine biosynthesis


Pssm-ID: 440264 [Multi-domain]  Cd Length: 394  Bit Score: 225.46  E-value: 1.48e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 251 FSEAVIEGLASDGGLfVPAkEFPKLSCGEWKSLVG-ATYIEraqiLLercihPADIPAARLgemietAYGENFA----CS 325
Cdd:COG0498  11 FSDALLYLCPDCGGL-LPD-SYPALSREDLASRRGlWRYRE----LL-----PFDDEEKAV------SLGEGGTplvkAP 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 326 KIApvRHLSGNQFILELFHGPTGSFKDLSLQLMPHIFAHcippSCNYMILVATSGdTGSAVLNGFSrlnknDKQRIAVVT 405
Cdd:COG0498  74 RLA--DELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALE----RGAKTIVCASSG-NGSAALAAYA-----ARAGIEVFV 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 406 FFPENGVSDFQKAQII--GSQrengwAVGVESDFDFCQTAIKRIFNDSDFtgfltveygtilSSANSINWGRLLPQVVYH 483
Cdd:COG0498 142 FVPEGKVSPGQLAQMLtyGAH-----VIAVDGNFDDAQRLVKELAADEGL------------YAVNSINPARLEGQKTYA 204

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 484 ASAYLDLVSqgfisfgSPVDVCIPTGNFGNILAAVYAKMM----GIPIR--KFI--CASNQNRVLTDFiKTGHyDLRERK 555
Cdd:COG0498 205 FEIAEQLGR-------VPDWVVVPTGNGGNILAGYKAFKElkelGLIDRlpRLIavQATGCNPILTAF-ETGR-DEYEPE 275

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 556 LAQTFSPSIDILKSSNLERHLHLMANKDGqlmtelfnqlesqhhfqiekvlveklqqdfVADWCSEGECLAAINSTYNTS 635
Cdd:COG0498 276 RPETIAPSMDIGNPSNGERALFALRESGG------------------------------TAVAVSDEEILEAIRLLARRE 325

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|..
gi 12698097 636 GYILDPHTAVA-----KVVADRVQDKTCPVIVSSTAHYSKFAPAIMQALKIK 682
Cdd:COG0498 326 GIFVEPATAVAvaglrKLREEGEIDPDEPVVVLSTGHGLKFPDAVREALGGE 377
SK cd00464
Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic ...
 57-211 4.32e-41

Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.


Pssm-ID: 238260 [Multi-domain]  Cd Length: 154  Bit Score: 147.32  E-value: 4.32e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097  57 NIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSAS-GSVISLTGSN 135
Cdd:cd00464   1 NIVLIGMMGAGKTTVGRLLAKALGLPFVDLDELI-EQRAGMSIPEIFAEEGEEGFRELEREVLLLLLTKeNAVIATGGGA 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12698097 136 PMHDASMWHLKKNGVIVYLDVPLLDLIHRLKLMKIDRIVGRNSGTSMKDLLKFRRQYYKKWYDARVFCEsGASPEE 211
Cdd:cd00464  80 VLREENRRLLLENGIVVWLDASPEELLERLARDKTRPLLQDEDPERLRELLEEREPLYREVADLTIDTD-ELSPEE 154
SKI pfam01202
Shikimate kinase;
64-221 2.13e-40

Shikimate kinase;


Pssm-ID: 426122 [Multi-domain]  Cd Length: 159  Bit Score: 145.42  E-value: 2.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097    64 PGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSAS-GSVISLTGSNPMHDASM 142
Cdd:pfam01202   1 MGAGKSTIGRLLAKALGLPFIDTDEEI-EKRTGMSIAEIFEEEGEEGFRRLESEVLKELLAEhGLVIATGGGAVLSEENR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   143 WHLKKNGVIVYLDVPLLDLIHRLKlMKIDRIV--GRNSGTSMKDLLKFRRQY-YKKwYDARVFCESGASPEEVADKVLNA 219
Cdd:pfam01202  80 DLLKERGIVIYLDAPLEVLLERLK-RDKTRPLlqNKDPEEELLELLFEERDPlYEE-AADIVIDTDESSPEEVATEILEA 157


                  ..
gi 12698097   220 IK 221
Cdd:pfam01202 158 LE 159
thrC TIGR00260
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ...
 289-670 5.47e-37

threonine synthase; Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 272986 [Multi-domain]  Cd Length: 327  Bit Score: 141.37  E-value: 5.47e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   289 IERAQILLErcihPADIPAARLGEMIEtaygENFACSKIaPVRHLSGNQFILELFHGPTGSFKDLSLQLMphiFAHcIPP 368
Cdd:TIGR00260   1 VWRYREFLP----VTEKDLVDLGEGVT----PLFRAPAL-AANVGIKNLYVKELGHNPTLSFKDRGMAVA---LTK-ALE 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   369 SCNYMILVATSGDTGSAVLNGFSRLNKNdkqriaVVTFFPENGVSDFQKAQIIGsqrENGWAVGVESDFDFCQTAIKRIF 448
Cdd:TIGR00260  68 LGNDTVLCASTGNTGAAAAAYAGKAGLK------VVVLYPAGKISLGKLAQALG---YNAEVVAIDGNFDDAQRLVKQLF 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   449 NDSdftgfltveYGTILSSANSInWGRLLPQvVYHASAYLDLVSQgfisfGSPVDVCIP---TGNFGNILAAVYAKMMG- 524
Cdd:TIGR00260 139 EDK---------PALGLNSANSI-PYRLEGQ-KTYAFEAVEQLGW-----EAPDKVVVPvpnSGNFGAIWKGFKEKKMLg 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   525 ---IPIRKFICASNQNRVLTDFIKTGHYDLRERKlaQTFSPSIDILKSSNLERHLHLMANKDGQlMTELfnqlesqhhfq 601
Cdd:TIGR00260 203 ldsLPVKRGIQAEGAADIVRAFLEGGQWEPIETP--ETLSTAMDIGNPANWPRALEAFRRSNGY-AEDL----------- 268

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12698097   602 iekvlveklqqdfvadwcSEGECLAAINSTYNTSGYILDPHTAVAKVVADRVQDKTcpvivssTAHYSK 670
Cdd:TIGR00260 269 ------------------SDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVEKG-------TADPAE 312
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
 58-222 4.37e-35

Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440467 [Multi-domain]  Cd Length: 165  Bit Score: 130.63  E-value: 4.37e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097  58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSA-SGSVISLTGSNP 136
Cdd:COG0703   1 IVLIGMMGAGKSTVGRLLAKRLGLPFVDTDAEI-EERAGMSIPEIFAEEGEAGFRELEREVLAELLEeENAVIATGGGAV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 137 MHDASMWHLKKNGVIVYLDVPLLDLIHRLKLMKiDR--IVGRNSGTSMKDLLKFRRQYYKKWYDARVFCeSGASPEEVAD 214
Cdd:COG0703  80 LSPENRELLKEHGTVVYLDASPETLLERLRRDD-NRplLQGEDPRERLEELLAEREPLYREVADITVDT-DGRSPEEVVD 157


                ....*...
gi 12698097 215 KVLNAIKR 222
Cdd:COG0703 158 EILEALEE 165
aroK PRK00131
shikimate kinase; Reviewed
 56-223 1.47e-32

shikimate kinase; Reviewed


Pssm-ID: 234654 [Multi-domain]  Cd Length: 175  Bit Score: 123.76  E-value: 1.47e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   56 KNIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEgKAVLNF--SASGSVISLTG 133
Cdd:PRK00131   5 PNIVLIGFMGAGKSTIGRLLAKRLGYDFIDTDHLI-EARAGKSIPEIFEEEGEAAFRELE-EEVLAEllARHNLVISTGG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097  134 SNPMHDASMWHLKKNGVIVYLDVPLLDLIHRLKlMKIDR--IVGRNSGTSMKDLLKFRRQYYKKWYDARVFCEsGASPEE 211
Cdd:PRK00131  83 GAVLREENRALLRERGTVVYLDASFEELLRRLR-RDRNRplLQTNDPKEKLRDLYEERDPLYEEVADITVETD-GRSPEE 160

                        170
                 ....*....|..
gi 12698097  212 VADKVLNAIKRY 223
Cdd:PRK00131 161 VVNEILEKLEAA 172
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 335-667 1.18e-25

Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.


Pssm-ID: 107202 [Multi-domain]  Cd Length: 244  Bit Score: 106.45  E-value: 1.18e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 335 GNQFILELFHGPTGSFKDLSLQLMPHIFAHCIPPScNYMILVATSGDTGSAVLNGFSRLNkndkqrIAVVTFFPEnGVSD 414
Cdd:cd00640  15 ANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLP-KGVIIESTGGNTGIALAAAAARLG------LKCTIVMPE-GASP 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 415 FQKAQIigsqRENG-WAVGVESDFDFCQTAIKRIFNDSDftgfltveygtILSSANS-INWGRLLPQVVYHASAYLDLVS 492
Cdd:cd00640  87 EKVAQM----RALGaEVVLVPGDFDDAIALAKELAEEDP-----------GAYYVNQfDNPANIAGQGTIGLEILEQLGG 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 493 QgfisfgSPVDVCIPTGNFGNILAAVYAKMMGIPIRKFICASNQnrvltdfiktghydlrerklaqtfspsidilkssnl 572
Cdd:cd00640 152 Q------KPDAVVVPVGGGGNIAGIARALKELLPNVKVIGVEPE------------------------------------ 189

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 573 erhlhlmankdgqlmtelfnqlesqhhfqiekvlveklqqdfvADWCSEGECLAAINSTYNTSGYILDPHTAVAKVVADR 652
Cdd:cd00640 190 -------------------------------------------VVTVSDEEALEAIRLLAREEGILVEPSSAAALAAALK 226

                       330
                ....*....|....*...
gi 12698097 653 VQDKTCP---VIVSSTAH 667
Cdd:cd00640 227 LAKKLGKgktVVVILTGG 244
Thr_synth_N pfam14821
Threonine synthase N terminus; This domain is found at the N-terminus of many threonine ...
 231-318 1.33e-16

Threonine synthase N terminus; This domain is found at the N-terminus of many threonine synthase enzymes.


Pssm-ID: 464335 [Multi-domain]  Cd Length: 79  Bit Score: 75.15  E-value: 1.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   231 FISTRhvwpkDCEQKVSakfFSEAVIEGLASDGGLFVPAkEFPKLSCGEWKSLVGATYIERAQILLERCIhPADIPAARL 310
Cdd:pfam14821   2 YISTR-----GGAPPLS---FEDALLKGLAPDGGLYVPE-EIPQLSAEELASWRGLSYQELAFEVLSLFI-GDDIPEEDL 71


                  ....*...
gi 12698097   311 GEMIETAY 318
Cdd:pfam14821  72 KALIERAY 79
PRK00625 PRK00625
shikimate kinase; Provisional
 56-165 1.65e-16

shikimate kinase; Provisional


Pssm-ID: 134335 [Multi-domain]  Cd Length: 173  Bit Score: 77.87  E-value: 1.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   56 KNIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDILEKTWNM---SVSEKLQDVGNEQFLEEEGKAVLNFSASGSVISLT 132
Cdd:PRK00625   1 MQIFLCGLPTVGKTSFGKALAKFLSLPFFDTDDLIVSNYHGAlysSPKEIYQAYGEEGFCREEFLALTSLPVIPSIVALG 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 12698097  133 GSNPMHDASMWHLKKNGVIVYLDVPLLDLIHRL 165
Cdd:PRK00625  81 GGTLMIEPSYAHIRNRGLLVLLSLPIATIYQRL 113
PRK13947 PRK13947
shikimate kinase; Provisional
 56-223 1.08e-15

shikimate kinase; Provisional


Pssm-ID: 184412 [Multi-domain]  Cd Length: 171  Bit Score: 75.51  E-value: 1.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   56 KNIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSA-SGSVISLTGS 134
Cdd:PRK13947   2 KNIVLIGFMGTGKTTVGKRVATTLSFGFIDTDKEI-EKMTGMTVAEIFEKDGEVRFRSEEKLLVKKLARlKNLVIATGGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097  135 NPMHDASMWHLKKNGVIVYLDVPLLDLIHRLKLMKIDRIVGR-NSGTSMKDLLKfRRQYYkkwYDARVFC--ESGASPEE 211
Cdd:PRK13947  81 VVLNPENVVQLRKNGVVICLKARPEVILRRVGKKKSRPLLMVgDPEERIKELLK-EREPF---YDFADYTidTGDMTIDE 156

                        170
                 ....*....|..
gi 12698097  212 VADKVlnaIKRY 223
Cdd:PRK13947 157 VAEEI---IKAY 165
PRK13946 PRK13946
shikimate kinase; Provisional
 50-230 6.29e-14

shikimate kinase; Provisional


Pssm-ID: 184411 [Multi-domain]  Cd Length: 184  Bit Score: 70.72  E-value: 6.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   50 HSLVGDKNIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSASGS-V 128
Cdd:PRK13946   5 RAALGKRTVVLVGLMGAGKSTVGRRLATMLGLPFLDADTEI-ERAARMTIAEIFAAYGEPEFRDLERRVIARLLKGGPlV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097  129 ISLTGSNPMHDASMWHLKKNGVIVYLDVPLLDLIHRLK------LMKidrivGRNSGTSMKDLLKFRRQYYKKwydARVF 202
Cdd:PRK13946  84 LATGGGAFMNEETRAAIAEKGISVWLKADLDVLWERVSrrdtrpLLR-----TADPKETLARLMEERYPVYAE---ADLT 155

                        170       180
                 ....*....|....*....|....*....
gi 12698097  203 CESGASPEEV-ADKVLNAIKRYQDVDSET 230
Cdd:PRK13946 156 VASRDVPKEVmADEVIEALAAYLEKEEAA 184
aroL PRK03731
shikimate kinase AroL;
58-220 1.25e-12

shikimate kinase AroL;


Pssm-ID: 235153 [Multi-domain]  Cd Length: 171  Bit Score: 66.50  E-value: 1.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDILEKTwNMSVSEKLQDVGNEQFLEEEGKAVLNFSASGSVISLTGSNPM 137
Cdd:PRK03731   5 LFLVGARGCGKTTVGMALAQALGYRFVDTDQWLQSTS-NMTVAEIVEREGWAGFRARESAALEAVTAPSTVIATGGGIIL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097  138 HDASMWHLKKNGVIVYLDVPLLDLIHRLKLMKID----RIVGRNSGTSMKDLLKFRRQYYKKwyDARVFCESGASPEEVA 213
Cdd:PRK03731  84 TEENRHFMRNNGIVIYLCAPVSVLANRLEANPEEdqrpTLTGKPISEEVAEVLAEREALYRE--VAHHIIDATQPPSQVV 161


                 ....*..
gi 12698097  214 DKVLNAI 220
Cdd:PRK03731 162 SEILSAL 168
PRK13949 PRK13949
shikimate kinase; Provisional
 56-195 1.77e-12

shikimate kinase; Provisional


Pssm-ID: 140006 [Multi-domain]  Cd Length: 169  Bit Score: 65.91  E-value: 1.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   56 KNIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSA-SGSVISLTGS 134
Cdd:PRK13949   2 ARIFLVGYMGAGKTTLGKALARELGLSFIDLDFFI-ENRFHKTVGDIFAERGEAVFRELERNMLHEVAEfEDVVISTGGG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12698097  135 NPMHDASMWHLKKNGVIVYLDVPLLDLIHRLKLMKIDR-IVGRNSGTSMKDL----LKFRRQYYKK 195
Cdd:PRK13949  81 APCFFDNMELMNASGTTVYLKVSPEVLFVRLRLAKQQRpLLKGKSDEELLDFiieaLEKRAPFYRQ 146
PLN02569 PLN02569
threonine synthase
 346-672 5.73e-12

threonine synthase


Pssm-ID: 178182 [Multi-domain]  Cd Length: 484  Bit Score: 68.69  E-value: 5.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097  346 PTGSFKDLSLQL------------MPHIFAHCippscnymilvATSGDTGSAVLNGFSRLNkndkqrIAVVTFFPENGVS 413
Cdd:PLN02569 161 HTGSFKDLGMTVlvsqvnrlrkmaKPVVGVGC-----------ASTGDTSAALSAYCAAAG------IPSIVFLPADKIS 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097  414 DFQKAQIIGsqreNGWAV-GVESDFDFCQTAIKRIfndsdftgflTVEYGTILssANSINWGRLLPQvvyhASAYLDLVS 492
Cdd:PLN02569 224 IAQLVQPIA----NGALVlSIDTDFDGCMRLIREV----------TAELPIYL--ANSLNSLRLEGQ----KTAAIEILQ 283

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097  493 QgfisFGSPVD--VCIPTGNFGNILAAVYA----KMMGI--PIRKFICASNQN-RVLTDFIKTGHYDLRERKLAQTFSPS 563
Cdd:PLN02569 284 Q----FDWEVPdwVIVPGGNLGNIYAFYKGfkmcKELGLvdRLPRLVCAQAANaNPLYRAYKSGWEEFKPVKANPTFASA 359

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097  564 IDILKSSNLERHLHLMANKDGqlmtelfnqlesqhhfqiekvLVEKLQQDFVADWCSEGEclaainstynTSGYILDPHT 643
Cdd:PLN02569 360 IQIGDPVSIDRAVYALKESNG---------------------IVEEATEEELMDAQAEAD----------KTGMFLCPHT 408

                        330       340       350
                 ....*....|....*....|....*....|....
gi 12698097  644 AVA-----KVVADRVQDKTCPVIVSSTAHYSKFA 672
Cdd:PLN02569 409 GVAlaalkKLRASGVIGPTDRTVVVSTAHGLKFT 442
PLN02199 PLN02199
shikimate kinase
 15-165 8.91e-11

shikimate kinase


Pssm-ID: 177850 [Multi-domain]  Cd Length: 303  Bit Score: 63.56  E-value: 8.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   15 QKCFSSIHVKTDKHAQQFLSR----TFALAELRKSWYSTHSLVGDKNIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDI 90
Cdd:PLN02199  58 RRAVSPAVSCSDNNSSALLETgsvyPFDEDILKRKAEEVKPYLNGRSMYLVGMMGSGKTTVGKLMSKVLGYTFFDCDTLI 137

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12698097   91 LEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSASGSVISLTGSNPMHDASMWHLKKNGVIVYLDVPLLDLIHRL 165
Cdd:PLN02199 138 EQAMNGTSVAEIFVHHGENFFRGKETDALKKLSSRYQVVVSTGGGAVIRPINWKYMHKGISIWLDVPLEALAHRI 212
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 340-656 1.26e-08

Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.


Pssm-ID: 459749 [Multi-domain]  Cd Length: 295  Bit Score: 56.94  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   340 LELFHgPTGSFKDLSLQlmpHIFAHCIPPSCNYMILVATSGDTGSAVLNGFSRLNkndkqrIAVVTFFPENGVSdfQKAQ 419
Cdd:pfam00291  28 LESLN-PTGSFKDRGAL---NLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLG------LKVTIVVPEDAPP--GKLL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   420 IIgsqRENGwA--VGVESDFDFCQTAIKRIFNDSDftgfltvEYGTILSSANSINWgrllpqvVYHASAYLDLVSQgfis 497
Cdd:pfam00291  96 LM---RALG-AevVLVGGDYDEAVAAARELAAEGP-------GAYYINQYDNPLNI-------EGYGTIGLEILEQ---- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   498 FGSPVD-VCIPTGNFGNILA-AVYAKMMGIPIRKFICASNQNRVLTDFIKTGHYDlrERKLAQTFSPSIDILKSSnlerh 575
Cdd:pfam00291 154 LGGDPDaVVVPVGGGGLIAGiARGLKELGPDVRVIGVEPEGAPALARSLAAGRPV--PVPVADTIADGLGVGDEP----- 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   576 lhlmANKDGQLMTELFnqlesqhhfqIEKVLVeklqqdfvadwcSEGECLAAINSTYNTSGYILDPHTAVAKVVADRVQD 655
Cdd:pfam00291 227 ----GALALDLLDEYV----------GEVVTV------------SDEEALEAMRLLARREGIVVEPSSAAALAALKLALA 280


                  .
gi 12698097   656 K 656
Cdd:pfam00291 281 G 281
CmkB COG1102
Cytidylate kinase [Nucleotide transport and metabolism];
62-224 3.30e-08

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440719 [Multi-domain]  Cd Length: 188  Bit Score: 54.06  E-value: 3.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097  62 GPPGAGKTTVGRIIGQKLGCCVidVDDDILEKTW---NMSVSE------------KLQDVGNEQFLEEEGKAVLNFSASG 126
Cdd:COG1102   7 REPGSGGTTIAKRLAEKLGLPL--YDGEILREAAkerGLSEEEfekldekapsllYRDTAEEDEIDRALDKVIRELARKG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097 127 SVIsLTGsnpmHDASmWHLK--KNGVIVYLDVPLLDlihrlklmKIDRIVGRNsGTSMKDLLKF-------RRQYYKK-- 195
Cdd:COG1102  85 NCV-IVG----RLAD-WILRdrPNVLKVFLTAPLEV--------RVKRIAERE-GISEEEAEKEikkrdksRAKYYKYyy 149

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 12698097 196 ---WYDAR----VFCESGASPEEVADKVLNAIKRYQ 224
Cdd:COG1102 150 gidWGDPSnydlVINTSRLGIEEAVDLILAAIEARE 185
aroK PRK05057
shikimate kinase AroK;
56-155 1.57e-07

shikimate kinase AroK;


Pssm-ID: 235335 [Multi-domain]  Cd Length: 172  Bit Score: 51.64  E-value: 1.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   56 KNIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDILEKT-----WNMSVS------EKLQDVGNEqfLEEEGKAVLNfSA 124
Cdd:PRK05057   5 RNIFLVGPMGAGKSTIGRQLAQQLNMEFYDSDQEIEKRTgadigWVFDVEgeegfrDREEKVINE--LTEKQGIVLA-TG 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 12698097  125 SGSVISLTGSNpmhdasmwHLKKNGVIVYLD 155
Cdd:PRK05057  82 GGSVKSRETRN--------RLSARGVVVYLE 104
PRK13951 PRK13951
bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;
58-196 5.18e-07

bifunctional shikimate kinase AroK/3-dehydroquinate synthase AroB;


Pssm-ID: 172457 [Multi-domain]  Cd Length: 488  Bit Score: 52.98  E-value: 5.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSASGSVISLTGSNPM 137
Cdd:PRK13951   3 IFLVGMMGSGKSTIGKRVSEVLDLQFIDMDEEI-ERREGRSVRRIFEEDGEEYFRLKEKELLRELVERDNVVVATGGGVV 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 12698097  138 HDASMWHLKKNGVIVYLDVPLLDLIHRLKLMkiDRIVGRNSGTSMKDLLKFRRQYYKKW 196
Cdd:PRK13951  82 IDPENRELLKKEKTLFLYAPPEVLMERVTTE--NRPLLREGKERIREIWERRKQFYTEF 138
PRK14021 PRK14021
bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional
 59-220 6.08e-07

bifunctional shikimate kinase/3-dehydroquinate synthase; Provisional


Pssm-ID: 184458 [Multi-domain]  Cd Length: 542  Bit Score: 52.94  E-value: 6.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   59 ILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEGKAVLNFSAS-GSVISLTGSNPM 137
Cdd:PRK14021  10 VIIGMMGAGKTRVGKEVAQMMRLPFADADVEI-EREIGMSIPSYFEEYGEPAFREVEADVVADMLEDfDGIFSLGGGAPM 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097  138 HDASMWHLKK----NGVIVYLDVPLLDLIHRlklmkidriVGRNSGTSM---------KDLLKFRRQYYKKWYDARVFCE 204
Cdd:PRK14021  89 TPSTQHALASyiahGGRVVYLDADPKEAMER---------ANRGGGRPMlngdankrwKKLFKQRDPVFRQVANVHVHTR 159

                        170
                 ....*....|....*.
gi 12698097  205 sGASPEEVADKVLNAI 220
Cdd:PRK14021 160 -GLTPQAAAKKLIDMV 174
PRK03839 PRK03839
putative kinase; Provisional
 58-222 1.86e-06

putative kinase; Provisional


Pssm-ID: 179660  Cd Length: 180  Bit Score: 48.95  E-value: 1.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDILEKTWNMSVSEKLQ-DVGN-EQFLEEEGKavlnfsasgsvisltGSN 135
Cdd:PRK03839   3 IAITGTPGVGKTTVSKLLAEKLGYEYVDLTEFALKKGIGEEKDDEMEiDFDKlAYFIEEEFK---------------EKN 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097  136 PMHDASMWHLKKNGVIVYLDVPLLDLIHRLKLMKIDR-IVGRNSGTSMKDLlkfrrqyykkwydarVFCES--------- 205
Cdd:PRK03839  68 VVLDGHLSHLLPVDYVIVLRAHPKIIKERLKERGYSKkKILENVEAELVDV---------------CLCEAleekekvie 132

                        170       180
                 ....*....|....*....|.
gi 12698097  206 ----GASPEEVADKVLNAIKR 222
Cdd:PRK03839 133 vdttGKTPEEVVEEILELIKS 153
ADK cd01428
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ...
 57-88 5.99e-06

Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine triphosphates (ATP) to adenosine monophosphates (AMP) and to yield adenosine diphosphates (ADP). This enzyme is required for the biosynthesis of ADP and is essential for homeostasis of adenosine phosphates.


Pssm-ID: 238713 [Multi-domain]  Cd Length: 194  Bit Score: 47.62  E-value: 5.99e-06
                        10        20        30
                ....*....|....*....|....*....|..
gi 12698097  57 NIILMGPPGAGKTTVGRIIGQKLGCCVIDVDD 88
Cdd:cd01428   1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGD 32
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
 58-89 7.19e-06

Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442496 [Multi-domain]  Cd Length: 164  Bit Score: 46.66  E-value: 7.19e-06
                        10        20        30
                ....*....|....*....|....*....|..
gi 12698097  58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVDDD 89
Cdd:COG3265   4 IVVMGVSGSGKSTVGQALAERLGWPFIDGDDF 35
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 58-88 9.84e-06

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 46.09  E-value: 9.84e-06
                        10        20        30
                ....*....|....*....|....*....|.
gi 12698097  58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVDD 88
Cdd:cd02021   2 IVVMGVSGSGKSTVGKALAERLGAPFIDGDD 32
Adk COG0563
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ...
 57-80 1.06e-05

Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or related kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440329 [Multi-domain]  Cd Length: 212  Bit Score: 47.04  E-value: 1.06e-05
                        10        20
                ....*....|....*....|....
gi 12698097  57 NIILMGPPGAGKTTVGRIIGQKLG 80
Cdd:COG0563   2 RIILLGPPGAGKGTQAKRLAEKYG 25
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
58-88 2.53e-05

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 45.29  E-value: 2.53e-05
                        10        20        30
                ....*....|....*....|....*....|.
gi 12698097  58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVDD 88
Cdd:COG0645   2 ILVCGLPGSGKSTLARALAERLGAVRLRSDV 32
PRK08118 PRK08118
DNA topology modulation protein;
56-115 5.92e-05

DNA topology modulation protein;


Pssm-ID: 181235  Cd Length: 167  Bit Score: 44.21  E-value: 5.92e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   56 KNIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDILEKTWNMSVSEKLQDVGNEQFLEEE 115
Cdd:PRK08118   2 KKIILIGSGGSGKSTLARQLGEKLNIPVHHLDALFWKPNWEGVPKEEQITVQNELVKEDE 61
adk PRK00279
adenylate kinase; Reviewed
 56-80 1.80e-04

adenylate kinase; Reviewed


Pssm-ID: 234711 [Multi-domain]  Cd Length: 215  Bit Score: 43.60  E-value: 1.80e-04
                         10        20
                 ....*....|....*....|....*
gi 12698097   56 KNIILMGPPGAGKTTVGRIIGQKLG 80
Cdd:PRK00279   1 MRLILLGPPGAGKGTQAKFIAEKYG 25
AAA_18 pfam13238
AAA domain;
58-166 2.05e-04

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 41.65  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097    58 IILMGPPGAGKTTVGRIIGQKLGcCVIDVDDDILEKTWNMSVSEKLQDVG--NEQFLEEEGKAVLNFSA--SGSVISLTG 133
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLG-FGDNVRDLALENGLVLGDDPETRESKrlDEDKLDRLLDLLEENAAleEGGNLIIDG 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 12698097   134 snpmHDASMW-HLKKNGVIVYLDVPLLDLIHRLK 166
Cdd:pfam13238  80 ----HLAELEpERAKDLVGIVLRASPEELLERLE 109
PRK13948 PRK13948
shikimate kinase; Provisional
 60-225 5.29e-04

shikimate kinase; Provisional


Pssm-ID: 184413 [Multi-domain]  Cd Length: 182  Bit Score: 41.70  E-value: 5.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097   60 LMGPPGAGKTTVGRIIGQKLGCCVIDVDDDIlEKTWNMSVSEKLQDVGNEQFLEEEGKAV-----LNFsasgSVISLTGS 134
Cdd:PRK13948  15 LAGFMGTGKSRIGWELSRALMLHFIDTDRYI-ERVTGKSIPEIFRHLGEAYFRRCEAEVVrrltrLDY----AVISLGGG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12698097  135 NPMHDASMWHLKKNGVIVYLDVPLLDLIHRLK-----LMKIDRIVGRnsgtsMKDLLKFRRQYYKKwydARVFCESGASP 209
Cdd:PRK13948  90 TFMHEENRRKLLSRGPVVVLWASPETIYERTRpgdrpLLQVEDPLGR-----IRTLLNEREPVYRQ---ATIHVSTDGRR 161

                        170
                 ....*....|....*..
gi 12698097  210 -EEVADKVLNAIKRYQD 225
Cdd:PRK13948 162 sEEVVEEIVEKLWAWAE 178
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 31-93 7.84e-04

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 42.59  E-value: 7.84e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12698097  31 QFLSRTFALAELRKSWYSTHSLVGDKNIILMGPPGAGKTTVGRIIGQKLGCCVIDVD-DDILEK 93
Cdd:COG0464 167 EELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDlSDLVSK 230
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 43-105 1.85e-03

ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 39.72  E-value: 1.85e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12698097  43 RKSWYSTHSLVG-DKNIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDILEKTWnMSVSEKLQD 105
Cdd:cd19520  22 RPELFDNSRLLQpPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKW-YGESQKLVA 84
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
 58-88 2.00e-03

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 39.22  E-value: 2.00e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 12698097    58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVDD 88
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEELGAVRLSSDD 32
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 35-106 2.26e-03

proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 39.19  E-value: 2.26e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12698097  35 RTFALAELRKSWYSTHSLVGDKNIILMGPPGAGKTTVGRIIGQKLGCCVIDVD-DDILEKtWNMSVSEKLQDV 106
Cdd:cd19481   6 REAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKlSSLLSK-YVGESEKNLRKI 77
PRK14528 PRK14528
adenylate kinase; Provisional
 56-108 2.50e-03

adenylate kinase; Provisional


Pssm-ID: 172994 [Multi-domain]  Cd Length: 186  Bit Score: 39.61  E-value: 2.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 12698097   56 KNIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDILEKTWNMSV----SEKLQDVGN 108
Cdd:PRK14528   2 KNIIFMGPPGAGKGTQAKILCERLSIPQISTGDILREAVKNQTAmgieAKRYMDAGD 58
therm_gnt_kin TIGR01313
carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of ...
 58-88 3.06e-03

carbohydrate kinase, thermoresistant glucokinase family; This model represents a subfamily of proteins that includes thermoresistant and thermosensitve isozymes of gluconate kinase (gluconokinase) in E. coli and other related proteins; members of this family are often named by similarity to the thermostable isozyme. These proteins show homology to shikimate kinases and adenylate kinases but not to gluconate kinases from the FGGY family of carbohydrate kinases.


Pssm-ID: 273551  Cd Length: 163  Bit Score: 38.92  E-value: 3.06e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 12698097    58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVDD 88
Cdd:TIGR01313   1 FVLMGVAGSGKSTIASALAHRLGAKFIEGDD 31
BREX_3_BrxF NF033453
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino ...
 58-110 4.38e-03

BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino acids in length includes BrxF from type 3 BREX (bacteriophage exclusion) systems. Most members have the P-loop motif GxxGxGKT, but the region is surprisingly poorly conserved in a sizable fraction of otherwise strongly similar proteins.


Pssm-ID: 468038  Cd Length: 149  Bit Score: 38.24  E-value: 4.38e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 12698097   58 IILMGPPGAGKTTVGRIIGQKLGCCVIDVdddilektwNMSVSEKLQDVGNEQ 110
Cdd:NF033453  19 ILLVGPPGSGKTALLRELAAKRGAPVINV---------NLELSRRLLELPEKQ 62
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 56-88 4.55e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 38.51  E-value: 4.55e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 12698097     56 KNIILMGPPGAGKTTVGRIIGQKL-----GCCVIDVDD 88
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELgppggGVIYIDGED 40
HypB COG0378
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ...
 58-94 4.56e-03

Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440147 [Multi-domain]  Cd Length: 200  Bit Score: 38.89  E-value: 4.56e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 12698097  58 IILMGPPGAGKTTV----GRIIGQKLGCCVI------DVDDDILEKT 94
Cdd:COG0378  16 VNLMGSPGSGKTTLlektIRALKDRLRIAVIegdiytTEDAERLRAA 62
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 56-103 4.79e-03

ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 38.49  E-value: 4.79e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 12698097  56 KNIILMGPPGAGKTTVGRIIGQKLGCCVIDVDDDILEKTWnMSVSEKL 103
Cdd:cd19509  33 RGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKW-VGESEKI 79
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
 62-80 5.07e-03

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 38.24  E-value: 5.07e-03
                        10
                ....*....|....*....
gi 12698097  62 GPPGAGKTTVGRIIGQKLG 80
Cdd:cd02020   6 GPAGSGKSTVAKLLAKKLG 24
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 56-129 5.15e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 38.28  E-value: 5.15e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12698097  56 KNIILMGPPGAGKTTVGRIIGQKLG-----CCVIDVDDDIlektwnmsvsEKLQDVGNEQFLEEEGKAVLNFSASGSVI 129
Cdd:cd00009  20 KNLLLYGPPGTGKTTLARAIANELFrpgapFLYLNASDLL----------EGLVVAELFGHFLVRLLFELAEKAKPGVL 88
cyt_kin_arch TIGR02173
cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. ...
 58-80 8.42e-03

cytidylate kinase, putative; Proteins in this family are believed to be cytidylate kinase. Members of this family are found in the archaea and in spirochaetes, and differ considerably from the common bacterial form of cytidylate kinase described by TIGR00017.


Pssm-ID: 274012 [Multi-domain]  Cd Length: 171  Bit Score: 37.79  E-value: 8.42e-03
                          10        20
                  ....*....|....*....|...
gi 12698097    58 IILMGPPGAGKTTVGRIIGQKLG 80
Cdd:TIGR02173   3 ITISGPPGSGKTTVAKILAEKLS 25
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 57-81 9.72e-03

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 38.91  E-value: 9.72e-03
                         10        20
                 ....*....|....*....|....*
gi 12698097   57 NIILMGPPGAGKTTVGRIIGQKLGC 81
Cdd:PRK13342  38 SMILWGPPGTGKTTLARIIAGATDA 62
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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