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Conserved domains on  [gi|913621191|gb|AKV03724|]
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Phosphoenolpyruvate phosphomutase [Labilithrix luteola]

Protein Classification

bifunctional phosphoenolpyruvate phosphomutase/phosphocholine cytidylyltransferase family protein( domain architecture ID 10798012)

bifunctional phosphoenolpyruvate phosphomutase/phosphocholine cytidylyltransferase family protein contains an N-terminal domain that catalyzes formation of a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr), and a C-terminal domain that may catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline

CATH:  3.20.20.60
EC:  5.4.2.9|2.4.-.-
Gene Ontology:  GO:0016757
PubMed:  10571990|15078090|9370319|9445404|10521532|12691742
SCOP:  4003532|4002789

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PEP_mutase TIGR02320
phosphoenolpyruvate mutase; This family consists of examples of phosphoenolpyruvate ...
 13-285 3.74e-148

phosphoenolpyruvate mutase; This family consists of examples of phosphoenolpyruvate phosphomutase, an enzyme that creates a C-P bond as the first step in the biosynthesis of natural products including antibiotics like bialaphos and phosphonothricin in Streptomyces species, phosphonate-modified molecules such as the polysaccharide B of Bacteroides fragilis, the phosphonolipids of Tetrahymena pyroformis, the glycosylinositolphospholipids of Trypanosoma cruzi. This gene generally occurs in prokaryotic organisms adjacent to the gene for phosphonopyruvate decarboxylase (aepY). Since the PEP phosphomutase reaction favors the substrate PEP energetically, the decarboxylase is required to drive the reaction in the direction of phosphonate production. Most often an aminotansferase (aepZ) is also present which leads to the production of the most common phosphonate compound, 2-aminoethylphosphonate (AEP). A closely related enzyme, phosphonopyruvate hydrolase from Variovorax sp. Pal2, is excluded from this model.


:

Pssm-ID: 274077  Cd Length: 284  Bit Score: 427.12  E-value: 3.74e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191   13 LRQMLEGQGLSFLMEAHNGLSAKIVEEA--------GFQGIWGSGLSISAALGVRDNNEASWTQVLEVVEFMADATTIPI 84
Cdd:TIGR02320   1 LRQLLHSKPLERLMEAHNGLSALIAEEArvevgdslGFDGIWSSSLTDSTSRGVPDIEEASWTQRLDVVEFMFDVTTKPI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191   85 LLDGDTGyGNFNSARRLVRKLEQRGIAGVCMEDKIFPKTNSFL-RSTAQPLADIEEFAGKIRAAKEAQTDSDFVVVARVE 163
Cdd:TIGR02320  81 ILDGDTG-GNFEHFRRLVRKLERRGVSAVCIEDKLGLKKNSLFgNDVAQPQASVEEFCGKIRAGKDAQTTEDFMIIARVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191  164 ALIAGHGLEEALKRGEAYRKAGADAILIHSKERHADEILAFKKEWGD---RLPLVIVPTKYYRTPTDVFREAGFKIVIWA 240
Cdd:TIGR02320 160 SLILGKGMEDALKRAEAYAEAGADGIMIHSRKKDPDEILEFARRFRNhypRTPLVIVPTSYYTTPTDEFRDAGISVVIYA 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 913621191  241 NHAMRSAITAMQATVKQIFQDEHLMNVEERVAPLADVFRLQGENE 285
Cdd:TIGR02320 240 NHLLRAAYAAMQQVAERILEHGRLVEVEDKCAPIKEIFRLIPGTE 284
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
302-545 1.77e-52

Choline kinase [Lipid transport and metabolism];


:

Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 178.51  E-value: 1.77e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 302 RGIVLAAGQGKELGELVTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVVRGFAKKTVDI------TGATYVDNDAYAT 375
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEalarpgPDVTFVYNPDYDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 376 TSEVASLACAKASLDGPCVVSYGDVLFKKYVLDELLDAEGDFVVAVDslpadeasanaaaalaknepvrrSDWAICSEpH 455
Cdd:COG1213   81 TNNIYSLWLAREALDEDFLLLNGDVVFDPAILKRLLASDGDIVLLVD-----------------------RKWEKPLD-E 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 456 SRKALFNQV-VLKDMTTDPTAAGITGEWTGLLKLSTQGAKFVREILDGMPASELETIKVPDLLRRLVRDGMTVRVVY-SR 533
Cdd:COG1213  137 EVKVRVDEDgRIVEIGKKLPPEEADGEYIGIFKFSAEGAAALREALEALIDEGGPNLYYEDALQELIDEGGPVKAVDiGG 216

                        250
                 ....*....|..
gi 913621191 534 GGWLDIDTIGDV 545
Cdd:COG1213  217 LPWVEIDTPEDL 228
 
Name Accession Description Interval E-value
PEP_mutase TIGR02320
phosphoenolpyruvate mutase; This family consists of examples of phosphoenolpyruvate ...
 13-285 3.74e-148

phosphoenolpyruvate mutase; This family consists of examples of phosphoenolpyruvate phosphomutase, an enzyme that creates a C-P bond as the first step in the biosynthesis of natural products including antibiotics like bialaphos and phosphonothricin in Streptomyces species, phosphonate-modified molecules such as the polysaccharide B of Bacteroides fragilis, the phosphonolipids of Tetrahymena pyroformis, the glycosylinositolphospholipids of Trypanosoma cruzi. This gene generally occurs in prokaryotic organisms adjacent to the gene for phosphonopyruvate decarboxylase (aepY). Since the PEP phosphomutase reaction favors the substrate PEP energetically, the decarboxylase is required to drive the reaction in the direction of phosphonate production. Most often an aminotansferase (aepZ) is also present which leads to the production of the most common phosphonate compound, 2-aminoethylphosphonate (AEP). A closely related enzyme, phosphonopyruvate hydrolase from Variovorax sp. Pal2, is excluded from this model.


Pssm-ID: 274077  Cd Length: 284  Bit Score: 427.12  E-value: 3.74e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191   13 LRQMLEGQGLSFLMEAHNGLSAKIVEEA--------GFQGIWGSGLSISAALGVRDNNEASWTQVLEVVEFMADATTIPI 84
Cdd:TIGR02320   1 LRQLLHSKPLERLMEAHNGLSALIAEEArvevgdslGFDGIWSSSLTDSTSRGVPDIEEASWTQRLDVVEFMFDVTTKPI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191   85 LLDGDTGyGNFNSARRLVRKLEQRGIAGVCMEDKIFPKTNSFL-RSTAQPLADIEEFAGKIRAAKEAQTDSDFVVVARVE 163
Cdd:TIGR02320  81 ILDGDTG-GNFEHFRRLVRKLERRGVSAVCIEDKLGLKKNSLFgNDVAQPQASVEEFCGKIRAGKDAQTTEDFMIIARVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191  164 ALIAGHGLEEALKRGEAYRKAGADAILIHSKERHADEILAFKKEWGD---RLPLVIVPTKYYRTPTDVFREAGFKIVIWA 240
Cdd:TIGR02320 160 SLILGKGMEDALKRAEAYAEAGADGIMIHSRKKDPDEILEFARRFRNhypRTPLVIVPTSYYTTPTDEFRDAGISVVIYA 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 913621191  241 NHAMRSAITAMQATVKQIFQDEHLMNVEERVAPLADVFRLQGENE 285
Cdd:TIGR02320 240 NHLLRAAYAAMQQVAERILEHGRLVEVEDKCAPIKEIFRLIPGTE 284
ICL_PEPM cd00377
Members of the ICL/PEPM enzyme family catalyze either P-C or C-C bond formation/cleavage. ...
 13-257 5.84e-87

Members of the ICL/PEPM enzyme family catalyze either P-C or C-C bond formation/cleavage. Known members are phosphoenolpyruvate mutase (PEPM), phosphonopyruvate hydrolase (PPH), carboxyPEP mutase (CPEP mutase), oxaloacetate hydrolase (OAH), isocitrate lyase (ICL), and 2-methylisocitrate lyase (MICL). Isocitrate lyase (ICL) catalyzes the conversion of isocitrate to succinate and glyoxylate, the first committed step in the glyoxylate pathway. This carbon-conserving pathway is present in most prokaryotes, lower eukaryotes and plants, but has not been observed in vertebrates. PEP mutase (PEPM) turns phosphoenolpyruvate (PEP) into phosphonopyruvate (P-pyr), an important intermediate in the formation of organophosphonates, which function as antibiotics or play a role in pathogenesis or signaling. P-pyr can be hydrolyzed by phosphonopyruvate hydrolase (PPH) to from pyruvate and phosphate. Oxaloacetate acetylhydrolase (OAH) catalyzes the hydrolytic cleavage of oxaloacetate to form acetate and oxalate, an important pathway to produce oxalate in filamentous fungi. 2-methylisocitrate lyase (MICL) cleaves 2-methylisocitrate to pyruvate and succinate, part of the methylcitrate cycle for the alpha-oxidation of propionate.


Pssm-ID: 119340 [Multi-domain]  Cd Length: 243  Bit Score: 268.97  E-value: 5.84e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191  13 LRQMLEGQGLSFLMEAHNGLSAKIVEEAGFQGIWGSGLSISAALGVRDNNEASWTQVLEVVEFMADATTIPILLDGDTGY 92
Cdd:cd00377    1 LRALLESGGPLVLPGAWDALSARLAERAGFKAIYTSGAGVAASLGLPDGGLLTLDEVLAAVRRIARAVDLPVIADADTGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191  93 GNFNSARRLVRKLEQRGIAGVCMEDKIFPKTNSFLRStaQPLADIEEFAGKIRAAKEAQTD-SDFVVVARVEALIAG-HG 170
Cdd:cd00377   81 GNALNVARTVRELEEAGAAGIHIEDQVGPKKCGHHGG--KVLVPIEEFVAKIKAARDARDDlPDFVIIARTDALLAGeEG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 171 LEEALKRGEAYRKAGADAILIHSKeRHADEILAFKKEWGdrLPLVIVPTKYYRTPT-DVFREAGFKIVIWANHAMRSAIT 249
Cdd:cd00377  159 LDEAIERAKAYAEAGADGIFVEGL-KDPEEIRAFAEAPD--VPLNVNMTPGGNLLTvAELAELGVRRVSYGLALLRAAAK 235


                 ....*...
gi 913621191 250 AMQATVKQ 257
Cdd:cd00377  236 AMREAARE 243
PrpB COG2513
2-Methylisocitrate lyase and related enzymes, PEP mutase family [Carbohydrate transport and ...
 8-295 1.91e-66

2-Methylisocitrate lyase and related enzymes, PEP mutase family [Carbohydrate transport and metabolism];


Pssm-ID: 442003  Cd Length: 288  Bit Score: 217.31  E-value: 1.91e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191   8 KKTTRLRQMLEGQGLSFLMEAHNGLSAKIVEEAGFQGIWGSGLSISAA-LGVRDNNEASWTQVLEVVEFMADATTIPILL 86
Cdd:COG2513    1 SKRARFRALLASGGILVLPGAWDALSARLAEQAGFEALYLSGAGVAASlLGLPDLGLLTLTEVLEHARRIARAVDLPVIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191  87 DGDTGYGNFNSARRLVRKLEQRGIAGVCMEDKIFPKTNSFLRStaQPLADIEEFAGKIRAAKEAQTDSDFVVVARVEALi 166
Cdd:COG2513   81 DADTGFGNALNVARTVRELERAGVAGIHIEDQVGPKRCGHLPG--KEVVPAEEMVERIRAAVDARRDPDFVIIARTDAR- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 167 AGHGLEEALKRGEAYRKAGADAILIhskE--RHADEILAFKKEWGdrLPLVIVPTKYYRTP---TDVFREAGFKIVIWAN 241
Cdd:COG2513  158 AVEGLDEAIERAKAYAEAGADVIFV---EalTSLEEIRRVAAAVD--VPLLANMTEGGKTPlltAAELAELGVRRVSYPV 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 913621191 242 HAMRSAITAMQATVKQIFQDEHLMNVEERVAPLADVFRLQGENELEQAEKAYLP 295
Cdd:COG2513  233 SLLRAAAKAAERALRELREDGTQAALLDAMQTFAELYELLGYDEYEALEKRYFK 286
PEP_mutase pfam13714
Phosphoenolpyruvate phosphomutase; This domain includes the enzyme Phosphoenolpyruvate ...
 13-259 2.90e-66

Phosphoenolpyruvate phosphomutase; This domain includes the enzyme Phosphoenolpyruvate phosphomutase (EC:5.4.2.9). This protein Swiss:O86937 has been characterized as catalysing the formation of a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr). This enzyme has a TIM barrel fold.


Pssm-ID: 433424  Cd Length: 241  Bit Score: 215.14  E-value: 2.90e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191   13 LRQMLEGQGLSFLMEAHNGLSAKIVEEAGFQGIWGSGLSISAALGVRDNNEASWTQVLEVVEFMADATTIPILLDGDTGY 92
Cdd:pfam13714   1 FRALHRPGGPLVLPNAWDAASARIVEAAGFPAIATSSAGVAASLGYPDGELLPRDELLAAARRIAAAVDLPVSADLETGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191   93 GN-FNSARRLVRKLEQRGIAGVCMEDKifpKTNsflrSTAQPLADIEEFAGKIRAAKEAQTDS--DFVVVARVEALIAGH 169
Cdd:pfam13714  81 GDsPEEVAETVRRLIAAGVVGVNIEDS---KTG----RPGGQLLDVEEAAARIRAARAAARAAgvPFVINARTDAFLLGR 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191  170 G--LEEALKRGEAYRKAGADAILIHSKeRHADEILAFKKEWGdrLPLVIVPTKYYrTPTDVFREAGFKIVIWANHAMRSA 247
Cdd:pfam13714 154 GdaLEEAIRRARAYAEAGADGIFVPGL-LDPADIAALVAAVP--GPVNVLAGPGT-LSVAELAALGVARISYGNHLARAA 229

                         250
                  ....*....|..
gi 913621191  248 ITAMQATVKQIF 259
Cdd:pfam13714 230 LAALRRAAEEIL 241
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
302-545 1.77e-52

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 178.51  E-value: 1.77e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 302 RGIVLAAGQGKELGELVTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVVRGFAKKTVDI------TGATYVDNDAYAT 375
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEalarpgPDVTFVYNPDYDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 376 TSEVASLACAKASLDGPCVVSYGDVLFKKYVLDELLDAEGDFVVAVDslpadeasanaaaalaknepvrrSDWAICSEpH 455
Cdd:COG1213   81 TNNIYSLWLAREALDEDFLLLNGDVVFDPAILKRLLASDGDIVLLVD-----------------------RKWEKPLD-E 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 456 SRKALFNQV-VLKDMTTDPTAAGITGEWTGLLKLSTQGAKFVREILDGMPASELETIKVPDLLRRLVRDGMTVRVVY-SR 533
Cdd:COG1213  137 EVKVRVDEDgRIVEIGKKLPPEEADGEYIGIFKFSAEGAAALREALEALIDEGGPNLYYEDALQELIDEGGPVKAVDiGG 216

                        250
                 ....*....|..
gi 913621191 534 GGWLDIDTIGDV 545
Cdd:COG1213  217 LPWVEIDTPEDL 228
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 304-544 2.61e-44

Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 156.62  E-value: 2.61e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 304 IVLAAGQGKELGELVTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVVRGFAKKTVDI-----TGATYVDNDAYATTSE 378
Cdd:cd02523    2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEEllkkyPNIKFVYNPDYAETNN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 379 VASLACAKASLDGPCVVSYGDVLFKKYVLDELLDAEGDFVVAVDSlpadeasanaaaalaknepvRRSDWAIcsepHSRK 458
Cdd:cd02523   82 IYSLYLARDFLDEDFLLLEGDVVFDPSILERLLSSPADNAILVDK--------------------KTKEWED----EYVK 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 459 ALFNQVVLKDMTTDPTAAG-ITGEWTGLLKLSTQGAKFVREILDGMPASELETIKVPDLLRRLV-RDGMTVRVVYSrGGW 536
Cdd:cd02523  138 DLDDAGVLLGIISKAKNLEeIQGEYVGISKFSPEDADRLAEALEELIEAGRVNLYYEDALQRLIsEEGVKVKDISD-GFW 216


                 ....*...
gi 913621191 537 LDIDTIGD 544
Cdd:cd02523  217 YEIDDLED 224
prpB PRK11320
2-methylisocitrate lyase; Provisional
 30-261 2.56e-26

2-methylisocitrate lyase; Provisional


Pssm-ID: 183086  Cd Length: 292  Bit Score: 108.83  E-value: 2.56e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191  30 NGLSAKIVEEAGFQGIWGSGLSISAA-LGVRDNNEASWTQVLEVVEFMADATTIPILLDGDTGYGN-FNSARRlVRKLEQ 107
Cdd:PRK11320  26 NAYHALLAERAGFKAIYLSGGGVAAAsLGLPDLGITTLDDVLIDVRRITDACDLPLLVDIDTGFGGaFNIART-VKSMIK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 108 RGIAGVCMEDKIFPKtnsflRSTAQP---LADIEEFAGKIRAAKEAQTDSDFVVVARVEALiAGHGLEEALKRGEAYRKA 184
Cdd:PRK11320 105 AGAAAVHIEDQVGAK-----RCGHRPnkeIVSQEEMVDRIKAAVDARTDPDFVIMARTDAL-AVEGLDAAIERAQAYVEA 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 185 GADAIL---IHSkerhADEILAFKKEwgdrlplVIVP-----TKYYRTP---TDVFREAGFKIVIWAnhamRSAITAMQA 253
Cdd:PRK11320 179 GADMIFpeaMTE----LEMYRRFADA-------VKVPilaniTEFGATPlftTEELASAGVAMVLYP----LSAFRAMNK 243


                 ....*...
gi 913621191 254 TVKQIFQD 261
Cdd:PRK11320 244 AAENVYEA 251
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 303-423 2.37e-08

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 53.35  E-value: 2.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191  303 GIVLAAGQGKELGelvtdRPKCMVPIAGKPILGHIMDAYRSAGvRDLIVVRGFAKKTVDI--TGATYVDNDAYAtTSEVA 380
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPAG-DEVVVVANDEEVLAALagLGVPVVPDPDPG-QGPLA 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 913621191  381 SLACA--KASLDGPCVVSYGDV-LFKKYVLDELLDA----EGDFVVAVDS 423
Cdd:pfam12804  74 GLLAAlrAAPGADAVLVLACDMpFLTPELLRRLLAAaeesGADIVVPVYD 123
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 304-400 2.91e-08

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 56.02  E-value: 2.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 304 IVLAAGQGKELGelvTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVVRGF-------AKKTVDITGATYVDNDAYATT 376
Cdd:PRK14353   9 IILAAGEGTRMK---SSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPgaeavaaAAAKIAPDAEIFVQKERLGTA 85

                         90       100
                 ....*....|....*....|....
gi 913621191 377 SEVASLACAKASLDGPCVVSYGDV 400
Cdd:PRK14353  86 HAVLAAREALAGGYGDVLVLYGDT 109
 
Name Accession Description Interval E-value
PEP_mutase TIGR02320
phosphoenolpyruvate mutase; This family consists of examples of phosphoenolpyruvate ...
 13-285 3.74e-148

phosphoenolpyruvate mutase; This family consists of examples of phosphoenolpyruvate phosphomutase, an enzyme that creates a C-P bond as the first step in the biosynthesis of natural products including antibiotics like bialaphos and phosphonothricin in Streptomyces species, phosphonate-modified molecules such as the polysaccharide B of Bacteroides fragilis, the phosphonolipids of Tetrahymena pyroformis, the glycosylinositolphospholipids of Trypanosoma cruzi. This gene generally occurs in prokaryotic organisms adjacent to the gene for phosphonopyruvate decarboxylase (aepY). Since the PEP phosphomutase reaction favors the substrate PEP energetically, the decarboxylase is required to drive the reaction in the direction of phosphonate production. Most often an aminotansferase (aepZ) is also present which leads to the production of the most common phosphonate compound, 2-aminoethylphosphonate (AEP). A closely related enzyme, phosphonopyruvate hydrolase from Variovorax sp. Pal2, is excluded from this model.


Pssm-ID: 274077  Cd Length: 284  Bit Score: 427.12  E-value: 3.74e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191   13 LRQMLEGQGLSFLMEAHNGLSAKIVEEA--------GFQGIWGSGLSISAALGVRDNNEASWTQVLEVVEFMADATTIPI 84
Cdd:TIGR02320   1 LRQLLHSKPLERLMEAHNGLSALIAEEArvevgdslGFDGIWSSSLTDSTSRGVPDIEEASWTQRLDVVEFMFDVTTKPI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191   85 LLDGDTGyGNFNSARRLVRKLEQRGIAGVCMEDKIFPKTNSFL-RSTAQPLADIEEFAGKIRAAKEAQTDSDFVVVARVE 163
Cdd:TIGR02320  81 ILDGDTG-GNFEHFRRLVRKLERRGVSAVCIEDKLGLKKNSLFgNDVAQPQASVEEFCGKIRAGKDAQTTEDFMIIARVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191  164 ALIAGHGLEEALKRGEAYRKAGADAILIHSKERHADEILAFKKEWGD---RLPLVIVPTKYYRTPTDVFREAGFKIVIWA 240
Cdd:TIGR02320 160 SLILGKGMEDALKRAEAYAEAGADGIMIHSRKKDPDEILEFARRFRNhypRTPLVIVPTSYYTTPTDEFRDAGISVVIYA 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 913621191  241 NHAMRSAITAMQATVKQIFQDEHLMNVEERVAPLADVFRLQGENE 285
Cdd:TIGR02320 240 NHLLRAAYAAMQQVAERILEHGRLVEVEDKCAPIKEIFRLIPGTE 284
ICL_PEPM cd00377
Members of the ICL/PEPM enzyme family catalyze either P-C or C-C bond formation/cleavage. ...
 13-257 5.84e-87

Members of the ICL/PEPM enzyme family catalyze either P-C or C-C bond formation/cleavage. Known members are phosphoenolpyruvate mutase (PEPM), phosphonopyruvate hydrolase (PPH), carboxyPEP mutase (CPEP mutase), oxaloacetate hydrolase (OAH), isocitrate lyase (ICL), and 2-methylisocitrate lyase (MICL). Isocitrate lyase (ICL) catalyzes the conversion of isocitrate to succinate and glyoxylate, the first committed step in the glyoxylate pathway. This carbon-conserving pathway is present in most prokaryotes, lower eukaryotes and plants, but has not been observed in vertebrates. PEP mutase (PEPM) turns phosphoenolpyruvate (PEP) into phosphonopyruvate (P-pyr), an important intermediate in the formation of organophosphonates, which function as antibiotics or play a role in pathogenesis or signaling. P-pyr can be hydrolyzed by phosphonopyruvate hydrolase (PPH) to from pyruvate and phosphate. Oxaloacetate acetylhydrolase (OAH) catalyzes the hydrolytic cleavage of oxaloacetate to form acetate and oxalate, an important pathway to produce oxalate in filamentous fungi. 2-methylisocitrate lyase (MICL) cleaves 2-methylisocitrate to pyruvate and succinate, part of the methylcitrate cycle for the alpha-oxidation of propionate.


Pssm-ID: 119340 [Multi-domain]  Cd Length: 243  Bit Score: 268.97  E-value: 5.84e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191  13 LRQMLEGQGLSFLMEAHNGLSAKIVEEAGFQGIWGSGLSISAALGVRDNNEASWTQVLEVVEFMADATTIPILLDGDTGY 92
Cdd:cd00377    1 LRALLESGGPLVLPGAWDALSARLAERAGFKAIYTSGAGVAASLGLPDGGLLTLDEVLAAVRRIARAVDLPVIADADTGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191  93 GNFNSARRLVRKLEQRGIAGVCMEDKIFPKTNSFLRStaQPLADIEEFAGKIRAAKEAQTD-SDFVVVARVEALIAG-HG 170
Cdd:cd00377   81 GNALNVARTVRELEEAGAAGIHIEDQVGPKKCGHHGG--KVLVPIEEFVAKIKAARDARDDlPDFVIIARTDALLAGeEG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 171 LEEALKRGEAYRKAGADAILIHSKeRHADEILAFKKEWGdrLPLVIVPTKYYRTPT-DVFREAGFKIVIWANHAMRSAIT 249
Cdd:cd00377  159 LDEAIERAKAYAEAGADGIFVEGL-KDPEEIRAFAEAPD--VPLNVNMTPGGNLLTvAELAELGVRRVSYGLALLRAAAK 235


                 ....*...
gi 913621191 250 AMQATVKQ 257
Cdd:cd00377  236 AMREAARE 243
PrpB COG2513
2-Methylisocitrate lyase and related enzymes, PEP mutase family [Carbohydrate transport and ...
 8-295 1.91e-66

2-Methylisocitrate lyase and related enzymes, PEP mutase family [Carbohydrate transport and metabolism];


Pssm-ID: 442003  Cd Length: 288  Bit Score: 217.31  E-value: 1.91e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191   8 KKTTRLRQMLEGQGLSFLMEAHNGLSAKIVEEAGFQGIWGSGLSISAA-LGVRDNNEASWTQVLEVVEFMADATTIPILL 86
Cdd:COG2513    1 SKRARFRALLASGGILVLPGAWDALSARLAEQAGFEALYLSGAGVAASlLGLPDLGLLTLTEVLEHARRIARAVDLPVIA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191  87 DGDTGYGNFNSARRLVRKLEQRGIAGVCMEDKIFPKTNSFLRStaQPLADIEEFAGKIRAAKEAQTDSDFVVVARVEALi 166
Cdd:COG2513   81 DADTGFGNALNVARTVRELERAGVAGIHIEDQVGPKRCGHLPG--KEVVPAEEMVERIRAAVDARRDPDFVIIARTDAR- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 167 AGHGLEEALKRGEAYRKAGADAILIhskE--RHADEILAFKKEWGdrLPLVIVPTKYYRTP---TDVFREAGFKIVIWAN 241
Cdd:COG2513  158 AVEGLDEAIERAKAYAEAGADVIFV---EalTSLEEIRRVAAAVD--VPLLANMTEGGKTPlltAAELAELGVRRVSYPV 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 913621191 242 HAMRSAITAMQATVKQIFQDEHLMNVEERVAPLADVFRLQGENELEQAEKAYLP 295
Cdd:COG2513  233 SLLRAAAKAAERALRELREDGTQAALLDAMQTFAELYELLGYDEYEALEKRYFK 286
PEP_mutase pfam13714
Phosphoenolpyruvate phosphomutase; This domain includes the enzyme Phosphoenolpyruvate ...
 13-259 2.90e-66

Phosphoenolpyruvate phosphomutase; This domain includes the enzyme Phosphoenolpyruvate phosphomutase (EC:5.4.2.9). This protein Swiss:O86937 has been characterized as catalysing the formation of a carbon-phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-Pyr). This enzyme has a TIM barrel fold.


Pssm-ID: 433424  Cd Length: 241  Bit Score: 215.14  E-value: 2.90e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191   13 LRQMLEGQGLSFLMEAHNGLSAKIVEEAGFQGIWGSGLSISAALGVRDNNEASWTQVLEVVEFMADATTIPILLDGDTGY 92
Cdd:pfam13714   1 FRALHRPGGPLVLPNAWDAASARIVEAAGFPAIATSSAGVAASLGYPDGELLPRDELLAAARRIAAAVDLPVSADLETGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191   93 GN-FNSARRLVRKLEQRGIAGVCMEDKifpKTNsflrSTAQPLADIEEFAGKIRAAKEAQTDS--DFVVVARVEALIAGH 169
Cdd:pfam13714  81 GDsPEEVAETVRRLIAAGVVGVNIEDS---KTG----RPGGQLLDVEEAAARIRAARAAARAAgvPFVINARTDAFLLGR 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191  170 G--LEEALKRGEAYRKAGADAILIHSKeRHADEILAFKKEWGdrLPLVIVPTKYYrTPTDVFREAGFKIVIWANHAMRSA 247
Cdd:pfam13714 154 GdaLEEAIRRARAYAEAGADGIFVPGL-LDPADIAALVAAVP--GPVNVLAGPGT-LSVAELAALGVARISYGNHLARAA 229

                         250
                  ....*....|..
gi 913621191  248 ITAMQATVKQIF 259
Cdd:pfam13714 230 LAALRRAAEEIL 241
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
302-545 1.77e-52

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 178.51  E-value: 1.77e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 302 RGIVLAAGQGKELGELVTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVVRGFAKKTVDI------TGATYVDNDAYAT 375
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEalarpgPDVTFVYNPDYDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 376 TSEVASLACAKASLDGPCVVSYGDVLFKKYVLDELLDAEGDFVVAVDslpadeasanaaaalaknepvrrSDWAICSEpH 455
Cdd:COG1213   81 TNNIYSLWLAREALDEDFLLLNGDVVFDPAILKRLLASDGDIVLLVD-----------------------RKWEKPLD-E 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 456 SRKALFNQV-VLKDMTTDPTAAGITGEWTGLLKLSTQGAKFVREILDGMPASELETIKVPDLLRRLVRDGMTVRVVY-SR 533
Cdd:COG1213  137 EVKVRVDEDgRIVEIGKKLPPEEADGEYIGIFKFSAEGAAALREALEALIDEGGPNLYYEDALQELIDEGGPVKAVDiGG 216

                        250
                 ....*....|..
gi 913621191 534 GGWLDIDTIGDV 545
Cdd:COG1213  217 LPWVEIDTPEDL 228
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 304-544 2.61e-44

Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 156.62  E-value: 2.61e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 304 IVLAAGQGKELGELVTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVVRGFAKKTVDI-----TGATYVDNDAYATTSE 378
Cdd:cd02523    2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEEllkkyPNIKFVYNPDYAETNN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 379 VASLACAKASLDGPCVVSYGDVLFKKYVLDELLDAEGDFVVAVDSlpadeasanaaaalaknepvRRSDWAIcsepHSRK 458
Cdd:cd02523   82 IYSLYLARDFLDEDFLLLEGDVVFDPSILERLLSSPADNAILVDK--------------------KTKEWED----EYVK 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 459 ALFNQVVLKDMTTDPTAAG-ITGEWTGLLKLSTQGAKFVREILDGMPASELETIKVPDLLRRLV-RDGMTVRVVYSrGGW 536
Cdd:cd02523  138 DLDDAGVLLGIISKAKNLEeIQGEYVGISKFSPEDADRLAEALEELIEAGRVNLYYEDALQRLIsEEGVKVKDISD-GFW 216


                 ....*...
gi 913621191 537 LDIDTIGD 544
Cdd:cd02523  217 YEIDDLED 224
prpB PRK11320
2-methylisocitrate lyase; Provisional
 30-261 2.56e-26

2-methylisocitrate lyase; Provisional


Pssm-ID: 183086  Cd Length: 292  Bit Score: 108.83  E-value: 2.56e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191  30 NGLSAKIVEEAGFQGIWGSGLSISAA-LGVRDNNEASWTQVLEVVEFMADATTIPILLDGDTGYGN-FNSARRlVRKLEQ 107
Cdd:PRK11320  26 NAYHALLAERAGFKAIYLSGGGVAAAsLGLPDLGITTLDDVLIDVRRITDACDLPLLVDIDTGFGGaFNIART-VKSMIK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 108 RGIAGVCMEDKIFPKtnsflRSTAQP---LADIEEFAGKIRAAKEAQTDSDFVVVARVEALiAGHGLEEALKRGEAYRKA 184
Cdd:PRK11320 105 AGAAAVHIEDQVGAK-----RCGHRPnkeIVSQEEMVDRIKAAVDARTDPDFVIMARTDAL-AVEGLDAAIERAQAYVEA 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 185 GADAIL---IHSkerhADEILAFKKEwgdrlplVIVP-----TKYYRTP---TDVFREAGFKIVIWAnhamRSAITAMQA 253
Cdd:PRK11320 179 GADMIFpeaMTE----LEMYRRFADA-------VKVPilaniTEFGATPlftTEELASAGVAMVLYP----LSAFRAMNK 243


                 ....*...
gi 913621191 254 TVKQIFQD 261
Cdd:PRK11320 244 AAENVYEA 251
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 302-544 4.20e-24

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 101.00  E-value: 4.20e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 302 RGIVLAAGQGKELGELVTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVVRGF------------AKKTVDITgatYVD 369
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYlaeqieeyfgdgSRFGVRIT---YVD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 370 NDayaTTSEVA-SLACAKASL-DGPCVVSYGDVLFKKYvLDELLDA----EGDFVVAVdslpadeasanaaaalaknepV 443
Cdd:COG1208   78 EG---EPLGTGgALKRALPLLgDEPFLVLNGDILTDLD-LAALLAFhrekGADATLAL---------------------V 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 444 RRsdwaicsEPHSRKALF---NQVVLKDMTTDPTAAGITGEWTGLLKLStqgakfvREILDGMPASEleTIKVPDLLRRL 520
Cdd:COG1208  133 PV-------PDPSRYGVVeldGDGRVTRFVEKPEEPPSNLINAGIYVLE-------PEIFDYIPEGE--PFDLEDLLPRL 196

                        250       260
                 ....*....|....*....|....
gi 913621191 521 VRDGmTVRVVYSRGGWLDIDTIGD 544
Cdd:COG1208  197 IAEG-RVYGYVHDGYWLDIGTPED 219
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 303-402 4.95e-17

NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 79.93  E-value: 4.95e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 303 GIVLAAGQGKELGELVTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVVRGF------------AKKTVDItgaTYVDN 370
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYlgeqieeyfgdgSKFGVNI---EYVVQ 77

                         90       100       110
                 ....*....|....*....|....*....|...
gi 913621191 371 DAYATTseVASLACAKASL-DGPCVVSYGDVLF 402
Cdd:cd04181   78 EEPLGT--AGAVRNAEDFLgDDDFLVVNGDVLT 108
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 303-420 3.51e-11

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 62.19  E-value: 3.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 303 GIVLAAGQGKELGelvtdRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVVRGF----AKKTVDITGATYVDNDAYAT--- 375
Cdd:cd04182    3 AIILAAGRSSRMG-----GNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAeadaVRAALAGLPVVVVINPDWEEgms 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 913621191 376 TSEVASLACAKASLDGpCVVSYGD-VLFKKYVLDELLDA---EGDFVVA 420
Cdd:cd04182   78 SSLAAGLEALPADADA-VLILLADqPLVTAETLRALIDAfreDGAGIVA 125
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 302-354 5.30e-11

G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 62.97  E-value: 5.30e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 913621191 302 RGIVLAAGQGKELGELVTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVVRG 354
Cdd:cd04189    2 KGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVG 54
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 304-413 8.01e-11

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 64.28  E-value: 8.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 304 IVLAAGQGKELGelvTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVVRGFA----KKTVDITGATYVDND-----AYA 374
Cdd:COG1207    6 VILAAGKGTRMK---SKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGaeqvRAALADLDVEFVLQEeqlgtGHA 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 913621191 375 ttsevasLACAKASL---DGPCVVSYGDV-LFKKYVLDELLDA 413
Cdd:COG1207   83 -------VQQALPALpgdDGTVLVLYGDVpLIRAETLKALLAA 118
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
303-416 1.12e-10

CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 60.94  E-value: 1.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 303 GIVLAAGQGKELGelvtdRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVVRGFA----KKTVDITGATYVDNDAYA---- 374
Cdd:COG2068    6 AIILAAGASSRMG-----RPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADaeevAAALAGLGVRVVVNPDWEegms 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 913621191 375 ---------------------------TTSEVASLACAKASLDGPCVV-SYGD-----VLFKKYVLDELLDAEGD 416
Cdd:COG2068   81 sslraglaalpadadavlvllgdqplvTAETLRRLLAAFRESPASIVApTYDGrrghpVLFSRRLFPELLALTGD 155
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 304-355 1.82e-10

G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.


Pssm-ID: 133015 [Multi-domain]  Cd Length: 253  Bit Score: 61.43  E-value: 1.82e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 913621191 304 IVLAAGQGKELGELVTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVVRGF 355
Cdd:cd02524    2 VILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGY 53
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 304-355 3.84e-10

WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars.


Pssm-ID: 133065 [Multi-domain]  Cd Length: 223  Bit Score: 59.87  E-value: 3.84e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 913621191 304 IVLAAGQGKELGELVTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVVRGF 355
Cdd:cd06915    2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGY 53
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 305-351 3.90e-10

NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 59.89  E-value: 3.90e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 913621191 305 VLAAGQGKELGELVTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIV 351
Cdd:cd06422    4 ILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVV 50
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 304-413 1.33e-09

N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 58.68  E-value: 1.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 304 IVLAAGQGKELGelvTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVVRGFA----KKTVDITGATYVDND-----AYA 374
Cdd:cd02540    2 VILAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGaeqvKKALANPNVEFVLQEeqlgtGHA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 913621191 375 ttsevasLACAKASLDGPC---VVSYGDV-LFKKYVLDELLDA 413
Cdd:cd02540   79 -------VKQALPALKDFEgdvLVLYGDVpLITPETLQRLLEA 114
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 304-544 1.16e-08

NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133048 [Multi-domain]  Cd Length: 220  Bit Score: 55.60  E-value: 1.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 304 IVLAAGQGKELGELVTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVVRGF------------AKKTVDItgaTYVDND 371
Cdd:cd06426    2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYlaemiedyfgdgSKFGVNI---SYVRED 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 372 AYATTSevASLACAKASLDGPCVVSYGDVLFKkyvLD--ELLDAEgdfvvavdslpadeasanaaaalAKNepvrRSDWA 449
Cdd:cd06426   79 KPLGTA--GALSLLPEKPTDPFLVMNGDILTN---LNyeHLLDFH-----------------------KEN----NADAT 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 450 ICSEPHSRKALF-----NQVVLKDMTTDPT-----AAGITgewtgLLKlstqgakfvREILDGMPASelETIKVPDLLRR 519
Cdd:cd06426  127 VCVREYEVQVPYgvvetEGGRITSIEEKPThsflvNAGIY-----VLE---------PEVLDLIPKN--EFFDMPDLIEK 190

                        250       260
                 ....*....|....*....|....*
gi 913621191 520 LVRDGMTVRVVYSRGGWLDIDTIGD 544
Cdd:cd06426  191 LIKEGKKVGVFPIHEYWLDIGRPED 215
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 303-423 2.37e-08

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 53.35  E-value: 2.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191  303 GIVLAAGQGKELGelvtdRPKCMVPIAGKPILGHIMDAYRSAGvRDLIVVRGFAKKTVDI--TGATYVDNDAYAtTSEVA 380
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPAG-DEVVVVANDEEVLAALagLGVPVVPDPDPG-QGPLA 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 913621191  381 SLACA--KASLDGPCVVSYGDV-LFKKYVLDELLDA----EGDFVVAVDS 423
Cdd:pfam12804  74 GLLAAlrAAPGADAVLVLACDMpFLTPELLRRLLAAaeesGADIVVPVYD 123
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 304-400 2.91e-08

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 56.02  E-value: 2.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 304 IVLAAGQGKELGelvTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVVRGF-------AKKTVDITGATYVDNDAYATT 376
Cdd:PRK14353   9 IILAAGEGTRMK---SSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPgaeavaaAAAKIAPDAEIFVQKERLGTA 85

                         90       100
                 ....*....|....*....|....
gi 913621191 377 SEVASLACAKASLDGPCVVSYGDV 400
Cdd:PRK14353  86 HAVLAAREALAGGYGDVLVLYGDT 109
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
302-413 9.87e-08

dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 53.56  E-value: 9.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 302 RGIVLAAGQGKELGELVTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVVRG------FAKKTVDIT--GA--TYVDND 371
Cdd:COG1209    2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTpedgpqFERLLGDGSqlGIkiSYAVQP 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 913621191 372 -----AYAttsevasLACAKASLDG-PCVVSYGDVLFKKYVLDELLDA 413
Cdd:COG1209   82 eplglAHA-------FIIAEDFIGGdPVALVLGDNIFYGDGLSELLRE 122
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 303-352 1.65e-07

The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 51.89  E-value: 1.65e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 913621191 303 GIVLAAGQGKELGELVTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVV 352
Cdd:cd04198    3 AVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVV 52
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 303-352 2.15e-07

The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 51.87  E-value: 2.15e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 913621191 303 GIVLAAGQGKELGELVTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVV 352
Cdd:cd02507    3 AVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVV 52
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 304-412 4.81e-07

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 52.14  E-value: 4.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 304 IVLAAGQGKELGelvTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVVRGFAKKTV-DITGatyvDNDAYATTSEVASL 382
Cdd:PRK14354   6 IILAAGKGTRMK---SKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVkEVLG----DRSEFALQEEQLGT 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 913621191 383 A----CAK---ASLDGPCVVSYGDV-LFKKYVLDELLD 412
Cdd:PRK14354  79 GhavmQAEeflADKEGTTLVICGDTpLITAETLKNLID 116
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 304-413 1.79e-06

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 50.71  E-value: 1.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 304 IVLAAGQGKELGelvTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVVRGFAKKTVditgATYVdnDAYATTSEVA--- 380
Cdd:PRK14352   8 IVLAAGAGTRMR---SDTPKVLHTLAGRSMLGHVLHAAAGLAPQHLVVVVGHDRERV----APAV--AELAPEVDIAvqd 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 913621191 381 -----------SLACAKASLDGPCVVSYGDV-LFKKYVLDELLDA 413
Cdd:PRK14352  79 eqpgtghavqcALEALPADFDGTVVVTAGDVpLLDGETLADLVAT 123
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 304-352 3.56e-06

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440824  Cd Length: 224  Bit Score: 48.20  E-value: 3.56e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 913621191 304 IVLAAGQGKELGelvTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVV 352
Cdd:COG1211    1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVV 46
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 303-331 1.24e-05

Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 47.76  E-value: 1.24e-05
                         10        20
                 ....*....|....*....|....*....
gi 913621191 303 GIVLAAGQGKELGELVTDRPKCMVPIAGK 331
Cdd:COG0448    4 AIILAGGRGSRLGPLTKDRAKPAVPFGGK 32
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 304-412 1.56e-05

bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 47.67  E-value: 1.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 304 IVLAAGQGKELGELVtdrPKCMVPIAGKPILGHIMDAYRSAGVRDLIVVRGFAKKTVDI----TGATYVDNDAYATTSEv 379
Cdd:PRK14358  11 VILAAGQGTRMKSAL---PKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAalqgSGVAFARQEQQLGTGD- 86

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 913621191 380 ASLACAKA--SLDGPCVVSYGDV-LFKKYVLDELLD 412
Cdd:PRK14358  87 AFLSGASAltEGDADILVLYGDTpLLRPDTLRALVA 122
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
304-352 2.12e-05

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 45.89  E-value: 2.12e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 913621191 304 IVLAAGQGKELGelvTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVV 352
Cdd:PRK00155   7 IIPAAGKGSRMG---ADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIV 52
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 304-352 1.76e-04

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 42.90  E-value: 1.76e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 913621191 304 IVLAAGQGKELGelvTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVV 352
Cdd:cd02516    4 IILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVV 49
ICL pfam00463
Isocitrate lyase family;
83-164 1.97e-04

Isocitrate lyase family;


Pssm-ID: 278869 [Multi-domain]  Cd Length: 526  Bit Score: 44.05  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191   83 PILLDGDTGYGNFNSARRLVRKLEQRGIAGVCMEDKIfPKTNSFLRSTAQPLADIEEFAGKIRAAKeAQTD---SDFVVV 159
Cdd:pfam00463 151 PIIADADTGHGGLTAVVKLTKLFIERGAAGIHIEDQA-PGTKKCGHMAGKVLVPIQEHINRLVAIR-AQADimgSDLLAV 228


                  ....*
gi 913621191  160 ARVEA 164
Cdd:pfam00463 229 ARTDS 233
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 304-425 5.33e-04

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 42.79  E-value: 5.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 304 IVLAAGQGKELGelvTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVVRGFAKKTVDitgATYVDNDAYATTSEVA--- 380
Cdd:PRK14356   9 LILAAGKGTRMH---SDKPKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVGHRADMVR---AAFPDEDARFVLQEQQlgt 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 913621191 381 --SLACA-----KASLDgPCVVSYGDV-LFKKYVLDELLDA--EGDFVVAVDSLP 425
Cdd:PRK14356  83 ghALQCAwpsltAAGLD-RVLVVNGDTpLVTTDTIDDFLKEaaGADLAFMTLTLP 136
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 303-331 6.07e-04

ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP. ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. While a homotetramer in bacteria, in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits. There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. It is a subfamily of a very diverse glycosy transferase family 2.


Pssm-ID: 133002 [Multi-domain]  Cd Length: 200  Bit Score: 41.37  E-value: 6.07e-04
                         10        20
                 ....*....|....*....|....*....
gi 913621191 303 GIVLAAGQGKELGELVTDRPKCMVPIAGK 331
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFGGR 29
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 303-353 7.52e-04

MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 40.64  E-value: 7.52e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 913621191 303 GIVLAAGQGKELGelvtdRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVVR 353
Cdd:cd02503    3 GVILAGGKSRRMG-----GDKALLELGGKPLLEHVLERLKPLVDEVVISAN 48
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 302-352 7.83e-04

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 41.47  E-value: 7.83e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 913621191  302 RGIVLAAGQGKELGELVTDRPKCMVPIAGK-PILGHIMDAYRSAGVRDLIVV 352
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVI 52
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 302-351 1.28e-03

N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 40.66  E-value: 1.28e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 913621191 302 RGIVLAAGQGKELGELVTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIV 351
Cdd:cd06425    2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIIL 51
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 303-352 2.15e-03

Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 39.41  E-value: 2.15e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 913621191 303 GIVLAAGQGKELGelvtdRPKCMVPIAGKPILGHIMDAYRSAgVRDLIVV 352
Cdd:COG0746    7 GVILAGGRSRRMG-----QDKALLPLGGRPLLERVLERLRPQ-VDEVVIV 50
PLN02892 PLN02892
isocitrate lyase
 83-167 2.29e-03

isocitrate lyase


Pssm-ID: 215482 [Multi-domain]  Cd Length: 570  Bit Score: 40.58  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191  83 PILLDGDTGYGNFNSARRLVRKLEQRGIAGVCMEDKIfPKTNSFLRSTAQPLADIEEFAGKIRAAKeAQTD---SDFVVV 159
Cdd:PLN02892 171 PIIADGDTGFGGTTATVKLCKLFVERGAAGVHIEDQS-SVTKKCGHMGGKVLVATSEHINRLVAAR-LQFDvmgVETVLV 248


                 ....*...
gi 913621191 160 ARVEALIA 167
Cdd:PLN02892 249 ARTDAVAA 256
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 304-352 3.97e-03

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes which catalyze the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from cytidine triphosphate and 2-C-methyl-D-erythritol 4-phosphate (MEP).


Pssm-ID: 460075  Cd Length: 219  Bit Score: 38.97  E-value: 3.97e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 913621191  304 IVLAAGQGKELGElvtDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVV 352
Cdd:pfam01128   2 VIPAAGSGKRMGA---GVPKQFLQLLGQPLLEHTVDAFLASPVVDRIVV 47
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 304-391 5.34e-03

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 39.34  E-value: 5.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 913621191 304 IVLAAGQGKELGelvTDRPKCMVPIAGKPILGHIMDAYRSAGVRDLIVVRGFAKKTVditgatyvdNDAYATTSEVA--- 380
Cdd:PRK14355   7 IILAAGKGTRMK---SDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKV---------REHFAGDGDVSfal 74

                         90       100
                 ....*....|....*....|
gi 913621191 381 ---------SLACAKASLDG 391
Cdd:PRK14355  75 qeeqlgtghAVACAAPALDG 94
 
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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