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Conserved domains on  [gi|247269309|ref|NP_034038|]
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N-acylneuraminate cytidylyltransferase isoform 1 [Mus musculus]

Protein Classification

N-acylneuraminate cytidylyltransferase( domain architecture ID 11551987)

N-acylneuraminate cytidylyltransferase catalyzes the activation of N-acetylneuraminic acid (NeuNAc) to cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuNAc), a substrate required for the addition of sialic acid; contains a HAD (haloacid dehalogenase) domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CMP-NeuAc_Synthase cd02513
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ...
 42-257 4.39e-91

CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; CMP-N-acetylneuraminic acid synthetase (CMP-NeuAc synthetase) or acylneuraminate cytidylyltransferase catalyzes the transfer the CMP moiety of CTP to the anomeric hydroxyl group of NeuAc in the presence of Mg++. It is the second to last step in the sialylation of the oligosaccharide component of glycoconjugates by providing the activated sugar-nucleotide cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-Neu5Ac), the substrate for sialyltransferases. Eukaryotic CMP-NeuAc synthetases are predominantly located in the nucleus. The activated CMP-Neu5Ac diffuses from the nucleus into the cytoplasm.


:

Pssm-ID: 133006  Cd Length: 223  Bit Score: 274.80  E-value: 4.39e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309  42 HLAALVLARGGSKGIPLKNIKRLAGVPLIGWVLRAALDAGVFQSVWVSTDHDEIENVAKQFGA-QVHRRSSETSKDSSTS 120
Cdd:cd02513    1 KILAIIPARGGSKGIPGKNIRPLGGKPLIAWTIEAALESKLFDRVVVSTDDEEIAEVARKYGAeVPFLRPAELATDTASS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309 121 LDAIVEFLNYHNE----VDIVGNIQATSPCLHPTDLQKVAEMIREEGYDSVFSVVRRHQFRWSEIQKGvREVTEPLNLNP 196
Cdd:cd02513   81 IDVILHALDQLEElgrdFDIVVLLQPTSPLRSAEDIDEAIELLLSEGADSVFSVTEFHRFPWRALGLD-DNGLEPVNYPE 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 247269309 197 AKRPRRQDWDGELYENGSFYFAKRH-LIEMGYLQGGKMAYYEMRAEHSVDIDVDIDWPIAEQ 257
Cdd:cd02513  160 DKRTRRQDLPPAYHENGAIYIAKREaLLESNSFFGGKTGPYEMPRERSIDIDTEEDFELAEA 221
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 273-417 7.79e-57

haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) phosphatase KdsC, and rainbow trout N-acylneuraminate cytidylyltransferase; KDO 8-P phosphatase catalyzes the hydrolysis of KDO 8-P to KDO (3-deoxy-D-manno-octulosonate) and inorganic phosphate and is the last enzyme in the KDO biosynthetic pathway. KDO is an 8-carbon sugar that links the lipid A and polysaccharide moieties of the lipopolysaccharide region in Gram-negative bacteria. An interruption in KDO biosynthesis leads to the accumulation of lipid A precursors and subsequent arrest in cell growth. The KDO biosynthesis pathway involves five sequential enzymatic reactions. This family also includes rainbow trout CMP-sialic acid synthetase which effectively converts both deaminoneuraminic acid (KDN, 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid) and N-acetylneuraminic acid (Neu5Ac) to CMP-KDN and CMP-Neu5Ac, respectively. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


:

Pssm-ID: 319769 [Multi-domain]  Cd Length: 146  Bit Score: 183.88  E-value: 7.79e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309 273 IKLLVCNIDGCLTNGHIYVSGDQKEIISYDVKDAIGISLLKKSGIEVRLISERAcSKQTLSALKLD--CKTEVSVSDKLA 350
Cdd:cd01630    1 IKLLVLDVDGVLTDGRIYYDSNGEELKSFNVRDGLGIKLLQKSGIEVAIITGRQ-SEAVRRRAKELgiEDLFQGVKDKLE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 247269309 351 TVDEWRKEMGLCWKEVAYLGNEVSDEECLKRVGLSAVPADACSGAQKAVGYICKCSGGRGAIREFAE 417
Cdd:cd01630   80 ALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGRGAVREVCE 146
 
Name Accession Description Interval E-value
CMP-NeuAc_Synthase cd02513
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ...
 42-257 4.39e-91

CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; CMP-N-acetylneuraminic acid synthetase (CMP-NeuAc synthetase) or acylneuraminate cytidylyltransferase catalyzes the transfer the CMP moiety of CTP to the anomeric hydroxyl group of NeuAc in the presence of Mg++. It is the second to last step in the sialylation of the oligosaccharide component of glycoconjugates by providing the activated sugar-nucleotide cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-Neu5Ac), the substrate for sialyltransferases. Eukaryotic CMP-NeuAc synthetases are predominantly located in the nucleus. The activated CMP-Neu5Ac diffuses from the nucleus into the cytoplasm.


Pssm-ID: 133006  Cd Length: 223  Bit Score: 274.80  E-value: 4.39e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309  42 HLAALVLARGGSKGIPLKNIKRLAGVPLIGWVLRAALDAGVFQSVWVSTDHDEIENVAKQFGA-QVHRRSSETSKDSSTS 120
Cdd:cd02513    1 KILAIIPARGGSKGIPGKNIRPLGGKPLIAWTIEAALESKLFDRVVVSTDDEEIAEVARKYGAeVPFLRPAELATDTASS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309 121 LDAIVEFLNYHNE----VDIVGNIQATSPCLHPTDLQKVAEMIREEGYDSVFSVVRRHQFRWSEIQKGvREVTEPLNLNP 196
Cdd:cd02513   81 IDVILHALDQLEElgrdFDIVVLLQPTSPLRSAEDIDEAIELLLSEGADSVFSVTEFHRFPWRALGLD-DNGLEPVNYPE 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 247269309 197 AKRPRRQDWDGELYENGSFYFAKRH-LIEMGYLQGGKMAYYEMRAEHSVDIDVDIDWPIAEQ 257
Cdd:cd02513  160 DKRTRRQDLPPAYHENGAIYIAKREaLLESNSFFGGKTGPYEMPRERSIDIDTEEDFELAEA 221
NeuA COG1083
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ...
 45-257 2.02e-72

CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440700  Cd Length: 228  Bit Score: 226.96  E-value: 2.02e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309  45 ALVLARGGSKGIPLKNIKRLAGVPLIGWVLRAALDAGVFQSVWVSTDHDEIENVAKQFGAQVHRRSSETSKDSSTSLDAI 124
Cdd:COG1083    5 AIIPARGGSKGIPGKNIRPLAGKPLIAYSIEAALKSGLFDRVVVSTDDEEIAEVAREYGAEVFLRPAELAGDTASTIDVI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309 125 VEFLNY----HNEVDIVGNIQATSPCLHPTDLQKVAEMIREEGYDSVFSVVRRHQFRWSEIQKGVREVTEPLNLNPAKRP 200
Cdd:COG1083   85 LHALEWleeqGEEFDYVVLLQPTSPLRTAEDIDEAIELLLESGADSVVSVTEAHHPPYWALKLDEDGRLEPLNPDPHNRP 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 247269309 201 RRQDWDGELYENGSFYFAKR-HLIEMGYLQGGKMAYYEMRAEHSVDIDVDIDWPIAEQ 257
Cdd:COG1083  165 RRQDLPPAYRENGAIYIFKReALLENKSRFGGKTGAYEMPEERSVDIDTEEDFELAEA 222
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 44-255 4.70e-72

Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) 3-deoxy-manno-octulosonate cytidylyltransferase,, EC:2.7.7.38 catalysing the reaction:- CTP + 3-deoxy-D-manno-octulosonate <=> diphosphate + CMP-3-deoxy-D-manno-octulosonate, 2) acylneuraminate cytidylyltransferase EC:2.7.7.43,, catalysing the reaction:- CTP + N-acylneuraminate <=> diphosphate + CMP-N-acylneuraminate. NeuAc cytydilyltransferase of Mannheimia haemolytica has been characterized describing kinetics and regulation by substrate charge, energetic charge and amino-sugar demand.


Pssm-ID: 396773  Cd Length: 217  Bit Score: 225.68  E-value: 4.70e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309   44 AALVLARGGSKGIPLKNIKRLAGVPLIGWVLRAALDAGVFQSVWVSTDHDEIENVAKQFGAQVHRRSSETSKDSSTSLDA 123
Cdd:pfam02348   1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDRFYEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309  124 IVEFLNYHNevDIVGNIQATSPCLHPTDLQKVAEMIREEGYDsvfsvvrrhqfRWSEIQKGVREVTEPLNLNPAKRPRRQ 203
Cdd:pfam02348  81 VKAFLNDHD--DIIVNIQGDNPLLQPEVILKAIETLLNNGEP-----------YMSTLVVPVGSAEEVLNANALKVVLDD 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 247269309  204 DWDGELYENGSFYFAKRHLIEMGYLQGGKMAYYEMRAEHsVDIDVDIDWPIA 255
Cdd:pfam02348 148 DGYALYFSRSVIPYIREHPAELYYVYLRHIGIYTFRKNM-PLIELVIDTPTA 198
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 273-417 7.79e-57

haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) phosphatase KdsC, and rainbow trout N-acylneuraminate cytidylyltransferase; KDO 8-P phosphatase catalyzes the hydrolysis of KDO 8-P to KDO (3-deoxy-D-manno-octulosonate) and inorganic phosphate and is the last enzyme in the KDO biosynthetic pathway. KDO is an 8-carbon sugar that links the lipid A and polysaccharide moieties of the lipopolysaccharide region in Gram-negative bacteria. An interruption in KDO biosynthesis leads to the accumulation of lipid A precursors and subsequent arrest in cell growth. The KDO biosynthesis pathway involves five sequential enzymatic reactions. This family also includes rainbow trout CMP-sialic acid synthetase which effectively converts both deaminoneuraminic acid (KDN, 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid) and N-acetylneuraminic acid (Neu5Ac) to CMP-KDN and CMP-Neu5Ac, respectively. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319769 [Multi-domain]  Cd Length: 146  Bit Score: 183.88  E-value: 7.79e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309 273 IKLLVCNIDGCLTNGHIYVSGDQKEIISYDVKDAIGISLLKKSGIEVRLISERAcSKQTLSALKLD--CKTEVSVSDKLA 350
Cdd:cd01630    1 IKLLVLDVDGVLTDGRIYYDSNGEELKSFNVRDGLGIKLLQKSGIEVAIITGRQ-SEAVRRRAKELgiEDLFQGVKDKLE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 247269309 351 TVDEWRKEMGLCWKEVAYLGNEVSDEECLKRVGLSAVPADACSGAQKAVGYICKCSGGRGAIREFAE 417
Cdd:cd01630   80 ALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGRGAVREVCE 146
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 267-419 6.72e-44

3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily phosphatases [Cell wall/membrane/envelope biogenesis, General function prediction only];


Pssm-ID: 441384 [Multi-domain]  Cd Length: 170  Bit Score: 150.97  E-value: 6.72e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309 267 KEKLKEIKLLVCNIDGCLTNGHIYVSGDQKEIISYDVKDAIGISLLKKSGIEVRLISERACS--KQTLSALKLDcktEV- 343
Cdd:COG1778    2 LERAKKIKLLIFDVDGVLTDGRIYYDEDGEELKRFNVRDGLGIKLLRKAGIKVAIITGRDSPavRRRAEELGIT---HVy 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 247269309 344 -SVSDKLATVDEWRKEMGLCWKEVAYLGNEVSDEECLKRVGLSAVPADACSGAQKAVGYICKCSGGRGAIREFAEHI 419
Cdd:COG1778   79 qGVKDKLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTTKPGGRGAVREVCELI 155
PseF TIGR03584
pseudaminic acid cytidylyltransferase; The sequences in this family include the pfam02348 ...
 45-256 6.48e-33

pseudaminic acid cytidylyltransferase; The sequences in this family include the pfam02348 (cytidyltransferase) domain and are homologous to the NeuA protein responsible for the transfer of CMP to neuraminic acid. According to, this gene is responsible for the transfer of CMP to the structurally related sugar, pseudaminic acid which is observed as a component of sugar modifications of flagellin in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci.


Pssm-ID: 274660  Cd Length: 222  Bit Score: 123.60  E-value: 6.48e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309   45 ALVLARGGSKGIPLKNIKRLAGVPLIGWVLRAALDAGVFQSVWVSTDHDEIENVAKQFGAQV-HRRSSETSKDSSTSLDA 123
Cdd:TIGR03584   2 AIIPARGGSKRIPRKNIKPFCGKPMIAYSIEAALNSGLFDKVVVSTDDEEIAEVAKSYGASVpFLRPKELADDFTGTAPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309  124 I---VEFLNYHNEVDIVGNIQATSPCLHPTDLQKVAEMIREEGYDSVFSVVRrhqFRWSeIQKGVR--EVTEPLNLNPAK 198
Cdd:TIGR03584  82 VkhaIEELKLQKQYDHACCIYATAPFLQAKILKEAFELLKQPNAHFVFSVTS---FAFP-IQRAFKlkENGGVEMFQPEH 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309  199 RPRR-QDWDGELYENGSFYFAKRH-LIEMGYLQGGKMAYYEMRAEHSVDIDVDIDWPIAE 256
Cdd:TIGR03584 158 FNTRsQDLEEAYHDAGQFYWGKSQaWLESGPIFSPHSIPIVLPRHLVQDIDTLEDWERAE 217
KdsC-phosphatas TIGR01670
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is ...
 273-422 2.70e-26

3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is a member of the IIIA subfamily of the haloacid dehalogenase (HAD) superfamily of hydrolases. All characterized members of this subfamily (TIGR01662) and most characterized members of the HAD superfamily are phosphatases. HAD superfamily phosphatases contain active site residues in several conserved catalytic motifs, all of which are found conserved here. One member of this family, the YrbI protein from H. influenzae has been cloned, expressed, purified and found to be an active 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase. Furthermore, its crystal structure has been determined. This family consists of sequences from beta, gamma and epsilon proteobacteria, Aquifex, Fusobacterium, Porphyromonas and Methanosarcina. The Methanosarcina sequence is distinctive in that it is linked to an N-terminal cytidylyltransferase domain (pfam02348) and is annotated as acylneuraminate cytidylyltransferase. This may give some clue as the function of these phosphatases. Several eukaryotic sequences scoring between trusted and noise are also closely related to this function such as the CMP-N-acetylneuraminic acid synthetase from mouse, but in these cases the phosphatase domain is clearly inactive as many of the active site residues are not conserved. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130731 [Multi-domain]  Cd Length: 154  Bit Score: 103.76  E-value: 2.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309  273 IKLLVCNIDGCLTNGHIYVSGDQKEIISYDVKDAIGISLLKKSGIEVRLISER--ACSKQTLSALKLDcKTEVSVSDKLA 350
Cdd:TIGR01670   1 IRLLILDVDGVLTDGKIYYTNNGEEIKAFNVRDGYGIRCALKSGIEVAIITGRkaKLVEDRCKTLGIT-HLYQGQSNKLI 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 247269309  351 TVDEWRKEMGLCWKEVAYLGNEVSDEECLKRVGLSAVPADACSGAQKAVGYICKCSGGRGAIREFAEHIFLL 422
Cdd:TIGR01670  80 AFSDILEKLALAPENVAYIGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTRIAGGRGAVREVCELLLLA 151
PRK09484 PRK09484
3-deoxy-manno-octulosonate-8-phosphatase KdsC;
268-421 4.48e-22

3-deoxy-manno-octulosonate-8-phosphatase KdsC;


Pssm-ID: 181898 [Multi-domain]  Cd Length: 183  Bit Score: 92.69  E-value: 4.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309 268 EKLKEIKLLVCNIDGCLTNGHIYVSGDQKEIISYDVKDAIGISLLKKSGIEVRLISERAcskqtlSALKLD-CKT-EVS- 344
Cdd:PRK09484  16 AKAENIRLLICDVDGVFSDGLIYMGNNGEELKAFNVRDGYGIRCLLTSGIEVAIITGRK------SKLVEDrMTTlGITh 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309 345 ----VSDKLATVDEWRKEMGLCWKEVAYLGNEVSDEECLKRVGLSAVPADACSGAQKAVGYICKCSGGRGAIREFAEHIF 420
Cdd:PRK09484  90 lyqgQSNKLIAFSDLLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRADYVTRIAGGRGAVREVCDLLL 169


                 .
gi 247269309 421 L 421
Cdd:PRK09484 170 L 170
PRK13368 PRK13368
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 44-161 7.75e-17

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 184007  Cd Length: 238  Bit Score: 79.62  E-value: 7.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309  44 AALVLARGGSKGIPLKNIKRLAGVPLIGWVLRAALDAGVFQSVWVSTDHDEIENVAKQFGAQVhrrsSETSKDSSTSLDA 123
Cdd:PRK13368   4 VVVIPARYGSSRLPGKPLLDILGKPMIQHVYERAAQAAGVEEVYVATDDQRIEDAVEAFGGKV----VMTSDDHLSGTDR 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 247269309 124 IVEFLNYhNEVDIVGNIQATSPCLHPTDLQKVAEMIRE 161
Cdd:PRK13368  80 LAEVMLK-IEADIYINVQGDEPMIRPRDIDTLIQPMLD 116
 
Name Accession Description Interval E-value
CMP-NeuAc_Synthase cd02513
CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; ...
 42-257 4.39e-91

CMP-NeuAc_Synthase activates N-acetylneuraminic acid by adding CMP moiety; CMP-N-acetylneuraminic acid synthetase (CMP-NeuAc synthetase) or acylneuraminate cytidylyltransferase catalyzes the transfer the CMP moiety of CTP to the anomeric hydroxyl group of NeuAc in the presence of Mg++. It is the second to last step in the sialylation of the oligosaccharide component of glycoconjugates by providing the activated sugar-nucleotide cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-Neu5Ac), the substrate for sialyltransferases. Eukaryotic CMP-NeuAc synthetases are predominantly located in the nucleus. The activated CMP-Neu5Ac diffuses from the nucleus into the cytoplasm.


Pssm-ID: 133006  Cd Length: 223  Bit Score: 274.80  E-value: 4.39e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309  42 HLAALVLARGGSKGIPLKNIKRLAGVPLIGWVLRAALDAGVFQSVWVSTDHDEIENVAKQFGA-QVHRRSSETSKDSSTS 120
Cdd:cd02513    1 KILAIIPARGGSKGIPGKNIRPLGGKPLIAWTIEAALESKLFDRVVVSTDDEEIAEVARKYGAeVPFLRPAELATDTASS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309 121 LDAIVEFLNYHNE----VDIVGNIQATSPCLHPTDLQKVAEMIREEGYDSVFSVVRRHQFRWSEIQKGvREVTEPLNLNP 196
Cdd:cd02513   81 IDVILHALDQLEElgrdFDIVVLLQPTSPLRSAEDIDEAIELLLSEGADSVFSVTEFHRFPWRALGLD-DNGLEPVNYPE 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 247269309 197 AKRPRRQDWDGELYENGSFYFAKRH-LIEMGYLQGGKMAYYEMRAEHSVDIDVDIDWPIAEQ 257
Cdd:cd02513  160 DKRTRRQDLPPAYHENGAIYIAKREaLLESNSFFGGKTGPYEMPRERSIDIDTEEDFELAEA 221
NeuA COG1083
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ...
 45-257 2.02e-72

CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440700  Cd Length: 228  Bit Score: 226.96  E-value: 2.02e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309  45 ALVLARGGSKGIPLKNIKRLAGVPLIGWVLRAALDAGVFQSVWVSTDHDEIENVAKQFGAQVHRRSSETSKDSSTSLDAI 124
Cdd:COG1083    5 AIIPARGGSKGIPGKNIRPLAGKPLIAYSIEAALKSGLFDRVVVSTDDEEIAEVAREYGAEVFLRPAELAGDTASTIDVI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309 125 VEFLNY----HNEVDIVGNIQATSPCLHPTDLQKVAEMIREEGYDSVFSVVRRHQFRWSEIQKGVREVTEPLNLNPAKRP 200
Cdd:COG1083   85 LHALEWleeqGEEFDYVVLLQPTSPLRTAEDIDEAIELLLESGADSVVSVTEAHHPPYWALKLDEDGRLEPLNPDPHNRP 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 247269309 201 RRQDWDGELYENGSFYFAKR-HLIEMGYLQGGKMAYYEMRAEHSVDIDVDIDWPIAEQ 257
Cdd:COG1083  165 RRQDLPPAYRENGAIYIFKReALLENKSRFGGKTGAYEMPEERSVDIDTEEDFELAEA 222
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 44-255 4.70e-72

Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) 3-deoxy-manno-octulosonate cytidylyltransferase,, EC:2.7.7.38 catalysing the reaction:- CTP + 3-deoxy-D-manno-octulosonate <=> diphosphate + CMP-3-deoxy-D-manno-octulosonate, 2) acylneuraminate cytidylyltransferase EC:2.7.7.43,, catalysing the reaction:- CTP + N-acylneuraminate <=> diphosphate + CMP-N-acylneuraminate. NeuAc cytydilyltransferase of Mannheimia haemolytica has been characterized describing kinetics and regulation by substrate charge, energetic charge and amino-sugar demand.


Pssm-ID: 396773  Cd Length: 217  Bit Score: 225.68  E-value: 4.70e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309   44 AALVLARGGSKGIPLKNIKRLAGVPLIGWVLRAALDAGVFQSVWVSTDHDEIENVAKQFGAQVHRRSSETSKDSSTSLDA 123
Cdd:pfam02348   1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDRFYEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309  124 IVEFLNYHNevDIVGNIQATSPCLHPTDLQKVAEMIREEGYDsvfsvvrrhqfRWSEIQKGVREVTEPLNLNPAKRPRRQ 203
Cdd:pfam02348  81 VKAFLNDHD--DIIVNIQGDNPLLQPEVILKAIETLLNNGEP-----------YMSTLVVPVGSAEEVLNANALKVVLDD 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 247269309  204 DWDGELYENGSFYFAKRHLIEMGYLQGGKMAYYEMRAEHsVDIDVDIDWPIA 255
Cdd:pfam02348 148 DGYALYFSRSVIPYIREHPAELYYVYLRHIGIYTFRKNM-PLIELVIDTPTA 198
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 273-417 7.79e-57

haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) phosphatase KdsC, and rainbow trout N-acylneuraminate cytidylyltransferase; KDO 8-P phosphatase catalyzes the hydrolysis of KDO 8-P to KDO (3-deoxy-D-manno-octulosonate) and inorganic phosphate and is the last enzyme in the KDO biosynthetic pathway. KDO is an 8-carbon sugar that links the lipid A and polysaccharide moieties of the lipopolysaccharide region in Gram-negative bacteria. An interruption in KDO biosynthesis leads to the accumulation of lipid A precursors and subsequent arrest in cell growth. The KDO biosynthesis pathway involves five sequential enzymatic reactions. This family also includes rainbow trout CMP-sialic acid synthetase which effectively converts both deaminoneuraminic acid (KDN, 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid) and N-acetylneuraminic acid (Neu5Ac) to CMP-KDN and CMP-Neu5Ac, respectively. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319769 [Multi-domain]  Cd Length: 146  Bit Score: 183.88  E-value: 7.79e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309 273 IKLLVCNIDGCLTNGHIYVSGDQKEIISYDVKDAIGISLLKKSGIEVRLISERAcSKQTLSALKLD--CKTEVSVSDKLA 350
Cdd:cd01630    1 IKLLVLDVDGVLTDGRIYYDSNGEELKSFNVRDGLGIKLLQKSGIEVAIITGRQ-SEAVRRRAKELgiEDLFQGVKDKLE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 247269309 351 TVDEWRKEMGLCWKEVAYLGNEVSDEECLKRVGLSAVPADACSGAQKAVGYICKCSGGRGAIREFAE 417
Cdd:cd01630   80 ALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGRGAVREVCE 146
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 267-419 6.72e-44

3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily phosphatases [Cell wall/membrane/envelope biogenesis, General function prediction only];


Pssm-ID: 441384 [Multi-domain]  Cd Length: 170  Bit Score: 150.97  E-value: 6.72e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309 267 KEKLKEIKLLVCNIDGCLTNGHIYVSGDQKEIISYDVKDAIGISLLKKSGIEVRLISERACS--KQTLSALKLDcktEV- 343
Cdd:COG1778    2 LERAKKIKLLIFDVDGVLTDGRIYYDEDGEELKRFNVRDGLGIKLLRKAGIKVAIITGRDSPavRRRAEELGIT---HVy 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 247269309 344 -SVSDKLATVDEWRKEMGLCWKEVAYLGNEVSDEECLKRVGLSAVPADACSGAQKAVGYICKCSGGRGAIREFAEHI 419
Cdd:COG1778   79 qGVKDKLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTTKPGGRGAVREVCELI 155
PseF TIGR03584
pseudaminic acid cytidylyltransferase; The sequences in this family include the pfam02348 ...
 45-256 6.48e-33

pseudaminic acid cytidylyltransferase; The sequences in this family include the pfam02348 (cytidyltransferase) domain and are homologous to the NeuA protein responsible for the transfer of CMP to neuraminic acid. According to, this gene is responsible for the transfer of CMP to the structurally related sugar, pseudaminic acid which is observed as a component of sugar modifications of flagellin in Campylobacter species. This gene is commonly observed in apparent operons with other genes responsible for the biosynthesis of pseudaminic acid and as a component of flagellar and exopolysaccharide biosynthesis loci.


Pssm-ID: 274660  Cd Length: 222  Bit Score: 123.60  E-value: 6.48e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309   45 ALVLARGGSKGIPLKNIKRLAGVPLIGWVLRAALDAGVFQSVWVSTDHDEIENVAKQFGAQV-HRRSSETSKDSSTSLDA 123
Cdd:TIGR03584   2 AIIPARGGSKRIPRKNIKPFCGKPMIAYSIEAALNSGLFDKVVVSTDDEEIAEVAKSYGASVpFLRPKELADDFTGTAPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309  124 I---VEFLNYHNEVDIVGNIQATSPCLHPTDLQKVAEMIREEGYDSVFSVVRrhqFRWSeIQKGVR--EVTEPLNLNPAK 198
Cdd:TIGR03584  82 VkhaIEELKLQKQYDHACCIYATAPFLQAKILKEAFELLKQPNAHFVFSVTS---FAFP-IQRAFKlkENGGVEMFQPEH 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309  199 RPRR-QDWDGELYENGSFYFAKRH-LIEMGYLQGGKMAYYEMRAEHSVDIDVDIDWPIAE 256
Cdd:TIGR03584 158 FNTRsQDLEEAYHDAGQFYWGKSQaWLESGPIFSPHSIPIVLPRHLVQDIDTLEDWERAE 217
KdsC-phosphatas TIGR01670
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is ...
 273-422 2.70e-26

3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is a member of the IIIA subfamily of the haloacid dehalogenase (HAD) superfamily of hydrolases. All characterized members of this subfamily (TIGR01662) and most characterized members of the HAD superfamily are phosphatases. HAD superfamily phosphatases contain active site residues in several conserved catalytic motifs, all of which are found conserved here. One member of this family, the YrbI protein from H. influenzae has been cloned, expressed, purified and found to be an active 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase. Furthermore, its crystal structure has been determined. This family consists of sequences from beta, gamma and epsilon proteobacteria, Aquifex, Fusobacterium, Porphyromonas and Methanosarcina. The Methanosarcina sequence is distinctive in that it is linked to an N-terminal cytidylyltransferase domain (pfam02348) and is annotated as acylneuraminate cytidylyltransferase. This may give some clue as the function of these phosphatases. Several eukaryotic sequences scoring between trusted and noise are also closely related to this function such as the CMP-N-acetylneuraminic acid synthetase from mouse, but in these cases the phosphatase domain is clearly inactive as many of the active site residues are not conserved. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130731 [Multi-domain]  Cd Length: 154  Bit Score: 103.76  E-value: 2.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309  273 IKLLVCNIDGCLTNGHIYVSGDQKEIISYDVKDAIGISLLKKSGIEVRLISER--ACSKQTLSALKLDcKTEVSVSDKLA 350
Cdd:TIGR01670   1 IRLLILDVDGVLTDGKIYYTNNGEEIKAFNVRDGYGIRCALKSGIEVAIITGRkaKLVEDRCKTLGIT-HLYQGQSNKLI 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 247269309  351 TVDEWRKEMGLCWKEVAYLGNEVSDEECLKRVGLSAVPADACSGAQKAVGYICKCSGGRGAIREFAEHIFLL 422
Cdd:TIGR01670  80 AFSDILEKLALAPENVAYIGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTRIAGGRGAVREVCELLLLA 151
PRK09484 PRK09484
3-deoxy-manno-octulosonate-8-phosphatase KdsC;
268-421 4.48e-22

3-deoxy-manno-octulosonate-8-phosphatase KdsC;


Pssm-ID: 181898 [Multi-domain]  Cd Length: 183  Bit Score: 92.69  E-value: 4.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309 268 EKLKEIKLLVCNIDGCLTNGHIYVSGDQKEIISYDVKDAIGISLLKKSGIEVRLISERAcskqtlSALKLD-CKT-EVS- 344
Cdd:PRK09484  16 AKAENIRLLICDVDGVFSDGLIYMGNNGEELKAFNVRDGYGIRCLLTSGIEVAIITGRK------SKLVEDrMTTlGITh 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309 345 ----VSDKLATVDEWRKEMGLCWKEVAYLGNEVSDEECLKRVGLSAVPADACSGAQKAVGYICKCSGGRGAIREFAEHIF 420
Cdd:PRK09484  90 lyqgQSNKLIAFSDLLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRADYVTRIAGGRGAVREVCDLLL 169


                 .
gi 247269309 421 L 421
Cdd:PRK09484 170 L 170
PRK13368 PRK13368
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 44-161 7.75e-17

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 184007  Cd Length: 238  Bit Score: 79.62  E-value: 7.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309  44 AALVLARGGSKGIPLKNIKRLAGVPLIGWVLRAALDAGVFQSVWVSTDHDEIENVAKQFGAQVhrrsSETSKDSSTSLDA 123
Cdd:PRK13368   4 VVVIPARYGSSRLPGKPLLDILGKPMIQHVYERAAQAAGVEEVYVATDDQRIEDAVEAFGGKV----VMTSDDHLSGTDR 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 247269309 124 IVEFLNYhNEVDIVGNIQATSPCLHPTDLQKVAEMIRE 161
Cdd:PRK13368  80 LAEVMLK-IEADIYINVQGDEPMIRPRDIDTLIQPMLD 116
CMP-KDO-Synthetase cd02517
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ...
 49-165 1.24e-16

CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the lipopolysaccharide; CMP-KDO Synthetase: 3-Deoxy-D-manno-octulosonate cytidylyltransferase (CMP-KDO synthetase) catalyzes the conversion of CTP and 3-deoxy-D-manno-octulosonate into CMP-3-deoxy-D-manno-octulosonate (CMP-KDO) and pyrophosphate. KDO is an essential component of the lipopolysaccharide found in the outer surface of gram-negative eubacteria. It is also a constituent of the capsular polysaccharides of some gram-negative eubacteria. Its presence in the cell wall polysaccharides of green algae and plant were also discovered. However, they have not been found in yeast and animals. The absence of the enzyme in mammalian cells makes it an attractive target molecule for drug design.


Pssm-ID: 133010  Cd Length: 239  Bit Score: 78.67  E-value: 1.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309  49 ARGGS---KGIPLKNIkrlAGVPLIGWVLRAALDAGVFQSVWVSTDHDEIENVAKQFGAQVHRrsseTSKDSSTSLDAIV 125
Cdd:cd02517    8 ARYASsrlPGKPLADI---AGKPMIQHVYERAKKAKGLDEVVVATDDERIADAVESFGGKVVM----TSPDHPSGTDRIA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 247269309 126 EFLN-YHNEVDIVGNIQATSPCLHPTDLQKVAE-MIREEGYD 165
Cdd:cd02517   81 EVAEkLDADDDIVVNVQGDEPLIPPEMIDQVVAaLKDDPGVD 122
PRK05450 PRK05450
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 49-174 1.01e-12

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 235473  Cd Length: 245  Bit Score: 67.45  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309  49 ARGGS---KGIPLKNIkrlAGVPLIGWVLRAALDAGVfQSVWVSTDHDEIENVAKQFGAQVHRrsseTSKD--SSTS-LD 122
Cdd:PRK05450   9 ARYAStrlPGKPLADI---GGKPMIVRVYERASKAGA-DRVVVATDDERIADAVEAFGGEVVM----TSPDhpSGTDrIA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 247269309 123 AIVEFLNYhNEVDIVGNIQATSPCLHPTDLQKVAEMIREEGYDSVFSVVRRH 174
Cdd:PRK05450  81 EAAAKLGL-ADDDIVVNVQGDEPLIPPEIIDQVAEPLANPEADMATLAVPIH 131
GT2_SpsF cd02518
SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat ...
 44-165 8.99e-06

SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat polysaccharide biosynthesis protein F (spsF) is a glycosyltransferase implicated in the synthesis of the spore coat in a variety of bacteria challenged by stress as starvation. The spsF gene is expressed in the late stage of coat development responsible for a terminal step in coat formation that involves the glycosylation of the coat. SpsF gene mutation resulted in spores that appeared normal. But, the spores tended to aggregate and had abnormal adsorption properties, indicating a surface alteration.


Pssm-ID: 133011  Cd Length: 233  Bit Score: 46.80  E-value: 8.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309  44 AALVLARGGSKGIPLKNIKRLAGVPLIGWVLRAALDAGVFQSVWVST----DHDEIENVAKQFGAQVHRRSSEtskDSST 119
Cdd:cd02518    1 VAIIQARMGSTRLPGKVLKPLGGKPLLEHLLDRLKRSKLIDEIVIATstneEDDPLEALAKKLGVKVFRGSEE---DVLG 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 247269309 120 SLDAIVEFlnyhNEVDIVGNIQATSPCLHPTDLQKVAEMIREEGYD 165
Cdd:cd02518   78 RYYQAAEE----YNADVVVRITGDCPLIDPEIIDAVIRLFLKSGAD 119
PLN02917 PLN02917
CMP-KDO synthetase
 54-169 1.06e-03

CMP-KDO synthetase


Pssm-ID: 215495  Cd Length: 293  Bit Score: 40.97  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269309  54 KGIPLKNIkrlAGVPLIGWVLRAALDAGVFQSVWVSTDHDEIENVAKQFGAQVhRRSSETSKDSSTSLDAIVEFLNYHne 133
Cdd:PLN02917  62 EGKPLVHI---LGKPMIQRTWERAKLATTLDHIVVATDDERIAECCRGFGADV-IMTSESCRNGTERCNEALKKLEKK-- 135

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 247269309 134 VDIVGNIQATSPCLHPTDLQKVAeMIREEGYDSVFS 169
Cdd:PLN02917 136 YDIVVNIQGDEPLIEPEIIDGVV-KALQAAPDAVFS 170
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 45-106 1.23e-03

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: 39.49  E-value: 1.23e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 247269309   45 ALVLA-----R-GGSKG-IPLknikrlAGVPLIGWVLRAAldAGVFQSVWVSTDHDEIENVAKQFGAQV 106
Cdd:pfam12804   1 AVILAggrssRmGGDKAlLPL------GGKPLLERVLERL--RPAGDEVVVVANDEEVLAALAGLGVPV 61
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 43-105 7.54e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 38.57  E-value: 7.54e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 247269309  43 LAALVLARGgsKGIPLKN-----IKRLAGVPLIGWVLRAALDAGVFQSVWVsTDHdEIENVAKQFGAQ 105
Cdd:PRK14355   4 LAAIILAAG--KGTRMKSdlvkvMHPLAGRPMVSWPVAAAREAGAGRIVLV-VGH-QAEKVREHFAGD 67
 
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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