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Conserved domains on  [gi|8923900|ref|NP_061156|]
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N-acylneuraminate cytidylyltransferase [Homo sapiens]

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; ...
 44-259 6.50e-93

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: 279.42  E-value: 6.50e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900   44 HLAALILARGGSKGIPLKNIKHLAGVPLIGWVLRAALDSGAFQSVWVSTDHDEIENVAKQFGA-QVHRRSSEVSKDSSTS 122
Cdd:cd02513   1 KILAIIPARGGSKGIPGKNIRPLGGKPLIAWTIEAALESKLFDRVVVSTDDEEIAEVARKYGAeVPFLRPAELATDTASS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900  123 LDAIIEFLNYHNE----VDIVGNIQATSPCLHPTDLQKVAEMIREEGYDSVFSVVRRHQFRWSEIQKGvREVTEPLNLNP 198
Cdd:cd02513  81 IDVILHALDQLEElgrdFDIVVLLQPTSPLRSAEDIDEAIELLLSEGADSVFSVTEFHRFPWRALGLD-DNGLEPVNYPE 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8923900  199 AKRPRRQDWDGELYENGSFYFAKRH-LIEMGYLQGGKMAYYEMRAEHSVDIDVDIDWPIAEQ 259
Cdd:cd02513 160 DKRTRRQDLPPAYHENGAIYIAKREaLLESNSFFGGKTGPYEMPRERSIDIDTEEDFELAEA 221
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 275-419 2.03e-56

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: 182.72  E-value: 2.03e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900  275 IKLLVCNIDGCLTNGHIYVSGDQKEIISYDVKDAIGISLLKKSGIEVRLISERAcSKQTLSSLKLD--CKMEVSVSDKLA 352
Cdd:cd01630   1 IKLLVLDVDGVLTDGRIYYDSNGEELKSFNVRDGLGIKLLQKSGIEVAIITGRQ-SEAVRRRAKELgiEDLFQGVKDKLE 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8923900  353 VVDEWRKEMGLCWKEVAYLGNEVSDEECLKRVGLSGAPADACSTAQKAVGYICKCNGGRGAIREFAE 419
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; ...
 44-259 6.50e-93

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: 279.42  E-value: 6.50e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900   44 HLAALILARGGSKGIPLKNIKHLAGVPLIGWVLRAALDSGAFQSVWVSTDHDEIENVAKQFGA-QVHRRSSEVSKDSSTS 122
Cdd:cd02513   1 KILAIIPARGGSKGIPGKNIRPLGGKPLIAWTIEAALESKLFDRVVVSTDDEEIAEVARKYGAeVPFLRPAELATDTASS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900  123 LDAIIEFLNYHNE----VDIVGNIQATSPCLHPTDLQKVAEMIREEGYDSVFSVVRRHQFRWSEIQKGvREVTEPLNLNP 198
Cdd:cd02513  81 IDVILHALDQLEElgrdFDIVVLLQPTSPLRSAEDIDEAIELLLSEGADSVFSVTEFHRFPWRALGLD-DNGLEPVNYPE 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8923900  199 AKRPRRQDWDGELYENGSFYFAKRH-LIEMGYLQGGKMAYYEMRAEHSVDIDVDIDWPIAEQ 259
Cdd:cd02513 160 DKRTRRQDLPPAYHENGAIYIAKREaLLESNSFFGGKTGPYEMPRERSIDIDTEEDFELAEA 221
NeuA COG1083
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ...
 47-259 2.00e-74

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


Pssm-ID: 440700  Cd Length: 228  Bit Score: 232.36  E-value: 2.00e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900   47 ALILARGGSKGIPLKNIKHLAGVPLIGWVLRAALDSGAFQSVWVSTDHDEIENVAKQFGAQVHRRSSEVSKDSSTSLDAI 126
Cdd:COG1083   5 AIIPARGGSKGIPGKNIRPLAGKPLIAYSIEAALKSGLFDRVVVSTDDEEIAEVAREYGAEVFLRPAELAGDTASTIDVI 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900  127 IEFLNY----HNEVDIVGNIQATSPCLHPTDLQKVAEMIREEGYDSVFSVVRRHQFRWSEIQKGVREVTEPLNLNPAKRP 202
Cdd:COG1083  85 LHALEWleeqGEEFDYVVLLQPTSPLRTAEDIDEAIELLLESGADSVVSVTEAHHPPYWALKLDEDGRLEPLNPDPHNRP 164

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 8923900  203 RRQDWDGELYENGSFYFAKR-HLIEMGYLQGGKMAYYEMRAEHSVDIDVDIDWPIAEQ 259
Cdd:COG1083 165 RRQDLPPAYRENGAIYIFKReALLENKSRFGGKTGAYEMPEERSVDIDTEEDFELAEA 222
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 46-265 3.72e-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: 226.06  E-value: 3.72e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900     46 AALILARGGSKGIPLKNIKHLAGVPLIGWVLRAALDSGAFQSVWVSTDHDEIENVAKQFGAQVHRRSSEVSKDSSTSLDA 125
Cdd:pfam02348   1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDRFYEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900    126 IIEFLNYHNevDIVGNIQATSPCLHPTDLQKVAEMIREEGYDsvfsvvrrhqfRWSEIQKGVREVTEPLNLNPAKRPRRQ 205
Cdd:pfam02348  81 VKAFLNDHD--DIIVNIQGDNPLLQPEVILKAIETLLNNGEP-----------YMSTLVVPVGSAEEVLNANALKVVLDD 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8923900    206 DWDGELYENGSFYFAKRHLIEMGYLQGGKMAYYEMRAEHsVDIDVDIDWPIA-------EQ-RVLRYG 265
Cdd:pfam02348 148 DGYALYFSRSVIPYIREHPAELYYVYLRHIGIYTFRKNM-PLIELVIDTPTAleyieklEQlRVLYNG 214
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 275-419 2.03e-56

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: 182.72  E-value: 2.03e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900  275 IKLLVCNIDGCLTNGHIYVSGDQKEIISYDVKDAIGISLLKKSGIEVRLISERAcSKQTLSSLKLD--CKMEVSVSDKLA 352
Cdd:cd01630   1 IKLLVLDVDGVLTDGRIYYDSNGEELKSFNVRDGLGIKLLQKSGIEVAIITGRQ-SEAVRRRAKELgiEDLFQGVKDKLE 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8923900  353 VVDEWRKEMGLCWKEVAYLGNEVSDEECLKRVGLSGAPADACSTAQKAVGYICKCNGGRGAIREFAE 419
Cdd:cd01630  80 ALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGRGAVREVCE 146
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 269-421 3.27e-45

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: 154.44  E-value: 3.27e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900  269 KEKLKEIKLLVCNIDGCLTNGHIYVSGDQKEIISYDVKDAIGISLLKKSGIEVRLISERACS--KQTLSSLKLDckmEV- 345
Cdd:COG1778   2 LERAKKIKLLIFDVDGVLTDGRIYYDEDGEELKRFNVRDGLGIKLLRKAGIKVAIITGRDSPavRRRAEELGIT---HVy 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8923900  346 -SVSDKLAVVDEWRKEMGLCWKEVAYLGNEVSDEECLKRVGLSGAPADACSTAQKAVGYICKCNGGRGAIREFAEHI 421
Cdd:COG1778  79 qGVKDKLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTTKPGGRGAVREVCELI 155
PseF TIGR03584
pseudaminic acid cytidylyltransferase; The sequences in this family include the pfam02348 ...
 47-258 6.18e-35

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: 128.99  E-value: 6.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900     47 ALILARGGSKGIPLKNIKHLAGVPLIGWVLRAALDSGAFQSVWVSTDHDEIENVAKQFGAQV-HRRSSEVSKDSSTSLDA 125
Cdd:TIGR03584   2 AIIPARGGSKRIPRKNIKPFCGKPMIAYSIEAALNSGLFDKVVVSTDDEEIAEVAKSYGASVpFLRPKELADDFTGTAPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900    126 I---IEFLNYHNEVDIVGNIQATSPCLHPTDLQKVAEMIREEGYDSVFSVVRrhqFRWSeIQKGVR--EVTEPLNLNPAK 200
Cdd:TIGR03584  82 VkhaIEELKLQKQYDHACCIYATAPFLQAKILKEAFELLKQPNAHFVFSVTS---FAFP-IQRAFKlkENGGVEMFQPEH 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900    201 RPRR-QDWDGELYENGSFYFAKRH-LIEMGYLQGGKMAYYEMRAEHSVDIDVDIDWPIAE 258
Cdd:TIGR03584 158 FNTRsQDLEEAYHDAGQFYWGKSQaWLESGPIFSPHSIPIVLPRHLVQDIDTLEDWERAE 217
KdsC-phosphatas TIGR01670
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is ...
 275-424 3.58e-28

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: 108.77  E-value: 3.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900    275 IKLLVCNIDGCLTNGHIYVSGDQKEIISYDVKDAIGISLLKKSGIEVRLISER--ACSKQTLSSLKLDcKMEVSVSDKLA 352
Cdd:TIGR01670   1 IRLLILDVDGVLTDGKIYYTNNGEEIKAFNVRDGYGIRCALKSGIEVAIITGRkaKLVEDRCKTLGIT-HLYQGQSNKLI 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8923900    353 VVDEWRKEMGLCWKEVAYLGNEVSDEECLKRVGLSGAPADACSTAQKAVGYICKCNGGRGAIREFAEHICLL 424
Cdd:TIGR01670  80 AFSDILEKLALAPENVAYIGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTRIAGGRGAVREVCELLLLA 151
PRK09484 PRK09484
3-deoxy-manno-octulosonate-8-phosphatase KdsC;
270-423 2.60e-23

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


Pssm-ID: 181898 [Multi-domain]  Cd Length: 183  Bit Score: 96.15  E-value: 2.60e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900   270 EKLKEIKLLVCNIDGCLTNGHIYVSGDQKEIISYDVKDAIGISLLKKSGIEVRLISERacskqtlSSLKLDCKMEV---- 345
Cdd:PRK09484  16 AKAENIRLLICDVDGVFSDGLIYMGNNGEELKAFNVRDGYGIRCLLTSGIEVAIITGR-------KSKLVEDRMTTlgit 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900   346 ----SVSDKLAVVDEWRKEMGLCWKEVAYLGNEVSDEECLKRVGLSGAPADACSTAQKAVGYICKCNGGRGAIREFAEHI 421
Cdd:PRK09484  89 hlyqGQSNKLIAFSDLLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRADYVTRIAGGRGAVREVCDLL 168


                 ..
gi 8923900   422 CL 423
Cdd:PRK09484 169 LL 170
PRK13368 PRK13368
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 46-163 4.70e-16

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 184007  Cd Length: 238  Bit Score: 77.31  E-value: 4.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900    46 AALILARGGSKGIPLKNIKHLAGVPLIGWVLRAALDSGAFQSVWVSTDHDEIENVAKQFGAQVhrrsSEVSKDSSTSLDA 125
Cdd:PRK13368   4 VVVIPARYGSSRLPGKPLLDILGKPMIQHVYERAAQAAGVEEVYVATDDQRIEDAVEAFGGKV----VMTSDDHLSGTDR 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 8923900   126 IIEFLNYhNEVDIVGNIQATSPCLHPTDLQKVAEMIRE 163
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; ...
 44-259 6.50e-93

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: 279.42  E-value: 6.50e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900   44 HLAALILARGGSKGIPLKNIKHLAGVPLIGWVLRAALDSGAFQSVWVSTDHDEIENVAKQFGA-QVHRRSSEVSKDSSTS 122
Cdd:cd02513   1 KILAIIPARGGSKGIPGKNIRPLGGKPLIAWTIEAALESKLFDRVVVSTDDEEIAEVARKYGAeVPFLRPAELATDTASS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900  123 LDAIIEFLNYHNE----VDIVGNIQATSPCLHPTDLQKVAEMIREEGYDSVFSVVRRHQFRWSEIQKGvREVTEPLNLNP 198
Cdd:cd02513  81 IDVILHALDQLEElgrdFDIVVLLQPTSPLRSAEDIDEAIELLLSEGADSVFSVTEFHRFPWRALGLD-DNGLEPVNYPE 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8923900  199 AKRPRRQDWDGELYENGSFYFAKRH-LIEMGYLQGGKMAYYEMRAEHSVDIDVDIDWPIAEQ 259
Cdd:cd02513 160 DKRTRRQDLPPAYHENGAIYIAKREaLLESNSFFGGKTGPYEMPRERSIDIDTEEDFELAEA 221
NeuA COG1083
CMP-N-acetylneuraminic acid synthetase, NeuA/PseF family [Cell wall/membrane/envelope ...
 47-259 2.00e-74

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


Pssm-ID: 440700  Cd Length: 228  Bit Score: 232.36  E-value: 2.00e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900   47 ALILARGGSKGIPLKNIKHLAGVPLIGWVLRAALDSGAFQSVWVSTDHDEIENVAKQFGAQVHRRSSEVSKDSSTSLDAI 126
Cdd:COG1083   5 AIIPARGGSKGIPGKNIRPLAGKPLIAYSIEAALKSGLFDRVVVSTDDEEIAEVAREYGAEVFLRPAELAGDTASTIDVI 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900  127 IEFLNY----HNEVDIVGNIQATSPCLHPTDLQKVAEMIREEGYDSVFSVVRRHQFRWSEIQKGVREVTEPLNLNPAKRP 202
Cdd:COG1083  85 LHALEWleeqGEEFDYVVLLQPTSPLRTAEDIDEAIELLLESGADSVVSVTEAHHPPYWALKLDEDGRLEPLNPDPHNRP 164

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 8923900  203 RRQDWDGELYENGSFYFAKR-HLIEMGYLQGGKMAYYEMRAEHSVDIDVDIDWPIAEQ 259
Cdd:COG1083 165 RRQDLPPAYRENGAIYIFKReALLENKSRFGGKTGAYEMPEERSVDIDTEEDFELAEA 222
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 46-265 3.72e-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: 226.06  E-value: 3.72e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900     46 AALILARGGSKGIPLKNIKHLAGVPLIGWVLRAALDSGAFQSVWVSTDHDEIENVAKQFGAQVHRRSSEVSKDSSTSLDA 125
Cdd:pfam02348   1 AAIIPARLGSKRLPGKNLLDLGGKPLIHHVLEAALKSGAFEKVIVATDSEEIADVAKEFGAGVVMTSGSLSSGTDRFYEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900    126 IIEFLNYHNevDIVGNIQATSPCLHPTDLQKVAEMIREEGYDsvfsvvrrhqfRWSEIQKGVREVTEPLNLNPAKRPRRQ 205
Cdd:pfam02348  81 VKAFLNDHD--DIIVNIQGDNPLLQPEVILKAIETLLNNGEP-----------YMSTLVVPVGSAEEVLNANALKVVLDD 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8923900    206 DWDGELYENGSFYFAKRHLIEMGYLQGGKMAYYEMRAEHsVDIDVDIDWPIA-------EQ-RVLRYG 265
Cdd:pfam02348 148 DGYALYFSRSVIPYIREHPAELYYVYLRHIGIYTFRKNM-PLIELVIDTPTAleyieklEQlRVLYNG 214
HAD_KDO-like cd01630
haloacid dehalogenase-like (HAD) hydrolase, similar to Escherichia coli ...
 275-419 2.03e-56

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: 182.72  E-value: 2.03e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900  275 IKLLVCNIDGCLTNGHIYVSGDQKEIISYDVKDAIGISLLKKSGIEVRLISERAcSKQTLSSLKLD--CKMEVSVSDKLA 352
Cdd:cd01630   1 IKLLVLDVDGVLTDGRIYYDSNGEELKSFNVRDGLGIKLLQKSGIEVAIITGRQ-SEAVRRRAKELgiEDLFQGVKDKLE 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8923900  353 VVDEWRKEMGLCWKEVAYLGNEVSDEECLKRVGLSGAPADACSTAQKAVGYICKCNGGRGAIREFAE 419
Cdd:cd01630  80 ALEELLEKLGLSDEEVAYMGDDLPDLPVMKRVGLSVAPADAHPEVREAADYVTRARGGRGAVREVCE 146
KdsC COG1778
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC and related HAD superfamily ...
 269-421 3.27e-45

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: 154.44  E-value: 3.27e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900  269 KEKLKEIKLLVCNIDGCLTNGHIYVSGDQKEIISYDVKDAIGISLLKKSGIEVRLISERACS--KQTLSSLKLDckmEV- 345
Cdd:COG1778   2 LERAKKIKLLIFDVDGVLTDGRIYYDEDGEELKRFNVRDGLGIKLLRKAGIKVAIITGRDSPavRRRAEELGIT---HVy 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8923900  346 -SVSDKLAVVDEWRKEMGLCWKEVAYLGNEVSDEECLKRVGLSGAPADACSTAQKAVGYICKCNGGRGAIREFAEHI 421
Cdd:COG1778  79 qGVKDKLEALEELLAKLGLSPEEVAYIGDDLPDLPVMRRVGLSVAPADAHPEVKAAADYVTTKPGGRGAVREVCELI 155
PseF TIGR03584
pseudaminic acid cytidylyltransferase; The sequences in this family include the pfam02348 ...
 47-258 6.18e-35

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: 128.99  E-value: 6.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900     47 ALILARGGSKGIPLKNIKHLAGVPLIGWVLRAALDSGAFQSVWVSTDHDEIENVAKQFGAQV-HRRSSEVSKDSSTSLDA 125
Cdd:TIGR03584   2 AIIPARGGSKRIPRKNIKPFCGKPMIAYSIEAALNSGLFDKVVVSTDDEEIAEVAKSYGASVpFLRPKELADDFTGTAPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900    126 I---IEFLNYHNEVDIVGNIQATSPCLHPTDLQKVAEMIREEGYDSVFSVVRrhqFRWSeIQKGVR--EVTEPLNLNPAK 200
Cdd:TIGR03584  82 VkhaIEELKLQKQYDHACCIYATAPFLQAKILKEAFELLKQPNAHFVFSVTS---FAFP-IQRAFKlkENGGVEMFQPEH 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900    201 RPRR-QDWDGELYENGSFYFAKRH-LIEMGYLQGGKMAYYEMRAEHSVDIDVDIDWPIAE 258
Cdd:TIGR03584 158 FNTRsQDLEEAYHDAGQFYWGKSQaWLESGPIFSPHSIPIVLPRHLVQDIDTLEDWERAE 217
KdsC-phosphatas TIGR01670
3-deoxy-D-manno-octulosonate 8-phosphate phosphatase, YrbI family; This family of proteins is ...
 275-424 3.58e-28

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: 108.77  E-value: 3.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900    275 IKLLVCNIDGCLTNGHIYVSGDQKEIISYDVKDAIGISLLKKSGIEVRLISER--ACSKQTLSSLKLDcKMEVSVSDKLA 352
Cdd:TIGR01670   1 IRLLILDVDGVLTDGKIYYTNNGEEIKAFNVRDGYGIRCALKSGIEVAIITGRkaKLVEDRCKTLGIT-HLYQGQSNKLI 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8923900    353 VVDEWRKEMGLCWKEVAYLGNEVSDEECLKRVGLSGAPADACSTAQKAVGYICKCNGGRGAIREFAEHICLL 424
Cdd:TIGR01670  80 AFSDILEKLALAPENVAYIGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTRIAGGRGAVREVCELLLLA 151
PRK09484 PRK09484
3-deoxy-manno-octulosonate-8-phosphatase KdsC;
270-423 2.60e-23

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


Pssm-ID: 181898 [Multi-domain]  Cd Length: 183  Bit Score: 96.15  E-value: 2.60e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900   270 EKLKEIKLLVCNIDGCLTNGHIYVSGDQKEIISYDVKDAIGISLLKKSGIEVRLISERacskqtlSSLKLDCKMEV---- 345
Cdd:PRK09484  16 AKAENIRLLICDVDGVFSDGLIYMGNNGEELKAFNVRDGYGIRCLLTSGIEVAIITGR-------KSKLVEDRMTTlgit 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900   346 ----SVSDKLAVVDEWRKEMGLCWKEVAYLGNEVSDEECLKRVGLSGAPADACSTAQKAVGYICKCNGGRGAIREFAEHI 421
Cdd:PRK09484  89 hlyqGQSNKLIAFSDLLEKLAIAPEQVAYIGDDLIDWPVMEKVGLSVAVADAHPLLLPRADYVTRIAGGRGAVREVCDLL 168


                 ..
gi 8923900   422 CL 423
Cdd:PRK09484 169 LL 170
CMP-KDO-Synthetase cd02517
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ...
 46-167 4.66e-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: 77.13  E-value: 4.66e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900   46 AALILARGGS---KGIPLKNIkhlAGVPLIGWVLRAALDSGAFQSVWVSTDHDEIENVAKQFGAQVhrrsseV--SKDSS 120
Cdd:cd02517   3 IVVIPARYASsrlPGKPLADI---AGKPMIQHVYERAKKAKGLDEVVVATDDERIADAVESFGGKV------VmtSPDHP 73

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 8923900  121 TSLDAIIEFLN-YHNEVDIVGNIQATSPCLHPTDLQKVAE-MIREEGYD 167
Cdd:cd02517  74 SGTDRIAEVAEkLDADDDIVVNVQGDEPLIPPEMIDQVVAaLKDDPGVD 122
PRK13368 PRK13368
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 46-163 4.70e-16

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 184007  Cd Length: 238  Bit Score: 77.31  E-value: 4.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900    46 AALILARGGSKGIPLKNIKHLAGVPLIGWVLRAALDSGAFQSVWVSTDHDEIENVAKQFGAQVhrrsSEVSKDSSTSLDA 125
Cdd:PRK13368   4 VVVIPARYGSSRLPGKPLLDILGKPMIQHVYERAAQAAGVEEVYVATDDQRIEDAVEAFGGKV----VMTSDDHLSGTDR 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 8923900   126 IIEFLNYhNEVDIVGNIQATSPCLHPTDLQKVAEMIRE 163
Cdd:PRK13368  80 LAEVMLK-IEADIYINVQGDEPMIRPRDIDTLIQPMLD 116
PRK05450 PRK05450
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 47-176 8.68e-14

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 235473  Cd Length: 245  Bit Score: 70.53  E-value: 8.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900    47 ALILARGGS---KGIPLKNIkhlAGVPLIGWVLRAALDSGAfQSVWVSTDHDEIENVAKQFGAQV------HR----RSS 113
Cdd:PRK05450   5 IIIPARYAStrlPGKPLADI---GGKPMIVRVYERASKAGA-DRVVVATDDERIADAVEAFGGEVvmtspdHPsgtdRIA 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8923900   114 EVSkdsstsldAIIEFlnyhNEVDIVGNIQATSPCLHPTDLQKVAEMIREEGYDSVFSVVRRH 176
Cdd:PRK05450  81 EAA--------AKLGL----ADDDIVVNVQGDEPLIPPEIIDQVAEPLANPEADMATLAVPIH 131
HAD_Pase cd07514
phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), ...
 277-421 1.53e-06

phosphatase, similar to Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PCPase), and Pyrococcus horikoshii PH1421, a magnesium-dependent phosphatase; belongs to the haloacid dehalogenase-like superfamily; Thermoplasma acidophilum TA0175 phosphoglycolate phosphatase (PGPase) catalyzes the magnesium-dependent dephosphorylation of phosphoglycolate. This family also includes Pyrococcus horikoshii OT3 PH1421, a magnesium-dependent phosphatase. 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: 319816 [Multi-domain]  Cd Length: 139  Bit Score: 47.20  E-value: 1.53e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900  277 LLVCNIDGCLTnghiyvsgDQKEIISYDVKDAIgiSLLKKSGIEVRLISERacskqTLSSLKLDCKM----EVSVS---- 348
Cdd:cd07514   1 LIAVDIDGTLT--------DRRRSIDLRAIEAI--RKLEKAGIPVVLVTGN-----SLPVARALAKYlglsGPVVAengg 65

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8923900  349 -DKLAVVDEWRKEMGLCWKEVAYLGNEVSDEECLKRVGLSGAPADACSTAQKAVGYICKCNGGRGaIREFAEHI 421
Cdd:cd07514  66 vDKGTGLEKLAERLGIDPEEVLAIGDSENDIEMFKVAGFKVAVANADEELKEAADYVTDASYGDG-VLEAIDKL 138
GT2_SpsF cd02518
SpsF is a glycosyltrnasferase implicated in the synthesis of the spore coat; Spore coat ...
 46-167 2.10e-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: 48.72  E-value: 2.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900   46 AALILARGGSKGIPLKNIKHLAGVPLIGWVLRAALDSGAFQSVWVST----DHDEIENVAKQFGAQVHRRSSE-Vskdss 120
Cdd:cd02518   1 VAIIQARMGSTRLPGKVLKPLGGKPLLEHLLDRLKRSKLIDEIVIATstneEDDPLEALAKKLGVKVFRGSEEdV----- 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 8923900  121 tsLDAIIEFLNYHNeVDIVGNIQATSPCLHPTDLQKVAEMIREEGYD 167
Cdd:cd02518  76 --LGRYYQAAEEYN-ADVVVRITGDCPLIDPEIIDAVIRLFLKSGAD 119
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
 361-423 3.00e-04

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 41.88  E-value: 3.00e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8923900   361 MGLCWKEVAYLGNEVSDEECLKRVGLSGAPADACSTAQKAVGYICKCNGGRGAiREFAEHICL 423
Cdd:PRK01158 169 MGIDPEEVAAIGDSENDLEMFEVAGFGVAVANADEELKEAADYVTEKSYGEGV-AEAIEHLLL 230
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 47-108 3.57e-04

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: 41.03  E-value: 3.57e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8923900     47 ALILA-----R-GGSKG-IPLknikhlAGVPLIGWVLRAAldSGAFQSVWVSTDHDEIENVAKQFGAQV 108
Cdd:pfam12804   1 AVILAggrssRmGGDKAlLPL------GGKPLLERVLERL--RPAGDEVVVVANDEEVLAALAGLGVPV 61
PLN02917 PLN02917
CMP-KDO synthetase
 36-171 8.91e-04

CMP-KDO synthetase


Pssm-ID: 215495  Cd Length: 293  Bit Score: 40.97  E-value: 8.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8923900    36 GRGVEKPPHLAALILARGGSKGIPLKNIKHLAGVPLIGWVLRAALDSGAFQSVWVSTDHDEIENVAKQFGAQVhRRSSEV 115
Cdd:PLN02917  39 RRSRKFRSRVVGIIPARFASSRFEGKPLVHILGKPMIQRTWERAKLATTLDHIVVATDDERIAECCRGFGADV-IMTSES 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 8923900   116 SKDSSTSLDAIIEFLNYHneVDIVGNIQATSPCLHPTDLQKVAeMIREEGYDSVFS 171
Cdd:PLN02917 118 CRNGTERCNEALKKLEKK--YDIVVNIQGDEPLIEPEIIDGVV-KALQAAPDAVFS 170
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 45-107 2.40e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 40.11  E-value: 2.40e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8923900    45 LAALILARGgsKGIPLKN----IKH-LAGVPLIGWVLRAALDSGAFQSVWVsTDHdEIENVAKQFGAQ 107
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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