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Conserved domains on  [gi|1376792677|gb|PTP86695|]
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N-acetyl sugar amidotransferase [Vibrio splendidus]

Protein Classification

adenine nucleotide alpha hydrolase family protein( domain architecture ID 188)

AANH (adenine nucleotide alpha hydrolase) family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AANH_superfamily super family cl00292
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase ...
4-353 8.78e-113

Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase (AANH) superfamily includes N-type ATP PPases, ATP sulfurylases, universal stress response proteins (USPs), and electron transfer flavoproteins (ETFs). The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.


The actual alignment was detected with superfamily member TIGR03573:

Pssm-ID: 469708  Cd Length: 343  Bit Score: 332.73  E-value: 8.78e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376792677   4 IKYCTSCMYPETKPDLWFNEQGKCSACINFEERAEIDWEERQKEFESITNKYKSIDGSNYDCIIPVSGGKDSTYQV-IRV 82
Cdd:TIGR03573   1 MKFCKRCVMPTTRPGITFDEDGVCSACRNFEEKSKIDWDEREKELEELVDKIKKKGGGRYDCIIGVSGGKDSTYQAhVLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376792677  83 LQAGLNPLCVTAETDSLSDIGRRNLENL-KRLGVDHVNVTTNPKIRRKLSRLALREVGDIQWAEHVTIFTIPIQVAVEKN 161
Cdd:TIGR03573  81 KKLGLNPLLVTVDPGWNTELGVKNLNNLiKKLGFDLHTITINPETFRKLQRAYFKKVGDPEWPQDHAIFASVYQVALKFN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376792677 162 IPLIIWGENSQHEYGGpAAAAENNVLDRRWLEEfgGMLGMRITDLVGqDDITRRDLIPYFYPSDEELKRVGVTGIFLGYY 241
Cdd:TIGR03573 161 IPLIIWGENIAEEYGG-DSEEELNPDEWKYNKR--GIDAANIKDFSD-KGLSERDLYAYTYPDKEKLQSKGVKVIYLGYY 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376792677 242 FPWDGYNNTLVAQA-YGFESYPTPteGSFVNYENLDNYYHRVHDYFKYIKYGFGRATDQANNHIRRGRLDRRDIVDFLKD 320
Cdd:TIGR03573 237 VKWDKKKNYEFIKKrGGWREGPHP--GTYENYKHIDSIFTIFHDYLKYLKFGFGRATDHASIDIRSGRITREEAIELVKE 314
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1376792677 321 NDGNYPDlylgRSLDSVLEEIDMSKDEFDDICD 353
Cdd:TIGR03573 315 YDGEFPK----EDLEYFLKYLGISEEEFWKTVE 343
 
Name Accession Description Interval E-value
WbuX TIGR03573
N-acetyl sugar amidotransferase; This enzyme has been implicated in the formation of the ...
4-353 8.78e-113

N-acetyl sugar amidotransferase; This enzyme has been implicated in the formation of the acetamido moiety (sugar-NC(=NH)CH3) which is found on some exopolysaccharides and is positively charged at neutral pH. The reaction involves ligation of ammonia with a sugar N-acetyl group, displacing water. In E. coli (O145 strain) and Pseudomonas aeruginosa (O12 strain) this gene is known as wbuX and ifnA respectively and likely acts on sialic acid. In Campylobacter jejuni, the gene is known as pseA and acts on pseudaminic acid in the process of flagellin glycosylation. In other Pseudomonas strains and various organisms it is unclear what the identity of the sugar substrate is, and in fact, the phylogenetic tree of this family sports a considerably deep branching suggestive of possible major differences in substrate structure. Nevertheless, the family is characterized by a conserved tetracysteine motif (CxxC.....[GN]xCxxC) possibly indicative of a metal binding site, as well as an invariable contextual association with homologs of the HisH and HisF proteins known as WbuY and WbuZ, respectively. These two proteins are believed to supply the enzyme with ammonium by hydrolysis of glutamine and delivery through an ammonium conduit.


Pssm-ID: 274658  Cd Length: 343  Bit Score: 332.73  E-value: 8.78e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376792677   4 IKYCTSCMYPETKPDLWFNEQGKCSACINFEERAEIDWEERQKEFESITNKYKSIDGSNYDCIIPVSGGKDSTYQV-IRV 82
Cdd:TIGR03573   1 MKFCKRCVMPTTRPGITFDEDGVCSACRNFEEKSKIDWDEREKELEELVDKIKKKGGGRYDCIIGVSGGKDSTYQAhVLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376792677  83 LQAGLNPLCVTAETDSLSDIGRRNLENL-KRLGVDHVNVTTNPKIRRKLSRLALREVGDIQWAEHVTIFTIPIQVAVEKN 161
Cdd:TIGR03573  81 KKLGLNPLLVTVDPGWNTELGVKNLNNLiKKLGFDLHTITINPETFRKLQRAYFKKVGDPEWPQDHAIFASVYQVALKFN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376792677 162 IPLIIWGENSQHEYGGpAAAAENNVLDRRWLEEfgGMLGMRITDLVGqDDITRRDLIPYFYPSDEELKRVGVTGIFLGYY 241
Cdd:TIGR03573 161 IPLIIWGENIAEEYGG-DSEEELNPDEWKYNKR--GIDAANIKDFSD-KGLSERDLYAYTYPDKEKLQSKGVKVIYLGYY 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376792677 242 FPWDGYNNTLVAQA-YGFESYPTPteGSFVNYENLDNYYHRVHDYFKYIKYGFGRATDQANNHIRRGRLDRRDIVDFLKD 320
Cdd:TIGR03573 237 VKWDKKKNYEFIKKrGGWREGPHP--GTYENYKHIDSIFTIFHDYLKYLKFGFGRATDHASIDIRSGRITREEAIELVKE 314
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1376792677 321 NDGNYPDlylgRSLDSVLEEIDMSKDEFDDICD 353
Cdd:TIGR03573 315 YDGEFPK----EDLEYFLKYLGISEEEFWKTVE 343
AANH_WbpG-like cd01996
Rhizobium leguminosarum WbpG protein and similar proteins; This subfamily includes Rhizobium ...
59-229 3.14e-43

Rhizobium leguminosarum WbpG protein and similar proteins; This subfamily includes Rhizobium leguminosarum WbpG and Campylobacter jejuni PseA proteins. They belong to the of adenine nucleotide alpha hydrolase (AANH) superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This subfamily of proteins is predicted to bind ATP. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467500 [Multi-domain]  Cd Length: 158  Bit Score: 147.90  E-value: 3.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376792677  59 DGSNYDCIIPVSGGKDSTYQVIRVLQ-AGLNPLCVTAETDSLSDIGRRNLENL-KRLGVDHVNVTTNPKIRRKLSRLALR 136
Cdd:cd01996     2 KGKPYDCIIGVSGGKDSTYAAHKAKEkYGLRPLLVTVDAGWNSPEAVKNIEKLvRALGVDLITFVPNWKEMRDLQRLAFK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376792677 137 EVGDIQWAEHVTIFTIPIQVAVEKNIPLIIWGENSQHEYGGPAAAAENNVLDRRWleefgGMLGMRItdlvgqdditrRD 216
Cdd:cd01996    82 SNGDQDWPQDHGIFTSLYKMAVKFGIPLIIWGENPAEELGGPRSELGVSTDETRH-----GFLGYKE-----------KD 145
                         170
                  ....*....|...
gi 1376792677 217 LIPYFYPSDEELK 229
Cdd:cd01996   146 LKFYGYPSVQELN 158
 
Name Accession Description Interval E-value
WbuX TIGR03573
N-acetyl sugar amidotransferase; This enzyme has been implicated in the formation of the ...
4-353 8.78e-113

N-acetyl sugar amidotransferase; This enzyme has been implicated in the formation of the acetamido moiety (sugar-NC(=NH)CH3) which is found on some exopolysaccharides and is positively charged at neutral pH. The reaction involves ligation of ammonia with a sugar N-acetyl group, displacing water. In E. coli (O145 strain) and Pseudomonas aeruginosa (O12 strain) this gene is known as wbuX and ifnA respectively and likely acts on sialic acid. In Campylobacter jejuni, the gene is known as pseA and acts on pseudaminic acid in the process of flagellin glycosylation. In other Pseudomonas strains and various organisms it is unclear what the identity of the sugar substrate is, and in fact, the phylogenetic tree of this family sports a considerably deep branching suggestive of possible major differences in substrate structure. Nevertheless, the family is characterized by a conserved tetracysteine motif (CxxC.....[GN]xCxxC) possibly indicative of a metal binding site, as well as an invariable contextual association with homologs of the HisH and HisF proteins known as WbuY and WbuZ, respectively. These two proteins are believed to supply the enzyme with ammonium by hydrolysis of glutamine and delivery through an ammonium conduit.


Pssm-ID: 274658  Cd Length: 343  Bit Score: 332.73  E-value: 8.78e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376792677   4 IKYCTSCMYPETKPDLWFNEQGKCSACINFEERAEIDWEERQKEFESITNKYKSIDGSNYDCIIPVSGGKDSTYQV-IRV 82
Cdd:TIGR03573   1 MKFCKRCVMPTTRPGITFDEDGVCSACRNFEEKSKIDWDEREKELEELVDKIKKKGGGRYDCIIGVSGGKDSTYQAhVLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376792677  83 LQAGLNPLCVTAETDSLSDIGRRNLENL-KRLGVDHVNVTTNPKIRRKLSRLALREVGDIQWAEHVTIFTIPIQVAVEKN 161
Cdd:TIGR03573  81 KKLGLNPLLVTVDPGWNTELGVKNLNNLiKKLGFDLHTITINPETFRKLQRAYFKKVGDPEWPQDHAIFASVYQVALKFN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376792677 162 IPLIIWGENSQHEYGGpAAAAENNVLDRRWLEEfgGMLGMRITDLVGqDDITRRDLIPYFYPSDEELKRVGVTGIFLGYY 241
Cdd:TIGR03573 161 IPLIIWGENIAEEYGG-DSEEELNPDEWKYNKR--GIDAANIKDFSD-KGLSERDLYAYTYPDKEKLQSKGVKVIYLGYY 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376792677 242 FPWDGYNNTLVAQA-YGFESYPTPteGSFVNYENLDNYYHRVHDYFKYIKYGFGRATDQANNHIRRGRLDRRDIVDFLKD 320
Cdd:TIGR03573 237 VKWDKKKNYEFIKKrGGWREGPHP--GTYENYKHIDSIFTIFHDYLKYLKFGFGRATDHASIDIRSGRITREEAIELVKE 314
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1376792677 321 NDGNYPDlylgRSLDSVLEEIDMSKDEFDDICD 353
Cdd:TIGR03573 315 YDGEFPK----EDLEYFLKYLGISEEEFWKTVE 343
AANH_WbpG-like cd01996
Rhizobium leguminosarum WbpG protein and similar proteins; This subfamily includes Rhizobium ...
59-229 3.14e-43

Rhizobium leguminosarum WbpG protein and similar proteins; This subfamily includes Rhizobium leguminosarum WbpG and Campylobacter jejuni PseA proteins. They belong to the of adenine nucleotide alpha hydrolase (AANH) superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This subfamily of proteins is predicted to bind ATP. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467500 [Multi-domain]  Cd Length: 158  Bit Score: 147.90  E-value: 3.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376792677  59 DGSNYDCIIPVSGGKDSTYQVIRVLQ-AGLNPLCVTAETDSLSDIGRRNLENL-KRLGVDHVNVTTNPKIRRKLSRLALR 136
Cdd:cd01996     2 KGKPYDCIIGVSGGKDSTYAAHKAKEkYGLRPLLVTVDAGWNSPEAVKNIEKLvRALGVDLITFVPNWKEMRDLQRLAFK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376792677 137 EVGDIQWAEHVTIFTIPIQVAVEKNIPLIIWGENSQHEYGGPAAAAENNVLDRRWleefgGMLGMRItdlvgqdditrRD 216
Cdd:cd01996    82 SNGDQDWPQDHGIFTSLYKMAVKFGIPLIIWGENPAEELGGPRSELGVSTDETRH-----GFLGYKE-----------KD 145
                         170
                  ....*....|...
gi 1376792677 217 LIPYFYPSDEELK 229
Cdd:cd01996   146 LKFYGYPSVQELN 158
 
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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