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Conserved domains on  [gi|194386426|dbj|BAG61023|]
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unnamed protein product [Homo sapiens]

Protein Classification

ATP-dependent (S)-NAD(P)H-hydrate dehydratase( domain architecture ID 10100258)

ATP-dependent (S)-NAD(P)H-hydrate dehydratase catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP; together with NAD(P)HX epimerase, repairs both epimers of NAD(P)HX, a damaged form of NAD(P)H

CATH:  3.40.1190.20
EC:  4.2.1.93
PubMed:  8382990|21994945
SCOP:  3001268

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
23-205 9.22e-43

B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of the ATP binding site, the substrate binding site and the Mg2+binding site and structural homology this group is a member of the ribokinase-like superfamily.


:

Pssm-ID: 238576  Cd Length: 254  Bit Score: 144.29  E-value: 9.22e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386426  23 VLAVGqSGLADE----GILEVSKARDIPVVIDADGLWLVAQQPALIHGYRKAVLTPNHVEFSRLYDAVlrgPMDSDDSHG 98
Cdd:cd01171   80 AVVIG-PGLGRDeeaaEILEKALAKDKPLVLDADALNLLADEPSLIKRYGPVVLTPHPGEFARLLGAL---VEEIQADRL 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386426  99 SVLRLSQALGNVTVVQKGERDILSNGQQVLVCSQEGSS-RRCGGQGDLLSGSLGVLVHWALlagpqktngssPLLVAAFG 177
Cdd:cd01171  156 AAAREAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPgLATGGSGDVLAGIIAALLAQGL-----------SPLEAAAL 224
                        170       180
                 ....*....|....*....|....*...
gi 194386426 178 ACSLTRQCNHQAFQKHGRSTTTSDMIAE 205
Cdd:cd01171  225 AVYLHGLAGDLAAKKKGAGLTAADLVAE 252
 
Name Accession Description Interval E-value
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
23-205 9.22e-43

B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of the ATP binding site, the substrate binding site and the Mg2+binding site and structural homology this group is a member of the ribokinase-like superfamily.


Pssm-ID: 238576  Cd Length: 254  Bit Score: 144.29  E-value: 9.22e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386426  23 VLAVGqSGLADE----GILEVSKARDIPVVIDADGLWLVAQQPALIHGYRKAVLTPNHVEFSRLYDAVlrgPMDSDDSHG 98
Cdd:cd01171   80 AVVIG-PGLGRDeeaaEILEKALAKDKPLVLDADALNLLADEPSLIKRYGPVVLTPHPGEFARLLGAL---VEEIQADRL 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386426  99 SVLRLSQALGNVTVVQKGERDILSNGQQVLVCSQEGSS-RRCGGQGDLLSGSLGVLVHWALlagpqktngssPLLVAAFG 177
Cdd:cd01171  156 AAAREAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPgLATGGSGDVLAGIIAALLAQGL-----------SPLEAAAL 224
                        170       180
                 ....*....|....*....|....*...
gi 194386426 178 ACSLTRQCNHQAFQKHGRSTTTSDMIAE 205
Cdd:cd01171  225 AVYLHGLAGDLAAKKKGAGLTAADLVAE 252
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
17-203 9.55e-24

Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also is a carbohydrate kinase. (personal obs Yeats C).


Pssm-ID: 396007  Cd Length: 242  Bit Score: 94.74  E-value: 9.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386426   17 AARWPWVLAVGqSGL-ADEG---ILEVSKARDIPVVIDADGLWLVAQQPALIHGYRKAVLTPNHVEFSRLYDAVlrgPMD 92
Cdd:pfam01256  62 KLSRYDAVVIG-PGLgRDEKgkaALEEVLAKDCPLVIDADALNLLAINNEKPAREGPTVLTPHPGEFERLCGLA---GIL 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386426   93 SDDSHGSVLRLSQALgNVTVVQKGERD-ILSNGQQVLVCSQEGSSRRCGGQGDLLSGSLGVLVHWALlagpqktngssPL 171
Cdd:pfam01256 138 GDDRLEAARELAQKL-NGTILLKGNVTvIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNE-----------DP 205
                         170       180       190
                  ....*....|....*....|....*....|..
gi 194386426  172 LVAAFGACSLTRQCNHQAFQKHGRSTTTSDMI 203
Cdd:pfam01256 206 YDAAIAAAWLHGAASDLAAENHGVYMLPTLLS 237
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
14-215 1.59e-17

NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport and metabolism];


Pssm-ID: 439833  Cd Length: 280  Bit Score: 78.63  E-value: 1.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386426  14 IRNAARWPWVLAVG----QSGLADEGILEVSKARDIPVVIDADGLWLVAQQPALIHGYRK-AVLTPNHVEFSRLydavlr 88
Cdd:COG0063   87 LLELLERADAVVIGpglgRDEETRELLRALLEAADKPLVLDADALNLLAEDPELLAALPApTVLTPHPGEFARL------ 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386426  89 GPMDSDDSH----GSVLRLSQALGnVTVVQKGERDIlsngqqvlVCSQEGSSRRC---------GGQGDLLSGSLGvlvh 155
Cdd:COG0063  161 LGCSVAEIQadrlEAAREAAKRYG-AVVVLKGAGTV--------IAAPDGRVYINptgnpglatAGSGDVLAGIIA---- 227
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386426 156 wALLAgpQktnGSSPLLVAAFGACsLTRQCNHQAFQKHGRSTTTSDMIAEVGAAFSKLFE 215
Cdd:COG0063  228 -GLLA--Q---GLDPFEAAAAGVY-LHGLAGDLAAEERGRGLLASDLIEALPAALRELLE 280
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
34-203 7.71e-15

yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length orthologs in a number of species, all of unknown function. However, yeast YNL200C is homologous and corresponds to the N-terminal region while yeast YKL151C and B. subtilis yxkO correspond to this C-terminal region only. The present model may hit hydroxyethylthiazole kinase, an enzyme associated with thiamine biosynthesis. [Unknown function, General]


Pssm-ID: 272955  Cd Length: 270  Bit Score: 71.26  E-value: 7.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386426   34 EGILEVSKardiPVVIDADGLWLVAQQPALihgYRKAVLTPNHVEFSRLYDAVlrgpMDSDDSHGSVLRLSQALgNVTVV 113
Cdd:TIGR00196 113 EEVLELDK----PVVLDADALNLLTYNQKR---EGEVILTPHPGEFKRLLGVN----EIQGDRLEAAQDIAQKL-QAVVV 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386426  114 QKGERDILSNGQ-QVLVCSQEGSSRRCGGQGDLLSGSLGvlvhwALLAgpqktNGSSPLLvAAFGACSLTRQCNHQAFQK 192
Cdd:TIGR00196 181 LKGAADVIAAPDgDLWINKTGNAALAKGGTGDVLAGLIG-----GLLA-----QNLDPFD-AACNAAFAHGLAGDLALKN 249
                         170
                  ....*....|..
gi 194386426  193 HG-RSTTTSDMI 203
Cdd:TIGR00196 250 HGaYGLTALDLI 261
 
Name Accession Description Interval E-value
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
23-205 9.22e-43

B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of the ATP binding site, the substrate binding site and the Mg2+binding site and structural homology this group is a member of the ribokinase-like superfamily.


Pssm-ID: 238576  Cd Length: 254  Bit Score: 144.29  E-value: 9.22e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386426  23 VLAVGqSGLADE----GILEVSKARDIPVVIDADGLWLVAQQPALIHGYRKAVLTPNHVEFSRLYDAVlrgPMDSDDSHG 98
Cdd:cd01171   80 AVVIG-PGLGRDeeaaEILEKALAKDKPLVLDADALNLLADEPSLIKRYGPVVLTPHPGEFARLLGAL---VEEIQADRL 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386426  99 SVLRLSQALGNVTVVQKGERDILSNGQQVLVCSQEGSS-RRCGGQGDLLSGSLGVLVHWALlagpqktngssPLLVAAFG 177
Cdd:cd01171  156 AAAREAAAKLGATVVLKGAVTVIADPDGRVYVNPTGNPgLATGGSGDVLAGIIAALLAQGL-----------SPLEAAAL 224
                        170       180
                 ....*....|....*....|....*...
gi 194386426 178 ACSLTRQCNHQAFQKHGRSTTTSDMIAE 205
Cdd:cd01171  225 AVYLHGLAGDLAAKKKGAGLTAADLVAE 252
Carb_kinase pfam01256
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ...
17-203 9.55e-24

Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also is a carbohydrate kinase. (personal obs Yeats C).


Pssm-ID: 396007  Cd Length: 242  Bit Score: 94.74  E-value: 9.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386426   17 AARWPWVLAVGqSGL-ADEG---ILEVSKARDIPVVIDADGLWLVAQQPALIHGYRKAVLTPNHVEFSRLYDAVlrgPMD 92
Cdd:pfam01256  62 KLSRYDAVVIG-PGLgRDEKgkaALEEVLAKDCPLVIDADALNLLAINNEKPAREGPTVLTPHPGEFERLCGLA---GIL 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386426   93 SDDSHGSVLRLSQALgNVTVVQKGERD-ILSNGQQVLVCSQEGSSRRCGGQGDLLSGSLGVLVHWALlagpqktngssPL 171
Cdd:pfam01256 138 GDDRLEAARELAQKL-NGTILLKGNVTvIAAPGGEVWINSTGNSALAKGGSGDVLAGLIGGLLAQNE-----------DP 205
                         170       180       190
                  ....*....|....*....|....*....|..
gi 194386426  172 LVAAFGACSLTRQCNHQAFQKHGRSTTTSDMI 203
Cdd:pfam01256 206 YDAAIAAAWLHGAASDLAAENHGVYMLPTLLS 237
Nnr2 COG0063
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ...
14-215 1.59e-17

NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport and metabolism];


Pssm-ID: 439833  Cd Length: 280  Bit Score: 78.63  E-value: 1.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386426  14 IRNAARWPWVLAVG----QSGLADEGILEVSKARDIPVVIDADGLWLVAQQPALIHGYRK-AVLTPNHVEFSRLydavlr 88
Cdd:COG0063   87 LLELLERADAVVIGpglgRDEETRELLRALLEAADKPLVLDADALNLLAEDPELLAALPApTVLTPHPGEFARL------ 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386426  89 GPMDSDDSH----GSVLRLSQALGnVTVVQKGERDIlsngqqvlVCSQEGSSRRC---------GGQGDLLSGSLGvlvh 155
Cdd:COG0063  161 LGCSVAEIQadrlEAAREAAKRYG-AVVVLKGAGTV--------IAAPDGRVYINptgnpglatAGSGDVLAGIIA---- 227
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386426 156 wALLAgpQktnGSSPLLVAAFGACsLTRQCNHQAFQKHGRSTTTSDMIAEVGAAFSKLFE 215
Cdd:COG0063  228 -GLLA--Q---GLDPFEAAAAGVY-LHGLAGDLAAEERGRGLLASDLIEALPAALRELLE 280
yjeF_cterm TIGR00196
yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length ...
34-203 7.71e-15

yjeF C-terminal region, hydroxyethylthiazole kinase-related; E. coli yjeF has full-length orthologs in a number of species, all of unknown function. However, yeast YNL200C is homologous and corresponds to the N-terminal region while yeast YKL151C and B. subtilis yxkO correspond to this C-terminal region only. The present model may hit hydroxyethylthiazole kinase, an enzyme associated with thiamine biosynthesis. [Unknown function, General]


Pssm-ID: 272955  Cd Length: 270  Bit Score: 71.26  E-value: 7.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386426   34 EGILEVSKardiPVVIDADGLWLVAQQPALihgYRKAVLTPNHVEFSRLYDAVlrgpMDSDDSHGSVLRLSQALgNVTVV 113
Cdd:TIGR00196 113 EEVLELDK----PVVLDADALNLLTYNQKR---EGEVILTPHPGEFKRLLGVN----EIQGDRLEAAQDIAQKL-QAVVV 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194386426  114 QKGERDILSNGQ-QVLVCSQEGSSRRCGGQGDLLSGSLGvlvhwALLAgpqktNGSSPLLvAAFGACSLTRQCNHQAFQK 192
Cdd:TIGR00196 181 LKGAADVIAAPDgDLWINKTGNAALAKGGTGDVLAGLIG-----GLLA-----QNLDPFD-AACNAAFAHGLAGDLALKN 249
                         170
                  ....*....|..
gi 194386426  193 HG-RSTTTSDMI 203
Cdd:TIGR00196 250 HGaYGLTALDLI 261
 
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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