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Conserved domains on  [gi|31417172|gb|AAH06140|]
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HYI protein [Homo sapiens]

Protein Classification

hydroxypyruvate isomerase family protein( domain architecture ID 11466508)

hydroxypyruvate isomerase (hyi) family protein similar to 2-oxo-tetronate isomerase that catalyzes the isomerization of 2-oxo-tetronate to 3-oxo-tetronate, and hydroxypyruvate isomerase that catalyzes the reversible isomerization between hydroxypyruvate and 2-hydroxy-3-oxopropanoate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Hyi COG3622
Hydroxypyruvate/dehydroerythronate isomerase, Hyi/OtnI family [Carbohydrate transport and ...
2-196 2.55e-89

Hydroxypyruvate/dehydroerythronate isomerase, Hyi/OtnI family [Carbohydrate transport and metabolism];


:

Pssm-ID: 442840  Cd Length: 260  Bit Score: 263.51  E-value: 2.55e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31417172   2 GLGAVPGRQAAFREGLEQAVRYAKALGCPRIHLMAGRVPQGADRiavkAEMEAVFLENLRHAAGVLAQEDLVGLLEPINT 81
Cdd:COG3622  72 GLAALPGREAEFRAGVDRALEYAAALGCKNLHVMAGNRPRGLDD----EAALATFVENLRYAADLAAPHGITLLIEPLNS 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31417172  82 RITdPQYFLDTPQQAAAILQKVGRPNLQLQMDIFHWQIMDGNLTGNIREFLPIVGHVQVAQVPGRGEPSSpGELNFPYLF 161
Cdd:COG3622 148 RDH-PGYFLDTTAQAVAIIEAVGSPNLKLLYDIYHMQIMEGDLIRTIRRHLPRIGHVQIADVPGRHEPGT-GELNYPAIF 225
                       170       180       190
                ....*....|....*....|....*....|....*
gi 31417172 162 QLLENEGYKGFVGCEYQPRGDTVEGLSWLRSYWDR 196
Cdd:COG3622 226 KALDALGYDGWVGCEYKPRGDTEAGLGWLKAYRVA 260
 
Name Accession Description Interval E-value
Hyi COG3622
Hydroxypyruvate/dehydroerythronate isomerase, Hyi/OtnI family [Carbohydrate transport and ...
2-196 2.55e-89

Hydroxypyruvate/dehydroerythronate isomerase, Hyi/OtnI family [Carbohydrate transport and metabolism];


Pssm-ID: 442840  Cd Length: 260  Bit Score: 263.51  E-value: 2.55e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31417172   2 GLGAVPGRQAAFREGLEQAVRYAKALGCPRIHLMAGRVPQGADRiavkAEMEAVFLENLRHAAGVLAQEDLVGLLEPINT 81
Cdd:COG3622  72 GLAALPGREAEFRAGVDRALEYAAALGCKNLHVMAGNRPRGLDD----EAALATFVENLRYAADLAAPHGITLLIEPLNS 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31417172  82 RITdPQYFLDTPQQAAAILQKVGRPNLQLQMDIFHWQIMDGNLTGNIREFLPIVGHVQVAQVPGRGEPSSpGELNFPYLF 161
Cdd:COG3622 148 RDH-PGYFLDTTAQAVAIIEAVGSPNLKLLYDIYHMQIMEGDLIRTIRRHLPRIGHVQIADVPGRHEPGT-GELNYPAIF 225
                       170       180       190
                ....*....|....*....|....*....|....*
gi 31417172 162 QLLENEGYKGFVGCEYQPRGDTVEGLSWLRSYWDR 196
Cdd:COG3622 226 KALDALGYDGWVGCEYKPRGDTEAGLGWLKAYRVA 260
OH-pyruv-isom TIGR03234
hydroxypyruvate isomerase; This enzyme interconverts tartronate semi-aldehyde (TSA, aka ...
2-190 3.01e-77

hydroxypyruvate isomerase; This enzyme interconverts tartronate semi-aldehyde (TSA, aka 2-hydroxy 3-oxopropionate) and hydroxypyruvate. The E. coli enzyme has been characterized and found to be specific for TSA, contain no cofactors, and have a rather high Km for hydroxypyruvate of 12.5 mM. The gene is ofter found in association with glyoxalate carboligase (which produces TSA), but has been shown to have no effect on growth on glyoxalate when knocked out. This is consistent with the fact that the gene for tartronate semialdehyde reductase (glxR) is also associated and may have primary responsibility for the catabolism of TSA.


Pssm-ID: 163190  Cd Length: 254  Bit Score: 232.61  E-value: 3.01e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31417172     2 GLGAVPGRQAAFREGLEQAVRYAKALGCPRIHLMAGRVPQGADRiavkAEMEAVFLENLRHAAGVLAQEDLVGLLEPINT 81
Cdd:TIGR03234  71 GIACLPGREEEFREGVALAIAYARALGCPQVNCLAGKRPAGVSP----EEARATLVENLRYAADALDRIGLTLLIEPINS 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31417172    82 RitD-PQYFLDTPQQAAAILQKVGRPNLQLQMDIFHWQIMDGNLTGNIREFLPIVGHVQVAQVPGRGEPSSpGELNFPYL 160
Cdd:TIGR03234 147 F--DmPGFFLTTTEQALAVIDDVGRENLKLQYDLYHMQRMGGDLARTLAAYAAHIGHVQIADNPGRHEPGT-GEINYRFL 223
                         170       180       190
                  ....*....|....*....|....*....|
gi 31417172   161 FQLLENEGYKGFVGCEYQPRGDTVEGLSWL 190
Cdd:TIGR03234 224 FAVLDRLGYDGWVGLEYKPLTDTEASLGWL 253
PRK09997 PRK09997
hydroxypyruvate isomerase; Provisional
2-193 3.32e-58

hydroxypyruvate isomerase; Provisional


Pssm-ID: 182188  Cd Length: 258  Bit Score: 184.39  E-value: 3.32e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31417172    2 GLGAVPGRQAAFREGLEQAVRYAKALGCPRIHLMAGRVPQGADriavKAEMEAVFLENLRHAAGVLAQEDLVGLLEPINt 81
Cdd:PRK09997  72 GIACIPGREEEFRDGVAAAIRYARALGNKKINCLVGKTPAGFS----SEQIHATLVENLRYAANMLMKEDILLLIEPIN- 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31417172   82 RITDPQYFLDTPQQAAAILQKVGRPNLQLQMDIFHWQIMDGNLTGNIREFLPIVGHVQVAQVPGRGEPSSpGELNFPYLF 161
Cdd:PRK09997 147 HFDIPGFHLTGTRQALKLIDDVGCCNLKIQYDIYHMQRMEGELTNTMTQWADKIGHLQIADNPHRGEPGT-GEINYDYLF 225
                        170       180       190
                 ....*....|....*....|....*....|..
gi 31417172  162 QLLENEGYKGFVGCEYQPRGDTVEGLSWLRSY 193
Cdd:PRK09997 226 KVIENSDYNGWVGCEYKPQTTTEAGLRWMDPY 257
AP_endonuc_2 pfam01261
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ...
2-193 2.58e-35

Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose isomerase and in endonuclease IV (EC:3.1.21.2). This domain is also found in the N termini of bacterial myo-inositol catabolism proteins. These are involved in the myo-inositol catabolism pathway, and is required for growth on myo-inositol in Rhizobium leguminosarum bv. viciae.


Pssm-ID: 426164 [Multi-domain]  Cd Length: 248  Bit Score: 125.18  E-value: 2.58e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31417172     2 GLGAVPGR-QAAFREGLEQAVRYAKALGCPRIHLMAGRVPqGADRiavkAEMEAVFLENLRHAAGVLAQEDLVGLLEPIN 80
Cdd:pfam01261  53 NLASPDEEeREKAIDRLKRAIELAAALGAKLVVFHPGSDL-GDDP----EEALARLAESLRELADLAEREGVRLALEPLA 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31417172    81 TRITdpqYFLDTPQQAAAILQKVGRPNLQLQMDIFHWQIMDGNLTGNIREFLPIVGHVQVAQV-------PGRGEPSSPG 153
Cdd:pfam01261 128 GKGT---NVGNTFEEALEIIDEVDSPNVGVCLDTGHLFAAGDGDLFELRLGDRYIGHVHLKDSknplgsgPDRHVPIGEG 204
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 31417172   154 ELNFPYLFQLLENEGYKGFVGCEY----QPRGDTVEGLSWLRSY 193
Cdd:pfam01261 205 VIDFEALFRALKEIGYDGPLSLETfndgPPEEGAREGLEWLREL 248
 
Name Accession Description Interval E-value
Hyi COG3622
Hydroxypyruvate/dehydroerythronate isomerase, Hyi/OtnI family [Carbohydrate transport and ...
2-196 2.55e-89

Hydroxypyruvate/dehydroerythronate isomerase, Hyi/OtnI family [Carbohydrate transport and metabolism];


Pssm-ID: 442840  Cd Length: 260  Bit Score: 263.51  E-value: 2.55e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31417172   2 GLGAVPGRQAAFREGLEQAVRYAKALGCPRIHLMAGRVPQGADRiavkAEMEAVFLENLRHAAGVLAQEDLVGLLEPINT 81
Cdd:COG3622  72 GLAALPGREAEFRAGVDRALEYAAALGCKNLHVMAGNRPRGLDD----EAALATFVENLRYAADLAAPHGITLLIEPLNS 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31417172  82 RITdPQYFLDTPQQAAAILQKVGRPNLQLQMDIFHWQIMDGNLTGNIREFLPIVGHVQVAQVPGRGEPSSpGELNFPYLF 161
Cdd:COG3622 148 RDH-PGYFLDTTAQAVAIIEAVGSPNLKLLYDIYHMQIMEGDLIRTIRRHLPRIGHVQIADVPGRHEPGT-GELNYPAIF 225
                       170       180       190
                ....*....|....*....|....*....|....*
gi 31417172 162 QLLENEGYKGFVGCEYQPRGDTVEGLSWLRSYWDR 196
Cdd:COG3622 226 KALDALGYDGWVGCEYKPRGDTEAGLGWLKAYRVA 260
OH-pyruv-isom TIGR03234
hydroxypyruvate isomerase; This enzyme interconverts tartronate semi-aldehyde (TSA, aka ...
2-190 3.01e-77

hydroxypyruvate isomerase; This enzyme interconverts tartronate semi-aldehyde (TSA, aka 2-hydroxy 3-oxopropionate) and hydroxypyruvate. The E. coli enzyme has been characterized and found to be specific for TSA, contain no cofactors, and have a rather high Km for hydroxypyruvate of 12.5 mM. The gene is ofter found in association with glyoxalate carboligase (which produces TSA), but has been shown to have no effect on growth on glyoxalate when knocked out. This is consistent with the fact that the gene for tartronate semialdehyde reductase (glxR) is also associated and may have primary responsibility for the catabolism of TSA.


Pssm-ID: 163190  Cd Length: 254  Bit Score: 232.61  E-value: 3.01e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31417172     2 GLGAVPGRQAAFREGLEQAVRYAKALGCPRIHLMAGRVPQGADRiavkAEMEAVFLENLRHAAGVLAQEDLVGLLEPINT 81
Cdd:TIGR03234  71 GIACLPGREEEFREGVALAIAYARALGCPQVNCLAGKRPAGVSP----EEARATLVENLRYAADALDRIGLTLLIEPINS 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31417172    82 RitD-PQYFLDTPQQAAAILQKVGRPNLQLQMDIFHWQIMDGNLTGNIREFLPIVGHVQVAQVPGRGEPSSpGELNFPYL 160
Cdd:TIGR03234 147 F--DmPGFFLTTTEQALAVIDDVGRENLKLQYDLYHMQRMGGDLARTLAAYAAHIGHVQIADNPGRHEPGT-GEINYRFL 223
                         170       180       190
                  ....*....|....*....|....*....|
gi 31417172   161 FQLLENEGYKGFVGCEYQPRGDTVEGLSWL 190
Cdd:TIGR03234 224 FAVLDRLGYDGWVGLEYKPLTDTEASLGWL 253
PRK09997 PRK09997
hydroxypyruvate isomerase; Provisional
2-193 3.32e-58

hydroxypyruvate isomerase; Provisional


Pssm-ID: 182188  Cd Length: 258  Bit Score: 184.39  E-value: 3.32e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31417172    2 GLGAVPGRQAAFREGLEQAVRYAKALGCPRIHLMAGRVPQGADriavKAEMEAVFLENLRHAAGVLAQEDLVGLLEPINt 81
Cdd:PRK09997  72 GIACIPGREEEFRDGVAAAIRYARALGNKKINCLVGKTPAGFS----SEQIHATLVENLRYAANMLMKEDILLLIEPIN- 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31417172   82 RITDPQYFLDTPQQAAAILQKVGRPNLQLQMDIFHWQIMDGNLTGNIREFLPIVGHVQVAQVPGRGEPSSpGELNFPYLF 161
Cdd:PRK09997 147 HFDIPGFHLTGTRQALKLIDDVGCCNLKIQYDIYHMQRMEGELTNTMTQWADKIGHLQIADNPHRGEPGT-GEINYDYLF 225
                        170       180       190
                 ....*....|....*....|....*....|..
gi 31417172  162 QLLENEGYKGFVGCEYQPRGDTVEGLSWLRSY 193
Cdd:PRK09997 226 KVIENSDYNGWVGCEYKPQTTTEAGLRWMDPY 257
PRK09989 PRK09989
HPr family phosphocarrier protein;
2-193 1.95e-57

HPr family phosphocarrier protein;


Pssm-ID: 182185  Cd Length: 258  Bit Score: 182.16  E-value: 1.95e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31417172    2 GLGAVPGRQAAFREGLEQAVRYAKALGCPRIHLMAGRVPQGADriavKAEMEAVFLENLRHAAGVLAQEDLVGLLEPINT 81
Cdd:PRK09989  72 GLSALPGREHEARADIDLALEYALALNCEQVHVMAGVVPAGED----AERYRAVFIDNLRYAADRFAPHGKRILVEALSP 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31417172   82 RITdPQYFLDTPQQAAAILQKVGRPNLQLQMDIFHWQIMDGNLTGNIREFLPIVGHVQVAQVPGRGEPSSpGELNFPYLF 161
Cdd:PRK09989 148 GVK-PHYLFSSQYQALAIVEEVARDNVFIQLDTFHAQKVDGNLTHLIRDYAGKYAHVQIAGLPDRHEPDD-GEINYPWLF 225
                        170       180       190
                 ....*....|....*....|....*....|..
gi 31417172  162 QLLENEGYKGFVGCEYQPRGDTVEGLSWLRSY 193
Cdd:PRK09989 226 RLFDEVGYQGWIGCEYKPRGLTEEGLGWFDAW 257
AP_endonuc_2 pfam01261
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ...
2-193 2.58e-35

Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose isomerase and in endonuclease IV (EC:3.1.21.2). This domain is also found in the N termini of bacterial myo-inositol catabolism proteins. These are involved in the myo-inositol catabolism pathway, and is required for growth on myo-inositol in Rhizobium leguminosarum bv. viciae.


Pssm-ID: 426164 [Multi-domain]  Cd Length: 248  Bit Score: 125.18  E-value: 2.58e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31417172     2 GLGAVPGR-QAAFREGLEQAVRYAKALGCPRIHLMAGRVPqGADRiavkAEMEAVFLENLRHAAGVLAQEDLVGLLEPIN 80
Cdd:pfam01261  53 NLASPDEEeREKAIDRLKRAIELAAALGAKLVVFHPGSDL-GDDP----EEALARLAESLRELADLAEREGVRLALEPLA 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31417172    81 TRITdpqYFLDTPQQAAAILQKVGRPNLQLQMDIFHWQIMDGNLTGNIREFLPIVGHVQVAQV-------PGRGEPSSPG 153
Cdd:pfam01261 128 GKGT---NVGNTFEEALEIIDEVDSPNVGVCLDTGHLFAAGDGDLFELRLGDRYIGHVHLKDSknplgsgPDRHVPIGEG 204
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 31417172   154 ELNFPYLFQLLENEGYKGFVGCEY----QPRGDTVEGLSWLRSY 193
Cdd:pfam01261 205 VIDFEALFRALKEIGYDGPLSLETfndgPPEEGAREGLEWLREL 248
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
3-194 7.26e-24

Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 95.08  E-value: 7.26e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31417172   3 LGAVPGRQAAFREGLEQAVRYAKALGCPRIHLMAGRVPQGADRIAvkaEMEAVFLENLRHAAGVLAQEDLVGLLEPIntr 82
Cdd:COG1082  66 LAPDPEVREAALERLKRAIDLAAELGAKVVVVHPGSPPPPDLPPE---EAWDRLAERLRELAELAEEAGVTLALENH--- 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31417172  83 itdPQYFLDTPQQAAAILQKVGRPNLQLQMDIFHWQIMDGNLTGNIREFLPIVGHVQVAQVPGR-----GEpsspGELNF 157
Cdd:COG1082 140 ---EGTFVNTPEEALRLLEAVDSPNVGLLLDTGHALLAGEDPVELLRKLGDRIKHVHLKDADGDqhlppGE----GDIDF 212
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 31417172 158 PYLFQLLENEGYKGFVGCEY-----QPRGDTVEGLSWLRSYW 194
Cdd:COG1082 213 AAILRALKEAGYDGWLSLEVesdpdDPEEAARESLEYLRKLL 254
 
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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