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Conserved domains on  [gi|16129476|ref|NP_416034|]
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3-hydroxy-2,4-pentadione 5-phosphate thiolase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase( domain architecture ID 10013022)

3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase catalyzes the transfer of an acetyl moiety from 3-hydroxy-5-phosphonooxypentane-2,4-dione to CoA to form glycerone phosphate and acetyl-CoA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK08227 PRK08227
3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase;
28-291 0e+00

3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase;


:

Pssm-ID: 181306 [Multi-domain]  Cd Length: 264  Bit Score: 558.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476   28 GCGALDWGMQSRLSRIFNPKTGKTVMLAFDHGYFQGPTTGLERIDINIAPLFEHADVLMCTRGILRSVVPPATNRPVVLR 107
Cdd:PRK08227   1 GAGALDWGMKNRLSRIFNPKTGRTVMLAFDHGYFQGPTTGLERIDINIAPLFPYADVLMCTRGILRSVVPPATNKPVVLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476  108 ASGANSILAELSNEAVALSMDDAVRLNSCAVAAQVYIGSEYEHQSIKNIIQLVDAGMKVGMPTMAVTGVGKDMVRDQRYF 187
Cdd:PRK08227  81 ASGGNSILKELSNEAVAVDMEDAVRLNACAVAAQVFIGSEYEHQSIKNIIQLVDAGLRYGMPVMAVTAVGKDMVRDARYF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476  188 SLATRIAAEMGAQIIKTYYVEKGFERIVAGCPVPIVIAGGKKLPEREALEMCWQAIDQGASGVDMGRNIFQSDHPVAMMK 267
Cdd:PRK08227 161 SLATRIAAEMGAQIIKTYYVEEGFERITAGCPVPIVIAGGKKLPERDALEMCYQAIDEGASGVDMGRNIFQSEHPVAMIK 240
                        250       260
                 ....*....|....*....|....
gi 16129476  268 AVQAVVHHNETADRAYELYLSEKQ 291
Cdd:PRK08227 241 AVHAVVHENETAKEAYELYLSEKN 264
 
Name Accession Description Interval E-value
PRK08227 PRK08227
3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase;
28-291 0e+00

3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase;


Pssm-ID: 181306 [Multi-domain]  Cd Length: 264  Bit Score: 558.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476   28 GCGALDWGMQSRLSRIFNPKTGKTVMLAFDHGYFQGPTTGLERIDINIAPLFEHADVLMCTRGILRSVVPPATNRPVVLR 107
Cdd:PRK08227   1 GAGALDWGMKNRLSRIFNPKTGRTVMLAFDHGYFQGPTTGLERIDINIAPLFPYADVLMCTRGILRSVVPPATNKPVVLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476  108 ASGANSILAELSNEAVALSMDDAVRLNSCAVAAQVYIGSEYEHQSIKNIIQLVDAGMKVGMPTMAVTGVGKDMVRDQRYF 187
Cdd:PRK08227  81 ASGGNSILKELSNEAVAVDMEDAVRLNACAVAAQVFIGSEYEHQSIKNIIQLVDAGLRYGMPVMAVTAVGKDMVRDARYF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476  188 SLATRIAAEMGAQIIKTYYVEKGFERIVAGCPVPIVIAGGKKLPEREALEMCWQAIDQGASGVDMGRNIFQSDHPVAMMK 267
Cdd:PRK08227 161 SLATRIAAEMGAQIIKTYYVEEGFERITAGCPVPIVIAGGKKLPERDALEMCYQAIDEGASGVDMGRNIFQSEHPVAMIK 240
                        250       260
                 ....*....|....*....|....
gi 16129476  268 AVQAVVHHNETADRAYELYLSEKQ 291
Cdd:PRK08227 241 AVHAVVHENETAKEAYELYLSEKN 264
FbaB COG1830
Fructose-bisphosphate aldolase class Ia, DhnA family [Carbohydrate transport and metabolism]; ...
33-282 9.69e-102

Fructose-bisphosphate aldolase class Ia, DhnA family [Carbohydrate transport and metabolism]; Fructose-bisphosphate aldolase class Ia, DhnA family is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 441435 [Multi-domain]  Cd Length: 259  Bit Score: 297.81  E-value: 9.69e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476  33 DWGMQSRLSRIFNPKTGKTVMLAFDHGYFQGPTTGLERIDINIAPLFE-HADVLMCTRGILRSVVPPATNR-PVVLRASG 110
Cdd:COG1830   1 DMGKKIRLSRIFNAGTGRLVIVAVDHGVEHGPNPGLEDPEEIVRLAAEgGADAVALTKGILERLARKYARDiPLILKLNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476 111 ANSILA-ELSNEAVALSMDDAVRLNSCAVAAQVYIGSEYEHQSIKNIIQLVDAGMKVGMPTMAVT-GVGKDMV--RDQRY 186
Cdd:COG1830  81 STSLGYpDPNDKVLVGSVEDAVRLGADAVGVTIYVGSEYEAEMLEELARVVEEAHRYGLPVLAWPyPRGPAVKdeTDPDL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476 187 FSLATRIAAEMGAQIIKTYYVE--KGFERIVAGCPVPIVIAGGKKLP-EREALEMCWQAIDQGASGVDMGRNIFQSDHPV 263
Cdd:COG1830 161 VAHAARIAAELGADIVKTKYPGdpESFREVVAACPVPVVIAGGPKTPdDEDFLEMVRDAIDAGAAGVAVGRNIFQRPNPE 240
                       250
                ....*....|....*....
gi 16129476 264 AMMKAVQAVVHHNETADRA 282
Cdd:COG1830 241 AMLRAISAIVHEGASVEEA 259
DhnA cd00958
Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs); Class ...
51-274 1.43e-87

Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs); Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs) found in bacteria and archaea. Catalysis of the enzymes proceeds via a Schiff-base mechanism like other class I aldolases, although this subfamily is clearly divergent based on sequence similarity to other class I and class II (metal dependent) aldolase subfamilies.


Pssm-ID: 188645 [Multi-domain]  Cd Length: 235  Bit Score: 260.99  E-value: 1.43e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476  51 TVMLAFDHGYFQ--GPTTGLERIDINIAPLFE-HADVLMCTRGILRSVVPP-ATNRPVVLRASGANSILA-ELSNEAVAL 125
Cdd:cd00958   1 LVILAVDHGIEHgfGPNPGLEDPEETVKLAAEgGADAVALTKGIARAYGREyAGDIPLIVKLNGSTSLSPkDDNDKVLVA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476 126 SMDDAVRLNSCAVAAQVYIGSEYEHQSIKNIIQLVDAGMKVGMPTMAVTGVGKDMV---RDQRYFSLATRIAAEMGAQII 202
Cdd:cd00958  81 SVEDAVRLGADAVGVTVYVGSEEEREMLEELARVAAEAHKYGLPLIAWMYPRGPAVkneKDPDLIAYAARIGAELGADIV 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129476 203 KTYYVE--KGFERIVAGCPVPIVIAGG-KKLPEREALEMCWQAIDQGASGVDMGRNIFQSDHPVAMMKAVQAVVH 274
Cdd:cd00958 161 KTKYTGdaESFKEVVEGCPVPVVIAGGpKKDSEEEFLKMVYDAMEAGAAGVAVGRNIFQRPDPVAMLRAISAVVH 235
DeoC pfam01791
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ...
51-259 4.04e-16

DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes the enzyme deoxyribose-phosphate aldolase EC:4.1.2.4, which is involved in nucleotide metabolism. The family also includes a group of related bacterial proteins of unknown function, see examples Swiss:Q57843 and Swiss:P76143. The family also includes tagatose 1,6-diphosphate aldolase (EC:4.1.2.40) is part of the tagatose-6-phosphate pathway of galactose-6-phosphate degradation.


Pssm-ID: 460332  Cd Length: 230  Bit Score: 75.50  E-value: 4.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476    51 TVMLAFDHGYFQGPTTGLERIDI--NIAPLFE-HADVLMCTRGILRSV-VPPATNRPVVLRASGANSiLAELSNEAV--A 124
Cdd:pfam01791   1 TSILAMDQGVANGPDFAFALEDPkvLVAEAATpGANAVLLDPGFIARAhRGYGKDIGLIVALNHGTD-LIPINGRDVdcV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476   125 LSMDDAVRLNSCAVAAQVYI---GSEYEHQSIKNIIQLVDAGMKVGMPTMA---VTGVGKDMVRDQRYFSLATRIAAEMG 198
Cdd:pfam01791  80 ASVEEAKAMGADAVKVVVYYrvdGSEEEQQMLDEIGRVKEDCHEWGMPLILegyLRGEAIKDEKDPDLVADAARLGAELG 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129476   199 AQIIKTYYVEKG----------FERIVAGCPVP-IVIAGGKKLPE-REALEMcwQAIDQGASGVDMGRNIFQS 259
Cdd:pfam01791 160 ADIVKVSYPKNMknageedadvFKRVIKAAPVPyVVLAGGVSEEDfLRTVRD--AMIEAGAMGVSSGRNIFQK 230
 
Name Accession Description Interval E-value
PRK08227 PRK08227
3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase;
28-291 0e+00

3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase;


Pssm-ID: 181306 [Multi-domain]  Cd Length: 264  Bit Score: 558.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476   28 GCGALDWGMQSRLSRIFNPKTGKTVMLAFDHGYFQGPTTGLERIDINIAPLFEHADVLMCTRGILRSVVPPATNRPVVLR 107
Cdd:PRK08227   1 GAGALDWGMKNRLSRIFNPKTGRTVMLAFDHGYFQGPTTGLERIDINIAPLFPYADVLMCTRGILRSVVPPATNKPVVLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476  108 ASGANSILAELSNEAVALSMDDAVRLNSCAVAAQVYIGSEYEHQSIKNIIQLVDAGMKVGMPTMAVTGVGKDMVRDQRYF 187
Cdd:PRK08227  81 ASGGNSILKELSNEAVAVDMEDAVRLNACAVAAQVFIGSEYEHQSIKNIIQLVDAGLRYGMPVMAVTAVGKDMVRDARYF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476  188 SLATRIAAEMGAQIIKTYYVEKGFERIVAGCPVPIVIAGGKKLPEREALEMCWQAIDQGASGVDMGRNIFQSDHPVAMMK 267
Cdd:PRK08227 161 SLATRIAAEMGAQIIKTYYVEEGFERITAGCPVPIVIAGGKKLPERDALEMCYQAIDEGASGVDMGRNIFQSEHPVAMIK 240
                        250       260
                 ....*....|....*....|....
gi 16129476  268 AVQAVVHHNETADRAYELYLSEKQ 291
Cdd:PRK08227 241 AVHAVVHENETAKEAYELYLSEKN 264
FbaB COG1830
Fructose-bisphosphate aldolase class Ia, DhnA family [Carbohydrate transport and metabolism]; ...
33-282 9.69e-102

Fructose-bisphosphate aldolase class Ia, DhnA family [Carbohydrate transport and metabolism]; Fructose-bisphosphate aldolase class Ia, DhnA family is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 441435 [Multi-domain]  Cd Length: 259  Bit Score: 297.81  E-value: 9.69e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476  33 DWGMQSRLSRIFNPKTGKTVMLAFDHGYFQGPTTGLERIDINIAPLFE-HADVLMCTRGILRSVVPPATNR-PVVLRASG 110
Cdd:COG1830   1 DMGKKIRLSRIFNAGTGRLVIVAVDHGVEHGPNPGLEDPEEIVRLAAEgGADAVALTKGILERLARKYARDiPLILKLNG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476 111 ANSILA-ELSNEAVALSMDDAVRLNSCAVAAQVYIGSEYEHQSIKNIIQLVDAGMKVGMPTMAVT-GVGKDMV--RDQRY 186
Cdd:COG1830  81 STSLGYpDPNDKVLVGSVEDAVRLGADAVGVTIYVGSEYEAEMLEELARVVEEAHRYGLPVLAWPyPRGPAVKdeTDPDL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476 187 FSLATRIAAEMGAQIIKTYYVE--KGFERIVAGCPVPIVIAGGKKLP-EREALEMCWQAIDQGASGVDMGRNIFQSDHPV 263
Cdd:COG1830 161 VAHAARIAAELGADIVKTKYPGdpESFREVVAACPVPVVIAGGPKTPdDEDFLEMVRDAIDAGAAGVAVGRNIFQRPNPE 240
                       250
                ....*....|....*....
gi 16129476 264 AMMKAVQAVVHHNETADRA 282
Cdd:COG1830 241 AMLRAISAIVHEGASVEEA 259
DhnA cd00958
Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs); Class ...
51-274 1.43e-87

Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs); Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs) found in bacteria and archaea. Catalysis of the enzymes proceeds via a Schiff-base mechanism like other class I aldolases, although this subfamily is clearly divergent based on sequence similarity to other class I and class II (metal dependent) aldolase subfamilies.


Pssm-ID: 188645 [Multi-domain]  Cd Length: 235  Bit Score: 260.99  E-value: 1.43e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476  51 TVMLAFDHGYFQ--GPTTGLERIDINIAPLFE-HADVLMCTRGILRSVVPP-ATNRPVVLRASGANSILA-ELSNEAVAL 125
Cdd:cd00958   1 LVILAVDHGIEHgfGPNPGLEDPEETVKLAAEgGADAVALTKGIARAYGREyAGDIPLIVKLNGSTSLSPkDDNDKVLVA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476 126 SMDDAVRLNSCAVAAQVYIGSEYEHQSIKNIIQLVDAGMKVGMPTMAVTGVGKDMV---RDQRYFSLATRIAAEMGAQII 202
Cdd:cd00958  81 SVEDAVRLGADAVGVTVYVGSEEEREMLEELARVAAEAHKYGLPLIAWMYPRGPAVkneKDPDLIAYAARIGAELGADIV 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16129476 203 KTYYVE--KGFERIVAGCPVPIVIAGG-KKLPEREALEMCWQAIDQGASGVDMGRNIFQSDHPVAMMKAVQAVVH 274
Cdd:cd00958 161 KTKYTGdaESFKEVVEGCPVPVVIAGGpKKDSEEEFLKMVYDAMEAGAAGVAVGRNIFQRPDPVAMLRAISAVVH 235
PRK07226 PRK07226
fructose-bisphosphate aldolase; Provisional
35-286 2.88e-56

fructose-bisphosphate aldolase; Provisional


Pssm-ID: 235973 [Multi-domain]  Cd Length: 267  Bit Score: 182.31  E-value: 2.88e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476   35 GMQSRLSRIFNPKTGKTVMLAFDHGYFQGPTTGLERIDINIAPLFEH-ADVLMCTRGILRSVvppatnRPVVLRASG--- 110
Cdd:PRK07226   5 GKRIRLERIFNRRTGRTVIVPMDHGVSHGPIDGLVDIRDTVNKVAEGgADAVLMHKGLARHG------HRGYGRDVGliv 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476  111 ---ANSILAELSNEAVAL-SMDDAVRLNSCAVAAQVYIGSEYEHQSIKNIIQLVDAGMKVGMPTMAVT---GVGKDMVRD 183
Cdd:PRK07226  79 hlsASTSLSPDPNDKVLVgTVEEAIKLGADAVSVHVNVGSETEAEMLEDLGEVAEECEEWGMPLLAMMyprGPGIKNEYD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476  184 QRYFSLATRIAAEMGAQIIKTYY---VEKgFERIVAGCPVPIVIAGGKKLP-EREALEMCWQAIDQGASGVDMGRNIFQS 259
Cdd:PRK07226 159 PEVVAHAARVAAELGADIVKTNYtgdPES-FREVVEGCPVPVVIAGGPKTDtDREFLEMVRDAMEAGAAGVAVGRNVFQH 237
                        250       260
                 ....*....|....*....|....*..
gi 16129476  260 DHPVAMMKAVQAVVHHNETADRAYELY 286
Cdd:PRK07226 238 EDPEAITRAISAVVHEGASVEEALKIL 264
Aldolase_Class_I cd00945
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ...
52-253 5.32e-22

Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which stabilizes a reaction intermediates via Schiff base formation, and have TIM beta/alpha barrel fold. The members of this family include 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-4-hydroxyglutarate (KHG) aldolases, transaldolase, dihydrodipicolinate synthase sub-family, Type I 3-dehydroquinate dehydratase, DeoC and DhnA proteins, and metal-independent fructose-1,6-bisphosphate aldolase. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin.


Pssm-ID: 188634 [Multi-domain]  Cd Length: 201  Bit Score: 90.85  E-value: 5.32e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476  52 VMLAFDHgyfqgPTTGLERIDINIAPLFE-HADVLMCTRGILRSVVPPATNRPVVLrASGANSILAELSNEAVALSMDDA 130
Cdd:cd00945   1 IDLTLLH-----PDATLEDIAKLCDEAIEyGFAAVCVNPGYVRLAADALAGSDVPV-IVVVGFPTGLTTTEVKVAEVEEA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476 131 VRLNSCAVAAQVYIGSEYEHQS---IKNIIQLVDAGmKVGMPTMAVTGVGKDmvRDQRYFSLATRIAAEMGAQIIKTYYV 207
Cdd:cd00945  75 IDLGADEIDVVINIGSLKEGDWeevLEEIAAVVEAA-DGGLPLKVILETRGL--KTADEIAKAARIAAEAGADFIKTSTG 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16129476 208 E-------KGFERIVAGC--PVPIVIAGGKKlpereALEMCWQAIDQGASGVDMG 253
Cdd:cd00945 152 FggggatvEDVKLMKEAVggRVGVKAAGGIK-----TLEDALAAIEAGADGIGTS 201
DeoC pfam01791
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ...
51-259 4.04e-16

DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes the enzyme deoxyribose-phosphate aldolase EC:4.1.2.4, which is involved in nucleotide metabolism. The family also includes a group of related bacterial proteins of unknown function, see examples Swiss:Q57843 and Swiss:P76143. The family also includes tagatose 1,6-diphosphate aldolase (EC:4.1.2.40) is part of the tagatose-6-phosphate pathway of galactose-6-phosphate degradation.


Pssm-ID: 460332  Cd Length: 230  Bit Score: 75.50  E-value: 4.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476    51 TVMLAFDHGYFQGPTTGLERIDI--NIAPLFE-HADVLMCTRGILRSV-VPPATNRPVVLRASGANSiLAELSNEAV--A 124
Cdd:pfam01791   1 TSILAMDQGVANGPDFAFALEDPkvLVAEAATpGANAVLLDPGFIARAhRGYGKDIGLIVALNHGTD-LIPINGRDVdcV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476   125 LSMDDAVRLNSCAVAAQVYI---GSEYEHQSIKNIIQLVDAGMKVGMPTMA---VTGVGKDMVRDQRYFSLATRIAAEMG 198
Cdd:pfam01791  80 ASVEEAKAMGADAVKVVVYYrvdGSEEEQQMLDEIGRVKEDCHEWGMPLILegyLRGEAIKDEKDPDLVADAARLGAELG 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129476   199 AQIIKTYYVEKG----------FERIVAGCPVP-IVIAGGKKLPE-REALEMcwQAIDQGASGVDMGRNIFQS 259
Cdd:pfam01791 160 ADIVKVSYPKNMknageedadvFKRVIKAAPVPyVVLAGGVSEEDfLRTVRD--AMIEAGAMGVSSGRNIFQK 230
PRK06852 PRK06852
aldolase; Validated
125-290 2.94e-11

aldolase; Validated


Pssm-ID: 180731  Cd Length: 304  Bit Score: 62.70  E-value: 2.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476  125 LSMDDAVR------LNSCAVAAQVYIGSEYEHQSIKNIIQLVDAGMKVGMptMAVTGV---GKdMVRDQRYFSL---ATR 192
Cdd:PRK06852 119 LDVEQVVEfkensgLNILGVGYTIYLGSEYESEMLSEAAQIIYEAHKHGL--IAVLWIyprGK-AVKDEKDPHLiagAAG 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476  193 IAAEMGAQIIKTYYVEKGF--------ERIVAGCPVPIVIAGGKKLPEREALEMCWQAID-QGASGVDMGRNIFQS--DH 261
Cdd:PRK06852 196 VAACLGADFVKVNYPKKEGanpaelfkEAVLAAGRTKVVCAGGSSTDPEEFLKQLYEQIHiSGASGNATGRNIHQKplDE 275
                        170       180
                 ....*....|....*....|....*....
gi 16129476  262 PVAMMKAVQAVVHHNETADRAYELYLSEK 290
Cdd:PRK06852 276 AVRMCNAIYAITVEDKSVEEALKIYNGEK 304
pdxS cd04727
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ...
219-277 1.00e-03

PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in deoxyxylulose 5-phosphate (DXP)-independent pathway for de novo biosynthesis of PLP, present in some eubacteria, in archaea, fungi, plants, plasmodia, and some metazoa. Together with PdxT, PdxS forms the PLP synthase, a heteromeric glutamine amidotransferase (GATase), whereby PdxT produces ammonia from glutamine and PdxS combines ammonia with five- and three-carbon phosphosugars to form PLP. PLP is the biologically active form of vitamin B6, an essential cofactor in many biochemical processes. PdxS subunits form two hexameric rings.


Pssm-ID: 240078  Cd Length: 283  Bit Score: 39.92  E-value: 1.00e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476 219 PVPIVIAGGKKLPEREALEMcwqaiDQGASGVDMGRNIFQSDHPVAMMKA-VQAVVHHNE 277
Cdd:cd04727 196 PVVNFAAGGVATPADAALMM-----QLGADGVFVGSGIFKSENPEKRARAiVEAVTHYDD 250
PRK09250 PRK09250
class I fructose-bisphosphate aldolase;
119-272 1.91e-03

class I fructose-bisphosphate aldolase;


Pssm-ID: 236431  Cd Length: 348  Bit Score: 39.12  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476  119 SNEAVALSMDDAVRLNSCAVAAQVYIGSEYEHQSIKNIIQLVDAGMKVGMPTmavtgV------GKDMVRDQRY------ 186
Cdd:PRK09250 144 YDQALTASVEDALRLGAVAVGATIYFGSEESRRQIEEISEAFEEAHELGLAT-----VlwsylrNSAFKKDGDYhtaadl 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129476  187 FSLATRIAAEMGAQIIK----TYYVE-------KGFERIVAGCPV--PI----------------VI-AGGKKLPEREAL 236
Cdd:PRK09250 219 TGQANHLAATIGADIIKqklpTNNGGykainfgKTDDRVYSKLTSdhPIdlvryqvancymgrrgLInSGGASKGEDDLL 298
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 16129476  237 EMCWQAI---DQGASGVDMGRNIFQSDHP--VAMMKAVQAV 272
Cdd:PRK09250 299 DAVRTAVinkRAGGMGLIIGRKAFQRPMAegVKLLNAIQDV 339
 
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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