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Conserved domains on  [gi|489936201|ref|WP_003839508|]
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MULTISPECIES: L-ribulose-5-phosphate 3-epimerase [Citrobacter]

Protein Classification

L-ribulose-5-phosphate 3-epimerase( domain architecture ID 11486478)

similar to L-ribulose-5-phosphate 3-epimerase, which catalyzes the isomerization of L-xylulose-5-phosphate to L-ribulose-5-phosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK13209 PRK13209
L-ribulose-5-phosphate 3-epimerase;
1-281 0e+00

L-ribulose-5-phosphate 3-epimerase;


:

Pssm-ID: 237307  Cd Length: 283  Bit Score: 552.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201   1 MLSKQVPLGIYEKALPGGECWLERLQLAKELGFDFVEMSVDETDARLARLDWNREQRLALVAAIADTGIRVPSMCLSAHR 80
Cdd:PRK13209   3 MLSKQIPLGIYEKALPAGECWLEKLAIAKTAGFDFVEMSVDESDERLARLDWSREQRLALVNALVETGFRVNSMCLSAHR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201  81 RFPLGSEDDAVREQGLEIMRKAIQFAQDIGIRVIQLAGYDVYYQQANNETRRRFRDGLKESVEMASRAQVTLAMEIMDYP 160
Cdd:PRK13209  83 RFPLGSEDDAVRAQALEIMRKAIQLAQDLGIRVIQLAGYDVYYEQANNETRRRFIDGLKESVELASRASVTLAFEIMDTP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201 161 LMNSISKALGYAHYLNNPWFQLYPDIGNLSAWDNDVQMELQAGMGHIVAVHVKDTKPGVFKNVPFGEGVVDFERCFATLK 240
Cdd:PRK13209 163 FMNSISKALGYAHYLNSPWFQLYPDIGNLSAWDNDVQMELQAGIGHIVAFHVKDTKPGVFKNVPFGEGVVDFERCFKTLK 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 489936201 241 QSGYCGPYLIEMWSETSDDPAREVAKARDWVKARMASAGLV 281
Cdd:PRK13209 243 QSGYCGPYLIEMWSETAEDPAAEVAKARDFVKARMAEAGMV 283
 
Name Accession Description Interval E-value
PRK13209 PRK13209
L-ribulose-5-phosphate 3-epimerase;
1-281 0e+00

L-ribulose-5-phosphate 3-epimerase;


Pssm-ID: 237307  Cd Length: 283  Bit Score: 552.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201   1 MLSKQVPLGIYEKALPGGECWLERLQLAKELGFDFVEMSVDETDARLARLDWNREQRLALVAAIADTGIRVPSMCLSAHR 80
Cdd:PRK13209   3 MLSKQIPLGIYEKALPAGECWLEKLAIAKTAGFDFVEMSVDESDERLARLDWSREQRLALVNALVETGFRVNSMCLSAHR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201  81 RFPLGSEDDAVREQGLEIMRKAIQFAQDIGIRVIQLAGYDVYYQQANNETRRRFRDGLKESVEMASRAQVTLAMEIMDYP 160
Cdd:PRK13209  83 RFPLGSEDDAVRAQALEIMRKAIQLAQDLGIRVIQLAGYDVYYEQANNETRRRFIDGLKESVELASRASVTLAFEIMDTP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201 161 LMNSISKALGYAHYLNNPWFQLYPDIGNLSAWDNDVQMELQAGMGHIVAVHVKDTKPGVFKNVPFGEGVVDFERCFATLK 240
Cdd:PRK13209 163 FMNSISKALGYAHYLNSPWFQLYPDIGNLSAWDNDVQMELQAGIGHIVAFHVKDTKPGVFKNVPFGEGVVDFERCFKTLK 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 489936201 241 QSGYCGPYLIEMWSETSDDPAREVAKARDWVKARMASAGLV 281
Cdd:PRK13209 243 QSGYCGPYLIEMWSETAEDPAAEVAKARDFVKARMAEAGMV 283
SgaU COG3623
L-ribulose-5-phosphate 3-epimerase UlaE [Carbohydrate transport and metabolism];
6-280 0e+00

L-ribulose-5-phosphate 3-epimerase UlaE [Carbohydrate transport and metabolism];


Pssm-ID: 442841  Cd Length: 277  Bit Score: 529.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201   6 VPLGIYEKALPGGECWLERLQLAKELGFDFVEMSVDETDARLARLDWNREQRLALVAAIADTGIRVPSMCLSAHRRFPLG 85
Cdd:COG3623    1 YRLGIYEKALPNTLSWPEKLALAKELGFDFVEISIDESDERLARLDWSDEERRELRDAMEETGIRIPSMCLSAHRRFPLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201  86 SEDDAVREQGLEIMRKAIQFAQDIGIRVIQLAGYDVYYQQANNETRRRFRDGLKESVEMASRAQVTLAMEIMDYPLMNSI 165
Cdd:COG3623   81 SADPAVRERALEIMEKAIDLASDLGIRTIQLAGYDVYYEPSDEETRQRFIEGLKKAVELAARAGVMLAIEIMDTPFMNSI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201 166 SKALGYAHYLNNPWFQLYPDIGNLSAWDNDVQMELQAGMGHIVAVHVKDTKPGVFKNVPFGEGVVDFERCFATLKQSGYC 245
Cdd:COG3623  161 SKAMELVKEIDSPWLQVYPDIGNLSAWGNDVADELELGIGHIVAIHLKDTLPGQFRDVPFGEGCVDFVAAFKTLKRLGYR 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 489936201 246 GPYLIEMWSETSDDPAREVAKARDWVKARMASAGL 280
Cdd:COG3623  241 GPFLIEMWNEDAEDWVAEIRQARDFLEQKLDEAGL 275
hxl6Piso_put TIGR00542
hexulose-6-phosphate isomerase, putative; This family shows similarity by PSI-BLAST to other ...
4-282 0e+00

hexulose-6-phosphate isomerase, putative; This family shows similarity by PSI-BLAST to other isomerases. Putative identification as hexulose-6-phosphate isomerase is reported in Swiss-Prot, attributing a discussion in Genome Sci. Technol. 1:53-75(1996). This family is conserved at better than 40 % identity among the four known examples from three species: Escherichia coli (SgbU and SgaU), Haemophilus influenzae, and Mycoplasma pneumoniae. The rarity of the family, high level of conservation, and proposed catabolic role suggests lateral transfer may be a part of the evolutionary history of this protein. [Energy metabolism, Sugars]


Pssm-ID: 129633  Cd Length: 279  Bit Score: 512.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201    4 KQVPLGIYEKALPGGECWLERLQLAKELGFDFVEMSVDETDARLARLDWNREQRLALVAAIADTGIRVPSMCLSAHRRFP 83
Cdd:TIGR00542   1 KKHPLGIYEKALPKGECWLERLQLAKTCGFDFVEMSVDETDDRLSRLDWSREQRLALVNAIIETGVRIPSMCLSAHRRFP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201   84 LGSEDDAVREQGLEIMRKAIQFAQDIGIRVIQLAGYDVYYQQANNETRRRFRDGLKESVEMASRAQVTLAMEIMDYPLMN 163
Cdd:TIGR00542  81 LGSKDKAVRQQGLEIMEKAIQLARDLGIRTIQLAGYDVYYEEHDEETRRRFREGLKEAVELAARAQVTLAVEIMDTPFMS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201  164 SISKALGYAHYLNNPWFQLYPDIGNLSAWDNDVQMELQAGMGHIVAVHVKDTKPGVFKNVPFGEGVVDFERCFATLKQSG 243
Cdd:TIGR00542 161 SISKWLKWDHYLNSPWFTLYPDIGNLSAWDNDVQMELQLGIDKIVAIHLKDTKPGQFKDVPFGEGCVDFERCFKTLKQLN 240
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 489936201  244 YCGPYLIEMWSETSDDPAREVAKARDWVKARMASAGLVE 282
Cdd:TIGR00542 241 YRGPFLIEMWSEKAEEPVAEIIQARDWIEARMAKAGMVC 279
AP_endonuc_2 pfam01261
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ...
25-274 7.02e-56

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: 180.26  E-value: 7.02e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201   25 LQLAKELGFDFVEMSVDetdaRLARLDWNREQRLALVAAIADTGIRVPSMCLSAHrrFPLGSEDDAVREQGLEIMRKAIQ 104
Cdd:pfam01261   1 LAAAAELGFDGVELFTR----RWFRPPLSDEEAEELKAALKEHGLEIVVHAPYLG--DNLASPDEEEREKAIDRLKRAIE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201  105 FAQDIGIRVIQL-AGYdvYYQQANNETRRRFRDGLKESVEMASRAQVTLAMEIM---DYPLMNSISKALGYAHYLNNPWF 180
Cdd:pfam01261  75 LAAALGAKLVVFhPGS--DLGDDPEEALARLAESLRELADLAEREGVRLALEPLagkGTNVGNTFEEALEIIDEVDSPNV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201  181 QLYPDIGNLSAWDNDVQMELQAGMGHIVAVHVKDTKP----GVFKNVPFGEGVVDFERCFATLKQSGYCGPYLIEMWSEt 256
Cdd:pfam01261 153 GVCLDTGHLFAAGDGDLFELRLGDRYIGHVHLKDSKNplgsGPDRHVPIGEGVIDFEALFRALKEIGYDGPLSLETFND- 231
                         250
                  ....*....|....*...
gi 489936201  257 sDDPAREVAKARDWVKAR 274
Cdd:pfam01261 232 -GPPEEGAREGLEWLREL 248
AP2Ec cd00019
AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester ...
8-274 1.35e-48

AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester bonds at apurinic or apyrimidinic sites; the alignment also contains hexulose-6-phosphate isomerases, enzymes that catalyze the epimerization of D-arabino-6-hexulose 3-phosphate to D-fructose 6-phosphate, via cleaving the phosphoesterbond with the sugar.


Pssm-ID: 237986  Cd Length: 279  Bit Score: 162.49  E-value: 1.35e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201   8 LGIYEKALPGGecWLERLQLAKELGFDFVEMSVDETDARLARLDwNREQRLALVAAIADTgirvPSMCLSAHRRFP--LG 85
Cdd:cd00019    1 IGAHVSAAGFG--LENALKRAKEIGFDTVAMFLGNPRSWLSRPL-KKERAEKFKAIAEEG----PSICLSVHAPYLinLA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201  86 SEDDAVREQGLEIMRKAIQFAQDIGIRviqLAGYDVYY--QQANNETRRRFRDGLKESVEMASRAQVTLAMEIMDYP--- 160
Cdd:cd00019   74 SPDKEKREKSIERLKDEIERCEELGIR---LLVFHPGSylGQSKEEGLKRVIEALNELIDKAETKGVVIALETMAGQgne 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201 161 LMNSISKaLGYA--HYLNNPWFQLYPDIGNLSAWDNDV-----------QMELQAGMGHIVAVHVKDTKP----GVFKNV 223
Cdd:cd00019  151 IGSSFEE-LKEIidLIKEKPRVGVCIDTCHIFAAGYDIstvegfekvleEFDKVIGLEYLKAIHLNDSKGelgsGKDRHE 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489936201 224 PFGEGVVDFERCFATLKQSGYC-GPYLIEMWSETSDDPAREvaKARDWVKAR 274
Cdd:cd00019  230 PIGEGDIDGEELFKELKKDPYQnIPLILETPSENRDAAKIK--KEIKLLRKL 279
coba_remo_CbiR NF041277
cobamide remodeling phosphodiesterase CbiR; Rare cobamides, analogs of B12 with critical ...
33-255 1.20e-03

cobamide remodeling phosphodiesterase CbiR; Rare cobamides, analogs of B12 with critical differences in the lower ligand, can become available for a salvage-like pathway to B12 biosynthesis through the action of enzymes that cleave the lower ligand. Members of this family are CbiR, a phosphodiesterase, which joins CbiZ, a previously discovered amidohydrolase, in the guild of cobamide remodeling enzymes.


Pssm-ID: 469174  Cd Length: 249  Bit Score: 39.54  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201  33 FDFVEMSVDETDARLARLDWNREQRlALVAAIADTGIRvpsmcLSAHrrFPL----GSEDDAVREQGLEIMRKAIQFAQD 108
Cdd:NF041277  25 VDEIELLLFESDECLENLPSPAEIR-ELAELAAELGLT-----YTVH--LPLdlplGSGDAAERRRSVEVLLRLIELTAP 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201 109 IGIR--VIQLAGydvyyqQANNETRRRFRDGLKESVEMASRAQV----TLAMEIMDyplmnsiskalGYAHYLNNPWFQL 182
Cdd:NF041277  97 LSPSayVLHPPG------DPSPDDLRRWQEQALESLEALLRGTGldpsKLAVENLE-----------GYPFELLWPVVEA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201 183 YP-----DIGNLSAWDNDVQMELQAGMGHIVAVHVKDTKPGvfKN-VPFGEGVVD-FERCFATLKQSGYCGPYLIEMWSE 255
Cdd:NF041277 160 LGlsvclDVGHLLLYGQDPLEFLDRWLPRVRVIHLHGVDPG--RDhLSLDHLPPEaLREVLDLLKDAGFDGVVTLEVFSE 237
 
Name Accession Description Interval E-value
PRK13209 PRK13209
L-ribulose-5-phosphate 3-epimerase;
1-281 0e+00

L-ribulose-5-phosphate 3-epimerase;


Pssm-ID: 237307  Cd Length: 283  Bit Score: 552.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201   1 MLSKQVPLGIYEKALPGGECWLERLQLAKELGFDFVEMSVDETDARLARLDWNREQRLALVAAIADTGIRVPSMCLSAHR 80
Cdd:PRK13209   3 MLSKQIPLGIYEKALPAGECWLEKLAIAKTAGFDFVEMSVDESDERLARLDWSREQRLALVNALVETGFRVNSMCLSAHR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201  81 RFPLGSEDDAVREQGLEIMRKAIQFAQDIGIRVIQLAGYDVYYQQANNETRRRFRDGLKESVEMASRAQVTLAMEIMDYP 160
Cdd:PRK13209  83 RFPLGSEDDAVRAQALEIMRKAIQLAQDLGIRVIQLAGYDVYYEQANNETRRRFIDGLKESVELASRASVTLAFEIMDTP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201 161 LMNSISKALGYAHYLNNPWFQLYPDIGNLSAWDNDVQMELQAGMGHIVAVHVKDTKPGVFKNVPFGEGVVDFERCFATLK 240
Cdd:PRK13209 163 FMNSISKALGYAHYLNSPWFQLYPDIGNLSAWDNDVQMELQAGIGHIVAFHVKDTKPGVFKNVPFGEGVVDFERCFKTLK 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 489936201 241 QSGYCGPYLIEMWSETSDDPAREVAKARDWVKARMASAGLV 281
Cdd:PRK13209 243 QSGYCGPYLIEMWSETAEDPAAEVAKARDFVKARMAEAGMV 283
SgaU COG3623
L-ribulose-5-phosphate 3-epimerase UlaE [Carbohydrate transport and metabolism];
6-280 0e+00

L-ribulose-5-phosphate 3-epimerase UlaE [Carbohydrate transport and metabolism];


Pssm-ID: 442841  Cd Length: 277  Bit Score: 529.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201   6 VPLGIYEKALPGGECWLERLQLAKELGFDFVEMSVDETDARLARLDWNREQRLALVAAIADTGIRVPSMCLSAHRRFPLG 85
Cdd:COG3623    1 YRLGIYEKALPNTLSWPEKLALAKELGFDFVEISIDESDERLARLDWSDEERRELRDAMEETGIRIPSMCLSAHRRFPLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201  86 SEDDAVREQGLEIMRKAIQFAQDIGIRVIQLAGYDVYYQQANNETRRRFRDGLKESVEMASRAQVTLAMEIMDYPLMNSI 165
Cdd:COG3623   81 SADPAVRERALEIMEKAIDLASDLGIRTIQLAGYDVYYEPSDEETRQRFIEGLKKAVELAARAGVMLAIEIMDTPFMNSI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201 166 SKALGYAHYLNNPWFQLYPDIGNLSAWDNDVQMELQAGMGHIVAVHVKDTKPGVFKNVPFGEGVVDFERCFATLKQSGYC 245
Cdd:COG3623  161 SKAMELVKEIDSPWLQVYPDIGNLSAWGNDVADELELGIGHIVAIHLKDTLPGQFRDVPFGEGCVDFVAAFKTLKRLGYR 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 489936201 246 GPYLIEMWSETSDDPAREVAKARDWVKARMASAGL 280
Cdd:COG3623  241 GPFLIEMWNEDAEDWVAEIRQARDFLEQKLDEAGL 275
hxl6Piso_put TIGR00542
hexulose-6-phosphate isomerase, putative; This family shows similarity by PSI-BLAST to other ...
4-282 0e+00

hexulose-6-phosphate isomerase, putative; This family shows similarity by PSI-BLAST to other isomerases. Putative identification as hexulose-6-phosphate isomerase is reported in Swiss-Prot, attributing a discussion in Genome Sci. Technol. 1:53-75(1996). This family is conserved at better than 40 % identity among the four known examples from three species: Escherichia coli (SgbU and SgaU), Haemophilus influenzae, and Mycoplasma pneumoniae. The rarity of the family, high level of conservation, and proposed catabolic role suggests lateral transfer may be a part of the evolutionary history of this protein. [Energy metabolism, Sugars]


Pssm-ID: 129633  Cd Length: 279  Bit Score: 512.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201    4 KQVPLGIYEKALPGGECWLERLQLAKELGFDFVEMSVDETDARLARLDWNREQRLALVAAIADTGIRVPSMCLSAHRRFP 83
Cdd:TIGR00542   1 KKHPLGIYEKALPKGECWLERLQLAKTCGFDFVEMSVDETDDRLSRLDWSREQRLALVNAIIETGVRIPSMCLSAHRRFP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201   84 LGSEDDAVREQGLEIMRKAIQFAQDIGIRVIQLAGYDVYYQQANNETRRRFRDGLKESVEMASRAQVTLAMEIMDYPLMN 163
Cdd:TIGR00542  81 LGSKDKAVRQQGLEIMEKAIQLARDLGIRTIQLAGYDVYYEEHDEETRRRFREGLKEAVELAARAQVTLAVEIMDTPFMS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201  164 SISKALGYAHYLNNPWFQLYPDIGNLSAWDNDVQMELQAGMGHIVAVHVKDTKPGVFKNVPFGEGVVDFERCFATLKQSG 243
Cdd:TIGR00542 161 SISKWLKWDHYLNSPWFTLYPDIGNLSAWDNDVQMELQLGIDKIVAIHLKDTKPGQFKDVPFGEGCVDFERCFKTLKQLN 240
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 489936201  244 YCGPYLIEMWSETSDDPAREVAKARDWVKARMASAGLVE 282
Cdd:TIGR00542 241 YRGPFLIEMWSEKAEEPVAEIIQARDWIEARMAKAGMVC 279
PRK13210 PRK13210
L-ribulose-5-phosphate 3-epimerase;
4-280 3.96e-164

L-ribulose-5-phosphate 3-epimerase;


Pssm-ID: 237308  Cd Length: 284  Bit Score: 456.68  E-value: 3.96e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201   4 KQVPLGIYEKALPGGECWLERLQLAKELGFDFVEMSVDETDARLARLDWNREQRLALVAAIADTGIRVPSMCLSAHRRFP 83
Cdd:PRK13210   1 RKHPLGIYEKALPKHLSWEERLVFAKELGFDFVEMSVDESDERLARLDWSKEERLSLVKAIYETGVRIPSMCLSGHRRFP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201  84 LGSEDDAVREQGLEIMRKAIQFAQDIGIRVIQLAGYDVYYQQANNETRRRFRDGLKESVEMASRAQVTLAMEIMDYPLMN 163
Cdd:PRK13210  81 FGSRDPATRERALEIMKKAIRLAQDLGIRTIQLAGYDVYYEEKSEETRQRFIEGLAWAVEQAAAAQVMLAVEIMDTPFMN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201 164 SISKALGYAHYLNNPWFQLYPDIGNLSAWDNDVQMELQAGMGHIVAVHVKDT------KPGVFKNVPFGEGVVDFERCFA 237
Cdd:PRK13210 161 SISKWKKWDKEIDSPWLTVYPDVGNLSAWGNDVWSELKLGIDHIAAIHLKDTyavtetSKGQFRDVPFGEGCVDFVGIFK 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 489936201 238 TLKQSGYCGPYLIEMWSETSDDPAREVAKARDWVKARMASAGL 280
Cdd:PRK13210 241 TLKELNYRGPFLIEMWTEKAEEPRAEIKQARRFLEPLMEEAGL 283
AP_endonuc_2 pfam01261
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ...
25-274 7.02e-56

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: 180.26  E-value: 7.02e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201   25 LQLAKELGFDFVEMSVDetdaRLARLDWNREQRLALVAAIADTGIRVPSMCLSAHrrFPLGSEDDAVREQGLEIMRKAIQ 104
Cdd:pfam01261   1 LAAAAELGFDGVELFTR----RWFRPPLSDEEAEELKAALKEHGLEIVVHAPYLG--DNLASPDEEEREKAIDRLKRAIE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201  105 FAQDIGIRVIQL-AGYdvYYQQANNETRRRFRDGLKESVEMASRAQVTLAMEIM---DYPLMNSISKALGYAHYLNNPWF 180
Cdd:pfam01261  75 LAAALGAKLVVFhPGS--DLGDDPEEALARLAESLRELADLAEREGVRLALEPLagkGTNVGNTFEEALEIIDEVDSPNV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201  181 QLYPDIGNLSAWDNDVQMELQAGMGHIVAVHVKDTKP----GVFKNVPFGEGVVDFERCFATLKQSGYCGPYLIEMWSEt 256
Cdd:pfam01261 153 GVCLDTGHLFAAGDGDLFELRLGDRYIGHVHLKDSKNplgsGPDRHVPIGEGVIDFEALFRALKEIGYDGPLSLETFND- 231
                         250
                  ....*....|....*...
gi 489936201  257 sDDPAREVAKARDWVKAR 274
Cdd:pfam01261 232 -GPPEEGAREGLEWLREL 248
AP2Ec cd00019
AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester ...
8-274 1.35e-48

AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester bonds at apurinic or apyrimidinic sites; the alignment also contains hexulose-6-phosphate isomerases, enzymes that catalyze the epimerization of D-arabino-6-hexulose 3-phosphate to D-fructose 6-phosphate, via cleaving the phosphoesterbond with the sugar.


Pssm-ID: 237986  Cd Length: 279  Bit Score: 162.49  E-value: 1.35e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201   8 LGIYEKALPGGecWLERLQLAKELGFDFVEMSVDETDARLARLDwNREQRLALVAAIADTgirvPSMCLSAHRRFP--LG 85
Cdd:cd00019    1 IGAHVSAAGFG--LENALKRAKEIGFDTVAMFLGNPRSWLSRPL-KKERAEKFKAIAEEG----PSICLSVHAPYLinLA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201  86 SEDDAVREQGLEIMRKAIQFAQDIGIRviqLAGYDVYY--QQANNETRRRFRDGLKESVEMASRAQVTLAMEIMDYP--- 160
Cdd:cd00019   74 SPDKEKREKSIERLKDEIERCEELGIR---LLVFHPGSylGQSKEEGLKRVIEALNELIDKAETKGVVIALETMAGQgne 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201 161 LMNSISKaLGYA--HYLNNPWFQLYPDIGNLSAWDNDV-----------QMELQAGMGHIVAVHVKDTKP----GVFKNV 223
Cdd:cd00019  151 IGSSFEE-LKEIidLIKEKPRVGVCIDTCHIFAAGYDIstvegfekvleEFDKVIGLEYLKAIHLNDSKGelgsGKDRHE 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489936201 224 PFGEGVVDFERCFATLKQSGYC-GPYLIEMWSETSDDPAREvaKARDWVKAR 274
Cdd:cd00019  230 PIGEGDIDGEELFKELKKDPYQnIPLILETPSENRDAAKIK--KEIKLLRKL 279
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
6-273 1.42e-40

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


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 140.92  E-value: 1.42e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201   6 VPLGIYEKALPGGEcWLERLQLAKELGFDFVEMSVDETDARLARldwnreqrlALVAAIADTGIRVPSMclsaHRRFPLG 85
Cdd:COG1082    1 MKLGLSTYSLPDLD-LEEALRAAAELGYDGVELAGGDLDEADLA---------ELRAALADHGLEISSL----HAPGLNL 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201  86 SEDDAVREQGLEIMRKAIQFAQDIGIRVIQL-AGYDVYYQQANNETRRRFRDGLKESVEMASRAQVTLAMEIMDYPLMNS 164
Cdd:COG1082   67 APDPEVREAALERLKRAIDLAAELGAKVVVVhPGSPPPPDLPPEEAWDRLAERLRELAELAEEAGVTLALENHEGTFVNT 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201 165 ISKALGYAHYLNNPWFQLYPDIGNLSAWDNDVQMELQAGMGHIVAVHVKDTKPGVFknVPFGEGVVDFERCFATLKQSGY 244
Cdd:COG1082  147 PEEALRLLEAVDSPNVGLLLDTGHALLAGEDPVELLRKLGDRIKHVHLKDADGDQH--LPPGEGDIDFAAILRALKEAGY 224
                        250       260
                 ....*....|....*....|....*....
gi 489936201 245 CGPYLIEmWSETSDDPAREVAKARDWVKA 273
Cdd:COG1082  225 DGWLSLE-VESDPDDPEEAARESLEYLRK 252
Hyi COG3622
Hydroxypyruvate/dehydroerythronate isomerase, Hyi/OtnI family [Carbohydrate transport and ...
8-246 9.42e-05

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


Pssm-ID: 442840  Cd Length: 260  Bit Score: 42.79  E-value: 9.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201   8 LGIYEKALPggecWLERLQLAKELGFDFVEM------SVDETDARLARLDwnreqrLALV-----AAIADTGIRVpsmcL 76
Cdd:COG3622    8 LSMLFTELP----FLDRFAAAAAAGFDAVEFlfpydrPAEEIAAALKKHG------LTLVlfnlpAGDWAAGERG----L 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201  77 SAHRrfplGSEDDAVREqgleiMRKAIQFAQDIGIR-VIQLAGY-----DVYYQQANnetrrrFRDGLKESVEMASRAQV 150
Cdd:COG3622   74 AALP----GREAEFRAG-----VDRALEYAAALGCKnLHVMAGNrprglDDEAALAT------FVENLRYAADLAAPHGI 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201 151 TLAME------IMDYPLmNSISKALGYAHYLNNPWFQLYPDI-------GNLSAWdndvqmeLQAGMGHIVAVHVKDTkP 217
Cdd:COG3622  139 TLLIEplnsrdHPGYFL-DTTAQAVAIIEAVGSPNLKLLYDIyhmqimeGDLIRT-------IRRHLPRIGHVQIADV-P 209
                        250       260
                 ....*....|....*....|....*....
gi 489936201 218 GvfKNVPfGEGVVDFERCFATLKQSGYCG 246
Cdd:COG3622  210 G--RHEP-GTGELNYPAIFKALDALGYDG 235
coba_remo_CbiR NF041277
cobamide remodeling phosphodiesterase CbiR; Rare cobamides, analogs of B12 with critical ...
33-255 1.20e-03

cobamide remodeling phosphodiesterase CbiR; Rare cobamides, analogs of B12 with critical differences in the lower ligand, can become available for a salvage-like pathway to B12 biosynthesis through the action of enzymes that cleave the lower ligand. Members of this family are CbiR, a phosphodiesterase, which joins CbiZ, a previously discovered amidohydrolase, in the guild of cobamide remodeling enzymes.


Pssm-ID: 469174  Cd Length: 249  Bit Score: 39.54  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201  33 FDFVEMSVDETDARLARLDWNREQRlALVAAIADTGIRvpsmcLSAHrrFPL----GSEDDAVREQGLEIMRKAIQFAQD 108
Cdd:NF041277  25 VDEIELLLFESDECLENLPSPAEIR-ELAELAAELGLT-----YTVH--LPLdlplGSGDAAERRRSVEVLLRLIELTAP 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201 109 IGIR--VIQLAGydvyyqQANNETRRRFRDGLKESVEMASRAQV----TLAMEIMDyplmnsiskalGYAHYLNNPWFQL 182
Cdd:NF041277  97 LSPSayVLHPPG------DPSPDDLRRWQEQALESLEALLRGTGldpsKLAVENLE-----------GYPFELLWPVVEA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489936201 183 YP-----DIGNLSAWDNDVQMELQAGMGHIVAVHVKDTKPGvfKN-VPFGEGVVD-FERCFATLKQSGYCGPYLIEMWSE 255
Cdd:NF041277 160 LGlsvclDVGHLLLYGQDPLEFLDRWLPRVRVIHLHGVDPG--RDhLSLDHLPPEaLREVLDLLKDAGFDGVVTLEVFSE 237
 
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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