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Conserved domains on  [gi|16132143|ref|NP_418742|]
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D-mannonate dehydratase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

mannonate dehydratase( domain architecture ID 11489524)

mannonate dehydratase catalyzes the dehydration of D-mannonate to 2-dehydro-3-deoxy-D-gluconate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UxuA COG1312
D-mannonate dehydratase [Carbohydrate transport and metabolism];
1-392 0e+00

D-mannonate dehydratase [Carbohydrate transport and metabolism];


:

Pssm-ID: 440923  Cd Length: 388  Bit Score: 775.10  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143   1 MEQTWRWYGPNDPVSLADVRQAGATGVVTALHHIPNGEVWSVEEILKRKAIIEDAGLVWSVVESVPIHEDIKTHTGNYEQ 80
Cdd:COG1312   1 MKMTWRWFGPNDPVTLEDIRQIGATGIVTALHHIPVGEVWPVEEIAERKAEIEAAGLEWSVVESVPVHEDIKLGLGDRDR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143  81 WIANYQQTLRNLAQCGIRTVCYNFMPVLDWTRTDLEYVLPDGSKALRFDQIEFAAFEMHILKRPGAEADYTEEEIAQAAE 160
Cdd:COG1312  81 YIENYKQSLRNLAAAGIKTVCYNFMPVLDWTRTDLAYPLPDGSTALRFDQADFAAFDLFILKRPGAEADYSEEVVADAKE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143 161 RFATMSDEDKARLTRNIIAGLPGAEEGYTLDQFRKHLELYKDIDKAKLRENFAVFLKAIIPVAEEVGVRMAVHPDDPPRP 240
Cdd:COG1312 161 RFEAMSEAEKARLTRNIIAGLPGWEEEYTLEEFRELLAAYKGIDEEKLRENLKYFLEEVIPVAEELGIKMAIHPDDPPWP 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143 241 ILGLPRIVSTIEDMQWMVDTVNSMANGFTMCTGSYGVRADNDLVDMIKQFGPRIYFTHLRSTMREDNpKTFHEAAHLNGD 320
Cdd:COG1312 241 IFGLPRIVSTEEDLRRLLDAVDSPANGLTLCTGSLGARPDNDLPAMARRFGDRIHFAHLRNVKREGD-GSFYEAAHLDGD 319
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132143 321 VDMYEVVKAIVEEEHRRKAEGKedlIPMRPDHGHQMLDDLKKKTNPGYSAIGRLKGLAEVRGVELAIQRAFF 392
Cdd:COG1312 320 VDMVAVVKALLDEEARRRADFD---IPMRPDHGRMILDDLGRKGRPGYGLIGRALGLAELRGLWEAIEKMLK 388
 
Name Accession Description Interval E-value
UxuA COG1312
D-mannonate dehydratase [Carbohydrate transport and metabolism];
1-392 0e+00

D-mannonate dehydratase [Carbohydrate transport and metabolism];


Pssm-ID: 440923  Cd Length: 388  Bit Score: 775.10  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143   1 MEQTWRWYGPNDPVSLADVRQAGATGVVTALHHIPNGEVWSVEEILKRKAIIEDAGLVWSVVESVPIHEDIKTHTGNYEQ 80
Cdd:COG1312   1 MKMTWRWFGPNDPVTLEDIRQIGATGIVTALHHIPVGEVWPVEEIAERKAEIEAAGLEWSVVESVPVHEDIKLGLGDRDR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143  81 WIANYQQTLRNLAQCGIRTVCYNFMPVLDWTRTDLEYVLPDGSKALRFDQIEFAAFEMHILKRPGAEADYTEEEIAQAAE 160
Cdd:COG1312  81 YIENYKQSLRNLAAAGIKTVCYNFMPVLDWTRTDLAYPLPDGSTALRFDQADFAAFDLFILKRPGAEADYSEEVVADAKE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143 161 RFATMSDEDKARLTRNIIAGLPGAEEGYTLDQFRKHLELYKDIDKAKLRENFAVFLKAIIPVAEEVGVRMAVHPDDPPRP 240
Cdd:COG1312 161 RFEAMSEAEKARLTRNIIAGLPGWEEEYTLEEFRELLAAYKGIDEEKLRENLKYFLEEVIPVAEELGIKMAIHPDDPPWP 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143 241 ILGLPRIVSTIEDMQWMVDTVNSMANGFTMCTGSYGVRADNDLVDMIKQFGPRIYFTHLRSTMREDNpKTFHEAAHLNGD 320
Cdd:COG1312 241 IFGLPRIVSTEEDLRRLLDAVDSPANGLTLCTGSLGARPDNDLPAMARRFGDRIHFAHLRNVKREGD-GSFYEAAHLDGD 319
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132143 321 VDMYEVVKAIVEEEHRRKAEGKedlIPMRPDHGHQMLDDLKKKTNPGYSAIGRLKGLAEVRGVELAIQRAFF 392
Cdd:COG1312 320 VDMVAVVKALLDEEARRRADFD---IPMRPDHGRMILDDLGRKGRPGYGLIGRALGLAELRGLWEAIEKMLK 388
uxuA TIGR00695
mannonate dehydratase; This Fe2+-requiring enzyme plays a role in D-glucuronate catabolism in ...
1-394 0e+00

mannonate dehydratase; This Fe2+-requiring enzyme plays a role in D-glucuronate catabolism in Escherichia coli. Mannonate dehydratase converts D-mannonate to 2-dehydro-3-deoxy-D-gluconate. An apparent equivalog is found in a glucuronate utilization operon in Bacillus stearothermophilus T-6. [Energy metabolism, Sugars]


Pssm-ID: 129778  Cd Length: 394  Bit Score: 769.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143     1 MEQTWRWYGPNDPVSLADVRQAGATGVVTALHHIPNGEVWSVEEILKRKAIIEDAGLVWSVVESVPIHEDIKTHTGNYEQ 80
Cdd:TIGR00695   1 MEQTWRWYGPNDPVSLADVRQAGATGIVTALHHIPNGEVWSVEEILKRKAIIEDAGLVWSVVESVPVHEDIKTHTGNYEQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143    81 WIANYQQTLRNLAQCGIRTVCYNFMPVLDWTRTDLEYVLPDGSKALRFDQIEFAAFEMHILKRPGAEADYTEEEIAQAAE 160
Cdd:TIGR00695  81 WIANYKQTLRNLAQCGIRTVCYNFMPVLDWTRTDLEYVLPDGSKALRFDQIEFAAFEMHILKRPGAEADYTEEEIAQAAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143   161 RFATMSDEDKARLTRNIIAGLPGAEEGYTLDQFRKHLELYKDIDKAKLRENFAVFLKAIIPVAEEVGVRMAVHPDDPPRP 240
Cdd:TIGR00695 161 RFATMSDEDKARLTRNIIAGLPGAEEGYTLDQFRKHLELYKDIDKEKLRENLAVFLKEIIPVAEEVGVRMAIHPDDPPRP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143   241 ILGLPRIVSTIEDMQWMVDTVNSMANGFTMCTGSYGVRADNDLVDMIKQFGPRIYFTHLRSTMREDNPKTFHEAAHLNGD 320
Cdd:TIGR00695 241 ILGLPRIVSTIEDMQWMVDTVNSPANGFTMCTGSYGVRADNDLVDMIKQFAPRIYFTHLRSTMREDNPKTFHEAAHLNGD 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16132143   321 VDMYEVVKAIVEEEHRRKAEGKEDLIPMRPDHGHQMLDDLKKKTNPGYSAIGRLKGLAEVRGVELAIQRAFFSR 394
Cdd:TIGR00695 321 VDMYEVVKAIVEEEHRRKAEGKEDLIPMRPDHGHQMLDDLKKKTNPGYSAIGRLKGLAEVRGLELAIQRAFFSR 394
PRK03906 PRK03906
mannonate dehydratase; Provisional
1-392 0e+00

mannonate dehydratase; Provisional


Pssm-ID: 235172  Cd Length: 385  Bit Score: 758.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143    1 MEQTWRWYGPNDPVSLADVRQAGATGVVTALHHIPNGEVWSVEEILKRKAIIEDAGLVWSVVESVPIHEDIKTHTGNYEQ 80
Cdd:PRK03906   1 MEMTWRWFGPNDPVTLEDIRQPGATGIVTALHDIPVGEVWPVEEILARKAEIEAAGLEWSVVESVPVHEDIKTGTPNRDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143   81 WIANYQQTLRNLAQCGIRTVCYNFMPVLDWTRTDLEYVLPDGSKALRFDQIEFAAFEMHILKRPGAEADYTEEEIAQAAE 160
Cdd:PRK03906  81 YIENYKQTLRNLAAAGIKVVCYNFMPVFDWTRTDLAYELPDGSTALRFDQIDFAAFDPHILKRPGAEADYGEEEIAQAAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143  161 RFATMSDEDKARLTRNIIAGLPGAEEGYTLDQFRKHLELYKDIDKAKLRENFAVFLKAIIPVAEEVGVRMAVHPDDPPRP 240
Cdd:PRK03906 161 RFAAMSEEDKARLTRNIIAGLPGWEEPYTLEQFRALLELYKDIDEEKLRENLAYFLKAIIPVAEEVGVKMAIHPDDPPRP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143  241 ILGLPRIVSTIEDMQWMVDTVNSMANGFTMCTGSYGVRADNDLVDMIKQFGPRIYFTHLRSTMREDnPKTFHEAAHLNGD 320
Cdd:PRK03906 241 IFGLPRIVSTEEDLQRLLDAVDSPANGLTLCTGSLGARPDNDLPAMIREFGDRIHFAHLRNVKREG-PGSFHEAAHLSGD 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132143  321 VDMYEVVKAIVEEEHRrkaegkedlIPMRPDHGHQMLDDLKKKTNPGYSAIGRLKGLAEVRGVELAIQRAFF 392
Cdd:PRK03906 320 VDMYAVVKALLDEEFR---------IPMRPDHGRMIWDDLGKKTNPGYGLYGRALGLAELRGLWEALEKAAK 382
UxuA pfam03786
D-mannonate dehydratase (UxuA); UxuA (this family) and UxuB are required for hexuronate ...
1-389 0e+00

D-mannonate dehydratase (UxuA); UxuA (this family) and UxuB are required for hexuronate degradation.


Pssm-ID: 397726  Cd Length: 351  Bit Score: 572.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143     1 MEQTWRWYGP-NDPVSLADVRQA-GATGVVTALHHIPNGEVWSVEEILKRKAIIEDAGLVWSVVESVPIHEDIKTHTGNY 78
Cdd:pfam03786   1 MELTFRWYGPgNDPVSLEDIRQIpGVKGVVGALHDIPVGEVWPKEEIMALKEEIEDAGLHLSVIESVPVHEDIKLGTPTR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143    79 EQWIANYQQTLRNLAQCGIRTVCYNFMPVLDWTRTDLEYVLPDGSKALRFDQIEFAAFEMHILKRPGAEADYTeeeiaqa 158
Cdd:pfam03786  81 DRYIENYKQTIRNLAQCGVKVVCYNFMPVFDWTRTDLHYPLEDGSKALRFDKIEIAAFEPQILRTPAAEGDFT------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143   159 aerfatmsdedkarltrniiagLPGAEEGYtLDQFRKHLELYKDIDKAKLRENFAVFLKAIIPVAEEVGVRMAVHPDDPP 238
Cdd:pfam03786 154 ----------------------LPGWEPEY-LDELKGLFEAYKDIDEEKLWDNLAYFLQEIIPVAEEVGVKMAIHPDDPP 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143   239 RPILGLPRIVSTIEDMQWMVDTVNSMANGFTMCTGSYGVRADNDLVDMIKQFGPRIYFTHLRSTMREDNPKTFHEAAHLN 318
Cdd:pfam03786 211 WPIFGLPRIVTNIEDYQRLLDLVDSPYNGITLCTGSLGANPANDLPEMIRQFADRIYFAHLRNIKREDGPKDFVETAHLS 290
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16132143   319 --GDVDMYEVVKAIVEEEHRRkaegkedliPMRPDHGHQMLDDlkkKTNPGYSAIGRLKGLAEVRGVELAIQR 389
Cdd:pfam03786 291 kdGSVDMYAVMKAYHEVGYRG---------YMRPDHGRQIWGE---LTRPGYGLYDRALGIAYLNGLWDALSK 351
 
Name Accession Description Interval E-value
UxuA COG1312
D-mannonate dehydratase [Carbohydrate transport and metabolism];
1-392 0e+00

D-mannonate dehydratase [Carbohydrate transport and metabolism];


Pssm-ID: 440923  Cd Length: 388  Bit Score: 775.10  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143   1 MEQTWRWYGPNDPVSLADVRQAGATGVVTALHHIPNGEVWSVEEILKRKAIIEDAGLVWSVVESVPIHEDIKTHTGNYEQ 80
Cdd:COG1312   1 MKMTWRWFGPNDPVTLEDIRQIGATGIVTALHHIPVGEVWPVEEIAERKAEIEAAGLEWSVVESVPVHEDIKLGLGDRDR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143  81 WIANYQQTLRNLAQCGIRTVCYNFMPVLDWTRTDLEYVLPDGSKALRFDQIEFAAFEMHILKRPGAEADYTEEEIAQAAE 160
Cdd:COG1312  81 YIENYKQSLRNLAAAGIKTVCYNFMPVLDWTRTDLAYPLPDGSTALRFDQADFAAFDLFILKRPGAEADYSEEVVADAKE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143 161 RFATMSDEDKARLTRNIIAGLPGAEEGYTLDQFRKHLELYKDIDKAKLRENFAVFLKAIIPVAEEVGVRMAVHPDDPPRP 240
Cdd:COG1312 161 RFEAMSEAEKARLTRNIIAGLPGWEEEYTLEEFRELLAAYKGIDEEKLRENLKYFLEEVIPVAEELGIKMAIHPDDPPWP 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143 241 ILGLPRIVSTIEDMQWMVDTVNSMANGFTMCTGSYGVRADNDLVDMIKQFGPRIYFTHLRSTMREDNpKTFHEAAHLNGD 320
Cdd:COG1312 241 IFGLPRIVSTEEDLRRLLDAVDSPANGLTLCTGSLGARPDNDLPAMARRFGDRIHFAHLRNVKREGD-GSFYEAAHLDGD 319
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132143 321 VDMYEVVKAIVEEEHRRKAEGKedlIPMRPDHGHQMLDDLKKKTNPGYSAIGRLKGLAEVRGVELAIQRAFF 392
Cdd:COG1312 320 VDMVAVVKALLDEEARRRADFD---IPMRPDHGRMILDDLGRKGRPGYGLIGRALGLAELRGLWEAIEKMLK 388
uxuA TIGR00695
mannonate dehydratase; This Fe2+-requiring enzyme plays a role in D-glucuronate catabolism in ...
1-394 0e+00

mannonate dehydratase; This Fe2+-requiring enzyme plays a role in D-glucuronate catabolism in Escherichia coli. Mannonate dehydratase converts D-mannonate to 2-dehydro-3-deoxy-D-gluconate. An apparent equivalog is found in a glucuronate utilization operon in Bacillus stearothermophilus T-6. [Energy metabolism, Sugars]


Pssm-ID: 129778  Cd Length: 394  Bit Score: 769.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143     1 MEQTWRWYGPNDPVSLADVRQAGATGVVTALHHIPNGEVWSVEEILKRKAIIEDAGLVWSVVESVPIHEDIKTHTGNYEQ 80
Cdd:TIGR00695   1 MEQTWRWYGPNDPVSLADVRQAGATGIVTALHHIPNGEVWSVEEILKRKAIIEDAGLVWSVVESVPVHEDIKTHTGNYEQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143    81 WIANYQQTLRNLAQCGIRTVCYNFMPVLDWTRTDLEYVLPDGSKALRFDQIEFAAFEMHILKRPGAEADYTEEEIAQAAE 160
Cdd:TIGR00695  81 WIANYKQTLRNLAQCGIRTVCYNFMPVLDWTRTDLEYVLPDGSKALRFDQIEFAAFEMHILKRPGAEADYTEEEIAQAAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143   161 RFATMSDEDKARLTRNIIAGLPGAEEGYTLDQFRKHLELYKDIDKAKLRENFAVFLKAIIPVAEEVGVRMAVHPDDPPRP 240
Cdd:TIGR00695 161 RFATMSDEDKARLTRNIIAGLPGAEEGYTLDQFRKHLELYKDIDKEKLRENLAVFLKEIIPVAEEVGVRMAIHPDDPPRP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143   241 ILGLPRIVSTIEDMQWMVDTVNSMANGFTMCTGSYGVRADNDLVDMIKQFGPRIYFTHLRSTMREDNPKTFHEAAHLNGD 320
Cdd:TIGR00695 241 ILGLPRIVSTIEDMQWMVDTVNSPANGFTMCTGSYGVRADNDLVDMIKQFAPRIYFTHLRSTMREDNPKTFHEAAHLNGD 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16132143   321 VDMYEVVKAIVEEEHRRKAEGKEDLIPMRPDHGHQMLDDLKKKTNPGYSAIGRLKGLAEVRGVELAIQRAFFSR 394
Cdd:TIGR00695 321 VDMYEVVKAIVEEEHRRKAEGKEDLIPMRPDHGHQMLDDLKKKTNPGYSAIGRLKGLAEVRGLELAIQRAFFSR 394
PRK03906 PRK03906
mannonate dehydratase; Provisional
1-392 0e+00

mannonate dehydratase; Provisional


Pssm-ID: 235172  Cd Length: 385  Bit Score: 758.59  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143    1 MEQTWRWYGPNDPVSLADVRQAGATGVVTALHHIPNGEVWSVEEILKRKAIIEDAGLVWSVVESVPIHEDIKTHTGNYEQ 80
Cdd:PRK03906   1 MEMTWRWFGPNDPVTLEDIRQPGATGIVTALHDIPVGEVWPVEEILARKAEIEAAGLEWSVVESVPVHEDIKTGTPNRDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143   81 WIANYQQTLRNLAQCGIRTVCYNFMPVLDWTRTDLEYVLPDGSKALRFDQIEFAAFEMHILKRPGAEADYTEEEIAQAAE 160
Cdd:PRK03906  81 YIENYKQTLRNLAAAGIKVVCYNFMPVFDWTRTDLAYELPDGSTALRFDQIDFAAFDPHILKRPGAEADYGEEEIAQAAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143  161 RFATMSDEDKARLTRNIIAGLPGAEEGYTLDQFRKHLELYKDIDKAKLRENFAVFLKAIIPVAEEVGVRMAVHPDDPPRP 240
Cdd:PRK03906 161 RFAAMSEEDKARLTRNIIAGLPGWEEPYTLEQFRALLELYKDIDEEKLRENLAYFLKAIIPVAEEVGVKMAIHPDDPPRP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143  241 ILGLPRIVSTIEDMQWMVDTVNSMANGFTMCTGSYGVRADNDLVDMIKQFGPRIYFTHLRSTMREDnPKTFHEAAHLNGD 320
Cdd:PRK03906 241 IFGLPRIVSTEEDLQRLLDAVDSPANGLTLCTGSLGARPDNDLPAMIREFGDRIHFAHLRNVKREG-PGSFHEAAHLSGD 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132143  321 VDMYEVVKAIVEEEHRrkaegkedlIPMRPDHGHQMLDDLKKKTNPGYSAIGRLKGLAEVRGVELAIQRAFF 392
Cdd:PRK03906 320 VDMYAVVKALLDEEFR---------IPMRPDHGRMIWDDLGKKTNPGYGLYGRALGLAELRGLWEALEKAAK 382
UxuA pfam03786
D-mannonate dehydratase (UxuA); UxuA (this family) and UxuB are required for hexuronate ...
1-389 0e+00

D-mannonate dehydratase (UxuA); UxuA (this family) and UxuB are required for hexuronate degradation.


Pssm-ID: 397726  Cd Length: 351  Bit Score: 572.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143     1 MEQTWRWYGP-NDPVSLADVRQA-GATGVVTALHHIPNGEVWSVEEILKRKAIIEDAGLVWSVVESVPIHEDIKTHTGNY 78
Cdd:pfam03786   1 MELTFRWYGPgNDPVSLEDIRQIpGVKGVVGALHDIPVGEVWPKEEIMALKEEIEDAGLHLSVIESVPVHEDIKLGTPTR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143    79 EQWIANYQQTLRNLAQCGIRTVCYNFMPVLDWTRTDLEYVLPDGSKALRFDQIEFAAFEMHILKRPGAEADYTeeeiaqa 158
Cdd:pfam03786  81 DRYIENYKQTIRNLAQCGVKVVCYNFMPVFDWTRTDLHYPLEDGSKALRFDKIEIAAFEPQILRTPAAEGDFT------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143   159 aerfatmsdedkarltrniiagLPGAEEGYtLDQFRKHLELYKDIDKAKLRENFAVFLKAIIPVAEEVGVRMAVHPDDPP 238
Cdd:pfam03786 154 ----------------------LPGWEPEY-LDELKGLFEAYKDIDEEKLWDNLAYFLQEIIPVAEEVGVKMAIHPDDPP 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143   239 RPILGLPRIVSTIEDMQWMVDTVNSMANGFTMCTGSYGVRADNDLVDMIKQFGPRIYFTHLRSTMREDNPKTFHEAAHLN 318
Cdd:pfam03786 211 WPIFGLPRIVTNIEDYQRLLDLVDSPYNGITLCTGSLGANPANDLPEMIRQFADRIYFAHLRNIKREDGPKDFVETAHLS 290
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16132143   319 --GDVDMYEVVKAIVEEEHRRkaegkedliPMRPDHGHQMLDDlkkKTNPGYSAIGRLKGLAEVRGVELAIQR 389
Cdd:pfam03786 291 kdGSVDMYAVMKAYHEVGYRG---------YMRPDHGRQIWGE---LTRPGYGLYDRALGIAYLNGLWDALSK 351
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
110-332 1.07e-09

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


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 58.49  E-value: 1.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143 110 WTRTDLEYVLpDGSKALRFDQIEFAAFEMHilkrpgaeaDYTEEEIAQAAE----RFATMSdedkaRLTRNIIAGLPGAE 185
Cdd:COG1082  10 LPDLDLEEAL-RAAAELGYDGVELAGGDLD---------EADLAELRAALAdhglEISSLH-----APGLNLAPDPEVRE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143 186 EgyTLDQFRKHLELYKDI-----------------DKAKLRENFAVFLKAIIPVAEEVGVRMAVHPDDpprpilglPRIV 248
Cdd:COG1082  75 A--ALERLKRAIDLAAELgakvvvvhpgsppppdlPPEEAWDRLAERLRELAELAEEAGVTLALENHE--------GTFV 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143 249 STIEDMQWMVDTVNSMANGFTMCTGSYgVRADNDLVDMIKQFGPRIYFTHLRstmreDNPKTFHEAAHlNGDVDMYEVVK 328
Cdd:COG1082 145 NTPEEALRLLEAVDSPNVGLLLDTGHA-LLAGEDPVELLRKLGDRIKHVHLK-----DADGDQHLPPG-EGDIDFAAILR 217

                ....
gi 16132143 329 AIVE 332
Cdd:COG1082 218 ALKE 221
AP_endonuc_2 pfam01261
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ...
133-332 7.36e-03

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: 37.74  E-value: 7.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143   133 FAAFEMHI-LKRPGAEADYTEEEIAQAAER-------FATMSDEDkarltrniIAGLPGAEEGYTLDQFRKHLEL----- 199
Cdd:pfam01261   9 FDGVELFTrRWFRPPLSDEEAEELKAALKEhgleivvHAPYLGDN--------LASPDEEEREKAIDRLKRAIELaaalg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132143   200 ----------YKDIDKAKLRENFAVFLKAIIPVAEEVGVRMAVHP-DDPPRPILglprivSTIEDMQWMVDTVNSMANGF 268
Cdd:pfam01261  81 aklvvfhpgsDLGDDPEEALARLAESLRELADLAEREGVRLALEPlAGKGTNVG------NTFEEALEIIDEVDSPNVGV 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16132143   269 TMCTGSYGVRADNDLVDMIKQFgPRIYFTHLRSTMREDNPKTFHeaaHLN---GDVDMYEVVKAIVE 332
Cdd:pfam01261 155 CLDTGHLFAAGDGDLFELRLGD-RYIGHVHLKDSKNPLGSGPDR---HVPigeGVIDFEALFRALKE 217
 
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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