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Conserved domains on  [gi|495144592|ref|WP_007869399|]
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MULTISPECIES: mannonate dehydratase [Cronobacter]

Protein Classification

mannonate dehydratase( domain architecture ID 10012089)

mannonate dehydratase catalyzes the dehydration of D-mannonate

CATH:  3.20.20.150
EC:  4.2.1.8
Gene Ontology:  GO:0008927|GO:0006064
PubMed:  19617363
SCOP:  4001951

Graphical summary

 Zoom to residue level

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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: 755.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592   1 MEQTWRWYGPNDPVSLDDIRQAGATGIVTALHHIPNGEVWPVEEIKKRQAELAQKGLTWSVVESIPVHEDIKTHTGQYDR 80
Cdd:COG1312    1 MKMTWRWFGPNDPVTLEDIRQIGATGIVTALHHIPVGEVWPVEEIAERKAEIEAAGLEWSVVESVPVHEDIKLGLGDRDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592  81 YIASYQQSIRNLAACGIDTVCYNFMPILDWTRTDLEYTLPDGSKALRFDHIAFAAFELHILKRDGARHDYTDDEQRQAQD 160
Cdd:COG1312   81 YIENYKQSLRNLAAAGIKTVCYNFMPVLDWTRTDLAYPLPDGSTALRFDQADFAAFDLFILKRPGAEADYSEEVVADAKE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592 161 YFSAMSEAQIETLTRNIIAGLPGAEEGYTLDQFRARLSEYDHIDKAALRDNMAYFLKAIVPVAEEAGVRLAVHPDDPPRP 240
Cdd:COG1312  161 RFEAMSEAEKARLTRNIIAGLPGWEEEYTLEEFRELLAAYKGIDEEKLRENLKYFLEEVIPVAEELGIKMAIHPDDPPWP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592 241 ILGLPRIVSTIEDMQWLKETVDSIHNGFTMCTGSYGVRADNDLVRMVETFADRIHFTHLRSTCREANpKTFHEAAHLYGD 320
Cdd:COG1312  241 IFGLPRIVSTEEDLRRLLDAVDSPANGLTLCTGSLGARPDNDLPAMARRFGDRIHFAHLRNVKREGD-GSFYEAAHLDGD 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495144592 321 VDMVAVVKAILTEEQRRKKAGDlrpIPFRPDHGHQMLDDLRKKTNPGYSAIGRLKGLAEVRGVELALKKVLF 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: 755.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592   1 MEQTWRWYGPNDPVSLDDIRQAGATGIVTALHHIPNGEVWPVEEIKKRQAELAQKGLTWSVVESIPVHEDIKTHTGQYDR 80
Cdd:COG1312    1 MKMTWRWFGPNDPVTLEDIRQIGATGIVTALHHIPVGEVWPVEEIAERKAEIEAAGLEWSVVESVPVHEDIKLGLGDRDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592  81 YIASYQQSIRNLAACGIDTVCYNFMPILDWTRTDLEYTLPDGSKALRFDHIAFAAFELHILKRDGARHDYTDDEQRQAQD 160
Cdd:COG1312   81 YIENYKQSLRNLAAAGIKTVCYNFMPVLDWTRTDLAYPLPDGSTALRFDQADFAAFDLFILKRPGAEADYSEEVVADAKE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592 161 YFSAMSEAQIETLTRNIIAGLPGAEEGYTLDQFRARLSEYDHIDKAALRDNMAYFLKAIVPVAEEAGVRLAVHPDDPPRP 240
Cdd:COG1312  161 RFEAMSEAEKARLTRNIIAGLPGWEEEYTLEEFRELLAAYKGIDEEKLRENLKYFLEEVIPVAEELGIKMAIHPDDPPWP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592 241 ILGLPRIVSTIEDMQWLKETVDSIHNGFTMCTGSYGVRADNDLVRMVETFADRIHFTHLRSTCREANpKTFHEAAHLYGD 320
Cdd:COG1312  241 IFGLPRIVSTEEDLRRLLDAVDSPANGLTLCTGSLGARPDNDLPAMARRFGDRIHFAHLRNVKREGD-GSFYEAAHLDGD 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495144592 321 VDMVAVVKAILTEEQRRKKAGDlrpIPFRPDHGHQMLDDLRKKTNPGYSAIGRLKGLAEVRGVELALKKVLF 392
Cdd:COG1312  320 VDMVAVVKALLDEEARRRADFD---IPMRPDHGRMILDDLGRKGRPGYGLIGRALGLAELRGLWEAIEKMLK 388
PRK03906 PRK03906
mannonate dehydratase; Provisional
1-395 0e+00

mannonate dehydratase; Provisional


Pssm-ID: 235172  Cd Length: 385  Bit Score: 743.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592   1 MEQTWRWYGPNDPVSLDDIRQAGATGIVTALHHIPNGEVWPVEEIKKRQAELAQKGLTWSVVESIPVHEDIKTHTGQYDR 80
Cdd:PRK03906   1 MEMTWRWFGPNDPVTLEDIRQPGATGIVTALHDIPVGEVWPVEEILARKAEIEAAGLEWSVVESVPVHEDIKTGTPNRDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592  81 YIASYQQSIRNLAACGIDTVCYNFMPILDWTRTDLEYTLPDGSKALRFDHIAFAAFELHILKRDGARHDYTDDEQRQAQD 160
Cdd:PRK03906  81 YIENYKQTLRNLAAAGIKVVCYNFMPVFDWTRTDLAYELPDGSTALRFDQIDFAAFDPHILKRPGAEADYGEEEIAQAAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592 161 YFSAMSEAQIETLTRNIIAGLPGAEEGYTLDQFRARLSEYDHIDKAALRDNMAYFLKAIVPVAEEAGVRLAVHPDDPPRP 240
Cdd:PRK03906 161 RFAAMSEEDKARLTRNIIAGLPGWEEPYTLEQFRALLELYKDIDEEKLRENLAYFLKAIIPVAEEVGVKMAIHPDDPPRP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592 241 ILGLPRIVSTIEDMQWLKETVDSIHNGFTMCTGSYGVRADNDLVRMVETFADRIHFTHLRSTCREAnPKTFHEAAHLYGD 320
Cdd:PRK03906 241 IFGLPRIVSTEEDLQRLLDAVDSPANGLTLCTGSLGARPDNDLPAMIREFGDRIHFAHLRNVKREG-PGSFHEAAHLSGD 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495144592 321 VDMVAVVKAILTEEQRrkkagdlrpIPFRPDHGHQMLDDLRKKTNPGYSAIGRLKGLAEVRGVELALKKVLFPDL 395
Cdd:PRK03906 320 VDMYAVVKALLDEEFR---------IPMRPDHGRMIWDDLGKKTNPGYGLYGRALGLAELRGLWEALEKAAKRKA 385
uxuA TIGR00695
mannonate dehydratase; This Fe2+-requiring enzyme plays a role in D-glucuronate catabolism in ...
1-392 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: 663.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592    1 MEQTWRWYGPNDPVSLDDIRQAGATGIVTALHHIPNGEVWPVEEIKKRQAELAQKGLTWSVVESIPVHEDIKTHTGQYDR 80
Cdd:TIGR00695   1 MEQTWRWYGPNDPVSLADVRQAGATGIVTALHHIPNGEVWSVEEILKRKAIIEDAGLVWSVVESVPVHEDIKTHTGNYEQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592   81 YIASYQQSIRNLAACGIDTVCYNFMPILDWTRTDLEYTLPDGSKALRFDHIAFAAFELHILKRDGARHDYTDDEQRQAQD 160
Cdd:TIGR00695  81 WIANYKQTLRNLAQCGIRTVCYNFMPVLDWTRTDLEYVLPDGSKALRFDQIEFAAFEMHILKRPGAEADYTEEEIAQAAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592  161 YFSAMSEAQIETLTRNIIAGLPGAEEGYTLDQFRARLSEYDHIDKAALRDNMAYFLKAIVPVAEEAGVRLAVHPDDPPRP 240
Cdd:TIGR00695 161 RFATMSDEDKARLTRNIIAGLPGAEEGYTLDQFRKHLELYKDIDKEKLRENLAVFLKEIIPVAEEVGVRMAIHPDDPPRP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592  241 ILGLPRIVSTIEDMQWLKETVDSIHNGFTMCTGSYGVRADNDLVRMVETFADRIHFTHLRSTCREANPKTFHEAAHLYGD 320
Cdd:TIGR00695 241 ILGLPRIVSTIEDMQWMVDTVNSPANGFTMCTGSYGVRADNDLVDMIKQFAPRIYFTHLRSTMREDNPKTFHEAAHLNGD 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495144592  321 VDMVAVVKAILTEEQRRKKAGDLRPIPFRPDHGHQMLDDLRKKTNPGYSAIGRLKGLAEVRGVELALKKVLF 392
Cdd:TIGR00695 321 VDMYEVVKAIVEEEHRRKAEGKEDLIPMRPDHGHQMLDDLKKKTNPGYSAIGRLKGLAEVRGLELAIQRAFF 392
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: 520.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592    1 MEQTWRWYGP-NDPVSLDDIRQA-GATGIVTALHHIPNGEVWPVEEIKKRQAELAQKGLTWSVVESIPVHEDIKTHTGQY 78
Cdd:pfam03786   1 MELTFRWYGPgNDPVSLEDIRQIpGVKGVVGALHDIPVGEVWPKEEIMALKEEIEDAGLHLSVIESVPVHEDIKLGTPTR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592   79 DRYIASYQQSIRNLAACGIDTVCYNFMPILDWTRTDLEYTLPDGSKALRFDHIAFAAFELHILKRDGARHDYTddeqrqa 158
Cdd:pfam03786  81 DRYIENYKQTIRNLAQCGVKVVCYNFMPVFDWTRTDLHYPLEDGSKALRFDKIEIAAFEPQILRTPAAEGDFT------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592  159 qdyfsamseaqietltrniiagLPGAEEGYtLDQFRARLSEYDHIDKAALRDNMAYFLKAIVPVAEEAGVRLAVHPDDPP 238
Cdd:pfam03786 154 ----------------------LPGWEPEY-LDELKGLFEAYKDIDEEKLWDNLAYFLQEIIPVAEEVGVKMAIHPDDPP 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592  239 RPILGLPRIVSTIEDMQWLKETVDSIHNGFTMCTGSYGVRADNDLVRMVETFADRIHFTHLRSTCREANPKTFHEAAHL- 317
Cdd:pfam03786 211 WPIFGLPRIVTNIEDYQRLLDLVDSPYNGITLCTGSLGANPANDLPEMIRQFADRIYFAHLRNIKREDGPKDFVETAHLs 290
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495144592  318 -YGDVDMVAVVKAILTEEQRRkkagdlrpiPFRPDHGHQMLDDlrkKTNPGYSAIGRLKGLAEVRGVELALKK 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: 755.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592   1 MEQTWRWYGPNDPVSLDDIRQAGATGIVTALHHIPNGEVWPVEEIKKRQAELAQKGLTWSVVESIPVHEDIKTHTGQYDR 80
Cdd:COG1312    1 MKMTWRWFGPNDPVTLEDIRQIGATGIVTALHHIPVGEVWPVEEIAERKAEIEAAGLEWSVVESVPVHEDIKLGLGDRDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592  81 YIASYQQSIRNLAACGIDTVCYNFMPILDWTRTDLEYTLPDGSKALRFDHIAFAAFELHILKRDGARHDYTDDEQRQAQD 160
Cdd:COG1312   81 YIENYKQSLRNLAAAGIKTVCYNFMPVLDWTRTDLAYPLPDGSTALRFDQADFAAFDLFILKRPGAEADYSEEVVADAKE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592 161 YFSAMSEAQIETLTRNIIAGLPGAEEGYTLDQFRARLSEYDHIDKAALRDNMAYFLKAIVPVAEEAGVRLAVHPDDPPRP 240
Cdd:COG1312  161 RFEAMSEAEKARLTRNIIAGLPGWEEEYTLEEFRELLAAYKGIDEEKLRENLKYFLEEVIPVAEELGIKMAIHPDDPPWP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592 241 ILGLPRIVSTIEDMQWLKETVDSIHNGFTMCTGSYGVRADNDLVRMVETFADRIHFTHLRSTCREANpKTFHEAAHLYGD 320
Cdd:COG1312  241 IFGLPRIVSTEEDLRRLLDAVDSPANGLTLCTGSLGARPDNDLPAMARRFGDRIHFAHLRNVKREGD-GSFYEAAHLDGD 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495144592 321 VDMVAVVKAILTEEQRRKKAGDlrpIPFRPDHGHQMLDDLRKKTNPGYSAIGRLKGLAEVRGVELALKKVLF 392
Cdd:COG1312  320 VDMVAVVKALLDEEARRRADFD---IPMRPDHGRMILDDLGRKGRPGYGLIGRALGLAELRGLWEAIEKMLK 388
PRK03906 PRK03906
mannonate dehydratase; Provisional
1-395 0e+00

mannonate dehydratase; Provisional


Pssm-ID: 235172  Cd Length: 385  Bit Score: 743.95  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592   1 MEQTWRWYGPNDPVSLDDIRQAGATGIVTALHHIPNGEVWPVEEIKKRQAELAQKGLTWSVVESIPVHEDIKTHTGQYDR 80
Cdd:PRK03906   1 MEMTWRWFGPNDPVTLEDIRQPGATGIVTALHDIPVGEVWPVEEILARKAEIEAAGLEWSVVESVPVHEDIKTGTPNRDR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592  81 YIASYQQSIRNLAACGIDTVCYNFMPILDWTRTDLEYTLPDGSKALRFDHIAFAAFELHILKRDGARHDYTDDEQRQAQD 160
Cdd:PRK03906  81 YIENYKQTLRNLAAAGIKVVCYNFMPVFDWTRTDLAYELPDGSTALRFDQIDFAAFDPHILKRPGAEADYGEEEIAQAAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592 161 YFSAMSEAQIETLTRNIIAGLPGAEEGYTLDQFRARLSEYDHIDKAALRDNMAYFLKAIVPVAEEAGVRLAVHPDDPPRP 240
Cdd:PRK03906 161 RFAAMSEEDKARLTRNIIAGLPGWEEPYTLEQFRALLELYKDIDEEKLRENLAYFLKAIIPVAEEVGVKMAIHPDDPPRP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592 241 ILGLPRIVSTIEDMQWLKETVDSIHNGFTMCTGSYGVRADNDLVRMVETFADRIHFTHLRSTCREAnPKTFHEAAHLYGD 320
Cdd:PRK03906 241 IFGLPRIVSTEEDLQRLLDAVDSPANGLTLCTGSLGARPDNDLPAMIREFGDRIHFAHLRNVKREG-PGSFHEAAHLSGD 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495144592 321 VDMVAVVKAILTEEQRrkkagdlrpIPFRPDHGHQMLDDLRKKTNPGYSAIGRLKGLAEVRGVELALKKVLFPDL 395
Cdd:PRK03906 320 VDMYAVVKALLDEEFR---------IPMRPDHGRMIWDDLGKKTNPGYGLYGRALGLAELRGLWEALEKAAKRKA 385
uxuA TIGR00695
mannonate dehydratase; This Fe2+-requiring enzyme plays a role in D-glucuronate catabolism in ...
1-392 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: 663.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592    1 MEQTWRWYGPNDPVSLDDIRQAGATGIVTALHHIPNGEVWPVEEIKKRQAELAQKGLTWSVVESIPVHEDIKTHTGQYDR 80
Cdd:TIGR00695   1 MEQTWRWYGPNDPVSLADVRQAGATGIVTALHHIPNGEVWSVEEILKRKAIIEDAGLVWSVVESVPVHEDIKTHTGNYEQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592   81 YIASYQQSIRNLAACGIDTVCYNFMPILDWTRTDLEYTLPDGSKALRFDHIAFAAFELHILKRDGARHDYTDDEQRQAQD 160
Cdd:TIGR00695  81 WIANYKQTLRNLAQCGIRTVCYNFMPVLDWTRTDLEYVLPDGSKALRFDQIEFAAFEMHILKRPGAEADYTEEEIAQAAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592  161 YFSAMSEAQIETLTRNIIAGLPGAEEGYTLDQFRARLSEYDHIDKAALRDNMAYFLKAIVPVAEEAGVRLAVHPDDPPRP 240
Cdd:TIGR00695 161 RFATMSDEDKARLTRNIIAGLPGAEEGYTLDQFRKHLELYKDIDKEKLRENLAVFLKEIIPVAEEVGVRMAIHPDDPPRP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592  241 ILGLPRIVSTIEDMQWLKETVDSIHNGFTMCTGSYGVRADNDLVRMVETFADRIHFTHLRSTCREANPKTFHEAAHLYGD 320
Cdd:TIGR00695 241 ILGLPRIVSTIEDMQWMVDTVNSPANGFTMCTGSYGVRADNDLVDMIKQFAPRIYFTHLRSTMREDNPKTFHEAAHLNGD 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495144592  321 VDMVAVVKAILTEEQRRKKAGDLRPIPFRPDHGHQMLDDLRKKTNPGYSAIGRLKGLAEVRGVELALKKVLF 392
Cdd:TIGR00695 321 VDMYEVVKAIVEEEHRRKAEGKEDLIPMRPDHGHQMLDDLKKKTNPGYSAIGRLKGLAEVRGLELAIQRAFF 392
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: 520.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592    1 MEQTWRWYGP-NDPVSLDDIRQA-GATGIVTALHHIPNGEVWPVEEIKKRQAELAQKGLTWSVVESIPVHEDIKTHTGQY 78
Cdd:pfam03786   1 MELTFRWYGPgNDPVSLEDIRQIpGVKGVVGALHDIPVGEVWPKEEIMALKEEIEDAGLHLSVIESVPVHEDIKLGTPTR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592   79 DRYIASYQQSIRNLAACGIDTVCYNFMPILDWTRTDLEYTLPDGSKALRFDHIAFAAFELHILKRDGARHDYTddeqrqa 158
Cdd:pfam03786  81 DRYIENYKQTIRNLAQCGVKVVCYNFMPVFDWTRTDLHYPLEDGSKALRFDKIEIAAFEPQILRTPAAEGDFT------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592  159 qdyfsamseaqietltrniiagLPGAEEGYtLDQFRARLSEYDHIDKAALRDNMAYFLKAIVPVAEEAGVRLAVHPDDPP 238
Cdd:pfam03786 154 ----------------------LPGWEPEY-LDELKGLFEAYKDIDEEKLWDNLAYFLQEIIPVAEEVGVKMAIHPDDPP 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592  239 RPILGLPRIVSTIEDMQWLKETVDSIHNGFTMCTGSYGVRADNDLVRMVETFADRIHFTHLRSTCREANPKTFHEAAHL- 317
Cdd:pfam03786 211 WPIFGLPRIVTNIEDYQRLLDLVDSPYNGITLCTGSLGANPANDLPEMIRQFADRIYFAHLRNIKREDGPKDFVETAHLs 290
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495144592  318 -YGDVDMVAVVKAILTEEQRRkkagdlrpiPFRPDHGHQMLDDlrkKTNPGYSAIGRLKGLAEVRGVELALKK 389
Cdd:pfam03786 291 kDGSVDMYAVMKAYHEVGYRG---------YMRPDHGRQIWGE---LTRPGYGLYDRALGIAYLNGLWDALSK 351
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
204-330 2.36e-08

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


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 54.63  E-value: 2.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495144592 204 DKAALRDNMAYFLKAIVPVAEEAGVRLAVHPDDpprpilglPRIVSTIEDMQWLKETVDSIHNGFTMCTGSYgVRADNDL 283
Cdd:COG1082  108 PPEEAWDRLAERLRELAELAEEAGVTLALENHE--------GTFVNTPEEALRLLEAVDSPNVGLLLDTGHA-LLAGEDP 178
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 495144592 284 VRMVETFADRIHFTHLrstcreanpKTFHEAAHLY---GDVDMVAVVKAI 330
Cdd:COG1082  179 VELLRKLGDRIKHVHL---------KDADGDQHLPpgeGDIDFAAILRAL 219
 
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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