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Conserved domains on  [gi|1339986393|gb|POT31456|]
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mannonate dehydratase [Citrobacter braakii]

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: 751.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393   1 MEQTWRWYGPNDPVSLDDVRQAGATGVVTALHHIPNGEVWPVEEIQQRQAILAEKGLTWSVVESIPVHEDIKTRSGQYQT 80
Cdd:COG1312     1 MKMTWRWFGPNDPVTLEDIRQIGATGIVTALHHIPVGEVWPVEEIAERKAEIEAAGLEWSVVESVPVHEDIKLGLGDRDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393  81 WIANYQQSIRNLATCGIDTVCYNFMPILDWTRTDLEYQLPDGSKALRFDQIAFAAFELHILQRPDAAADYTAEEQRQALN 160
Cdd:COG1312    81 YIENYKQSLRNLAAAGIKTVCYNFMPVLDWTRTDLAYPLPDGSTALRFDQADFAAFDLFILKRPGAEADYSEEVVADAKE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393 161 YFNAMSDADIEKLTRNIIAGLPGAEEGYTLDQFRARLAEYDGISKDDLRDNMAVFLRAIVPVAEEVGVRLAVHPDDPPRP 240
Cdd:COG1312   161 RFEAMSEAEKARLTRNIIAGLPGWEEEYTLEEFRELLAAYKGIDEEKLRENLKYFLEEVIPVAEELGIKMAIHPDDPPWP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393 241 ILGLPRIVSTIEDMQWLKETVDSINNGFTMCTGSYGVRADNDLVKMIETFGDRIHFTHLRSTCREDNpKTFHEGAHLQGD 320
Cdd:COG1312   241 IFGLPRIVSTEEDLRRLLDAVDSPANGLTLCTGSLGARPDNDLPAMARRFGDRIHFAHLRNVKREGD-GSFYEAAHLDGD 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1339986393 321 VDMVSVVAAILSEEQRRKKAGDlrpIPMRPDHGHQMLDDLHKKTNPGYSAIGRLKGLAEVRGVELALKQTQF 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: 751.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393   1 MEQTWRWYGPNDPVSLDDVRQAGATGVVTALHHIPNGEVWPVEEIQQRQAILAEKGLTWSVVESIPVHEDIKTRSGQYQT 80
Cdd:COG1312     1 MKMTWRWFGPNDPVTLEDIRQIGATGIVTALHHIPVGEVWPVEEIAERKAEIEAAGLEWSVVESVPVHEDIKLGLGDRDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393  81 WIANYQQSIRNLATCGIDTVCYNFMPILDWTRTDLEYQLPDGSKALRFDQIAFAAFELHILQRPDAAADYTAEEQRQALN 160
Cdd:COG1312    81 YIENYKQSLRNLAAAGIKTVCYNFMPVLDWTRTDLAYPLPDGSTALRFDQADFAAFDLFILKRPGAEADYSEEVVADAKE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393 161 YFNAMSDADIEKLTRNIIAGLPGAEEGYTLDQFRARLAEYDGISKDDLRDNMAVFLRAIVPVAEEVGVRLAVHPDDPPRP 240
Cdd:COG1312   161 RFEAMSEAEKARLTRNIIAGLPGWEEEYTLEEFRELLAAYKGIDEEKLRENLKYFLEEVIPVAEELGIKMAIHPDDPPWP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393 241 ILGLPRIVSTIEDMQWLKETVDSINNGFTMCTGSYGVRADNDLVKMIETFGDRIHFTHLRSTCREDNpKTFHEGAHLQGD 320
Cdd:COG1312   241 IFGLPRIVSTEEDLRRLLDAVDSPANGLTLCTGSLGARPDNDLPAMARRFGDRIHFAHLRNVKREGD-GSFYEAAHLDGD 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1339986393 321 VDMVSVVAAILSEEQRRKKAGDlrpIPMRPDHGHQMLDDLHKKTNPGYSAIGRLKGLAEVRGVELALKQTQF 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: 746.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393   1 MEQTWRWYGPNDPVSLDDVRQAGATGVVTALHHIPNGEVWPVEEIQQRQAILAEKGLTWSVVESIPVHEDIKTRSGQYQT 80
Cdd:PRK03906    1 MEMTWRWFGPNDPVTLEDIRQPGATGIVTALHDIPVGEVWPVEEILARKAEIEAAGLEWSVVESVPVHEDIKTGTPNRDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393  81 WIANYQQSIRNLATCGIDTVCYNFMPILDWTRTDLEYQLPDGSKALRFDQIAFAAFELHILQRPDAAADYTAEEQRQALN 160
Cdd:PRK03906   81 YIENYKQTLRNLAAAGIKVVCYNFMPVFDWTRTDLAYELPDGSTALRFDQIDFAAFDPHILKRPGAEADYGEEEIAQAAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393 161 YFNAMSDADIEKLTRNIIAGLPGAEEGYTLDQFRARLAEYDGISKDDLRDNMAVFLRAIVPVAEEVGVRLAVHPDDPPRP 240
Cdd:PRK03906  161 RFAAMSEEDKARLTRNIIAGLPGWEEPYTLEQFRALLELYKDIDEEKLRENLAYFLKAIIPVAEEVGVKMAIHPDDPPRP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393 241 ILGLPRIVSTIEDMQWLKETVDSINNGFTMCTGSYGVRADNDLVKMIETFGDRIHFTHLRSTCREDnPKTFHEGAHLQGD 320
Cdd:PRK03906  241 IFGLPRIVSTEEDLQRLLDAVDSPANGLTLCTGSLGARPDNDLPAMIREFGDRIHFAHLRNVKREG-PGSFHEAAHLSGD 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1339986393 321 VDMVSVVAAILSEEQRrkkagdlrpIPMRPDHGHQMLDDLHKKTNPGYSAIGRLKGLAEVRGVELALKQTQFRDL 395
Cdd:PRK03906  320 VDMYAVVKALLDEEFR---------IPMRPDHGRMIWDDLGKKTNPGYGLYGRALGLAELRGLWEALEKAAKRKA 385
uxuA TIGR00695
mannonate dehydratase; This Fe2+-requiring enzyme plays a role in D-glucuronate catabolism in ...
1-393 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: 665.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393   1 MEQTWRWYGPNDPVSLDDVRQAGATGVVTALHHIPNGEVWPVEEIQQRQAILAEKGLTWSVVESIPVHEDIKTRSGQYQT 80
Cdd:TIGR00695   1 MEQTWRWYGPNDPVSLADVRQAGATGIVTALHHIPNGEVWSVEEILKRKAIIEDAGLVWSVVESVPVHEDIKTHTGNYEQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393  81 WIANYQQSIRNLATCGIDTVCYNFMPILDWTRTDLEYQLPDGSKALRFDQIAFAAFELHILQRPDAAADYTAEEQRQALN 160
Cdd:TIGR00695  81 WIANYKQTLRNLAQCGIRTVCYNFMPVLDWTRTDLEYVLPDGSKALRFDQIEFAAFEMHILKRPGAEADYTEEEIAQAAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393 161 YFNAMSDADIEKLTRNIIAGLPGAEEGYTLDQFRARLAEYDGISKDDLRDNMAVFLRAIVPVAEEVGVRLAVHPDDPPRP 240
Cdd:TIGR00695 161 RFATMSDEDKARLTRNIIAGLPGAEEGYTLDQFRKHLELYKDIDKEKLRENLAVFLKEIIPVAEEVGVRMAIHPDDPPRP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393 241 ILGLPRIVSTIEDMQWLKETVDSINNGFTMCTGSYGVRADNDLVKMIETFGDRIHFTHLRSTCREDNPKTFHEGAHLQGD 320
Cdd:TIGR00695 241 ILGLPRIVSTIEDMQWMVDTVNSPANGFTMCTGSYGVRADNDLVDMIKQFAPRIYFTHLRSTMREDNPKTFHEAAHLNGD 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1339986393 321 VDMVSVVAAILSEEQRRKKAGDLRPIPMRPDHGHQMLDDLHKKTNPGYSAIGRLKGLAEVRGVELALKQTQFR 393
Cdd:TIGR00695 321 VDMYEVVKAIVEEEHRRKAEGKEDLIPMRPDHGHQMLDDLKKKTNPGYSAIGRLKGLAEVRGLELAIQRAFFS 393
UxuA pfam03786
D-mannonate dehydratase (UxuA); UxuA (this family) and UxuB are required for hexuronate ...
1-388 0e+00

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


Pssm-ID: 397726  Cd Length: 351  Bit Score: 511.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393   1 MEQTWRWYGP-NDPVSLDDVRQA-GATGVVTALHHIPNGEVWPVEEIQQRQAILAEKGLTWSVVESIPVHEDIKTRSGQY 78
Cdd:pfam03786   1 MELTFRWYGPgNDPVSLEDIRQIpGVKGVVGALHDIPVGEVWPKEEIMALKEEIEDAGLHLSVIESVPVHEDIKLGTPTR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393  79 QTWIANYQQSIRNLATCGIDTVCYNFMPILDWTRTDLEYQLPDGSKALRFDQIAFAAFELHILQRPDAAADYTaeeqrqa 158
Cdd:pfam03786  81 DRYIENYKQTIRNLAQCGVKVVCYNFMPVFDWTRTDLHYPLEDGSKALRFDKIEIAAFEPQILRTPAAEGDFT------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393 159 lnyfnamsdadiekltrniiagLPGAEEGYtLDQFRARLAEYDGISKDDLRDNMAVFLRAIVPVAEEVGVRLAVHPDDPP 238
Cdd:pfam03786 154 ----------------------LPGWEPEY-LDELKGLFEAYKDIDEEKLWDNLAYFLQEIIPVAEEVGVKMAIHPDDPP 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393 239 RPILGLPRIVSTIEDMQWLKETVDSINNGFTMCTGSYGVRADNDLVKMIETFGDRIHFTHLRSTCREDNPKTFHEGAHLQ 318
Cdd:pfam03786 211 WPIFGLPRIVTNIEDYQRLLDLVDSPYNGITLCTGSLGANPANDLPEMIRQFADRIYFAHLRNIKREDGPKDFVETAHLS 290
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1339986393 319 --GDVDMVSVVAAILSEEQRRkkagdlrpiPMRPDHGHQMLDDlhkKTNPGYSAIGRLKGLAEVRGVELALK 388
Cdd:pfam03786 291 kdGSVDMYAVMKAYHEVGYRG---------YMRPDHGRQIWGE---LTRPGYGLYDRALGIAYLNGLWDALS 350
 
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: 751.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393   1 MEQTWRWYGPNDPVSLDDVRQAGATGVVTALHHIPNGEVWPVEEIQQRQAILAEKGLTWSVVESIPVHEDIKTRSGQYQT 80
Cdd:COG1312     1 MKMTWRWFGPNDPVTLEDIRQIGATGIVTALHHIPVGEVWPVEEIAERKAEIEAAGLEWSVVESVPVHEDIKLGLGDRDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393  81 WIANYQQSIRNLATCGIDTVCYNFMPILDWTRTDLEYQLPDGSKALRFDQIAFAAFELHILQRPDAAADYTAEEQRQALN 160
Cdd:COG1312    81 YIENYKQSLRNLAAAGIKTVCYNFMPVLDWTRTDLAYPLPDGSTALRFDQADFAAFDLFILKRPGAEADYSEEVVADAKE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393 161 YFNAMSDADIEKLTRNIIAGLPGAEEGYTLDQFRARLAEYDGISKDDLRDNMAVFLRAIVPVAEEVGVRLAVHPDDPPRP 240
Cdd:COG1312   161 RFEAMSEAEKARLTRNIIAGLPGWEEEYTLEEFRELLAAYKGIDEEKLRENLKYFLEEVIPVAEELGIKMAIHPDDPPWP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393 241 ILGLPRIVSTIEDMQWLKETVDSINNGFTMCTGSYGVRADNDLVKMIETFGDRIHFTHLRSTCREDNpKTFHEGAHLQGD 320
Cdd:COG1312   241 IFGLPRIVSTEEDLRRLLDAVDSPANGLTLCTGSLGARPDNDLPAMARRFGDRIHFAHLRNVKREGD-GSFYEAAHLDGD 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1339986393 321 VDMVSVVAAILSEEQRRKKAGDlrpIPMRPDHGHQMLDDLHKKTNPGYSAIGRLKGLAEVRGVELALKQTQF 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: 746.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393   1 MEQTWRWYGPNDPVSLDDVRQAGATGVVTALHHIPNGEVWPVEEIQQRQAILAEKGLTWSVVESIPVHEDIKTRSGQYQT 80
Cdd:PRK03906    1 MEMTWRWFGPNDPVTLEDIRQPGATGIVTALHDIPVGEVWPVEEILARKAEIEAAGLEWSVVESVPVHEDIKTGTPNRDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393  81 WIANYQQSIRNLATCGIDTVCYNFMPILDWTRTDLEYQLPDGSKALRFDQIAFAAFELHILQRPDAAADYTAEEQRQALN 160
Cdd:PRK03906   81 YIENYKQTLRNLAAAGIKVVCYNFMPVFDWTRTDLAYELPDGSTALRFDQIDFAAFDPHILKRPGAEADYGEEEIAQAAA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393 161 YFNAMSDADIEKLTRNIIAGLPGAEEGYTLDQFRARLAEYDGISKDDLRDNMAVFLRAIVPVAEEVGVRLAVHPDDPPRP 240
Cdd:PRK03906  161 RFAAMSEEDKARLTRNIIAGLPGWEEPYTLEQFRALLELYKDIDEEKLRENLAYFLKAIIPVAEEVGVKMAIHPDDPPRP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393 241 ILGLPRIVSTIEDMQWLKETVDSINNGFTMCTGSYGVRADNDLVKMIETFGDRIHFTHLRSTCREDnPKTFHEGAHLQGD 320
Cdd:PRK03906  241 IFGLPRIVSTEEDLQRLLDAVDSPANGLTLCTGSLGARPDNDLPAMIREFGDRIHFAHLRNVKREG-PGSFHEAAHLSGD 319
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1339986393 321 VDMVSVVAAILSEEQRrkkagdlrpIPMRPDHGHQMLDDLHKKTNPGYSAIGRLKGLAEVRGVELALKQTQFRDL 395
Cdd:PRK03906  320 VDMYAVVKALLDEEFR---------IPMRPDHGRMIWDDLGKKTNPGYGLYGRALGLAELRGLWEALEKAAKRKA 385
uxuA TIGR00695
mannonate dehydratase; This Fe2+-requiring enzyme plays a role in D-glucuronate catabolism in ...
1-393 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: 665.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393   1 MEQTWRWYGPNDPVSLDDVRQAGATGVVTALHHIPNGEVWPVEEIQQRQAILAEKGLTWSVVESIPVHEDIKTRSGQYQT 80
Cdd:TIGR00695   1 MEQTWRWYGPNDPVSLADVRQAGATGIVTALHHIPNGEVWSVEEILKRKAIIEDAGLVWSVVESVPVHEDIKTHTGNYEQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393  81 WIANYQQSIRNLATCGIDTVCYNFMPILDWTRTDLEYQLPDGSKALRFDQIAFAAFELHILQRPDAAADYTAEEQRQALN 160
Cdd:TIGR00695  81 WIANYKQTLRNLAQCGIRTVCYNFMPVLDWTRTDLEYVLPDGSKALRFDQIEFAAFEMHILKRPGAEADYTEEEIAQAAE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393 161 YFNAMSDADIEKLTRNIIAGLPGAEEGYTLDQFRARLAEYDGISKDDLRDNMAVFLRAIVPVAEEVGVRLAVHPDDPPRP 240
Cdd:TIGR00695 161 RFATMSDEDKARLTRNIIAGLPGAEEGYTLDQFRKHLELYKDIDKEKLRENLAVFLKEIIPVAEEVGVRMAIHPDDPPRP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393 241 ILGLPRIVSTIEDMQWLKETVDSINNGFTMCTGSYGVRADNDLVKMIETFGDRIHFTHLRSTCREDNPKTFHEGAHLQGD 320
Cdd:TIGR00695 241 ILGLPRIVSTIEDMQWMVDTVNSPANGFTMCTGSYGVRADNDLVDMIKQFAPRIYFTHLRSTMREDNPKTFHEAAHLNGD 320
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1339986393 321 VDMVSVVAAILSEEQRRKKAGDLRPIPMRPDHGHQMLDDLHKKTNPGYSAIGRLKGLAEVRGVELALKQTQFR 393
Cdd:TIGR00695 321 VDMYEVVKAIVEEEHRRKAEGKEDLIPMRPDHGHQMLDDLKKKTNPGYSAIGRLKGLAEVRGLELAIQRAFFS 393
UxuA pfam03786
D-mannonate dehydratase (UxuA); UxuA (this family) and UxuB are required for hexuronate ...
1-388 0e+00

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


Pssm-ID: 397726  Cd Length: 351  Bit Score: 511.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393   1 MEQTWRWYGP-NDPVSLDDVRQA-GATGVVTALHHIPNGEVWPVEEIQQRQAILAEKGLTWSVVESIPVHEDIKTRSGQY 78
Cdd:pfam03786   1 MELTFRWYGPgNDPVSLEDIRQIpGVKGVVGALHDIPVGEVWPKEEIMALKEEIEDAGLHLSVIESVPVHEDIKLGTPTR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393  79 QTWIANYQQSIRNLATCGIDTVCYNFMPILDWTRTDLEYQLPDGSKALRFDQIAFAAFELHILQRPDAAADYTaeeqrqa 158
Cdd:pfam03786  81 DRYIENYKQTIRNLAQCGVKVVCYNFMPVFDWTRTDLHYPLEDGSKALRFDKIEIAAFEPQILRTPAAEGDFT------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393 159 lnyfnamsdadiekltrniiagLPGAEEGYtLDQFRARLAEYDGISKDDLRDNMAVFLRAIVPVAEEVGVRLAVHPDDPP 238
Cdd:pfam03786 154 ----------------------LPGWEPEY-LDELKGLFEAYKDIDEEKLWDNLAYFLQEIIPVAEEVGVKMAIHPDDPP 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393 239 RPILGLPRIVSTIEDMQWLKETVDSINNGFTMCTGSYGVRADNDLVKMIETFGDRIHFTHLRSTCREDNPKTFHEGAHLQ 318
Cdd:pfam03786 211 WPIFGLPRIVTNIEDYQRLLDLVDSPYNGITLCTGSLGANPANDLPEMIRQFADRIYFAHLRNIKREDGPKDFVETAHLS 290
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1339986393 319 --GDVDMVSVVAAILSEEQRRkkagdlrpiPMRPDHGHQMLDDlhkKTNPGYSAIGRLKGLAEVRGVELALK 388
Cdd:pfam03786 291 kdGSVDMYAVMKAYHEVGYRG---------YMRPDHGRQIWGE---LTRPGYGLYDRALGIAYLNGLWDALS 350
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
201-330 2.89e-10

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


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 60.41  E-value: 2.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339986393 201 DGISKDDLRDNMAVFLRAIVPVAEEVGVRLAVHPDDpprpilglPRIVSTIEDMQWLKETVDSINNGFTMCTGSYgVRAD 280
Cdd:COG1082   105 PDLPPEEAWDRLAERLRELAELAEEAGVTLALENHE--------GTFVNTPEEALRLLEAVDSPNVGLLLDTGHA-LLAG 175
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1339986393 281 NDLVKMIETFGDRIHFTHLrstcrednpKTFHEGAHL---QGDVDMVSVVAAI 330
Cdd:COG1082   176 EDPVELLRKLGDRIKHVHL---------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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