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Conserved domains on  [gi|511205215|gb|AFH64790|]
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sugar isomerase [Paenibacillus mucilaginosus K02]

Protein Classification

COG4952 family protein( domain architecture ID 10008979)

COG4952 family protein

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
COG4952 COG4952
L-rhamnose isomerase [Cell wall/membrane/envelope biogenesis];
5-408 0e+00

L-rhamnose isomerase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 443979  Cd Length: 408  Bit Score: 701.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215   5 DRAYALFEEQQQARGINLEEVKSRLKALHIETPSWGYGDSGTRFKVFQKEGVPRNPFEKFEDAAQVHGLTGLCPSVAIHI 84
Cdd:COG4952    6 QRDYEALGEQLARRGIDIEAIKAKLAAFQIEIPSWAYGNGGTRFGRFPGPGEPRNLFEKLEDAAQVHQLTGAAPSVSLHI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215  85 PWDKVEDYGKLRNHAESLGLKIGAVNPNLFQEDDYMLGSVTNADPAVRRKATDHLLECVDIAKETGSRDLSLWFADGTNY 164
Cdd:COG4952   86 PWDKVDDYAALKALAAELGLGFGAVNSNTFQDQSYKFGSLTHPDAAVRQQAVDHNLECIEIGKALGSKDLTVWLADGSNY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215 165 PGQGDIRKRKAWMFEALNEMYKAMTPEMRMLIEYKCFEPAFYHTDIADWGMAYNYALKLGPQAEVLVDTGHHLPGANIEH 244
Cdd:COG4952  166 PGQDNFRRRFDRLLESLAEIYAALPDDWRLLLEYKPFEPAFYSTDIPDWGTSYLLAQALGPKAQVLVDLGHHAPNTNIEQ 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215 245 IVAYLIDENRLGGFHFNSRKYADDDLVVGSVNPYELFLIFYQILSAANDDDakirsTVDNIAYMIDQSHNIEQKIPAMLR 324
Cdd:COG4952  246 IVARLLREGKLGGFHFNDRKYGDDDLTVGSIDPYQLFLIFNELVDAEALDP-----TAFGVAYMIDQSHNVEDKIEALIQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215 325 SVLNVQTQYAKALLINHAEVEEAQLRGDVLGAEDAVRRAFEFDVTPLLHALREEQGLPVDPMKAYLSSSYGKDILVRGKG 404
Cdd:COG4952  321 SVLNVQEAYAKALLVDRAALAAAQEANDVLGAQEILMDAFRTDVRPLLAEAREEAGGAIDPIAAYRASGYREKIAAERGG 400

                 ....*.
gi 511205215 405 G--ASW 408
Cdd:COG4952  401 GtqAGG 406
 
Name Accession Description Interval E-value
COG4952 COG4952
L-rhamnose isomerase [Cell wall/membrane/envelope biogenesis];
5-408 0e+00

L-rhamnose isomerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443979  Cd Length: 408  Bit Score: 701.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215   5 DRAYALFEEQQQARGINLEEVKSRLKALHIETPSWGYGDSGTRFKVFQKEGVPRNPFEKFEDAAQVHGLTGLCPSVAIHI 84
Cdd:COG4952    6 QRDYEALGEQLARRGIDIEAIKAKLAAFQIEIPSWAYGNGGTRFGRFPGPGEPRNLFEKLEDAAQVHQLTGAAPSVSLHI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215  85 PWDKVEDYGKLRNHAESLGLKIGAVNPNLFQEDDYMLGSVTNADPAVRRKATDHLLECVDIAKETGSRDLSLWFADGTNY 164
Cdd:COG4952   86 PWDKVDDYAALKALAAELGLGFGAVNSNTFQDQSYKFGSLTHPDAAVRQQAVDHNLECIEIGKALGSKDLTVWLADGSNY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215 165 PGQGDIRKRKAWMFEALNEMYKAMTPEMRMLIEYKCFEPAFYHTDIADWGMAYNYALKLGPQAEVLVDTGHHLPGANIEH 244
Cdd:COG4952  166 PGQDNFRRRFDRLLESLAEIYAALPDDWRLLLEYKPFEPAFYSTDIPDWGTSYLLAQALGPKAQVLVDLGHHAPNTNIEQ 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215 245 IVAYLIDENRLGGFHFNSRKYADDDLVVGSVNPYELFLIFYQILSAANDDDakirsTVDNIAYMIDQSHNIEQKIPAMLR 324
Cdd:COG4952  246 IVARLLREGKLGGFHFNDRKYGDDDLTVGSIDPYQLFLIFNELVDAEALDP-----TAFGVAYMIDQSHNVEDKIEALIQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215 325 SVLNVQTQYAKALLINHAEVEEAQLRGDVLGAEDAVRRAFEFDVTPLLHALREEQGLPVDPMKAYLSSSYGKDILVRGKG 404
Cdd:COG4952  321 SVLNVQEAYAKALLVDRAALAAAQEANDVLGAQEILMDAFRTDVRPLLAEAREEAGGAIDPIAAYRASGYREKIAAERGG 400

                 ....*.
gi 511205215 405 G--ASW 408
Cdd:COG4952  401 GtqAGG 406
RhaI_grampos TIGR02635
L-rhamnose isomerase, Streptomyces subtype; This clade of sequences is closely related to the ...
22-403 0e+00

L-rhamnose isomerase, Streptomyces subtype; This clade of sequences is closely related to the L-rhamnose isomerases found in Pseudomonas stutzeri and in a number of the Rhizobiales (TIGR02629). The genes of the family represented here are found in similar genomic contexts which contain genes apparently involved in rhamnose catabolism such as rhamnulose-1-phosphate aldolase (TIGR02632), sugar kinases, and sugar transporters. [Energy metabolism, Sugars]


Pssm-ID: 274239  Cd Length: 378  Bit Score: 641.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215   22 LEEVKSRLKALHIETPSWGYGDSGTRFKVFQKEGVPRNPFEKFEDAAQVHGLTGLCPSVAIHIPWDKVEDYGKLRNHAES 101
Cdd:TIGR02635   1 LEEVEKKLKALKIETPSWAYGNSGTRFKVFHQEGAARNVFEKIEDAALVHRLTGICPTVALHIPWDRVEDYEELARYAEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215  102 LGLKIGAVNPNLFQEDDYMLGSVTNADPAVRRKATDHLLECVDIAKETGSRDLSLWFADGTNYPGQGDIRKRKAWMFEAL 181
Cdd:TIGR02635  81 LGLKIGAINPNLFQDDDYKFGSLTHPDKRIRRKAIDHLLECVDIAKKTGSKDISLWLADGTNYPGQDDFRSRKDRLEESL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215  182 NEMYKAMTPEMRMLIEYKCFEPAFYHTDIADWGMAYNYALKLGPQAEVLVDTGHHLPGANIEHIVAYLIDENRLGGFHFN 261
Cdd:TIGR02635 161 AEVYEHLGADMRLLIEYKFFEPAFYHTDIPDWGTAYALSEKLGERALVLVDTGHHAQGTNIEFIVATLLDEKKLGGFHFN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215  262 SRKYADDDLVVGSVNPYELFLIFYQILSAANDDDakirSTVDNIAYMIDQSHNIEQKIPAMLRSVLNVQTQYAKALLINH 341
Cdd:TIGR02635 241 SRKYADDDLTVGAINPYELFLIFKEIVRAGRDPE----DSASDVALMLDQCHNLEPKIPAMIRSVLNVQELFAKALLVDR 316
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 511205215  342 AEVEEAQLRGDVLGAEDAVRRAFEFDVTPLLHALREEQGLPVDPMKAYLSSSYGKDILVRGK 403
Cdd:TIGR02635 317 DALRKAQENGDVLEAEAVLMDAFETDVRPLLAEVREEMGLPEDPLKAYRESGYMEKIAAERR 378
AP_endonuc_2 pfam01261
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ...
64-271 4.39e-07

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: 50.83  E-value: 4.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215   64 FEDAAQvHGLTG--LCPSVAIHIPWDKvEDYGKLRNHAESLGLKIGAVNPnlfqeddYMLGSVTNADPAVRRKATDHLLE 141
Cdd:pfam01261   1 LAAAAE-LGFDGveLFTRRWFRPPLSD-EEAEELKAALKEHGLEIVVHAP-------YLGDNLASPDEEEREKAIDRLKR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215  142 CVDIAKETGSRDLSLWfadgTNYPGQGDIRKRKAWMFEALNEMYK-AMTPEMRMLIEykcFEPAFYHTDIADWGMAYNYA 220
Cdd:pfam01261  72 AIELAAALGAKLVVFH----PGSDLGDDPEEALARLAESLRELADlAEREGVRLALE---PLAGKGTNVGNTFEEALEII 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 511205215  221 LKLG-PQAEVLVDTGHHLPGANIEHIVAYLiDENRLGGFHFNSRKYADDDLV 271
Cdd:pfam01261 145 DEVDsPNVGVCLDTGHLFAAGDGDLFELRL-GDRYIGHVHLKDSKNPLGSGP 195
 
Name Accession Description Interval E-value
COG4952 COG4952
L-rhamnose isomerase [Cell wall/membrane/envelope biogenesis];
5-408 0e+00

L-rhamnose isomerase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443979  Cd Length: 408  Bit Score: 701.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215   5 DRAYALFEEQQQARGINLEEVKSRLKALHIETPSWGYGDSGTRFKVFQKEGVPRNPFEKFEDAAQVHGLTGLCPSVAIHI 84
Cdd:COG4952    6 QRDYEALGEQLARRGIDIEAIKAKLAAFQIEIPSWAYGNGGTRFGRFPGPGEPRNLFEKLEDAAQVHQLTGAAPSVSLHI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215  85 PWDKVEDYGKLRNHAESLGLKIGAVNPNLFQEDDYMLGSVTNADPAVRRKATDHLLECVDIAKETGSRDLSLWFADGTNY 164
Cdd:COG4952   86 PWDKVDDYAALKALAAELGLGFGAVNSNTFQDQSYKFGSLTHPDAAVRQQAVDHNLECIEIGKALGSKDLTVWLADGSNY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215 165 PGQGDIRKRKAWMFEALNEMYKAMTPEMRMLIEYKCFEPAFYHTDIADWGMAYNYALKLGPQAEVLVDTGHHLPGANIEH 244
Cdd:COG4952  166 PGQDNFRRRFDRLLESLAEIYAALPDDWRLLLEYKPFEPAFYSTDIPDWGTSYLLAQALGPKAQVLVDLGHHAPNTNIEQ 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215 245 IVAYLIDENRLGGFHFNSRKYADDDLVVGSVNPYELFLIFYQILSAANDDDakirsTVDNIAYMIDQSHNIEQKIPAMLR 324
Cdd:COG4952  246 IVARLLREGKLGGFHFNDRKYGDDDLTVGSIDPYQLFLIFNELVDAEALDP-----TAFGVAYMIDQSHNVEDKIEALIQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215 325 SVLNVQTQYAKALLINHAEVEEAQLRGDVLGAEDAVRRAFEFDVTPLLHALREEQGLPVDPMKAYLSSSYGKDILVRGKG 404
Cdd:COG4952  321 SVLNVQEAYAKALLVDRAALAAAQEANDVLGAQEILMDAFRTDVRPLLAEAREEAGGAIDPIAAYRASGYREKIAAERGG 400

                 ....*.
gi 511205215 405 G--ASW 408
Cdd:COG4952  401 GtqAGG 406
RhaI_grampos TIGR02635
L-rhamnose isomerase, Streptomyces subtype; This clade of sequences is closely related to the ...
22-403 0e+00

L-rhamnose isomerase, Streptomyces subtype; This clade of sequences is closely related to the L-rhamnose isomerases found in Pseudomonas stutzeri and in a number of the Rhizobiales (TIGR02629). The genes of the family represented here are found in similar genomic contexts which contain genes apparently involved in rhamnose catabolism such as rhamnulose-1-phosphate aldolase (TIGR02632), sugar kinases, and sugar transporters. [Energy metabolism, Sugars]


Pssm-ID: 274239  Cd Length: 378  Bit Score: 641.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215   22 LEEVKSRLKALHIETPSWGYGDSGTRFKVFQKEGVPRNPFEKFEDAAQVHGLTGLCPSVAIHIPWDKVEDYGKLRNHAES 101
Cdd:TIGR02635   1 LEEVEKKLKALKIETPSWAYGNSGTRFKVFHQEGAARNVFEKIEDAALVHRLTGICPTVALHIPWDRVEDYEELARYAEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215  102 LGLKIGAVNPNLFQEDDYMLGSVTNADPAVRRKATDHLLECVDIAKETGSRDLSLWFADGTNYPGQGDIRKRKAWMFEAL 181
Cdd:TIGR02635  81 LGLKIGAINPNLFQDDDYKFGSLTHPDKRIRRKAIDHLLECVDIAKKTGSKDISLWLADGTNYPGQDDFRSRKDRLEESL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215  182 NEMYKAMTPEMRMLIEYKCFEPAFYHTDIADWGMAYNYALKLGPQAEVLVDTGHHLPGANIEHIVAYLIDENRLGGFHFN 261
Cdd:TIGR02635 161 AEVYEHLGADMRLLIEYKFFEPAFYHTDIPDWGTAYALSEKLGERALVLVDTGHHAQGTNIEFIVATLLDEKKLGGFHFN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215  262 SRKYADDDLVVGSVNPYELFLIFYQILSAANDDDakirSTVDNIAYMIDQSHNIEQKIPAMLRSVLNVQTQYAKALLINH 341
Cdd:TIGR02635 241 SRKYADDDLTVGAINPYELFLIFKEIVRAGRDPE----DSASDVALMLDQCHNLEPKIPAMIRSVLNVQELFAKALLVDR 316
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 511205215  342 AEVEEAQLRGDVLGAEDAVRRAFEFDVTPLLHALREEQGLPVDPMKAYLSSSYGKDILVRGK 403
Cdd:TIGR02635 317 DALRKAQENGDVLEAEAVLMDAFETDVRPLLAEVREEMGLPEDPLKAYRESGYMEKIAAERR 378
L_rham_iso_rhiz TIGR02629
L-rhamnose catabolism isomerase, Pseudomonas stutzeri subtype; Members of this family are ...
6-394 4.11e-120

L-rhamnose catabolism isomerase, Pseudomonas stutzeri subtype; Members of this family are isomerases in the pathway of L-rhamnose catabolism as found in Pseudomonas stutzeri and in a number of the Rhizobiales. This family differs from the L-rhamnose isomerases of Escherichia coli (see TIGR01748). This enzyme catalyzes the isomerization step in rhamnose catabolism. Genetic evidence in Rhizobium leguminosarum bv. trifolii suggests phosphorylation occurs first, then isomerization of the the phosphorylated sugar, but characterization of the recombinant enzyme from Pseudomonas


Pssm-ID: 131677  Cd Length: 412  Bit Score: 355.10  E-value: 4.11e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215    6 RAYALFEEQQQARGINLEEVKSRLKALHIETPSWGYGDSGTRFKVFQKEGVPRNPFEKFEDAAQVHGLTGLCPSVAIHIP 85
Cdd:TIGR02629  15 RDYESLGARLARRGIDIDAVTAKVEKFFVAVPSWGVGTGGTRFARFPGTGEPRGIFDKLEDCAVIQQLTRATPNVSLHIP 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215   86 WDKVeDYGKLRNHAESLGLKIGAVNPNLF-----QEDDYMLGSVTNADPAVRRKATDHLLECVDIAKETGSRDLSLWFAD 160
Cdd:TIGR02629  95 WDKA-DPKELKARGSALGLGFDAMNSNTFsdapgQAHSYKFGSLSHTDAATRRQAVEHNLECIEIGKALGSKALTVWIGD 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215  161 GTNYPGQGDIRKRKAWMFEALNEMYKAMTPEMRMLIEYKCFEPAFYHTDIADWGMAYNYALKLGPQAEVLVDTGHHLPGA 240
Cdd:TIGR02629 174 GSNFPGQSNFTRAFERYLDAMKAVYAGLPDDWKLFTEHKMYEPAFYSTVVQDWGTNYLIAQELGPKAFCLVDLGHHAPNV 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215  241 NIEHIVAYLIDENRLGGFHFNSRKYADDDLVVGSVNPYELFLIFYQILsaanddDAKIRSTVD-NIAYMIDQSHNIEQKI 319
Cdd:TIGR02629 254 NIEMIVARLIQFKKLGGFHFNDSKYGDDDLDAGSIDPYRLFLVFNELV------DAEARGAKGfDPAHMLDQSHNVTDPI 327
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 511205215  320 PAMLRSVLNVQTQYAKALLINHAEVEEAQLRGDVLGAEDAVRRAFEFDVTPLLHALREEQGLPVDPMKAYLSSSY 394
Cdd:TIGR02629 328 ESLMNSANEVRRAYAQALLVDRKALSGYQEDNDALMATETLKRAYRTDVEPILAEARLRTGGAIDPVATYRASGY 402
AP_endonuc_2 pfam01261
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ...
64-271 4.39e-07

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: 50.83  E-value: 4.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215   64 FEDAAQvHGLTG--LCPSVAIHIPWDKvEDYGKLRNHAESLGLKIGAVNPnlfqeddYMLGSVTNADPAVRRKATDHLLE 141
Cdd:pfam01261   1 LAAAAE-LGFDGveLFTRRWFRPPLSD-EEAEELKAALKEHGLEIVVHAP-------YLGDNLASPDEEEREKAIDRLKR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215  142 CVDIAKETGSRDLSLWfadgTNYPGQGDIRKRKAWMFEALNEMYK-AMTPEMRMLIEykcFEPAFYHTDIADWGMAYNYA 220
Cdd:pfam01261  72 AIELAAALGAKLVVFH----PGSDLGDDPEEALARLAESLRELADlAEREGVRLALE---PLAGKGTNVGNTFEEALEII 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 511205215  221 LKLG-PQAEVLVDTGHHLPGANIEHIVAYLiDENRLGGFHFNSRKYADDDLV 271
Cdd:pfam01261 145 DEVDsPNVGVCLDTGHLFAAGDGDLFELRL-GDRYIGHVHLKDSKNPLGSGP 195
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
56-273 2.12e-04

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


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 42.69  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215  56 VPRNPFEKFEDAAQVHGLTGlcpsvaIHIPWDKVEDYG--KLRNHAESLGLKIGAVNPNLFQeddymlgsvTNADPAVRR 133
Cdd:COG1082   10 LPDLDLEEALRAAAELGYDG------VELAGGDLDEADlaELRAALADHGLEISSLHAPGLN---------LAPDPEVRE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511205215 134 KATDHLLECVDIAKETGSRDLSLWfaDGTNYPGQGDIRKRKAWMFEALNEMYKAMTPE-MRMLIEykcFEPAFYHTDIAD 212
Cdd:COG1082   75 AALERLKRAIDLAAELGAKVVVVH--PGSPPPPDLPPEEAWDRLAERLRELAELAEEAgVTLALE---NHEGTFVNTPEE 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 511205215 213 wgmaynyALKL-----GPQAEVLVDTGH-HLPGANIEHIVAYLIDenRLGGFHFNSRKyADDDLVVG 273
Cdd:COG1082  150 -------ALRLleavdSPNVGLLLDTGHaLLAGEDPVELLRKLGD--RIKHVHLKDAD-GDQHLPPG 206
 
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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