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Conserved domains on  [gi|446626568|ref|WP_000703914|]
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ureidoglycolate dehydrogenase [Escherichia coli]

Protein Classification

ureidoglycolate dehydrogenase( domain architecture ID 10014943)

ureidoglycolate dehydrogenase (NAD(+)) catalyzes the oxidation of ureidoglycolate to oxalurate, playing a pivotal role as a metabolic branch-point enzyme in nitrogen utilization via the assimilation of allantoin

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK15025 PRK15025
ureidoglycolate dehydrogenase; Provisional
1-349 0e+00

ureidoglycolate dehydrogenase; Provisional


:

Pssm-ID: 184985  Cd Length: 349  Bit Score: 728.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568   1 MKISRETLHQLIENKLCQAGLKREHAATVAEVLVYADARGIHSHGAVRVEYYAERISKGGTNREPEFRLEETGPCSAILH 80
Cdd:PRK15025   1 MKISRETLHQLIKNKLCKAGLKREHAATVAEVLVYADARGIHSHGAVRVEYYAERISKGGTNREPEFRFEETGPCSAILH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568  81 ADNAAGQVAAKMGMEHAIKTAQQNGVAVVGISRMGHSGAISYFVQQAARAGLIGISMCQSDPMVVPFGGAEIYYGTNPLA 160
Cdd:PRK15025  81 ADNAAGQVAAKMGMEHAIETAKQNGVAVVGISRMGHSGAISYFVQQAARAGLIGLSMCQSDPMVVPFGGAEIYYGTNPLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568 161 FAAPGEGDEILTFDMATTVQAWGKVLDARSRNMSIPDTWAVDKNGAPTTDPFAVHALLPAAGPKGYGLMMMIDVLSGVLL 240
Cdd:PRK15025 161 FAAPGEGDEIITFDMATTVQAWGKVLDARSRNMSIPDTWAVDKNGAPTTDPFAVHALLPAAGPKGYGLMMMVDVLSGVLL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568 241 GLPFGRQVSSMYDDLHAGRNLGQLHVVINPNFFSSSELFRQHLSQTMRELNAITPAPGFNQVYYPGQDQDIKQRQAAVEG 320
Cdd:PRK15025 241 GLPFGRQVSSMYDDLHAGRNLGQLHIVINPAFFSSSELFRQHISQTMRELNAITPAPGFNQVYYPGQDQDIKQKKAAVEG 320
                        330       340
                 ....*....|....*....|....*....
gi 446626568 321 IEIVDDIYQYLISDALYNTSYETKNPFAQ 349
Cdd:PRK15025 321 IEIVDDIYQYLISDALYNTSYETKNPFAQ 349
 
Name Accession Description Interval E-value
PRK15025 PRK15025
ureidoglycolate dehydrogenase; Provisional
1-349 0e+00

ureidoglycolate dehydrogenase; Provisional


Pssm-ID: 184985  Cd Length: 349  Bit Score: 728.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568   1 MKISRETLHQLIENKLCQAGLKREHAATVAEVLVYADARGIHSHGAVRVEYYAERISKGGTNREPEFRLEETGPCSAILH 80
Cdd:PRK15025   1 MKISRETLHQLIKNKLCKAGLKREHAATVAEVLVYADARGIHSHGAVRVEYYAERISKGGTNREPEFRFEETGPCSAILH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568  81 ADNAAGQVAAKMGMEHAIKTAQQNGVAVVGISRMGHSGAISYFVQQAARAGLIGISMCQSDPMVVPFGGAEIYYGTNPLA 160
Cdd:PRK15025  81 ADNAAGQVAAKMGMEHAIETAKQNGVAVVGISRMGHSGAISYFVQQAARAGLIGLSMCQSDPMVVPFGGAEIYYGTNPLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568 161 FAAPGEGDEILTFDMATTVQAWGKVLDARSRNMSIPDTWAVDKNGAPTTDPFAVHALLPAAGPKGYGLMMMIDVLSGVLL 240
Cdd:PRK15025 161 FAAPGEGDEIITFDMATTVQAWGKVLDARSRNMSIPDTWAVDKNGAPTTDPFAVHALLPAAGPKGYGLMMMVDVLSGVLL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568 241 GLPFGRQVSSMYDDLHAGRNLGQLHVVINPNFFSSSELFRQHLSQTMRELNAITPAPGFNQVYYPGQDQDIKQRQAAVEG 320
Cdd:PRK15025 241 GLPFGRQVSSMYDDLHAGRNLGQLHIVINPAFFSSSELFRQHISQTMRELNAITPAPGFNQVYYPGQDQDIKQKKAAVEG 320
                        330       340
                 ....*....|....*....|....*....
gi 446626568 321 IEIVDDIYQYLISDALYNTSYETKNPFAQ 349
Cdd:PRK15025 321 IEIVDDIYQYLISDALYNTSYETKNPFAQ 349
AllD TIGR03175
ureidoglycolate dehydrogenase; This enzyme converts ureidoglycolate to oxalureate in the ...
1-349 0e+00

ureidoglycolate dehydrogenase; This enzyme converts ureidoglycolate to oxalureate in the non-urea-forming catabolism of allantoin (GenProp0687). The pathway has been characterized in E. coli and is observed in the genomes of Entercoccus faecalis and Bacillus licheniformis.


Pssm-ID: 274470  Cd Length: 349  Bit Score: 680.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568    1 MKISRETLHQLIENKLCQAGLKREHAATVAEVLVYADARGIHSHGAVRVEYYAERISKGGTNREPEFRLEETGPCSAILH 80
Cdd:TIGR03175   1 MKVSRETLHQLIKQKLEKAGLKREHAAEVADVLTFADARGIHSHGAVRVEYYAERIAKGGITREPEFRFEKTGPCTAIFH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568   81 ADNAAGQVAAKMGMEHAIKTAQQNGVAVVGISRMGHSGAISYFVQQAARAGLIGISMCQSDPMVVPFGGAEIYYGTNPLA 160
Cdd:TIGR03175  81 GDNGAGQVAAKMAMEHAIELAKESGVAVVGISRMSHSGALSYFVKQAAEQGMVALSMCQSDPMVVPFGGTEIYFGTNPIA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568  161 FAAPGEGDEILTFDMATTVQAWGKVLDARSRNMSIPDTWAVDKNGAPTTDPFAVHALLPAAGPKGYGLMMMIDVLSGVLL 240
Cdd:TIGR03175 161 FAAPSAGDEIITFDMATTVQAWGKVLDARSRNESIPDTWAVDKNGAPTTDPFAVHALLPIAGPKGYGLMMMVDVLSGSLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568  241 GLPFGRQVSSMYDDLHAGRNLGQLHVVINPNFFSSSELFRQHLSQTMRELNAITPAPGFNQVYYPGQDQDIKQRQAAVEG 320
Cdd:TIGR03175 241 GLPFGRHVSSMYADLTAGRNLGQLHLVINPAFFTDSELFKQHISQMMEELNAVPPAEGFQQVYYPGEDGDLKQQKADSEG 320
                         330       340
                  ....*....|....*....|....*....
gi 446626568  321 IEIVDDIYQYLISDALYNTSYETKNPFAQ 349
Cdd:TIGR03175 321 IEIVDDIYQYLVSDAVHYDSYEGKNPFAQ 349
AllD COG2055
Malate/lactate/ureidoglycolate dehydrogenase, LDH2 family [Energy production and conversion]; ...
1-335 4.26e-146

Malate/lactate/ureidoglycolate dehydrogenase, LDH2 family [Energy production and conversion]; Malate/lactate/ureidoglycolate dehydrogenase, LDH2 family is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 441658  Cd Length: 337  Bit Score: 415.68  E-value: 4.26e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568   1 MKISRETLHQLIENKLCQAGLKREHAATVAEVLVYADARGIHSHGAVRVEYYAERISKGGTNREPEFRLEETGPCSAILH 80
Cdd:COG2055    1 MRVSAEELRALVARVLLAAGVSEEDAAAVADVLVEADLRGIDSHGVARLPRYVERLRAGGINPNAEPEVVRETPATAVVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568  81 ADNAAGQVAAKMGMEHAIKTAQQNGVAVVGISRMGHSGAISYFVQQAARAGLIGISMCQSDPMVVPFGGAEIYYGTNPLA 160
Cdd:COG2055   81 GDNGLGQVAARRAMELAIEKAKEHGIGAVAVRNSNHFGALGYYAEMAAEAGLIGIAFTNSPPLVAPWGGREPLLGTNPIA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568 161 FAAPGEGDEILTFDMATTVQAWGKVLDARSRNMSIPDTWAVDKNGAPTTDPFAVH---ALLPAAGPKGYGLMMMIDVLSG 237
Cdd:COG2055  161 FAAPRGGGPPFVLDMATSVVARGKIEVAARKGEPIPEGWAVDADGNPTTDPAAALeggALLPLGGHKGYGLALMVELLAG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568 238 VLLGLPFGRQVSSMYDDlHAGRNLGQLHVVINPNFFSSSELFRQHLSQTMRELNAITPAPGFNQVYYPGQDQDIKQRQAA 317
Cdd:COG2055  241 VLSGGGFGPEVSSFYDD-GGPPGLGHFFIAIDPAAFGGLEAFKARMDALLDALRASPPAPGGDPVRLPGEREAAARAERL 319
                        330
                 ....*....|....*...
gi 446626568 318 VEGIEIVDDIYQYLISDA 335
Cdd:COG2055  320 AEGIPLPDALWAELRALA 337
Ldh_2 pfam02615
Malate/L-lactate dehydrogenase; This family consists of bacterial and archaeal Malate ...
6-331 1.92e-142

Malate/L-lactate dehydrogenase; This family consists of bacterial and archaeal Malate/L-lactate dehydrogenase. L-lactate dehydrogenase, EC:1.1.1.27, catalyzes the reaction (S)-lactate + NAD(+) <=> pyruvate + NADH. Malate dehydrogenase, EC:1.1.1.37 and EC:1.1.1.82, catalyzes the reactions: (S)-malate + NAD(+) <=> oxaloacetate + NADH, and (S)-malate + NADP(+) <=> oxaloacetate + NADPH respectively.


Pssm-ID: 460620  Cd Length: 330  Bit Score: 406.06  E-value: 1.92e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568    6 ETLHQLIENKLCQAGLKREHAATVAEVLVYADARGIHSHGAVRVEYYAERISKGGTNREPEFRLEETGPCSAILHADNAA 85
Cdd:pfam02615   1 EELRAFVERVLLAAGVPEEDAEIVADVLVEADLRGVDSHGVNRLPRYVDRIRAGRINPNAEPEVVRETPAVAVVDGDNGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568   86 GQVAAKMGMEHAIKTAQQNGVAVVGISRMGHSGAISYFVQQAARAGLIGISMCQSDPMVVPFGGAEIYYGTNPLAFAAPG 165
Cdd:pfam02615  81 GQVAAHKAMELAIEKAKEHGIGAVAVRNSNHFGAAGYYAEMAAEAGLIGIAFTNSSPLVAPWGGKEPRLGTNPIAFAAPA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568  166 EGDEILTFDMATTVQAWGKVLDARSRNMSIPDTWAVDKNGAPTTDPFAV---HALLPAAGPKGYGLMMMIDVLSGVLLGL 242
Cdd:pfam02615 161 GGGPPFVLDMATSVVARGKIEVAARKGKPIPEGWALDADGNPTTDPAAAlegGALLPLGGHKGYGLALMVELLAGVLSGA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568  243 PFGRQVSSMYDDLHAGRNLGQLHVVINPNFFSSSELFRQHLSQTMRELNAITPAPGFNQVYYPGQDQDIKQRQAAVEGIE 322
Cdd:pfam02615 241 AFGPEVSGDYDPGGPPRKVGHFFIAIDPAAFGDAEEFKARMDALIDELRASPPAPGGDPVYLPGEREAAARAERLREGIP 320

                  ....*....
gi 446626568  323 IVDDIYQYL 331
Cdd:pfam02615 321 LDDAVWAEL 329
 
Name Accession Description Interval E-value
PRK15025 PRK15025
ureidoglycolate dehydrogenase; Provisional
1-349 0e+00

ureidoglycolate dehydrogenase; Provisional


Pssm-ID: 184985  Cd Length: 349  Bit Score: 728.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568   1 MKISRETLHQLIENKLCQAGLKREHAATVAEVLVYADARGIHSHGAVRVEYYAERISKGGTNREPEFRLEETGPCSAILH 80
Cdd:PRK15025   1 MKISRETLHQLIKNKLCKAGLKREHAATVAEVLVYADARGIHSHGAVRVEYYAERISKGGTNREPEFRFEETGPCSAILH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568  81 ADNAAGQVAAKMGMEHAIKTAQQNGVAVVGISRMGHSGAISYFVQQAARAGLIGISMCQSDPMVVPFGGAEIYYGTNPLA 160
Cdd:PRK15025  81 ADNAAGQVAAKMGMEHAIETAKQNGVAVVGISRMGHSGAISYFVQQAARAGLIGLSMCQSDPMVVPFGGAEIYYGTNPLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568 161 FAAPGEGDEILTFDMATTVQAWGKVLDARSRNMSIPDTWAVDKNGAPTTDPFAVHALLPAAGPKGYGLMMMIDVLSGVLL 240
Cdd:PRK15025 161 FAAPGEGDEIITFDMATTVQAWGKVLDARSRNMSIPDTWAVDKNGAPTTDPFAVHALLPAAGPKGYGLMMMVDVLSGVLL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568 241 GLPFGRQVSSMYDDLHAGRNLGQLHVVINPNFFSSSELFRQHLSQTMRELNAITPAPGFNQVYYPGQDQDIKQRQAAVEG 320
Cdd:PRK15025 241 GLPFGRQVSSMYDDLHAGRNLGQLHIVINPAFFSSSELFRQHISQTMRELNAITPAPGFNQVYYPGQDQDIKQKKAAVEG 320
                        330       340
                 ....*....|....*....|....*....
gi 446626568 321 IEIVDDIYQYLISDALYNTSYETKNPFAQ 349
Cdd:PRK15025 321 IEIVDDIYQYLISDALYNTSYETKNPFAQ 349
AllD TIGR03175
ureidoglycolate dehydrogenase; This enzyme converts ureidoglycolate to oxalureate in the ...
1-349 0e+00

ureidoglycolate dehydrogenase; This enzyme converts ureidoglycolate to oxalureate in the non-urea-forming catabolism of allantoin (GenProp0687). The pathway has been characterized in E. coli and is observed in the genomes of Entercoccus faecalis and Bacillus licheniformis.


Pssm-ID: 274470  Cd Length: 349  Bit Score: 680.82  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568    1 MKISRETLHQLIENKLCQAGLKREHAATVAEVLVYADARGIHSHGAVRVEYYAERISKGGTNREPEFRLEETGPCSAILH 80
Cdd:TIGR03175   1 MKVSRETLHQLIKQKLEKAGLKREHAAEVADVLTFADARGIHSHGAVRVEYYAERIAKGGITREPEFRFEKTGPCTAIFH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568   81 ADNAAGQVAAKMGMEHAIKTAQQNGVAVVGISRMGHSGAISYFVQQAARAGLIGISMCQSDPMVVPFGGAEIYYGTNPLA 160
Cdd:TIGR03175  81 GDNGAGQVAAKMAMEHAIELAKESGVAVVGISRMSHSGALSYFVKQAAEQGMVALSMCQSDPMVVPFGGTEIYFGTNPIA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568  161 FAAPGEGDEILTFDMATTVQAWGKVLDARSRNMSIPDTWAVDKNGAPTTDPFAVHALLPAAGPKGYGLMMMIDVLSGVLL 240
Cdd:TIGR03175 161 FAAPSAGDEIITFDMATTVQAWGKVLDARSRNESIPDTWAVDKNGAPTTDPFAVHALLPIAGPKGYGLMMMVDVLSGSLL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568  241 GLPFGRQVSSMYDDLHAGRNLGQLHVVINPNFFSSSELFRQHLSQTMRELNAITPAPGFNQVYYPGQDQDIKQRQAAVEG 320
Cdd:TIGR03175 241 GLPFGRHVSSMYADLTAGRNLGQLHLVINPAFFTDSELFKQHISQMMEELNAVPPAEGFQQVYYPGEDGDLKQQKADSEG 320
                         330       340
                  ....*....|....*....|....*....
gi 446626568  321 IEIVDDIYQYLISDALYNTSYETKNPFAQ 349
Cdd:TIGR03175 321 IEIVDDIYQYLVSDAVHYDSYEGKNPFAQ 349
AllD COG2055
Malate/lactate/ureidoglycolate dehydrogenase, LDH2 family [Energy production and conversion]; ...
1-335 4.26e-146

Malate/lactate/ureidoglycolate dehydrogenase, LDH2 family [Energy production and conversion]; Malate/lactate/ureidoglycolate dehydrogenase, LDH2 family is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 441658  Cd Length: 337  Bit Score: 415.68  E-value: 4.26e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568   1 MKISRETLHQLIENKLCQAGLKREHAATVAEVLVYADARGIHSHGAVRVEYYAERISKGGTNREPEFRLEETGPCSAILH 80
Cdd:COG2055    1 MRVSAEELRALVARVLLAAGVSEEDAAAVADVLVEADLRGIDSHGVARLPRYVERLRAGGINPNAEPEVVRETPATAVVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568  81 ADNAAGQVAAKMGMEHAIKTAQQNGVAVVGISRMGHSGAISYFVQQAARAGLIGISMCQSDPMVVPFGGAEIYYGTNPLA 160
Cdd:COG2055   81 GDNGLGQVAARRAMELAIEKAKEHGIGAVAVRNSNHFGALGYYAEMAAEAGLIGIAFTNSPPLVAPWGGREPLLGTNPIA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568 161 FAAPGEGDEILTFDMATTVQAWGKVLDARSRNMSIPDTWAVDKNGAPTTDPFAVH---ALLPAAGPKGYGLMMMIDVLSG 237
Cdd:COG2055  161 FAAPRGGGPPFVLDMATSVVARGKIEVAARKGEPIPEGWAVDADGNPTTDPAAALeggALLPLGGHKGYGLALMVELLAG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568 238 VLLGLPFGRQVSSMYDDlHAGRNLGQLHVVINPNFFSSSELFRQHLSQTMRELNAITPAPGFNQVYYPGQDQDIKQRQAA 317
Cdd:COG2055  241 VLSGGGFGPEVSSFYDD-GGPPGLGHFFIAIDPAAFGGLEAFKARMDALLDALRASPPAPGGDPVRLPGEREAAARAERL 319
                        330
                 ....*....|....*...
gi 446626568 318 VEGIEIVDDIYQYLISDA 335
Cdd:COG2055  320 AEGIPLPDALWAELRALA 337
Ldh_2 pfam02615
Malate/L-lactate dehydrogenase; This family consists of bacterial and archaeal Malate ...
6-331 1.92e-142

Malate/L-lactate dehydrogenase; This family consists of bacterial and archaeal Malate/L-lactate dehydrogenase. L-lactate dehydrogenase, EC:1.1.1.27, catalyzes the reaction (S)-lactate + NAD(+) <=> pyruvate + NADH. Malate dehydrogenase, EC:1.1.1.37 and EC:1.1.1.82, catalyzes the reactions: (S)-malate + NAD(+) <=> oxaloacetate + NADH, and (S)-malate + NADP(+) <=> oxaloacetate + NADPH respectively.


Pssm-ID: 460620  Cd Length: 330  Bit Score: 406.06  E-value: 1.92e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568    6 ETLHQLIENKLCQAGLKREHAATVAEVLVYADARGIHSHGAVRVEYYAERISKGGTNREPEFRLEETGPCSAILHADNAA 85
Cdd:pfam02615   1 EELRAFVERVLLAAGVPEEDAEIVADVLVEADLRGVDSHGVNRLPRYVDRIRAGRINPNAEPEVVRETPAVAVVDGDNGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568   86 GQVAAKMGMEHAIKTAQQNGVAVVGISRMGHSGAISYFVQQAARAGLIGISMCQSDPMVVPFGGAEIYYGTNPLAFAAPG 165
Cdd:pfam02615  81 GQVAAHKAMELAIEKAKEHGIGAVAVRNSNHFGAAGYYAEMAAEAGLIGIAFTNSSPLVAPWGGKEPRLGTNPIAFAAPA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568  166 EGDEILTFDMATTVQAWGKVLDARSRNMSIPDTWAVDKNGAPTTDPFAV---HALLPAAGPKGYGLMMMIDVLSGVLLGL 242
Cdd:pfam02615 161 GGGPPFVLDMATSVVARGKIEVAARKGKPIPEGWALDADGNPTTDPAAAlegGALLPLGGHKGYGLALMVELLAGVLSGA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568  243 PFGRQVSSMYDDLHAGRNLGQLHVVINPNFFSSSELFRQHLSQTMRELNAITPAPGFNQVYYPGQDQDIKQRQAAVEGIE 322
Cdd:pfam02615 241 AFGPEVSGDYDPGGPPRKVGHFFIAIDPAAFGDAEEFKARMDALIDELRASPPAPGGDPVYLPGEREAAARAERLREGIP 320

                  ....*....
gi 446626568  323 IVDDIYQYL 331
Cdd:pfam02615 321 LDDAVWAEL 329
PLN00105 PLN00105
malate/L-lactate dehydrogenase; Provisional
20-335 6.18e-53

malate/L-lactate dehydrogenase; Provisional


Pssm-ID: 215057  Cd Length: 330  Bit Score: 177.74  E-value: 6.18e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568  20 GLKREHAATVAEVLVYADARGiHSHGAVRVeyYAERISKGGTNREPEFRLEETgPCSAILHADNAAGQVAAKMGMEHAIK 99
Cdd:PLN00105  13 GYDDEDAEVLLDVMMYAQLRG-NNQGLIKV--TTKGILAPDPNATPITIEHET-KTSAAVDGNKNAGMLVLHHAMDMAID 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568 100 TAQQNGVAVVGISRMG-HSGAISYFVQQAARAGLIGISMCQSDPMVVPFGGAEIYYGTNPLAFAAPGEGDEILTFDMATT 178
Cdd:PLN00105  89 KAKTHGVGIVGTCNTStSTGALGYYAEKVAQQGLIGLVFANSPEFVAPAGGIEPIFGTNPIGVGIPSSDGFPFVLDMATS 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568 179 VQAWGKVLDARSRNMSIPDTWAVDKNGAPTTDPFAV---HALLPAAGPKGYGLMMMIDVLSGVLLGLPFGRQVSSMYddl 255
Cdd:PLN00105 169 AYSFFGLLEAKTAGKKLPRGVAIDKQGILTTDPNEVldgGAIDTFGGYKGSGLALTVELLAGALVGAAWGEDVTGKM--- 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568 256 hAGRNLGQLHVVINPNFFSSSElFRQHLSQTMRELNAITPAPGFNQVYYPGQ-DQDIKQRQAAVEGIEIVDDIYQYLISD 334
Cdd:PLN00105 246 -SAKNWGHLFVAIDPKLLGQDD-FEKNAAEVTQAVKDSKKAPGVDEIWLPGErGNDARVERTAQGGMKVPIPLWKNMKAL 323

                 .
gi 446626568 335 A 335
Cdd:PLN00105 324 A 324
PRK10098 PRK10098
putative dehydrogenase; Provisional
2-335 4.64e-48

putative dehydrogenase; Provisional


Pssm-ID: 182240  Cd Length: 350  Bit Score: 165.21  E-value: 4.64e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568   2 KISRETLHQLIENKLCQAGLKREHAATVAEVLVYADARGIHSHGAVRVEYYAERISKGG--TNREPEFrLEETGPCSAiL 79
Cdd:PRK10098   6 RFDAQTLHSFVQAVWRQAGSEEREAKLVADHLVAANLAGHDSHGVGMIPSYVRSWSQGHlqLNHHAKI-VKDAGAVLT-L 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568  80 HADNAAGQVAAKMGMEHAIKTAQQNGVAVVGISRMGHSGAISYFVQQAARAGLIGISMCQ--SDPMVVPFGGAEIYYGTN 157
Cdd:PRK10098  84 DGDRGFGQVVAHEAMALGIERARQHGICAVALRNSHHIGRIGHWAEQCAAAGLVSIHFVNvvGDPMVAPFHGRDSRFGTN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568 158 PLAFAAPGEGDEILTFDMATTVQAWGKVLDARSRNMSIPDTWAVDKNGAPTTDPFAVH-----ALLPAAGPKGYGLMMMI 232
Cdd:PRK10098 164 PFCVVFPRKGKPPLLLDFATSAIAFGKTRVAWNKGVPVPPGCLIDVNGVPTTDPAVMQesplgALLTFGEHKGYALAAMC 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568 233 DVLSGVLLGlpfGRQVSSMYDD-LHAGRNlGQLHVVINPNFFSSSElfRQHLSQTMRELNAITPAPGFNQVYYPGQDQDI 311
Cdd:PRK10098 244 EILGGALSG---GKTTHQETLQtSDAILN-CMLTIIIDPAAFGAPD--CSAEAEAFVEWVKASPHDGDKPILLPGEPERA 317
                        330       340
                 ....*....|....*....|....
gi 446626568 312 KQRQAAVEGIEIVDDIYQYLISDA 335
Cdd:PRK10098 318 TRAERQAQGIPLDAGTWQQICDAA 341
PRK13260 PRK13260
2,3-diketo-L-gulonate reductase; Provisional
1-333 1.62e-27

2,3-diketo-L-gulonate reductase; Provisional


Pssm-ID: 183926  Cd Length: 332  Bit Score: 110.19  E-value: 1.62e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568   1 MKISRETLHQLIENKLCQAGLKREHAATVAEVLVYADARGIHSHGAVRVEYYAERISKGGT--NREPEfRLEETGpcsAI 78
Cdd:PRK13260   1 MKVTFEELKAAFKRVLLSRGVDEETADACAEMFARTTESGVYSHGVNRFPRFIQQLENGDIipDAQPQ-RVTSLG---AI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568  79 LHAD--NAAGQVAAKMGMEHAIKTAQQNGVAVVGISRMGH---SGAisyFVQQAARAGLIGISMCQSDPMVVPFGGAEIY 153
Cdd:PRK13260  77 EQWDaqRAIGNLTAKKMMDRAIELARDHGIGLVALRNANHwmrGGS---YGWQAAEKGYIGICWTNSIAVMPPWGAKECR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568 154 YGTNPLAFAAPgeGDEILTFDMATTVQAWGKVLDARSRNMSIPDTWAVDKNGAPTTDPFAVHA---LLPAAGPKGYGLMM 230
Cdd:PRK13260 154 IGTNPLIVAIP--STPITMVDMSMSMFSYGMLEVNRLAGRQLPVDGGFDDEGNLTKDPGVIEKnrrILPMGYWKGSGLSI 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446626568 231 MIDVLSGVLLGlpfGRQVSSMYDDLHAGRNLGQLHVVINPNFFSSSELFRQHLSQTMRELNAITPAPGFNQVYYPGQD-- 308
Cdd:PRK13260 232 VLDMIATLLSG---GASVAEVTEDNSDEYGVSQIFIAIEVDKLIDGATRDAKLQRIMDYVTTAERADENQAIRLPGHEft 308
                        330       340
                 ....*....|....*....|....*
gi 446626568 309 QDIKQRQAavEGIEIVDDIYQYLIS 333
Cdd:PRK13260 309 TLLAENRR--NGIPVDDSVWAKIQA 331
 
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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