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Conserved domains on  [gi|446136675|ref|WP_000214530|]
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Ldh family oxidoreductase [Escherichia coli]

Protein Classification

Ldh family oxidoreductase( domain architecture ID 10005235)

Ldh family oxidoreductase is an NAD(P)-dependent oxidoreductase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AllD COG2055
Malate/lactate/ureidoglycolate dehydrogenase, LDH2 family [Energy production and conversion]; ...
4-335 2.42e-131

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: 377.93  E-value: 2.42e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675   4 VYVSEENLKSLVHHKLHTAGLDADTAQQVTDVLIHADITGVHSHGVMRVEHYCTRLAAGGLNKAPQFSIEQISPSVAILD 83
Cdd:COG2055    1 MRVSAEELRALVARVLLAAGVSEEDAAAVADVLVEADLRGIDSHGVARLPRYVERLRAGGINPNAEPEVVRETPATAVVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675  84 SDDGMGHSALISATEHAIKLALEEGLGFVSVKNTSHCGALSYFAEMVTNKGLVAIVMTQTDTCVAPHGGAERFLGTNPIA 163
Cdd:COG2055   81 GDNGLGQVAARRAMELAIEKAKEHGIGAVAVRNSNHFGALGYYAEMAAEAGLIGIAFTNSPPLVAPWGGREPLLGTNPIA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675 164 FGFPVENSHPMIVDMATSATAFGKILHAKETGKHIGEGLAIDKDGYGTTDPHKIEN---LLPFGQHKGSGIALAIDALTG 240
Cdd:COG2055  161 FAAPRGGGPPFVLDMATSVVARGKIEVAARKGEPIPEGWAVDADGNPTTDPAAALEggaLLPLGGHKGYGLALMVELLAG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675 241 MLMNANFGNHIVRMYGDyDKMRKLASLVIAIDPKKLGNP-VFAKTMAQMVTELHAVKPAPGIEKVLAPNDPQMHYKEKCQ 319
Cdd:COG2055  241 VLSGGGFGPEVSSFYDD-GGPPGLGHFFIAIDPAAFGGLeAFKARMDALLDALRASPPAPGGDPVRLPGEREAAARAERL 319
                        330
                 ....*....|....*.
gi 446136675 320 QEGIPVPAGIFHYLAE 335
Cdd:COG2055  320 AEGIPLPDALWAELRA 335
 
Name Accession Description Interval E-value
AllD COG2055
Malate/lactate/ureidoglycolate dehydrogenase, LDH2 family [Energy production and conversion]; ...
4-335 2.42e-131

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: 377.93  E-value: 2.42e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675   4 VYVSEENLKSLVHHKLHTAGLDADTAQQVTDVLIHADITGVHSHGVMRVEHYCTRLAAGGLNKAPQFSIEQISPSVAILD 83
Cdd:COG2055    1 MRVSAEELRALVARVLLAAGVSEEDAAAVADVLVEADLRGIDSHGVARLPRYVERLRAGGINPNAEPEVVRETPATAVVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675  84 SDDGMGHSALISATEHAIKLALEEGLGFVSVKNTSHCGALSYFAEMVTNKGLVAIVMTQTDTCVAPHGGAERFLGTNPIA 163
Cdd:COG2055   81 GDNGLGQVAARRAMELAIEKAKEHGIGAVAVRNSNHFGALGYYAEMAAEAGLIGIAFTNSPPLVAPWGGREPLLGTNPIA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675 164 FGFPVENSHPMIVDMATSATAFGKILHAKETGKHIGEGLAIDKDGYGTTDPHKIEN---LLPFGQHKGSGIALAIDALTG 240
Cdd:COG2055  161 FAAPRGGGPPFVLDMATSVVARGKIEVAARKGEPIPEGWAVDADGNPTTDPAAALEggaLLPLGGHKGYGLALMVELLAG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675 241 MLMNANFGNHIVRMYGDyDKMRKLASLVIAIDPKKLGNP-VFAKTMAQMVTELHAVKPAPGIEKVLAPNDPQMHYKEKCQ 319
Cdd:COG2055  241 VLSGGGFGPEVSSFYDD-GGPPGLGHFFIAIDPAAFGGLeAFKARMDALLDALRASPPAPGGDPVRLPGEREAAARAERL 319
                        330
                 ....*....|....*.
gi 446136675 320 QEGIPVPAGIFHYLAE 335
Cdd:COG2055  320 AEGIPLPDALWAELRA 335
Ldh_2 pfam02615
Malate/L-lactate dehydrogenase; This family consists of bacterial and archaeal Malate ...
9-333 9.43e-129

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: 371.01  E-value: 9.43e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675    9 ENLKSLVHHKLHTAGLDADTAQQVTDVLIHADITGVHSHGVMRVEHYCTRLAAGGLNKAPQFSIEQISPSVAILDSDDGM 88
Cdd:pfam02615   1 EELRAFVERVLLAAGVPEEDAEIVADVLVEADLRGVDSHGVNRLPRYVDRIRAGRINPNAEPEVVRETPAVAVVDGDNGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675   89 GHSALISATEHAIKLALEEGLGFVSVKNTSHCGALSYFAEMVTNKGLVAIVMTQTDTCVAPHGGAERFLGTNPIAFGFPV 168
Cdd:pfam02615  81 GQVAAHKAMELAIEKAKEHGIGAVAVRNSNHFGAAGYYAEMAAEAGLIGIAFTNSSPLVAPWGGKEPRLGTNPIAFAAPA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675  169 ENSHPMIVDMATSATAFGKILHAKETGKHIGEGLAIDKDGYGTTDPHKIEN---LLPFGQHKGSGIALAIDALTGMLMNA 245
Cdd:pfam02615 161 GGGPPFVLDMATSVVARGKIEVAARKGKPIPEGWALDADGNPTTDPAAALEggaLLPLGGHKGYGLALMVELLAGVLSGA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675  246 NFGNHIVRMYGDYDKMRKLASLVIAIDPKKLGNP-VFAKTMAQMVTELHAVKPAPGIEKVLAPNDPQMHYKEKCQQEGIP 324
Cdd:pfam02615 241 AFGPEVSGDYDPGGPPRKVGHFFIAIDPAAFGDAeEFKARMDALIDELRASPPAPGGDPVYLPGEREAAARAERLREGIP 320

                  ....*....
gi 446136675  325 VPAGIFHYL 333
Cdd:pfam02615 321 LDDAVWAEL 329
PRK15025 PRK15025
ureidoglycolate dehydrogenase; Provisional
4-333 7.04e-118

ureidoglycolate dehydrogenase; Provisional


Pssm-ID: 184985  Cd Length: 349  Bit Score: 344.00  E-value: 7.04e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675   4 VYVSEENLKSLVHHKLHTAGLDADTAQQVTDVLIHADITGVHSHGVMRVEHYCTRLAAGGLNKAPQFSIEQISPSVAILD 83
Cdd:PRK15025   1 MKISRETLHQLIKNKLCKAGLKREHAATVAEVLVYADARGIHSHGAVRVEYYAERISKGGTNREPEFRFEETGPCSAILH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675  84 SDDGMGHSALISATEHAIKLALEEGLGFVSVKNTSHCGALSYFAEMVTNKGLVAIVMTQTDTCVAPHGGAERFLGTNPIA 163
Cdd:PRK15025  81 ADNAAGQVAAKMGMEHAIETAKQNGVAVVGISRMGHSGAISYFVQQAARAGLIGLSMCQSDPMVVPFGGAEIYYGTNPLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675 164 FGFPVENSHPMIVDMATSATAFGKILHAKETGKHIGEGLAIDKDGYGTTDPHKIENLLPFGQHKGSGIALAIDALTGMLM 243
Cdd:PRK15025 161 FAAPGEGDEIITFDMATTVQAWGKVLDARSRNMSIPDTWAVDKNGAPTTDPFAVHALLPAAGPKGYGLMMMVDVLSGVLL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675 244 NANFGNHIVRMYGDYDKMRKLASLVIAIDPKKLGNP-VFAKTMAQMVTELHAVKPAPGIEKVLAPNDPQMHYKEKCQQEG 322
Cdd:PRK15025 241 GLPFGRQVSSMYDDLHAGRNLGQLHIVINPAFFSSSeLFRQHISQTMRELNAITPAPGFNQVYYPGQDQDIKQKKAAVEG 320
                        330
                 ....*....|.
gi 446136675 323 IPVPAGIFHYL 333
Cdd:PRK15025 321 IEIVDDIYQYL 331
 
Name Accession Description Interval E-value
AllD COG2055
Malate/lactate/ureidoglycolate dehydrogenase, LDH2 family [Energy production and conversion]; ...
4-335 2.42e-131

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: 377.93  E-value: 2.42e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675   4 VYVSEENLKSLVHHKLHTAGLDADTAQQVTDVLIHADITGVHSHGVMRVEHYCTRLAAGGLNKAPQFSIEQISPSVAILD 83
Cdd:COG2055    1 MRVSAEELRALVARVLLAAGVSEEDAAAVADVLVEADLRGIDSHGVARLPRYVERLRAGGINPNAEPEVVRETPATAVVD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675  84 SDDGMGHSALISATEHAIKLALEEGLGFVSVKNTSHCGALSYFAEMVTNKGLVAIVMTQTDTCVAPHGGAERFLGTNPIA 163
Cdd:COG2055   81 GDNGLGQVAARRAMELAIEKAKEHGIGAVAVRNSNHFGALGYYAEMAAEAGLIGIAFTNSPPLVAPWGGREPLLGTNPIA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675 164 FGFPVENSHPMIVDMATSATAFGKILHAKETGKHIGEGLAIDKDGYGTTDPHKIEN---LLPFGQHKGSGIALAIDALTG 240
Cdd:COG2055  161 FAAPRGGGPPFVLDMATSVVARGKIEVAARKGEPIPEGWAVDADGNPTTDPAAALEggaLLPLGGHKGYGLALMVELLAG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675 241 MLMNANFGNHIVRMYGDyDKMRKLASLVIAIDPKKLGNP-VFAKTMAQMVTELHAVKPAPGIEKVLAPNDPQMHYKEKCQ 319
Cdd:COG2055  241 VLSGGGFGPEVSSFYDD-GGPPGLGHFFIAIDPAAFGGLeAFKARMDALLDALRASPPAPGGDPVRLPGEREAAARAERL 319
                        330
                 ....*....|....*.
gi 446136675 320 QEGIPVPAGIFHYLAE 335
Cdd:COG2055  320 AEGIPLPDALWAELRA 335
Ldh_2 pfam02615
Malate/L-lactate dehydrogenase; This family consists of bacterial and archaeal Malate ...
9-333 9.43e-129

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: 371.01  E-value: 9.43e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675    9 ENLKSLVHHKLHTAGLDADTAQQVTDVLIHADITGVHSHGVMRVEHYCTRLAAGGLNKAPQFSIEQISPSVAILDSDDGM 88
Cdd:pfam02615   1 EELRAFVERVLLAAGVPEEDAEIVADVLVEADLRGVDSHGVNRLPRYVDRIRAGRINPNAEPEVVRETPAVAVVDGDNGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675   89 GHSALISATEHAIKLALEEGLGFVSVKNTSHCGALSYFAEMVTNKGLVAIVMTQTDTCVAPHGGAERFLGTNPIAFGFPV 168
Cdd:pfam02615  81 GQVAAHKAMELAIEKAKEHGIGAVAVRNSNHFGAAGYYAEMAAEAGLIGIAFTNSSPLVAPWGGKEPRLGTNPIAFAAPA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675  169 ENSHPMIVDMATSATAFGKILHAKETGKHIGEGLAIDKDGYGTTDPHKIEN---LLPFGQHKGSGIALAIDALTGMLMNA 245
Cdd:pfam02615 161 GGGPPFVLDMATSVVARGKIEVAARKGKPIPEGWALDADGNPTTDPAAALEggaLLPLGGHKGYGLALMVELLAGVLSGA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675  246 NFGNHIVRMYGDYDKMRKLASLVIAIDPKKLGNP-VFAKTMAQMVTELHAVKPAPGIEKVLAPNDPQMHYKEKCQQEGIP 324
Cdd:pfam02615 241 AFGPEVSGDYDPGGPPRKVGHFFIAIDPAAFGDAeEFKARMDALIDELRASPPAPGGDPVYLPGEREAAARAERLREGIP 320

                  ....*....
gi 446136675  325 VPAGIFHYL 333
Cdd:pfam02615 321 LDDAVWAEL 329
PRK15025 PRK15025
ureidoglycolate dehydrogenase; Provisional
4-333 7.04e-118

ureidoglycolate dehydrogenase; Provisional


Pssm-ID: 184985  Cd Length: 349  Bit Score: 344.00  E-value: 7.04e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675   4 VYVSEENLKSLVHHKLHTAGLDADTAQQVTDVLIHADITGVHSHGVMRVEHYCTRLAAGGLNKAPQFSIEQISPSVAILD 83
Cdd:PRK15025   1 MKISRETLHQLIKNKLCKAGLKREHAATVAEVLVYADARGIHSHGAVRVEYYAERISKGGTNREPEFRFEETGPCSAILH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675  84 SDDGMGHSALISATEHAIKLALEEGLGFVSVKNTSHCGALSYFAEMVTNKGLVAIVMTQTDTCVAPHGGAERFLGTNPIA 163
Cdd:PRK15025  81 ADNAAGQVAAKMGMEHAIETAKQNGVAVVGISRMGHSGAISYFVQQAARAGLIGLSMCQSDPMVVPFGGAEIYYGTNPLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675 164 FGFPVENSHPMIVDMATSATAFGKILHAKETGKHIGEGLAIDKDGYGTTDPHKIENLLPFGQHKGSGIALAIDALTGMLM 243
Cdd:PRK15025 161 FAAPGEGDEIITFDMATTVQAWGKVLDARSRNMSIPDTWAVDKNGAPTTDPFAVHALLPAAGPKGYGLMMMVDVLSGVLL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675 244 NANFGNHIVRMYGDYDKMRKLASLVIAIDPKKLGNP-VFAKTMAQMVTELHAVKPAPGIEKVLAPNDPQMHYKEKCQQEG 322
Cdd:PRK15025 241 GLPFGRQVSSMYDDLHAGRNLGQLHIVINPAFFSSSeLFRQHISQTMRELNAITPAPGFNQVYYPGQDQDIKQKKAAVEG 320
                        330
                 ....*....|.
gi 446136675 323 IPVPAGIFHYL 333
Cdd:PRK15025 321 IEIVDDIYQYL 331
PLN00105 PLN00105
malate/L-lactate dehydrogenase; Provisional
11-329 1.48e-61

malate/L-lactate dehydrogenase; Provisional


Pssm-ID: 215057  Cd Length: 330  Bit Score: 199.69  E-value: 1.48e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675  11 LKSLVHHKLHTAGLDADTAQQVTDVLIHADITGvHSHGVMRVehYCTRLAAGGLNKAPqFSIEQISPSVAILDSDDGMGH 90
Cdd:PLN00105   1 LKETTRKAIKTYGYDDEDAEVLLDVMMYAQLRG-NNQGLIKV--TTKGILAPDPNATP-ITIEHETKTSAAVDGNKNAGM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675  91 SALISATEHAIKLALEEGLGFVSVKNTS-HCGALSYFAEMVTNKGLVAIVMTQTDTCVAPHGGAERFLGTNPIAFGFPVE 169
Cdd:PLN00105  77 LVLHHAMDMAIDKAKTHGVGIVGTCNTStSTGALGYYAEKVAQQGLIGLVFANSPEFVAPAGGIEPIFGTNPIGVGIPSS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675 170 NSHPMIVDMATSATAFGKILHAKETGKHIGEGLAIDKDGYGTTDPHKIEN---LLPFGQHKGSGIALAIDALTGMLMNAN 246
Cdd:PLN00105 157 DGFPFVLDMATSAYSFFGLLEAKTAGKKLPRGVAIDKQGILTTDPNEVLDggaIDTFGGYKGSGLALTVELLAGALVGAA 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675 247 FGNHIVrmygdyDKM--RKLASLVIAIDPKKLGNPVFAKTMAQMVTELHAVKPAPGIEKVLAPNDPQMHY-KEKCQQEGI 323
Cdd:PLN00105 237 WGEDVT------GKMsaKNWGHLFVAIDPKLLGQDDFEKNAAEVTQAVKDSKKAPGVDEIWLPGERGNDArVERTAQGGM 310

                 ....*.
gi 446136675 324 PVPAGI 329
Cdd:PLN00105 311 KVPIPL 316
PRK10098 PRK10098
putative dehydrogenase; Provisional
1-328 3.90e-50

putative dehydrogenase; Provisional


Pssm-ID: 182240  Cd Length: 350  Bit Score: 170.60  E-value: 3.90e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675   1 MTTVYVSEENLKSLVHHKLHTAGLDADTAQQVTDVLIHADITGVHSHGVMRVEHYCTRLAAGGLNKAPQFSIEQISPSVA 80
Cdd:PRK10098   2 ESGHRFDAQTLHSFVQAVWRQAGSEEREAKLVADHLVAANLAGHDSHGVGMIPSYVRSWSQGHLQLNHHAKIVKDAGAVL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675  81 ILDSDDGMGHSALISATEHAIKLALEEGLGFVSVKNTSHCGALSYFAEMVTNKGLVAI--VMTQTDTCVAPHGGAERFLG 158
Cdd:PRK10098  82 TLDGDRGFGQVVAHEAMALGIERARQHGICAVALRNSHHIGRIGHWAEQCAAAGLVSIhfVNVVGDPMVAPFHGRDSRFG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675 159 TNPIAFGFPVENSHPMIVDMATSATAFGKILHAKETGKHIGEGLAIDKDGYGTTDPHKIEN-----LLPFGQHKGSGIAL 233
Cdd:PRK10098 162 TNPFCVVFPRKGKPPLLLDFATSAIAFGKTRVAWNKGVPVPPGCLIDVNGVPTTDPAVMQEsplgaLLTFGEHKGYALAA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675 234 AIDALTGMLMnanfGNHIVRMYGDyDKMRKLAS--LVIAIDPKKLGNPVFAKTMAQMVTELHAVKPApGIEKVLAPNDPQ 311
Cdd:PRK10098 242 MCEILGGALS----GGKTTHQETL-QTSDAILNcmLTIIIDPAAFGAPDCSAEAEAFVEWVKASPHD-GDKPILLPGEPE 315
                        330
                 ....*....|....*..
gi 446136675 312 MHYKEKCQQEGIPVPAG 328
Cdd:PRK10098 316 RATRAERQAQGIPLDAG 332
PRK13260 PRK13260
2,3-diketo-L-gulonate reductase; Provisional
6-329 5.33e-25

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


Pssm-ID: 183926  Cd Length: 332  Bit Score: 102.87  E-value: 5.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675   6 VSEENLKSLVHHKLHTAGLDADTAQQVTDVLIHADITGVHSHGVMRVEHYCTRLAAGGL--NKAPQF-----SIEQisps 78
Cdd:PRK13260   3 VTFEELKAAFKRVLLSRGVDEETADACAEMFARTTESGVYSHGVNRFPRFIQQLENGDIipDAQPQRvtslgAIEQ---- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675  79 vaiLDSDDGMGHSALISATEHAIKLALEEGLGFVSVKNTSHC---GALSYFAemvTNKGLVAIVMTQTDTCVAPHGGAER 155
Cdd:PRK13260  79 ---WDAQRAIGNLTAKKMMDRAIELARDHGIGLVALRNANHWmrgGSYGWQA---AEKGYIGICWTNSIAVMPPWGAKEC 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675 156 FLGTNPIAFGFPvENSHPMiVDMATSATAFGKIlhakETGKHIGEGLAI----DKDGYGTTDPHKIEN---LLPFGQHKG 228
Cdd:PRK13260 153 RIGTNPLIVAIP-STPITM-VDMSMSMFSYGML----EVNRLAGRQLPVdggfDDEGNLTKDPGVIEKnrrILPMGYWKG 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446136675 229 SGIALAIDALTGMLMNanfGNHIVRMYGDYDKMRKLASLVIAIDPKKLGN-PVFAKTMAQMVTELHAVKPAPGIEKVLAP 307
Cdd:PRK13260 227 SGLSIVLDMIATLLSG---GASVAEVTEDNSDEYGVSQIFIAIEVDKLIDgATRDAKLQRIMDYVTTAERADENQAIRLP 303
                        330       340
                 ....*....|....*....|..
gi 446136675 308 NDPQMHYKEKCQQEGIPVPAGI 329
Cdd:PRK13260 304 GHEFTTLLAENRRNGIPVDDSV 325
 
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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