NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|501568763|ref|WP_012573197|]
View 

prephenate dehydrogenase/arogenate dehydrogenase family protein [Candidatus Azobacteroides pseudotrichonymphae]

Protein Classification

prephenate dehydrogenase( domain architecture ID 11416637)

prephenate dehydrogenase catalyzes the conversion of prephenate and NAD(+) to 4-hydroxyphenylpyruvate, CO(2) and NADH

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 1-253 5.11e-43

Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


:

Pssm-ID: 440056 [Multi-domain]  Cd Length: 278  Bit Score: 147.19  E-value: 5.11e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763   1 MKIQIVGAGKMGAFFADVLS---FDHEVAIFDVDPERLRfTYNCIRI-----SHIEEIAHfKPEILINAATVQYTVRAFE 72
Cdd:COG0287    2 MRIAIIGLGLIGGSLALALKragLAHEVVGVDRSPETLE-RALELGVidraaTDLEEAVA-DADLVVLAVPVGATIEVLA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763  73 QILPYLTDSCIISDIASVKTGLKEFYEN---SGHPFVSTHPMFG-----PTFANLSNLSSENAIII--SESGHLGKVFFR 142
Cdd:COG0287   80 ELAPHLKPGAIVTDVGSVKGAVVEAAEAllpDGVRFVGGHPMAGteksgPEAADADLFEGAPYILTptEGTDPEALERVE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763 143 NLYNSLKLNICEYSFEEHDKTVAYSLSIPFASTLIFTSVMKRQEAP-------GTTFRkhmDIAhRLLSEDDYLLTEILF 215
Cdd:COG0287  160 ELWEALGARVVEMDPEEHDRVVAAVSHLPHLLAFALVNTVADLEDEeeilrlaAGGFR---DTT-RIAASDPEMWRDIFL 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 501568763 216 N--PHTSKQLERIQKKLSFLFQIIENKDVQAMKTFLNEVR 253
Cdd:COG0287  236 AnrEALLEALDRFIEELDALRDALEAGDGEALEELLERAR 275
 
Name Accession Description Interval E-value
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 1-253 5.11e-43

Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440056 [Multi-domain]  Cd Length: 278  Bit Score: 147.19  E-value: 5.11e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763   1 MKIQIVGAGKMGAFFADVLS---FDHEVAIFDVDPERLRfTYNCIRI-----SHIEEIAHfKPEILINAATVQYTVRAFE 72
Cdd:COG0287    2 MRIAIIGLGLIGGSLALALKragLAHEVVGVDRSPETLE-RALELGVidraaTDLEEAVA-DADLVVLAVPVGATIEVLA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763  73 QILPYLTDSCIISDIASVKTGLKEFYEN---SGHPFVSTHPMFG-----PTFANLSNLSSENAIII--SESGHLGKVFFR 142
Cdd:COG0287   80 ELAPHLKPGAIVTDVGSVKGAVVEAAEAllpDGVRFVGGHPMAGteksgPEAADADLFEGAPYILTptEGTDPEALERVE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763 143 NLYNSLKLNICEYSFEEHDKTVAYSLSIPFASTLIFTSVMKRQEAP-------GTTFRkhmDIAhRLLSEDDYLLTEILF 215
Cdd:COG0287  160 ELWEALGARVVEMDPEEHDRVVAAVSHLPHLLAFALVNTVADLEDEeeilrlaAGGFR---DTT-RIAASDPEMWRDIFL 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 501568763 216 N--PHTSKQLERIQKKLSFLFQIIENKDVQAMKTFLNEVR 253
Cdd:COG0287  236 AnrEALLEALDRFIEELDALRDALEAGDGEALEELLERAR 275
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
 1-247 2.93e-17

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 80.42  E-value: 2.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763   1 MKIQIVGA-GKMGAFFADVLS-FDHEVAIFDVDPERLRFTYNCIRISHIEE--IAHFKPEILINAATVQYTVRAFEQILP 76
Cdd:PRK08655   1 MKISIIGGtGGLGKWFARFLKeKGFEVIVTGRDPKKGKEVAKELGVEYANDniDAAKDADIVIISVPINVTEDVIKEVAP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763  77 YLTDSCIISDIASVKTG---LKEFYENSGHPFVSTHPMFGPTFANLSNlsseNAIIISESGHLGKVFFRNLYNSLK---L 150
Cdd:PRK08655  81 HVKEGSLLMDVTSVKERpveAMEEYAPEGVEILPTHPMFGPRTPSLKG----QVVILTPTEKRSNPWFDKVKNFLEkegA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763 151 NICEYSFEEHDKTVAYSLS------IPFASTLIF--TSVMKRQEAPGTTFRKHMDIAHRLLSEDDYLLTEI-LFNPHTSK 221
Cdd:PRK08655 157 RVIVTSPEEHDRIMSVVQGlthfayISIASTLKRlgVDIKESRKFASPIYELMIDIIGRILGQNPYLYASIqMNNPQIPE 236

                        250       260       270
                 ....*....|....*....|....*....|
gi 501568763 222 QLERIQKKLSFLFQIIENKD----VQAMKT 247
Cdd:PRK08655 237 IHETFIKECEELSELVKNGDreefVERMKE 266
PDH_N pfam02153
Prephenate dehydrogenase, nucleotide-binding domain; Members of this family are prephenate ...
 21-150 1.91e-06

Prephenate dehydrogenase, nucleotide-binding domain; Members of this family are prephenate dehydrogenases (PDHs) EC:1.3.1.12 involved in tyrosine biosynthesis. This is the N-terminal nucleotide-binding domain of PDHs, which has a modified Rossmann nucleotide-binding fold with an extended beta-sheet sandwiched by three helices on each face.


Pssm-ID: 460467 [Multi-domain]  Cd Length: 154  Bit Score: 46.61  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763   21 FDHEVAIFDVDPE------RLRFTYNCI-RISHIEEIAhfkpeILINAATVQYTVRAFEQILPYLTDSCIISDIASVKTG 93
Cdd:pfam02153  10 FFVTVIGYDINPEaavaalRLGLGDEATdDIEAVREAD-----IVFLAVPVEQTLPVLKELAPHLKEDALITDVGSVKVK 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501568763   94 LKEFYENSG--HPFVSTHPMFGPTF----ANLSNLSSENAIIISESGHLGKVFFRNLYNSLKL 150
Cdd:pfam02153  85 IIRELEQHLpdKSFVPGHPMAGTEKsgpdAARANLFENAPVILTPTEKTDTEALNCVKELLEG 147
GH4_alpha_glucosidase_galactosidase cd05297
Glycoside Hydrolases Family 4; Alpha-glucosidases and alpha-galactosidases; Glucosidases ...
 1-39 2.84e-03

Glycoside Hydrolases Family 4; Alpha-glucosidases and alpha-galactosidases; Glucosidases cleave glycosidic bonds to release glucose from oligosaccharides. Alpha-glucosidases and alpha-galactosidases release alpha-D-glucose and alpha-D-galactose, respectively, via the hydrolysis of alpha-glycopyranoside bonds. Some bacteria simultaneously translocate and phosphorylate disaccharides via the phosphoenolpyruvate-dependent phosphotransferase system (PEP-PTS). After translocation, these phospho-disaccharides may be hydrolyzed by the GH4 glycoside hydrolases such as the alpha-glucosidases. Other organsisms (such as archaea and Thermotoga maritima) lack the PEP-PTS system, but have several enzymes normally associated with the PEP-PTS operon. Alpha-glucosidases and alpha-galactosidases are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133433 [Multi-domain]  Cd Length: 423  Bit Score: 38.70  E-value: 2.84e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 501568763   1 MKIQIVGAGKMG---AFFADVLSF----DHEVAIFDVDPERLRFTY 39
Cdd:cd05297    1 IKIAFIGAGSVVftkNLVGDLLKTpelsGSTIALMDIDEERLETVE 46
 
Name Accession Description Interval E-value
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 1-253 5.11e-43

Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440056 [Multi-domain]  Cd Length: 278  Bit Score: 147.19  E-value: 5.11e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763   1 MKIQIVGAGKMGAFFADVLS---FDHEVAIFDVDPERLRfTYNCIRI-----SHIEEIAHfKPEILINAATVQYTVRAFE 72
Cdd:COG0287    2 MRIAIIGLGLIGGSLALALKragLAHEVVGVDRSPETLE-RALELGVidraaTDLEEAVA-DADLVVLAVPVGATIEVLA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763  73 QILPYLTDSCIISDIASVKTGLKEFYEN---SGHPFVSTHPMFG-----PTFANLSNLSSENAIII--SESGHLGKVFFR 142
Cdd:COG0287   80 ELAPHLKPGAIVTDVGSVKGAVVEAAEAllpDGVRFVGGHPMAGteksgPEAADADLFEGAPYILTptEGTDPEALERVE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763 143 NLYNSLKLNICEYSFEEHDKTVAYSLSIPFASTLIFTSVMKRQEAP-------GTTFRkhmDIAhRLLSEDDYLLTEILF 215
Cdd:COG0287  160 ELWEALGARVVEMDPEEHDRVVAAVSHLPHLLAFALVNTVADLEDEeeilrlaAGGFR---DTT-RIAASDPEMWRDIFL 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 501568763 216 N--PHTSKQLERIQKKLSFLFQIIENKDVQAMKTFLNEVR 253
Cdd:COG0287  236 AnrEALLEALDRFIEELDALRDALEAGDGEALEELLERAR 275
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
 1-247 2.93e-17

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 80.42  E-value: 2.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763   1 MKIQIVGA-GKMGAFFADVLS-FDHEVAIFDVDPERLRFTYNCIRISHIEE--IAHFKPEILINAATVQYTVRAFEQILP 76
Cdd:PRK08655   1 MKISIIGGtGGLGKWFARFLKeKGFEVIVTGRDPKKGKEVAKELGVEYANDniDAAKDADIVIISVPINVTEDVIKEVAP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763  77 YLTDSCIISDIASVKTG---LKEFYENSGHPFVSTHPMFGPTFANLSNlsseNAIIISESGHLGKVFFRNLYNSLK---L 150
Cdd:PRK08655  81 HVKEGSLLMDVTSVKERpveAMEEYAPEGVEILPTHPMFGPRTPSLKG----QVVILTPTEKRSNPWFDKVKNFLEkegA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763 151 NICEYSFEEHDKTVAYSLS------IPFASTLIF--TSVMKRQEAPGTTFRKHMDIAHRLLSEDDYLLTEI-LFNPHTSK 221
Cdd:PRK08655 157 RVIVTSPEEHDRIMSVVQGlthfayISIASTLKRlgVDIKESRKFASPIYELMIDIIGRILGQNPYLYASIqMNNPQIPE 236

                        250       260       270
                 ....*....|....*....|....*....|
gi 501568763 222 QLERIQKKLSFLFQIIENKD----VQAMKT 247
Cdd:PRK08655 237 IHETFIKECEELSELVKNGDreefVERMKE 266
tyrA PRK11199
bifunctional chorismate mutase/prephenate dehydrogenase; Provisional
 2-119 4.10e-09

bifunctional chorismate mutase/prephenate dehydrogenase; Provisional


Pssm-ID: 183035 [Multi-domain]  Cd Length: 374  Bit Score: 56.42  E-value: 4.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763   2 KIQIVG-AGKMGAFFADVLSF-DHEVAIFDVDperlrftyncirishieEIAHFKpEILINAATVQYTV--RAFEQI--- 74
Cdd:PRK11199 100 PVVIVGgKGQLGRLFAKMLTLsGYQVRILEQD-----------------DWDRAE-DILADAGMVIVSVpiHLTEEViar 161

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 501568763  75 LPYLTDSCIISDIASVKTG-LKEFYE-NSGhPFVSTHPMFGPTFANL 119
Cdd:PRK11199 162 LPPLPEDCILVDLTSVKNApLQAMLAaHSG-PVLGLHPMFGPDVGSL 207
PDH_N pfam02153
Prephenate dehydrogenase, nucleotide-binding domain; Members of this family are prephenate ...
 21-150 1.91e-06

Prephenate dehydrogenase, nucleotide-binding domain; Members of this family are prephenate dehydrogenases (PDHs) EC:1.3.1.12 involved in tyrosine biosynthesis. This is the N-terminal nucleotide-binding domain of PDHs, which has a modified Rossmann nucleotide-binding fold with an extended beta-sheet sandwiched by three helices on each face.


Pssm-ID: 460467 [Multi-domain]  Cd Length: 154  Bit Score: 46.61  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763   21 FDHEVAIFDVDPE------RLRFTYNCI-RISHIEEIAhfkpeILINAATVQYTVRAFEQILPYLTDSCIISDIASVKTG 93
Cdd:pfam02153  10 FFVTVIGYDINPEaavaalRLGLGDEATdDIEAVREAD-----IVFLAVPVEQTLPVLKELAPHLKEDALITDVGSVKVK 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501568763   94 LKEFYENSG--HPFVSTHPMFGPTF----ANLSNLSSENAIIISESGHLGKVFFRNLYNSLKL 150
Cdd:pfam02153  85 IIRELEQHLpdKSFVPGHPMAGTEKsgpdAARANLFENAPVILTPTEKTDTEALNCVKELLEG 147
PRK08507 PRK08507
prephenate dehydrogenase; Validated
 1-192 9.65e-06

prephenate dehydrogenase; Validated


Pssm-ID: 181452 [Multi-domain]  Cd Length: 275  Bit Score: 45.66  E-value: 9.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763   1 MKIQIVGAGKMGAFFADVL---SFDHEVAIFDVDPERLRftyNCIRISHIEEIAHF----KPEILINAATVQYTVRAFEQ 73
Cdd:PRK08507   1 MKIGIIGLGLMGGSLGLALkekGLISKVYGYDHNELHLK---KALELGLVDEIVSFeelkKCDVIFLAIPVDAIIEILPK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763  74 ILPyLTDSCIISDIASVKTG-LKEFYENSGHPFVSTHPM-----FGPTfANLSNLSSENAIII---SESGHLGKVFFRNL 144
Cdd:PRK08507  78 LLD-IKENTTIIDLGSTKAKiIESVPKHIRKNFIAAHPMagtenSGPK-AAIKGLYEGKVVVLcdvEKSGEKHQERAKEI 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 501568763 145 YNSLKLNICEYSFEEHDKTVAYSLSIPFASTL-IFTSVMKrQEAPGTTF 192
Cdd:PRK08507 156 FSGLGMRIVYMDAKEHDLHAAYISHLPHIISFaLANTVLK-EEDERNIF 203
PRK07417 PRK07417
prephenate/arogenate dehydrogenase;
72-165 1.49e-04

prephenate/arogenate dehydrogenase;


Pssm-ID: 180970 [Multi-domain]  Cd Length: 279  Bit Score: 42.19  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763  72 EQILPYLTDSCIISDIASVKTGLKEFYENSgHP-FVSTHPMFGPTF----ANLSNLSSENAIII-----SESGHLGKVff 141
Cdd:PRK07417  75 EQLIPALPPEAIVTDVGSVKAPIVEAWEKL-HPrFVGSHPMAGTAEsgveAGQRGLFKNRPWVLtptenTDLNALAIV-- 151

                         90       100
                 ....*....|....*....|....
gi 501568763 142 RNLYNSLKLNICEYSFEEHDKTVA 165
Cdd:PRK07417 152 EELAVSLGSKIYTADPEEHDRAVA 175
trkA PRK09496
Trk system potassium transporter TrkA;
1-36 1.73e-04

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 42.42  E-value: 1.73e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 501568763   1 MKIQIVGAGKMGAFFADVLSF-DHEVAIFDVDPERLR 36
Cdd:PRK09496   1 MKIIIVGAGQVGYTLAENLSGeNNDVTVIDTDEERLR 37
PRK06545 PRK06545
prephenate dehydrogenase; Validated
 5-113 9.93e-04

prephenate dehydrogenase; Validated


Pssm-ID: 235824 [Multi-domain]  Cd Length: 359  Bit Score: 39.89  E-value: 9.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763   5 IVGAGKMGAFFADVLSFDH-EVAIFDVDPERLRFTYNCiRISHIEEIAHF------KPEILINAATVQYTVRAFEQILPY 77
Cdd:PRK06545   5 IVGLGLIGGSLALAIKAAGpDVFIIGYDPSAAQLARAL-GFGVIDELAADlqraaaEADLIVLAVPVDATAALLAELADL 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 501568763  78 -LTDSCIISDIASVKTG---LKEFYENSGHPFVSTHPMFG 113
Cdd:PRK06545  84 eLKPGVIVTDVGSVKGAilaEAEALLGDLIRFVGGHPMAG 123
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
 2-245 1.02e-03

bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; Provisional


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 40.36  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763   2 KIQIVGAGKMGAFFADVL---SFDHEVAIFDVDPERLRFTYNCIRISHIEE-IAHF--KPEILINAATVQYTVRAFEQIL 75
Cdd:PRK14806   5 RVVVIGLGLIGGSFAKALrerGLAREVVAVDRRAKSLELAVSLGVIDRGEEdLAEAvsGADVIVLAVPVLAMEKVLADLK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763  76 PYLTDSCIISDIASVKTGL----KEFYENSGHPFVSTHPMFGptfANLSNLSSENA-------IIISESGH-----LGKV 139
Cdd:PRK14806  85 PLLSEHAIVTDVGSTKGNVvdaaRAVFGELPAGFVPGHPIAG---SEKSGVHAANAdlfrnhkVILTPLAEtdpaaLARV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763 140 ffRNLYNSLKLNICEYSFEEHDKTVAYSLSIP--FASTLIfTSVMKRQE-------APGtTFRKHMDIAhrllSEDDYLL 210
Cdd:PRK14806 162 --DRLWRAVGADVLHMDVAHHDEVLAATSHLPhlLAFSLV-DQLANREDnldifryAAG-GFRDFTRIA----ASDPVMW 233

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 501568763 211 TEILF--NPHTSKQLERIQKKLSFLFQIIENKDVQAM 245
Cdd:PRK14806 234 HDIFLanKEAVLRALDHFRDDLDALRAAIEAGDGHAL 270
PRK06444 PRK06444
prephenate dehydrogenase; Provisional
 86-219 1.99e-03

prephenate dehydrogenase; Provisional


Pssm-ID: 102381 [Multi-domain]  Cd Length: 197  Bit Score: 38.29  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763  86 DIASVKTGLKEFyenSGHpFVSTHPMFGPtfANLSNLSSENAIIISEsghLGKVFFRNLYNSLKLN--ICEYSFEEHDKT 163
Cdd:PRK06444  57 EISSVKWPFKKY---SGK-IVSIHPLFGP--MSYNDGVHRTVIFIND---ISRDNYLNEINEMFRGyhFVEMTADEHDLL 127

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 501568763 164 VAYSLSIPFASTLIftsvMKRQEAPGTT--FRKHMDIAHRLLSED-DYLLTEILFNPHT 219
Cdd:PRK06444 128 MSEIMVKPYIISMI----LKDIKSDIKTgsFDKLLEVSEIKEKENwEVFNDTIIYNPYT 182
PRK05472 PRK05472
redox-sensing transcriptional repressor Rex; Provisional
 2-59 2.59e-03

redox-sensing transcriptional repressor Rex; Provisional


Pssm-ID: 235486 [Multi-domain]  Cd Length: 213  Bit Score: 38.17  E-value: 2.59e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501568763   2 KIQIVGAGKMGAFFADVLSFDHE----VAIFDVDPERLRFTYNCIRISHIEE----IAHFKPEILI 59
Cdd:PRK05472  86 NVALVGAGNLGRALLNYNGFEKRgfkiVAAFDVDPEKIGTKIGGIPVYHIDEleevVKENDIEIGI 151
GH4_alpha_glucosidase_galactosidase cd05297
Glycoside Hydrolases Family 4; Alpha-glucosidases and alpha-galactosidases; Glucosidases ...
 1-39 2.84e-03

Glycoside Hydrolases Family 4; Alpha-glucosidases and alpha-galactosidases; Glucosidases cleave glycosidic bonds to release glucose from oligosaccharides. Alpha-glucosidases and alpha-galactosidases release alpha-D-glucose and alpha-D-galactose, respectively, via the hydrolysis of alpha-glycopyranoside bonds. Some bacteria simultaneously translocate and phosphorylate disaccharides via the phosphoenolpyruvate-dependent phosphotransferase system (PEP-PTS). After translocation, these phospho-disaccharides may be hydrolyzed by the GH4 glycoside hydrolases such as the alpha-glucosidases. Other organsisms (such as archaea and Thermotoga maritima) lack the PEP-PTS system, but have several enzymes normally associated with the PEP-PTS operon. Alpha-glucosidases and alpha-galactosidases are part of the NAD(P)-binding Rossmann fold superfamily, which includes a wide variety of protein families including the NAD(P)-binding domains of alcohol dehydrogenases, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate dehydrogenases, formate/glycerate dehydrogenases, siroheme synthases, 6-phosphogluconate dehydrogenases, aminoacid dehydrogenases, repressor rex, and NAD-binding potassium channel domains, among others.


Pssm-ID: 133433 [Multi-domain]  Cd Length: 423  Bit Score: 38.70  E-value: 2.84e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 501568763   1 MKIQIVGAGKMG---AFFADVLSF----DHEVAIFDVDPERLRFTY 39
Cdd:cd05297    1 IKIAFIGAGSVVftkNLVGDLLKTpelsGSTIALMDIDEERLETVE 46
PRK15076 PRK15076
alpha-galactosidase; Provisional
 1-36 3.13e-03

alpha-galactosidase; Provisional


Pssm-ID: 185035 [Multi-domain]  Cd Length: 431  Bit Score: 38.66  E-value: 3.13e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 501568763   1 MKIQIVGAGKMGaF----FADVLSF----DHEVAIFDVDPERLR 36
Cdd:PRK15076   2 PKITFIGAGSTV-FtknlLGDILSVpalrDAEIALMDIDPERLE 44
PLN02712 PLN02712
arogenate dehydrogenase
 1-114 3.67e-03

arogenate dehydrogenase


Pssm-ID: 215382 [Multi-domain]  Cd Length: 667  Bit Score: 38.42  E-value: 3.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763   1 MKIQIVGAGKMGAFFADVL-SFDHEV-----AIFDVDPERLRFTYncirISHIEEIAHFKPEILINAATVQYTVRAFEQi 74
Cdd:PLN02712 370 LKIAIVGFGNFGQFLAKTMvKQGHTVlaysrSDYSDEAQKLGVSY----FSDADDLCEEHPEVILLCTSILSTEKVLKS- 444

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 501568763  75 LPY--LTDSCIISDIASVKtglkEFYEN-------SGHPFVSTHPMFGP 114
Cdd:PLN02712 445 LPFqrLKRSTLFVDVLSVK----EFPRNlflqhlpQDFDILCTHPMFGP 489
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
 3-84 6.81e-03

Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also known as ketopantoate reductases, EC:1.1.1.169. The reaction catalyzed by this enzyme is: (R)-pantoate + NADP(+) <=> 2-dehydropantoate + NADPH. AbpA catalyzes the NADPH reduction of ketopantoic acid to pantoic acid in the alternative pyrimidine biosynthetic (APB) pathway. ApbA and PanE are allelic. ApbA, the ketopantoate reductase enzyme is required for the synthesis of thiamine via the APB biosynthetic pathway.


Pssm-ID: 426831 [Multi-domain]  Cd Length: 147  Bit Score: 36.06  E-value: 6.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501568763    3 IQIVGAGKMGAFFADVLSF-DHEVAIFDVDPERLRFTYNCIRISHIEEIAHFKPEILINAA-----------TV--QYTV 68
Cdd:pfam02558   1 IAILGAGAIGSLLGARLAKaGHDVTLILRGAELAAIKKNGLRLTSPGGERIVPPPAVTSASeslgpidlvivTVkaYQTE 80

                          90
                  ....*....|....*.
gi 501568763   69 RAFEQILPYLTDSCII 84
Cdd:pfam02558  81 EALEDIAPLLGPNTVV 96
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-36 6.90e-03

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 37.21  E-value: 6.90e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 501568763   1 MKIQIVGAGKMGAFFADVLSFDHE---VAIFDVDPERLR 36
Cdd:COG0673    4 LRVGIIGAGGIGRAHAPALAALPGvelVAVADRDPERAE 42
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 1-36 8.51e-03

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 36.97  E-value: 8.51e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 501568763   1 MKIQIVGAGKMGAFFADVLS-FDHEVAIFDVDPERLR 36
Cdd:COG0569   96 MHVIIIGAGRVGRSLARELEeEGHDVVVIDKDPERVE 132
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH