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Conserved domains on  [gi|2734719472|ref|WP_346701022|]
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prephenate dehydrogenase/arogenate dehydrogenase family protein [Barnesiella sp. An22]

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

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List of domain hits

 Name Accession Description Interval E-value
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 1-254 1.87e-46

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: 156.05  E-value: 1.87e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472   1 MKIVILGAGKMGSFFADVLS---FDHEVALYDVDPQRLRFAfntLRM-------TRPEEIGEFApDLVINAATVKYTIEA 70
Cdd:COG0287     2 MRIAIIGLGLIGGSLALALKragLAHEVVGVDRSPETLERA---LELgvidraaTDLEEAVADA-DLVVLAVPVGATIEV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472  71 FESVLPYLPARTILSDIASVKTGLPEFYARA---GHPFVSTHPMFG-----PTFANlSDLSTQHAIIIT---EGDHLGKV 139
Cdd:COG0287    78 LAELAPHLKPGAIVTDVGSVKGAVVEAAEALlpdGVRFVGGHPMAGteksgPEAAD-ADLFEGAPYILTpteGTDPEALE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472 140 FFKDIYQRLRLNIFEYSFREHDETIAYSLSIPFTSTLVFASIMKHQDAP-------GTTFKkhmDIARgLLSEDDYLLTE 212
Cdd:COG0287   157 RVEELWEALGARVVEMDPEEHDRVVAAVSHLPHLLAFALVNTVADLEDEeeilrlaAGGFR---DTTR-IAASDPEMWRD 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2734719472 213 ILFN--PNTPQQVRQIQEQLSVLLDIVEQKDTDRMKEYLTRVRK 254
Cdd:COG0287   233 IFLAnrEALLEALDRFIEELDALRDALEAGDGEALEELLERARA 276
 
Name Accession Description Interval E-value
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 1-254 1.87e-46

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: 156.05  E-value: 1.87e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472   1 MKIVILGAGKMGSFFADVLS---FDHEVALYDVDPQRLRFAfntLRM-------TRPEEIGEFApDLVINAATVKYTIEA 70
Cdd:COG0287     2 MRIAIIGLGLIGGSLALALKragLAHEVVGVDRSPETLERA---LELgvidraaTDLEEAVADA-DLVVLAVPVGATIEV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472  71 FESVLPYLPARTILSDIASVKTGLPEFYARA---GHPFVSTHPMFG-----PTFANlSDLSTQHAIIIT---EGDHLGKV 139
Cdd:COG0287    78 LAELAPHLKPGAIVTDVGSVKGAVVEAAEALlpdGVRFVGGHPMAGteksgPEAAD-ADLFEGAPYILTpteGTDPEALE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472 140 FFKDIYQRLRLNIFEYSFREHDETIAYSLSIPFTSTLVFASIMKHQDAP-------GTTFKkhmDIARgLLSEDDYLLTE 212
Cdd:COG0287   157 RVEELWEALGARVVEMDPEEHDRVVAAVSHLPHLLAFALVNTVADLEDEeeilrlaAGGFR---DTTR-IAASDPEMWRD 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2734719472 213 ILFN--PNTPQQVRQIQEQLSVLLDIVEQKDTDRMKEYLTRVRK 254
Cdd:COG0287   233 IFLAnrEALLEALDRFIEELDALRDALEAGDGEALEELLERARA 276
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
 1-257 5.86e-17

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 79.65  E-value: 5.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472   1 MKIVILGA-GKMGSFFADVLS-FDHEVALYDVDPQRLRFAfntlrmtrPEEIG-EFAPDLVINAAT-----VKYTIEAFE 72
Cdd:PRK08655    1 MKISIIGGtGGLGKWFARFLKeKGFEVIVTGRDPKKGKEV--------AKELGvEYANDNIDAAKDadiviISVPINVTE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472  73 SVL----PYLPARTILSDIASVKTG---LPEFYARAGHPFVSTHPMFGPTfanLSDLSTQhAIIITEGDHLGKVFFKDIY 145
Cdd:PRK08655   73 DVIkevaPHVKEGSLLMDVTSVKERpveAMEEYAPEGVEILPTHPMFGPR---TPSLKGQ-VVILTPTEKRSNPWFDKVK 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472 146 QRLR---LNIFEYSFREHDETIAYSLSIPFTSTLVFASIMKH--------QDAPGTTFKKHMDIARGLLSEDDYLLTEI- 213
Cdd:PRK08655  149 NFLEkegARVIVTSPEEHDRIMSVVQGLTHFAYISIASTLKRlgvdikesRKFASPIYELMIDIIGRILGQNPYLYASIq 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2734719472 214 LFNPNTPQQVRQIQEQLSVLLDIVEQKDTDRMKEYLTRVRKNIE 257
Cdd:PRK08655  229 MNNPQIPEIHETFIKECEELSELVKNGDREEFVERMKEAAKHFG 272
PDH_N pfam02153
Prephenate dehydrogenase, nucleotide-binding domain; Members of this family are prephenate ...
 21-145 9.27e-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: 44.68  E-value: 9.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472  21 FDHEVALYDVDPQ------RLRFAFNtlRMTRPEEIGEFapDLVINAATVKYTIEAFESVLPYLPARTILSDIASVKTG- 93
Cdd:pfam02153  10 FFVTVIGYDINPEaavaalRLGLGDE--ATDDIEAVREA--DIVFLAVPVEQTLPVLKELAPHLKEDALITDVGSVKVKi 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2734719472  94 ---LPEFYARAGhpFVSTHPMFGPTF----ANLSDLSTQHAIIITEGDHLGKVFFKDIY 145
Cdd:pfam02153  86 ireLEQHLPDKS--FVPGHPMAGTEKsgpdAARANLFENAPVILTPTEKTDTEALNCVK 142
GH4_alpha_glucosidase_galactosidase cd05297
Glycoside Hydrolases Family 4; Alpha-glucosidases and alpha-galactosidases; Glucosidases ...
 1-74 1.10e-04

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: 42.94  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472   1 MKIVILGAGKMG---SFFADVLSF----DHEVALYDVDPQRLRFAFNTL-RMTrpEEIG-----EFAPDL---------V 58
Cdd:cd05297     1 IKIAFIGAGSVVftkNLVGDLLKTpelsGSTIALMDIDEERLETVEILAkKIV--EELGaplkiEATTDRrealdgadfV 78

                          90
                  ....*....|....*.
gi 2734719472  59 INAATVKYTiEAFESV 74
Cdd:cd05297    79 INTIQVGGH-EYTETD 93
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 2-62 2.14e-04

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 40.57  E-value: 2.14e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2734719472    2 KIVILGAGKMGSFFADVL-SFDHEVALYDVDPQRLRFA-------FNTLrMTRPEEIGEFAP--DLVINAA 62
Cdd:smart01002  22 KVVVIGAGVVGLGAAATAkGLGAEVTVLDVRPARLRQLesllgarFTTL-YSQAELLEEAVKeaDLVIGAV 91
 
Name Accession Description Interval E-value
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 1-254 1.87e-46

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: 156.05  E-value: 1.87e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472   1 MKIVILGAGKMGSFFADVLS---FDHEVALYDVDPQRLRFAfntLRM-------TRPEEIGEFApDLVINAATVKYTIEA 70
Cdd:COG0287     2 MRIAIIGLGLIGGSLALALKragLAHEVVGVDRSPETLERA---LELgvidraaTDLEEAVADA-DLVVLAVPVGATIEV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472  71 FESVLPYLPARTILSDIASVKTGLPEFYARA---GHPFVSTHPMFG-----PTFANlSDLSTQHAIIIT---EGDHLGKV 139
Cdd:COG0287    78 LAELAPHLKPGAIVTDVGSVKGAVVEAAEALlpdGVRFVGGHPMAGteksgPEAAD-ADLFEGAPYILTpteGTDPEALE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472 140 FFKDIYQRLRLNIFEYSFREHDETIAYSLSIPFTSTLVFASIMKHQDAP-------GTTFKkhmDIARgLLSEDDYLLTE 212
Cdd:COG0287   157 RVEELWEALGARVVEMDPEEHDRVVAAVSHLPHLLAFALVNTVADLEDEeeilrlaAGGFR---DTTR-IAASDPEMWRD 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2734719472 213 ILFN--PNTPQQVRQIQEQLSVLLDIVEQKDTDRMKEYLTRVRK 254
Cdd:COG0287   233 IFLAnrEALLEALDRFIEELDALRDALEAGDGEALEELLERARA 276
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
 1-257 5.86e-17

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 79.65  E-value: 5.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472   1 MKIVILGA-GKMGSFFADVLS-FDHEVALYDVDPQRLRFAfntlrmtrPEEIG-EFAPDLVINAAT-----VKYTIEAFE 72
Cdd:PRK08655    1 MKISIIGGtGGLGKWFARFLKeKGFEVIVTGRDPKKGKEV--------AKELGvEYANDNIDAAKDadiviISVPINVTE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472  73 SVL----PYLPARTILSDIASVKTG---LPEFYARAGHPFVSTHPMFGPTfanLSDLSTQhAIIITEGDHLGKVFFKDIY 145
Cdd:PRK08655   73 DVIkevaPHVKEGSLLMDVTSVKERpveAMEEYAPEGVEILPTHPMFGPR---TPSLKGQ-VVILTPTEKRSNPWFDKVK 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472 146 QRLR---LNIFEYSFREHDETIAYSLSIPFTSTLVFASIMKH--------QDAPGTTFKKHMDIARGLLSEDDYLLTEI- 213
Cdd:PRK08655  149 NFLEkegARVIVTSPEEHDRIMSVVQGLTHFAYISIASTLKRlgvdikesRKFASPIYELMIDIIGRILGQNPYLYASIq 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2734719472 214 LFNPNTPQQVRQIQEQLSVLLDIVEQKDTDRMKEYLTRVRKNIE 257
Cdd:PRK08655  229 MNNPQIPEIHETFIKECEELSELVKNGDREEFVERMKEAAKHFG 272
PRK08507 PRK08507
prephenate dehydrogenase; Validated
 1-186 4.35e-09

prephenate dehydrogenase; Validated


Pssm-ID: 181452 [Multi-domain]  Cd Length: 275  Bit Score: 55.67  E-value: 4.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472   1 MKIVILGAGKMGSFFADVL---SFDHEVALYDVDPQRLRFAfntLRMTRPEEIGEF----APDLVINAATVKYTIEAFES 73
Cdd:PRK08507    1 MKIGIIGLGLMGGSLGLALkekGLISKVYGYDHNELHLKKA---LELGLVDEIVSFeelkKCDVIFLAIPVDAIIEILPK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472  74 VLPYLPARTILsDIASVKTGLPEfyARAGH---PFVSTHPM-----FGPTfANLSDLSTQHAIIITE-----GDHLGKVf 140
Cdd:PRK08507   78 LLDIKENTTII-DLGSTKAKIIE--SVPKHirkNFIAAHPMagtenSGPK-AAIKGLYEGKVVVLCDveksgEKHQERA- 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2734719472 141 fKDIYQRLRLNIFEYSFREHDETIAYSLSIPFTSTLVFA-SIMKHQD 186
Cdd:PRK08507  153 -KEIFSGLGMRIVYMDAKEHDLHAAYISHLPHIISFALAnTVLKEED 198
tyrA PRK11199
bifunctional chorismate mutase/prephenate dehydrogenase; Provisional
 2-119 1.80e-08

bifunctional chorismate mutase/prephenate dehydrogenase; Provisional


Pssm-ID: 183035 [Multi-domain]  Cd Length: 374  Bit Score: 54.11  E-value: 1.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472   2 KIVILG-AGKMGSFFADVLSF-DHEVALYDVDpqrlrfafntlRMTRPEEIGEFApDLVINAATVKYTIEAFESvLPYLP 79
Cdd:PRK11199  100 PVVIVGgKGQLGRLFAKMLTLsGYQVRILEQD-----------DWDRAEDILADA-GMVIVSVPIHLTEEVIAR-LPPLP 166

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2734719472  80 ARTILSDIASVKTGlPEFYARAGH--PFVSTHPMFGPTFANL 119
Cdd:PRK11199  167 EDCILVDLTSVKNA-PLQAMLAAHsgPVLGLHPMFGPDVGSL 207
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
 2-253 9.34e-07

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


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 49.61  E-value: 9.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472   2 KIVILGAGKMGSFFADVL---SFDHEVALYDVDPQRLRFAFNTLRMTRPEE-IGEF--APDLVINAATVKYTIEAFESVL 75
Cdd:PRK14806    5 RVVVIGLGLIGGSFAKALrerGLAREVVAVDRRAKSLELAVSLGVIDRGEEdLAEAvsGADVIVLAVPVLAMEKVLADLK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472  76 PYLPARTILSDIASVKTGLPEFYARA--GHP--FVSTHPMFGP----TFANLSDLSTQHAIIITEGDH-----LGKVffK 142
Cdd:PRK14806   85 PLLSEHAIVTDVGSTKGNVVDAARAVfgELPagFVPGHPIAGSeksgVHAANADLFRNHKVILTPLAEtdpaaLARV--D 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472 143 DIYQRLRLNIFEYSFREHDETIAYSLSIP----FTSTLVFASIMKHQD----APGtTFKKHMDIArgllSEDDYLLTEIl 214
Cdd:PRK14806  163 RLWRAVGADVLHMDVAHHDEVLAATSHLPhllaFSLVDQLANREDNLDifryAAG-GFRDFTRIA----ASDPVMWHDI- 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2734719472 215 FNPNTPQQVRQIQE---QLSVLLDIVEQKDTDRMKEYLTRVR 253
Cdd:PRK14806  237 FLANKEAVLRALDHfrdDLDALRAAIEAGDGHALLGVFTRAR 278
PRK07530 PRK07530
3-hydroxybutyryl-CoA dehydrogenase; Validated
 2-84 1.61e-06

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181018 [Multi-domain]  Cd Length: 292  Bit Score: 48.08  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472   2 KIVILGAGKMGSFFADVLSF-DHEVALYDVDPQRLRFAFNTL-----------------------RMTRPEEIGEFAP-D 56
Cdd:PRK07530    6 KVGVIGAGQMGNGIAHVCALaGYDVLLNDVSADRLEAGLATIngnlarqvakgkiseearaaalaRISTATDLEDLADcD 85

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2734719472  57 LVINAAT----VKYTIeaFESVLPYLPARTIL 84
Cdd:PRK07530   86 LVIEAATedetVKRKI--FAQLCPVLKPEAIL 115
PLN02712 PLN02712
arogenate dehydrogenase
 1-226 2.23e-06

arogenate dehydrogenase


Pssm-ID: 215382 [Multi-domain]  Cd Length: 667  Bit Score: 48.44  E-value: 2.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472   1 MKIVILGAGKMGSFFADVL------SFDHEVALYDVDPQRLRFAFntlrMTRPEEIGEFAPDLVINAATvkytIEAFESV 74
Cdd:PLN02712   53 LKIAIIGFGNYGQFLAKTLisqghtVLAHSRSDHSLAARSLGVSF----FLDPHDLCERHPDVILLCTS----IISTENV 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472  75 LPYLPAR-----TILSDIASVKtglpEF-------YARAGHPFVSTHPMFGPTFANLS----DLSTQHAIIITEGDHLGK 138
Cdd:PLN02712  125 LKSLPLQrlkrnTLFVDVLSVK----EFaknllldYLPEDFDIICSHPMFGPQSAKHGwdglRFVYEKVRIGNEELRVSR 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472 139 V-FFKDIYQRLRLNIFEYSFREHDETIAYSLSIPFTSTLVFaSIMKHQDAPGTT--FKKHMDIARGlLSEDDYLLTEILF 215
Cdd:PLN02712  201 CkSFLEVFEREGCKMVEMSCTEHDKYAAESQFITHTVGRVL-EMLKLESTPINTkgYESLLDLVEN-TCGDSFDLYYGLF 278

                         250
                  ....*....|...
gi 2734719472 216 --NPNTPQQVRQI 226
Cdd:PLN02712  279 myNKNSLEMLERL 291
PRK07417 PRK07417
prephenate/arogenate dehydrogenase;
56-113 4.76e-06

prephenate/arogenate dehydrogenase;


Pssm-ID: 180970 [Multi-domain]  Cd Length: 279  Bit Score: 46.81  E-value: 4.76e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2734719472  56 DLVINAATVKYTIEAFESVLPYLPARTILSDIASVKTGLPEfYARAGHP-FVSTHPMFG 113
Cdd:PRK07417   59 DLVILALPIGLLLPPSEQLIPALPPEAIVTDVGSVKAPIVE-AWEKLHPrFVGSHPMAG 116
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 1-84 5.73e-06

Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 441497 [Multi-domain]  Cd Length: 305  Bit Score: 46.39  E-value: 5.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472   1 MKIVILGAGKMGSFFADVLS-FDHEVALYDVDPQ---------RLRFAFNTLR------MTRPEEIGEFapDLVINAatV 64
Cdd:COG1893     1 MKIAILGAGAIGGLLGARLArAGHDVTLVARGAHaealrenglRLESPDGDRTtvpvpaVTDPEELGPA--DLVLVA--V 76

                          90       100
                  ....*....|....*....|..
gi 2734719472  65 KY--TIEAFESVLPYLPARTIL 84
Cdd:COG1893    77 KAydLEAAAEALAPLLGPDTVV 98
PDH_N pfam02153
Prephenate dehydrogenase, nucleotide-binding domain; Members of this family are prephenate ...
 21-145 9.27e-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: 44.68  E-value: 9.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472  21 FDHEVALYDVDPQ------RLRFAFNtlRMTRPEEIGEFapDLVINAATVKYTIEAFESVLPYLPARTILSDIASVKTG- 93
Cdd:pfam02153  10 FFVTVIGYDINPEaavaalRLGLGDE--ATDDIEAVREA--DIVFLAVPVEQTLPVLKELAPHLKEDALITDVGSVKVKi 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2734719472  94 ---LPEFYARAGhpFVSTHPMFGPTF----ANLSDLSTQHAIIITEGDHLGKVFFKDIY 145
Cdd:pfam02153  86 ireLEQHLPDKS--FVPGHPMAGTEKsgpdAARANLFENAPVILTPTEKTDTEALNCVK 142
trkA PRK09496
Trk system potassium transporter TrkA;
1-42 1.20e-05

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 45.88  E-value: 1.20e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2734719472   1 MKIVILGAGKMGSFFADVLSF-DHEVALYDVDPQRLRFAFNTL 42
Cdd:PRK09496    1 MKIIIVGAGQVGYTLAENLSGeNNDVTVIDTDEERLRRLQDRL 43
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 1-84 1.59e-05

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 45.23  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472   1 MKIVILGAGKMGSFFADVLSF-DHEVALYDVDPQRLR-------------FAFNTLRMTRPEEIGEFapDLVINaaTVKY 66
Cdd:PRK06522    1 MKIAILGAGAIGGLFGAALAQaGHDVTLVARRGAHLDalnenglrledgeITVPVLAADDPAELGPQ--DLVIL--AVKA 76

                          90       100
                  ....*....|....*....|
gi 2734719472  67 --TIEAFESVLPYLPARTIL 84
Cdd:PRK06522   77 yqLPAALPSLAPLLGPDTPV 96
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
 3-84 1.65e-05

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: 43.76  E-value: 1.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472   3 IVILGAGKMGSFFADVLSF-DHEVALYDVDPQRLRFAFNTLRMTRPEEIGEFAPDLVINAA-----------TVKY--TI 68
Cdd:pfam02558   1 IAILGAGAIGSLLGARLAKaGHDVTLILRGAELAAIKKNGLRLTSPGGERIVPPPAVTSASeslgpidlvivTVKAyqTE 80

                          90
                  ....*....|....*.
gi 2734719472  69 EAFESVLPYLPARTIL 84
Cdd:pfam02558  81 EALEDIAPLLGPNTVV 96
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 2-111 4.18e-05

3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 42.91  E-value: 4.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472   2 KIVILGAGKMGSFFADVL-SFDHEVALYDVDPQRLRFAFNTL-----------RMTRPE------------EIGEFA-PD 56
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFaLAGLEVVLVDISEEALEKALERIesslerlvekgRITEEEvdaalarisfttDLAAAVdAD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2734719472  57 LVINAATVKYTI--EAFESVLPYLPARTILsdiASVKTGLP--EFYARAGHP--FVSTHPM 111
Cdd:pfam02737  81 LVIEAVPENLELkrKLFAELDAIAPPDAIL---ATNTSSLSitELAAATKRPerFIGLHFF 138
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 1-111 8.38e-05

3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA dehydrogenase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440862 [Multi-domain]  Cd Length: 281  Bit Score: 42.79  E-value: 8.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472   1 MKIVILGAGKMGSFFADVL-SFDHEVALYDVDPQRLRFAFNTL-----------RMTRPE------------EIGEFAP- 55
Cdd:COG1250     3 KKVAVIGAGTMGAGIAAVFaNAGYEVVLLDISPEALERARARIaklldklvkkgKLTEEEadaalaritpttDLAALADa 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2734719472  56 DLVINAAT----VKytIEAFESVLPYLPARTILsdiASVKTGLP--EFYARAGHP--FVSTHPM 111
Cdd:COG1250    83 DLVIEAVPedldLK--QEVFAELDAVAPPDAIL---ASNTSSLSitELAAATKRPerFIGLHFF 141
CelF COG1486
Alpha-galactosidase/6-phospho-beta-glucosidase, family 4 of glycosyl hydrolase [Carbohydrate ...
 1-36 9.95e-05

Alpha-galactosidase/6-phospho-beta-glucosidase, family 4 of glycosyl hydrolase [Carbohydrate transport and metabolism];


Pssm-ID: 441095 [Multi-domain]  Cd Length: 423  Bit Score: 43.17  E-value: 9.95e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2734719472   1 MKIVILGAGkmGSFFA-----DVLSFD----HEVALYDVDPQRLR 36
Cdd:COG1486     1 MKIAIIGGG--STYTPelllgDLLRYPelpvSEIALYDIDEERLE 43
GH4_alpha_glucosidase_galactosidase cd05297
Glycoside Hydrolases Family 4; Alpha-glucosidases and alpha-galactosidases; Glucosidases ...
 1-74 1.10e-04

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: 42.94  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472   1 MKIVILGAGKMG---SFFADVLSF----DHEVALYDVDPQRLRFAFNTL-RMTrpEEIG-----EFAPDL---------V 58
Cdd:cd05297     1 IKIAFIGAGSVVftkNLVGDLLKTpelsGSTIALMDIDEERLETVEILAkKIV--EELGaplkiEATTDRrealdgadfV 78

                          90
                  ....*....|....*.
gi 2734719472  59 INAATVKYTiEAFESV 74
Cdd:cd05297    79 INTIQVGGH-EYTETD 93
PRK06545 PRK06545
prephenate dehydrogenase; Validated
 3-113 1.79e-04

prephenate dehydrogenase; Validated


Pssm-ID: 235824 [Multi-domain]  Cd Length: 359  Bit Score: 42.20  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472   3 IVILGAGKMGSFFADVLSFDH-EVALYDVDP--QRLRFAFNTLRMTRPEEIGEFA---PDLVINAATVKYTIEAFESVLP 76
Cdd:PRK06545    3 VLIVGLGLIGGSLALAIKAAGpDVFIIGYDPsaAQLARALGFGVIDELAADLQRAaaeADLIVLAVPVDATAALLAELAD 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2734719472  77 Y-LPARTILSDIASVKTGLPEFYARAGHP---FVSTHPMFG 113
Cdd:PRK06545   83 LeLKPGVIVTDVGSVKGAILAEAEALLGDlirFVGGHPMAG 123
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 2-62 2.14e-04

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 40.57  E-value: 2.14e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2734719472    2 KIVILGAGKMGSFFADVL-SFDHEVALYDVDPQRLRFA-------FNTLrMTRPEEIGEFAP--DLVINAA 62
Cdd:smart01002  22 KVVVIGAGVVGLGAAATAkGLGAEVTVLDVRPARLRQLesllgarFTTL-YSQAELLEEAVKeaDLVIGAV 91
PRK15076 PRK15076
alpha-galactosidase; Provisional
 1-43 3.26e-04

alpha-galactosidase; Provisional


Pssm-ID: 185035 [Multi-domain]  Cd Length: 431  Bit Score: 41.36  E-value: 3.26e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2734719472   1 MKIVILGAGKMGsF----FADVLSF----DHEVALYDVDPQRLRFAFNTLR 43
Cdd:PRK15076    2 PKITFIGAGSTV-FtknlLGDILSVpalrDAEIALMDIDPERLEESEIVAR 51
PRK06444 PRK06444
prephenate dehydrogenase; Provisional
 86-235 4.06e-04

prephenate dehydrogenase; Provisional


Pssm-ID: 102381 [Multi-domain]  Cd Length: 197  Bit Score: 40.22  E-value: 4.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472  86 DIASVKTGLPEFYARaghpFVSTHPMFGPTFANlsdlstqhaiiitEGDHLGKVFFKDIYQRLRLNIFEYSFR------- 158
Cdd:PRK06444   57 EISSVKWPFKKYSGK----IVSIHPLFGPMSYN-------------DGVHRTVIFINDISRDNYLNEINEMFRgyhfvem 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472 159 ---EHDETIAYSLSIPFTSTLVFASImkHQDAPGTTFKKHMDIARGLLSED-DYLLTEILFNPNTpQQVRQIQEQLSVLL 234
Cdd:PRK06444  120 tadEHDLLMSEIMVKPYIISMILKDI--KSDIKTGSFDKLLEVSEIKEKENwEVFNDTIIYNPYT-NVINDLIERLNKVI 196


                  .
gi 2734719472 235 D 235
Cdd:PRK06444  197 D 197
PLN02712 PLN02712
arogenate dehydrogenase
 1-173 1.25e-03

arogenate dehydrogenase


Pssm-ID: 215382 [Multi-domain]  Cd Length: 667  Bit Score: 39.96  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472   1 MKIVILGAGKMGSFFADVLSFDHEVAL------YDVDPQRLRFAFntlrMTRPEEIGEFAPDLVINAATVKYTIEAFESv 74
Cdd:PLN02712  370 LKIAIVGFGNFGQFLAKTMVKQGHTVLaysrsdYSDEAQKLGVSY----FSDADDLCEEHPEVILLCTSILSTEKVLKS- 444

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472  75 LPY--LPARTILSDIASVK--------TGLPEFYaraghPFVSTHPMFGPT-----FANLSDLSTQHAIIITEGDHLGKV 139
Cdd:PLN02712  445 LPFqrLKRSTLFVDVLSVKefprnlflQHLPQDF-----DILCTHPMFGPEsgkngWNNLAFVFDKVRIGSDDRRVSRCD 519

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2734719472 140 FFKDIYQRLRLNIFEYSFREHDETIAYSLSIPFT 173
Cdd:PLN02712  520 SFLDIFAREGCRMVEMSCAEHDWHAAGSQFITHT 553
PLN02256 PLN02256
arogenate dehydrogenase
 1-114 1.54e-03

arogenate dehydrogenase


Pssm-ID: 215144 [Multi-domain]  Cd Length: 304  Bit Score: 39.26  E-value: 1.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472   1 MKIVILGAGKMGSFFADVL-SFDHEV-----ALYDVDPQRLRFAFntlrMTRPEEIGEFAPDLVINAATvkytIEAFESV 74
Cdd:PLN02256   37 LKIGIVGFGNFGQFLAKTFvKQGHTVlatsrSDYSDIAAELGVSF----FRDPDDFCEEHPDVVLLCTS----ILSTEAV 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2734719472  75 LPYLPAR-----TILSDIASVKTG--------LPEfyaraGHPFVSTHPMFGP 114
Cdd:PLN02256  109 LRSLPLQrlkrsTLFVDVLSVKEFpknlllqvLPE-----EFDILCTHPMFGP 156
PRK08293 PRK08293
3-hydroxyacyl-CoA dehydrogenase;
2-118 2.30e-03

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 181359 [Multi-domain]  Cd Length: 287  Bit Score: 38.38  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2734719472   2 KIVILGAGKMGS---FFADVLSFDheVALYDVDPQ-----RLRFAFNTLRMTR-----PEEIGEFAP------------- 55
Cdd:PRK08293    5 NVTVAGAGVLGSqiaFQTAFHGFD--VTIYDISDEalekaKERIAKLADRYVRdleatKEAPAEAALnritlttdlaeav 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2734719472  56 ---DLVINAAT--VKYTIEAFESVLPYLPARTILSDIASvkTGLP-EFYARAGHP--FVSTHpmfgptFAN 118
Cdd:PRK08293   83 kdaDLVIEAVPedPEIKGDFYEELAKVAPEKTIFATNSS--TLLPsQFAEATGRPekFLALH------FAN 145
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 1-38 2.93e-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: 38.12  E-value: 2.93e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2734719472   1 MKIVILGAGKMGSFFADVLS-FDHEVALYDVDPQRLRFA 38
Cdd:COG0569    96 MHVIIIGAGRVGRSLARELEeEGHDVVVIDKDPERVERL 134
 
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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