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Conserved domains on  [gi|502822720|ref|WP_013057696|]
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MULTISPECIES: prephenate dehydrogenase [Priestia]

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 ...
 4-280 2.16e-113

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: 327.85  E-value: 2.16e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720   4 RVLLIGVGLIGGSLALAMKK-HRHVTVVGADINTNEVQVANQLGIVDYVAEDIKTEAAQADYIVLATPVEYTTAWIHDLS 82
Cdd:COG0287    3 RIAIIGLGLIGGSLALALKRaGLAHEVVGVDRSPETLERALELGVIDRAATDLEEAVADADLVVLAVPVGATIEVLAELA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720  83 TwKLKETVIVTDVGSTKGEIMKAAEALNKKRISFIGGHPMAGSHTSGAVNARADLFCSARYILTPFENEQKEKIDALMHL 162
Cdd:COG0287   83 P-HLKPGAIVTDVGSVKGAVVEAAEALLPDGVRFVGGHPMAGTEKSGPEAADADLFEGAPYILTPTEGTDPEALERVEEL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720 163 LEPTGAQFVPLDAATHDQITGVVSHLPHVIATSLVRQVKGySAQNHLVTEMAAGGFRDITRIASSNPHMWRDILKQNRSM 242
Cdd:COG0287  162 WEALGARVVEMDPEEHDRVVAAVSHLPHLLAFALVNTVAD-LEDEEEILRLAAGGFRDTTRIAASDPEMWRDIFLANREA 240

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 502822720 243 LLTLLDDWMKEMEQVKLLVEKGDGHELFDYFSDAKEFR 280
Cdd:COG0287  241 LLEALDRFIEELDALRDALEAGDGEALEELLERARAAR 278
 
Name Accession Description Interval E-value
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 4-280 2.16e-113

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: 327.85  E-value: 2.16e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720   4 RVLLIGVGLIGGSLALAMKK-HRHVTVVGADINTNEVQVANQLGIVDYVAEDIKTEAAQADYIVLATPVEYTTAWIHDLS 82
Cdd:COG0287    3 RIAIIGLGLIGGSLALALKRaGLAHEVVGVDRSPETLERALELGVIDRAATDLEEAVADADLVVLAVPVGATIEVLAELA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720  83 TwKLKETVIVTDVGSTKGEIMKAAEALNKKRISFIGGHPMAGSHTSGAVNARADLFCSARYILTPFENEQKEKIDALMHL 162
Cdd:COG0287   83 P-HLKPGAIVTDVGSVKGAVVEAAEALLPDGVRFVGGHPMAGTEKSGPEAADADLFEGAPYILTPTEGTDPEALERVEEL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720 163 LEPTGAQFVPLDAATHDQITGVVSHLPHVIATSLVRQVKGySAQNHLVTEMAAGGFRDITRIASSNPHMWRDILKQNRSM 242
Cdd:COG0287  162 WEALGARVVEMDPEEHDRVVAAVSHLPHLLAFALVNTVAD-LEDEEEILRLAAGGFRDTTRIAASDPEMWRDIFLANREA 240

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 502822720 243 LLTLLDDWMKEMEQVKLLVEKGDGHELFDYFSDAKEFR 280
Cdd:COG0287  241 LLEALDRFIEELDALRDALEAGDGEALEELLERARAAR 278
PRK06545 PRK06545
prephenate dehydrogenase; Validated
 5-283 9.38e-110

prephenate dehydrogenase; Validated


Pssm-ID: 235824 [Multi-domain]  Cd Length: 359  Bit Score: 321.86  E-value: 9.38e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720   5 VLLIGVGLIGGSLALAMKK-HRHVTVVGADINTNEVQVANQLGIVDYVAEDIKTEAAQADYIVLATPVEYTTAWIHDLST 83
Cdd:PRK06545   3 VLIVGLGLIGGSLALAIKAaGPDVFIIGYDPSAAQLARALGFGVIDELAADLQRAAAEADLIVLAVPVDATAALLAELAD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720  84 WKLKETVIVTDVGSTKGEIMKAAEALNKKRISFIGGHPMAGSHTSGAVNARADLFCSARYILTPFENEQKEKIDALMHLL 163
Cdd:PRK06545  83 LELKPGVIVTDVGSVKGAILAEAEALLGDLIRFVGGHPMAGSHKSGVAAARADLFENAPWVLTPDDHTDPDAVAELKDLL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720 164 EPTGAQFVPLDAATHDQITGVVSHLPHVIATSLVRQvkgYSAQNHLVTEMAAGGFRDITRIASSNPHMWRDILKQNRSML 243
Cdd:PRK06545 163 SGTGAKFVVLDAEEHDRAVALVSHLPHILASSLAAR---LAGEHPLALRLAAGGFRDITRIASSDPGMWRDILESNAEAL 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 502822720 244 LTLLDDWMKEMEQVKLLVEKGDGHELFDYFSDAKEFRDSL 283
Cdd:PRK06545 240 LDALDEWIEDLDRARDALESGDAEAIAELFDAGKAGRDRL 279
PDH_N pfam02153
Prephenate dehydrogenase, nucleotide-binding domain; Members of this family are prephenate ...
 17-171 3.67e-32

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: 116.33  E-value: 3.67e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720   17 LALAMKKH-RHVTVVGADINTNEVQVANQLGIVDYVAEDIKTeAAQADYIVLATPVEYTTAWIHDLSTwKLKETVIVTDV 95
Cdd:pfam02153   1 LALALRRHgFFVTVIGYDINPEAAVAALRLGLGDEATDDIEA-VREADIVFLAVPVEQTLPVLKELAP-HLKEDALITDV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502822720   96 GSTKGEIMKAAEAlNKKRISFIGGHPMAGSHTSGAVNARADLFCSARYILTPFENEQKEKIDALMHLLEPTGAQFV 171
Cdd:pfam02153  79 GSVKVKIIRELEQ-HLPDKSFVPGHPMAGTEKSGPDAARANLFENAPVILTPTEKTDTEALNCVKELLEGVGARVI 153
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 4-64 4.78e-04

2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176217 [Multi-domain]  Cd Length: 277  Bit Score: 40.72  E-value: 4.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502822720   4 RVLLIGVGLIGGSLALAMKKHRHVTVVGADINTNEVQVANQLGIVDYVAEDIKTEAAQADY 64
Cdd:cd08255  100 RVAVVGLGLVGLLAAQLAKAAGAREVVGVDPDAARRELAEALGPADPVAADTADEIGGRGA 160
 
Name Accession Description Interval E-value
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 4-280 2.16e-113

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: 327.85  E-value: 2.16e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720   4 RVLLIGVGLIGGSLALAMKK-HRHVTVVGADINTNEVQVANQLGIVDYVAEDIKTEAAQADYIVLATPVEYTTAWIHDLS 82
Cdd:COG0287    3 RIAIIGLGLIGGSLALALKRaGLAHEVVGVDRSPETLERALELGVIDRAATDLEEAVADADLVVLAVPVGATIEVLAELA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720  83 TwKLKETVIVTDVGSTKGEIMKAAEALNKKRISFIGGHPMAGSHTSGAVNARADLFCSARYILTPFENEQKEKIDALMHL 162
Cdd:COG0287   83 P-HLKPGAIVTDVGSVKGAVVEAAEALLPDGVRFVGGHPMAGTEKSGPEAADADLFEGAPYILTPTEGTDPEALERVEEL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720 163 LEPTGAQFVPLDAATHDQITGVVSHLPHVIATSLVRQVKGySAQNHLVTEMAAGGFRDITRIASSNPHMWRDILKQNRSM 242
Cdd:COG0287  162 WEALGARVVEMDPEEHDRVVAAVSHLPHLLAFALVNTVAD-LEDEEEILRLAAGGFRDTTRIAASDPEMWRDIFLANREA 240

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 502822720 243 LLTLLDDWMKEMEQVKLLVEKGDGHELFDYFSDAKEFR 280
Cdd:COG0287  241 LLEALDRFIEELDALRDALEAGDGEALEELLERARAAR 278
PRK06545 PRK06545
prephenate dehydrogenase; Validated
 5-283 9.38e-110

prephenate dehydrogenase; Validated


Pssm-ID: 235824 [Multi-domain]  Cd Length: 359  Bit Score: 321.86  E-value: 9.38e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720   5 VLLIGVGLIGGSLALAMKK-HRHVTVVGADINTNEVQVANQLGIVDYVAEDIKTEAAQADYIVLATPVEYTTAWIHDLST 83
Cdd:PRK06545   3 VLIVGLGLIGGSLALAIKAaGPDVFIIGYDPSAAQLARALGFGVIDELAADLQRAAAEADLIVLAVPVDATAALLAELAD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720  84 WKLKETVIVTDVGSTKGEIMKAAEALNKKRISFIGGHPMAGSHTSGAVNARADLFCSARYILTPFENEQKEKIDALMHLL 163
Cdd:PRK06545  83 LELKPGVIVTDVGSVKGAILAEAEALLGDLIRFVGGHPMAGSHKSGVAAARADLFENAPWVLTPDDHTDPDAVAELKDLL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720 164 EPTGAQFVPLDAATHDQITGVVSHLPHVIATSLVRQvkgYSAQNHLVTEMAAGGFRDITRIASSNPHMWRDILKQNRSML 243
Cdd:PRK06545 163 SGTGAKFVVLDAEEHDRAVALVSHLPHILASSLAAR---LAGEHPLALRLAAGGFRDITRIASSDPGMWRDILESNAEAL 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 502822720 244 LTLLDDWMKEMEQVKLLVEKGDGHELFDYFSDAKEFRDSL 283
Cdd:PRK06545 240 LDALDEWIEDLDRARDALESGDAEAIAELFDAGKAGRDRL 279
PRK14806 PRK14806
bifunctional cyclohexadienyl dehydrogenase/ 3-phosphoshikimate 1-carboxyvinyltransferase; ...
 4-281 9.43e-70

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


Pssm-ID: 237820 [Multi-domain]  Cd Length: 735  Bit Score: 228.73  E-value: 9.43e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720   4 RVLLIGVGLIGGSLALAMKKHRHV-TVVGADINTNEVQVANQLGIVDYVAEDIKTEAAQADYIVLATPVEYTTAWIHDLS 82
Cdd:PRK14806   5 RVVVIGLGLIGGSFAKALRERGLArEVVAVDRRAKSLELAVSLGVIDRGEEDLAEAVSGADVIVLAVPVLAMEKVLADLK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720  83 TWkLKETVIVTDVGSTKGEIMKAA-EALNKKRISFIGGHPMAGSHTSGAVNARADLFCSARYILTPFENEQKEKIDALMH 161
Cdd:PRK14806  85 PL-LSEHAIVTDVGSTKGNVVDAArAVFGELPAGFVPGHPIAGSEKSGVHAANADLFRNHKVILTPLAETDPAALARVDR 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720 162 LLEPTGAQFVPLDAATHDQITGVVSHLPHVIATSLVRQVKGYSaQNHLVTEMAAGGFRDITRIASSNPHMWRDILKQNRS 241
Cdd:PRK14806 164 LWRAVGADVLHMDVAHHDEVLAATSHLPHLLAFSLVDQLANRE-DNLDIFRYAAGGFRDFTRIAASDPVMWHDIFLANKE 242

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 502822720 242 MLLTLLDDWMKEMEQVKLLVEKGDGHELFDYFSDAKEFRD 281
Cdd:PRK14806 243 AVLRALDHFRDDLDALRAAIEAGDGHALLGVFTRARAARE 282
PRK08507 PRK08507
prephenate dehydrogenase; Validated
 1-283 5.18e-63

prephenate dehydrogenase; Validated


Pssm-ID: 181452 [Multi-domain]  Cd Length: 275  Bit Score: 199.74  E-value: 5.18e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720   1 MKtrVLLIGVGLIGGSLALAMK-KHRHVTVVGADINTNEVQVANQLGIVDYVAEDikTEAAQADYIVLATPVEYTTAWIH 79
Cdd:PRK08507   1 MK--IGIIGLGLMGGSLGLALKeKGLISKVYGYDHNELHLKKALELGLVDEIVSF--EELKKCDVIFLAIPVDAIIEILP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720  80 DLStwKLKETVIVTDVGSTKGEIMKAAEalNKKRISFIGGHPMAGSHTSGAVNARADLFCSARYILTPFENEQKEKIDAL 159
Cdd:PRK08507  77 KLL--DIKENTTIIDLGSTKAKIIESVP--KHIRKNFIAAHPMAGTENSGPKAAIKGLYEGKVVVLCDVEKSGEKHQERA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720 160 MHLLEPTGAQFVPLDAATHDQITGVVSHLPHVIATSLVRQVKGYSAQNHLVtEMAAGGFRDITRIASSNPHMWRDILKQN 239
Cdd:PRK08507 153 KEIFSGLGMRIVYMDAKEHDLHAAYISHLPHIISFALANTVLKEEDERNIF-DLAGGGFRSMSRLAKSSPAMWSDIFKQN 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 502822720 240 RSMLLTLLDDWMKEMEQVKLLVEKGDGHELFDYFSDAKEFRDSL 283
Cdd:PRK08507 232 KENVLEAIDEFIKELEQFKQLIENEDWEELEEWMEQANKLREIL 275
PRK07502 PRK07502
prephenate/arogenate dehydrogenase family protein;
4-274 7.83e-61

prephenate/arogenate dehydrogenase family protein;


Pssm-ID: 236034 [Multi-domain]  Cd Length: 307  Bit Score: 195.19  E-value: 7.83e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720   4 RVLLIGVGLIGGSLALAMKKHR-HVTVVGADINTNEVQVANQLGIVDYVAEDIKTEAAQADYIVLATPV---EYTTAWIH 79
Cdd:PRK07502   8 RVALIGIGLIGSSLARAIRRLGlAGEIVGADRSAETRARARELGLGDRVTTSAAEAVKGADLVILCVPVgasGAVAAEIA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720  80 DLstwkLKETVIVTDVGSTKGEIMKAAEALNKKRISFIGGHPMAGSHTSGAVNARADLFCSARYILTPFENEQKEKIDAL 159
Cdd:PRK07502  88 PH----LKPGAIVTDVGSVKASVIAAMAPHLPEGVHFIPGHPLAGTEHSGPDAGFAELFENRWCILTPPEGTDPAAVARL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720 160 MHLLEPTGAQFVPLDAATHDQITGVVSHLPHVIATSLVrqvkGYSAQNHLVTE-----MAAGGFRDITRIASSNPHMWRD 234
Cdd:PRK07502 164 TAFWRALGARVEEMDPEHHDLVLAITSHLPHLIAYTIV----GTADDLERVTEsevikYSASGFRDFTRIAASDPTMWRD 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 502822720 235 ILKQNRSMLLTLLDDWMKEMEQVKLLVEKGDGHELFDYFS 274
Cdd:PRK07502 240 VFLHNKDAVLEMLGRFTEDLAALQRAIRWGDGDALFDLFT 279
PRK07417 PRK07417
prephenate/arogenate dehydrogenase;
4-280 2.98e-47

prephenate/arogenate dehydrogenase;


Pssm-ID: 180970 [Multi-domain]  Cd Length: 279  Bit Score: 159.29  E-value: 2.98e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720   4 RVLLIGVGLIGGSLALAMKKhRHVTVVGADINTNEVQVANQLGIVDYVAEDIKTEAAqADYIVLATPVEYTTAWIHDLsT 83
Cdd:PRK07417   2 KIGIVGLGLIGGSLGLDLRS-LGHTVYGVSRRESTCERAIERGLVDEASTDLSLLKD-CDLVILALPIGLLLPPSEQL-I 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720  84 WKLKETVIVTDVGSTKGEIMKAAEALNKKrisFIGGHPMAGSHTSGAVNARADLFCSARYILTPFENEQKEKIDALMHLL 163
Cdd:PRK07417  79 PALPPEAIVTDVGSVKAPIVEAWEKLHPR---FVGSHPMAGTAESGVEAGQRGLFKNRPWVLTPTENTDLNALAIVEELA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720 164 EPTGAQFVPLDAATHDQITGVVSHLPHVIATSLVRQVKGYSAQN--HLVTEMAAGGFRDITRIASSNPHMWRDILKQNRS 241
Cdd:PRK07417 156 VSLGSKIYTADPEEHDRAVALISHLPVMVSAALIQTCGTEKDPSvlKLAQNLASSGFADTSRVGGGNPELGVMMAEYNRA 235

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 502822720 242 MLLTLLDDWMKEMEQVKLLVEKGDGHELFDYFSDAKEFR 280
Cdd:PRK07417 236 ALLRSLASYRQSLDQLEELIEQENWSALEQKLEQTQELR 274
PRK11861 PRK11861
bifunctional prephenate dehydrogenase/3-phosphoshikimate 1-carboxyvinyltransferase; Provisional
 65-280 8.45e-35

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


Pssm-ID: 183343 [Multi-domain]  Cd Length: 673  Bit Score: 132.52  E-value: 8.45e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720  65 IVLATPVEYTTAWIHDLSTWkLKETVIVTDVGSTKGEIMKAAEALNKKRI-SFIGGHPMAGSHTSGAVNARADLFCSARY 143
Cdd:PRK11861   1 VLLAAPVAQTGPLLARIAPF-LDASTIVTDAGSTKSDVVAAARAALGARIgQFVPGHPIAGRESSGVDAALADLYVGRNV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720 144 ILTPFENEQKEKIDALMHLLEPTGAQFVPLDAATHDQITGVVSHLPHVIATSLVRQVKGYSaQNHLVTEMAAGGFRDITR 223
Cdd:PRK11861  80 VLCALPENAPDALARVEAMWRAARADVRAMSAEQHDRVFAAVSHLPHVLSFALVEQILGES-DAELKFSYAAGGFRDFTR 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 502822720 224 IASSNPHMWRDILKQNRSMLLTLLDDWMKEMEQVKLLVEKGDGHELFDYFSDAKEFR 280
Cdd:PRK11861 159 IAASSPEMWRDVCLANRAALLDELDAYTAVLARLRAAIDAGDGAALEAVFARSRAAR 215
PDH_N pfam02153
Prephenate dehydrogenase, nucleotide-binding domain; Members of this family are prephenate ...
 17-171 3.67e-32

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: 116.33  E-value: 3.67e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720   17 LALAMKKH-RHVTVVGADINTNEVQVANQLGIVDYVAEDIKTeAAQADYIVLATPVEYTTAWIHDLSTwKLKETVIVTDV 95
Cdd:pfam02153   1 LALALRRHgFFVTVIGYDINPEAAVAALRLGLGDEATDDIEA-VREADIVFLAVPVEQTLPVLKELAP-HLKEDALITDV 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502822720   96 GSTKGEIMKAAEAlNKKRISFIGGHPMAGSHTSGAVNARADLFCSARYILTPFENEQKEKIDALMHLLEPTGAQFV 171
Cdd:pfam02153  79 GSVKVKIIRELEQ-HLPDKSFVPGHPMAGTEKSGPDAARANLFENAPVILTPTEKTDTEALNCVKELLEGVGARVI 153
PDH_C pfam20463
Prephenate dehydrogenase, dimerization domain; Members of this family are prephenate ...
 174-273 9.93e-30

Prephenate dehydrogenase, dimerization domain; Members of this family are prephenate dehydrogenases EC:1.3.1.12 (PDHs) involved in tyrosine biosynthesis. This is the C-terminal, helical dimerization domain of PDHs.


Pssm-ID: 466612 [Multi-domain]  Cd Length: 102  Bit Score: 108.24  E-value: 9.93e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720  174 DAATHDQITGVVSHLPHVIATSLVRQVKGYSAQNHLVTEMAAGGFRDITRIASSNPHMWRDILKQNRSMLLTLLDDWMKE 253
Cdd:pfam20463   1 SPETHDRVVAVVSHLPHFVAIALAATLAELGVDIKEARKLASGGFRDMTRIAGSNPELWADIQTHNARAVLEALDDFIAE 80

                          90       100
                  ....*....|....*....|
gi 502822720  254 MEQVKLLVEKGDGHELFDYF 273
Cdd:pfam20463  81 LKQLKELIRNGDWEELVEYM 100
PRK08655 PRK08655
prephenate dehydrogenase; Provisional
 10-278 2.43e-17

prephenate dehydrogenase; Provisional


Pssm-ID: 236326 [Multi-domain]  Cd Length: 437  Bit Score: 81.19  E-value: 2.43e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720  10 VGLIGGS------LALAMKKHRH-VTVVGADINTNEvQVANQLGiVDYVAEDIKTeAAQADYIVLATPVEYTTAWIHDLS 82
Cdd:PRK08655   3 ISIIGGTgglgkwFARFLKEKGFeVIVTGRDPKKGK-EVAKELG-VEYANDNIDA-AKDADIVIISVPINVTEDVIKEVA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720  83 TwKLKETVIVTDVGSTKGEIMKAAEALNKKRISFIGGHPMAGSHTS---GAVnaradlfcsarYILTPFENEQKEKIDAL 159
Cdd:PRK08655  80 P-HVKEGSLLMDVTSVKERPVEAMEEYAPEGVEILPTHPMFGPRTPslkGQV-----------VILTPTEKRSNPWFDKV 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720 160 MHLLEPTGAQFVPLDAATHDQITGVVSHLPHVIATSLVRQVKgysAQNHLVTEM--AAGGFRD-----ITRIASSNPHMW 232
Cdd:PRK08655 148 KNFLEKEGARVIVTSPEEHDRIMSVVQGLTHFAYISIASTLK---RLGVDIKESrkFASPIYElmidiIGRILGQNPYLY 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 502822720 233 RDILKQNrSMLLTLLDDWMKEMEQVKLLVEKGDGHELFDYFSDAKE 278
Cdd:PRK08655 225 ASIQMNN-PQIPEIHETFIKECEELSELVKNGDREEFVERMKEAAK 269
PRK08818 PRK08818
prephenate dehydrogenase; Provisional
 10-265 4.02e-04

prephenate dehydrogenase; Provisional


Pssm-ID: 181561 [Multi-domain]  Cd Length: 370  Bit Score: 41.39  E-value: 4.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720  10 VGLIGGS------LALAMKKHRHVTVVGADIntnevqvanqlgiVDYVAEDIKTEAAQADYIVLATPVEYTTAWIHD--- 80
Cdd:PRK08818   7 VGIVGSAgaygrwLARFLRTRMQLEVIGHDP-------------ADPGSLDPATLLQRADVLIFSAPIRHTAALIEEyva 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720  81 LSTWKLKETVI--VTDVGSTKGEIMKAAEAlnkkriSFIGGHPMAGSHTSGAVNARADLFCSARYiltpfeneqKEKIDA 158
Cdd:PRK08818  74 LAGGRAAGQLWldVTSIKQAPVAAMLASQA------EVVGLHPMTAPPKSPTLKGRVMVVCEARL---------QHWSPW 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720 159 LMHLLEPTGAQFVPLDAATHDQITGVVS---HLPHVIATSLVRQ-----------VKGYSAQNHLVTEMaaggfrdITRI 224
Cdd:PRK08818 139 VQSLCSALQAECVYATPEHHDRVMALVQamvHATHLAQAGVLRDyapllgelralMPYRSASFELDTAV-------IARI 211

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 502822720 225 ASSNPHMWRDILKQNrSMLLTLLDDWMKEMEQVKLLVEKGD 265
Cdd:PRK08818 212 LSLNPSIYEDIQFGN-PYVGEMLDRLLAQLQELRALVAQGD 251
2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ cd08255
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ...
 4-64 4.78e-04

2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176217 [Multi-domain]  Cd Length: 277  Bit Score: 40.72  E-value: 4.78e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502822720   4 RVLLIGVGLIGGSLALAMKKHRHVTVVGADINTNEVQVANQLGIVDYVAEDIKTEAAQADY 64
Cdd:cd08255  100 RVAVVGLGLVGLLAAQLAKAAGAREVVGVDPDAARRELAEALGPADPVAADTADEIGGRGA 160
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 1-68 1.53e-03

Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis


Pssm-ID: 440114 [Multi-domain]  Cd Length: 267  Bit Score: 39.28  E-value: 1.53e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502822720   1 MKTRVLLIGVGLIGGSLALAMKKH----RHVTVVGADINTNEvQVANQLGIVdyVAEDIKTEAAQADYIVLA 68
Cdd:COG0345    1 MSMKIGFIGAGNMGSAIIKGLLKSgvppEDIIVSDRSPERLE-ALAERYGVR--VTTDNAEAAAQADVVVLA 69
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-70 1.90e-03

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 39.14  E-value: 1.90e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502822720   1 MKTRVLLIGVGLIGGSLALAMKKHRHVTVVG-ADINTNEVQ-VANQLGIVDYvaEDIKT--EAAQADYIVLATP 70
Cdd:COG0673    2 DKLRVGIIGAGGIGRAHAPALAALPGVELVAvADRDPERAEaFAEEYGVRVY--TDYEEllADPDIDAVVIATP 73
E1_enzyme_family cd01483
Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes ...
 4-124 4.50e-03

Superfamily of activating enzymes (E1) of the ubiquitin-like proteins. This family includes classical ubiquitin-activating enzymes E1, ubiquitin-like (ubl) activating enzymes and other mechanistic homologes, like MoeB, Thif1 and others. The common reaction mechanism catalyzed by MoeB, ThiF and the E1 enzymes begins with a nucleophilic attack of the C-terminal carboxylate of MoaD, ThiS and ubiquitin, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS.


Pssm-ID: 238760 [Multi-domain]  Cd Length: 143  Bit Score: 36.86  E-value: 4.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502822720   4 RVLLIGVGLIGG--SLALAMKKHRHVTVVGADIntneVQVAN---QLGivdYVAEDI---KTEAAQADY--IVLATPVEY 73
Cdd:cd01483    1 RVLLVGLGGLGSeiALNLARSGVGKITLIDFDT----VELSNlnrQFL---ARQADIgkpKAEVAARRLneLNPGVNVTA 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 502822720  74 TTAWIHDLST-WKLKETVIVTDVGSTKGEIMKAAEALNKKRISFI--GGHPMAG 124
Cdd:cd01483   74 VPEGISEDNLdDFLDGVDLVIDAIDNIAVRRALNRACKELGIPVIdaGGLGLGG 127
 
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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