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Conserved domains on  [gi|21730849]
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Chain B, Trk system potassium uptake protein trkA homolog

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
trkA super family cl35844
Trk system potassium transporter TrkA;
5-140 2.28e-47

Trk system potassium transporter TrkA;


The actual alignment was detected with superfamily member PRK09496:

Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 158.36  E-value: 2.28e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21730849    5 MYIIIAGIGRVGYTLAKSLSEKGHDIVLIDIDKDICKKASAEIDALVINGDCTKIKTLEDAGIEDADMYIAVTGKEEVNL 84
Cdd:PRK09496   1 MKIIIVGAGQVGYTLAENLSGENNDVTVIDTDEERLRRLQDRLDVRTVVGNGSSPDVLREAGAEDADLLIAVTDSDETNM 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21730849   85 MSSLLAKS-YGINKTIARISEIEY---KDVFER--LGVDVVVSPELIAANYIEKLIERPGIL 140
Cdd:PRK09496  81 VACQIAKSlFGAPTTIARVRNPEYaeyDKLFSKeaLGIDLLISPELLVAREIARLIEYPGAL 142
 
Name Accession Description Interval E-value
trkA PRK09496
Trk system potassium transporter TrkA;
5-140 2.28e-47

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 158.36  E-value: 2.28e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21730849    5 MYIIIAGIGRVGYTLAKSLSEKGHDIVLIDIDKDICKKASAEIDALVINGDCTKIKTLEDAGIEDADMYIAVTGKEEVNL 84
Cdd:PRK09496   1 MKIIIVGAGQVGYTLAENLSGENNDVTVIDTDEERLRRLQDRLDVRTVVGNGSSPDVLREAGAEDADLLIAVTDSDETNM 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21730849   85 MSSLLAKS-YGINKTIARISEIEY---KDVFER--LGVDVVVSPELIAANYIEKLIERPGIL 140
Cdd:PRK09496  81 VACQIAKSlFGAPTTIARVRNPEYaeyDKLFSKeaLGIDLLISPELLVAREIARLIEYPGAL 142
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 5-140 2.36e-47

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: 154.45  E-value: 2.36e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21730849   5 MYIIIAGIGRVGYTLAKSLSEKGHDIVLIDIDKDICKKAsAEIDALVINGDCTKIKTLEDAGIEDADMYIAVTGKEEVNL 84
Cdd:COG0569  96 MHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERL-AEEDVLVIVGDATDEEVLEEAGIEDADAVIAATGDDEANI 174

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21730849  85 MSSLLAKSYGINKTIARISEIEYKDVFERLGVDVVVSPELIAANYIEKLIERPGIL 140
Cdd:COG0569 175 LACLLAKELGVPRIIARANDPEYADLLERLGADVVISPERLAARRIARLLLRPGVL 230
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
 7-122 1.16e-30

TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD.


Pssm-ID: 426679 [Multi-domain]  Cd Length: 115  Bit Score: 106.07  E-value: 1.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21730849     7 IIIAGIGRVGYTLAKSLSEkGHDIVLIDIDKDICKKAsAEIDALVINGDCTKIKTLEDAGIEDADMYIAVTGKEEVNLMS 86
Cdd:pfam02254   1 IIIIGYGRVGRSLAEELSE-GGDVVVIDKDEERVEEL-REEGVPVVVGDATDEEVLEEAGIEEADAVIAATGDDEANILI 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 21730849    87 SLLAKS-YGINKTIARISEIEYKDVFERLGVDVVVSP 122
Cdd:pfam02254  79 VLLARElNPDKKIIARANDPEHAELLRRLGADHVISP 115
NAD_bind_Leu_Phe_Val_DH cd01075
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine ...
 3-49 7.47e-06

NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine dehydrogenase; Amino acid dehydrogenase (DH) is a widely distributed family of enzymes that catalyzes the oxidative deamination of an amino acid to its keto acid and ammonia with concomitant reduction of NADP+. For example, leucine DH catalyzes the reversible oxidative deamination of L-leucine and several other straight or branched chain amino acids to the corresponding 2-oxoacid derivative. Amino acid DH -like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133444  Cd Length: 200  Bit Score: 43.35  E-value: 7.47e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 21730849   3 HGMYIIIAGIGRVGYTLAKSLSEKGHDIVLIDIDKDICKKASAEIDA 49
Cdd:cd01075  27 EGKTVAVQGLGKVGYKLAEHLLEEGAKLIVADINEEAVARAAELFGA 73
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 5-74 2.41e-05

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 42.60  E-value: 2.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21730849     5 MYIIIAGIGRVGYTLAKSLSEKGHDIVLIDIDKDICKK--------ASAEIDALV---INGDCTKIKTLEDAGIEDADMY 73
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKlnkgkspiYEPGLDELLakaLKAGRLRATTDYEEAIRDADVI 80


                  .
gi 21730849    74 I 74
Cdd:TIGR03026  81 I 81
 
Name Accession Description Interval E-value
trkA PRK09496
Trk system potassium transporter TrkA;
5-140 2.28e-47

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 158.36  E-value: 2.28e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21730849    5 MYIIIAGIGRVGYTLAKSLSEKGHDIVLIDIDKDICKKASAEIDALVINGDCTKIKTLEDAGIEDADMYIAVTGKEEVNL 84
Cdd:PRK09496   1 MKIIIVGAGQVGYTLAENLSGENNDVTVIDTDEERLRRLQDRLDVRTVVGNGSSPDVLREAGAEDADLLIAVTDSDETNM 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21730849   85 MSSLLAKS-YGINKTIARISEIEY---KDVFER--LGVDVVVSPELIAANYIEKLIERPGIL 140
Cdd:PRK09496  81 VACQIAKSlFGAPTTIARVRNPEYaeyDKLFSKeaLGIDLLISPELLVAREIARLIEYPGAL 142
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 5-140 2.36e-47

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: 154.45  E-value: 2.36e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21730849   5 MYIIIAGIGRVGYTLAKSLSEKGHDIVLIDIDKDICKKAsAEIDALVINGDCTKIKTLEDAGIEDADMYIAVTGKEEVNL 84
Cdd:COG0569  96 MHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERL-AEEDVLVIVGDATDEEVLEEAGIEDADAVIAATGDDEANI 174

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21730849  85 MSSLLAKSYGINKTIARISEIEYKDVFERLGVDVVVSPELIAANYIEKLIERPGIL 140
Cdd:COG0569 175 LACLLAKELGVPRIIARANDPEYADLLERLGADVVISPERLAARRIARLLLRPGVL 230
trkA PRK09496
Trk system potassium transporter TrkA;
7-140 1.64e-38

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 134.86  E-value: 1.64e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21730849    7 IIIAGIGRVGYTLAKSLSEKGHDIVLIDIDKDICKKASAEI-DALVINGDCTKIKTLEDAGIEDADMYIAVTGKEEVNLM 85
Cdd:PRK09496 234 VMIVGGGNIGYYLAKLLEKEGYSVKLIERDPERAEELAEELpNTLVLHGDGTDQELLEEEGIDEADAFIALTNDDEANIL 313

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 21730849   86 SSLLAKSYGINKTIARISEIEYKDVFERLGVDVVVSPELIAANYIEKLIERPGIL 140
Cdd:PRK09496 314 SSLLAKRLGAKKVIALVNRPAYVDLVEGLGIDIAISPRQATASEILRHVRRGDIV 368
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
 7-122 1.16e-30

TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD.


Pssm-ID: 426679 [Multi-domain]  Cd Length: 115  Bit Score: 106.07  E-value: 1.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21730849     7 IIIAGIGRVGYTLAKSLSEkGHDIVLIDIDKDICKKAsAEIDALVINGDCTKIKTLEDAGIEDADMYIAVTGKEEVNLMS 86
Cdd:pfam02254   1 IIIIGYGRVGRSLAEELSE-GGDVVVIDKDEERVEEL-REEGVPVVVGDATDEEVLEEAGIEEADAVIAATGDDEANILI 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 21730849    87 SLLAKS-YGINKTIARISEIEYKDVFERLGVDVVVSP 122
Cdd:pfam02254  79 VLLARElNPDKKIIARANDPEHAELLRRLGADHVISP 115
Kch COG1226
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];
7-127 2.66e-14

Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];


Pssm-ID: 440839 [Multi-domain]  Cd Length: 279  Bit Score: 67.45  E-value: 2.66e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21730849   7 IIIAGIGRVGYTLAKSLSEKGHDIVLIDIDKDICKKASAEiDALVINGDCTKIKTLEDAGIEDADMYIAVTGKEEVNLMS 86
Cdd:COG1226 127 VIIAGFGRVGQIVARLLRAEGIPFVVIDLDPERVEELRRF-GIKVYYGDATRPDVLEAAGIERARALVVAIDDPEAALRI 205

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 21730849  87 SLLAKSygIN---KTIARISEIEYKDVFERLGVDVVVSPELIAA 127
Cdd:COG1226 206 VELARE--LNpdlKIIARARDREHAEELRQAGADEVVRETFESA 247
NAD_bind_Leu_Phe_Val_DH cd01075
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine ...
 3-49 7.47e-06

NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine dehydrogenase; Amino acid dehydrogenase (DH) is a widely distributed family of enzymes that catalyzes the oxidative deamination of an amino acid to its keto acid and ammonia with concomitant reduction of NADP+. For example, leucine DH catalyzes the reversible oxidative deamination of L-leucine and several other straight or branched chain amino acids to the corresponding 2-oxoacid derivative. Amino acid DH -like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133444  Cd Length: 200  Bit Score: 43.35  E-value: 7.47e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 21730849   3 HGMYIIIAGIGRVGYTLAKSLSEKGHDIVLIDIDKDICKKASAEIDA 49
Cdd:cd01075  27 EGKTVAVQGLGKVGYKLAEHLLEEGAKLIVADINEEAVARAAELFGA 73
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 5-74 2.41e-05

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 42.60  E-value: 2.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21730849     5 MYIIIAGIGRVGYTLAKSLSEKGHDIVLIDIDKDICKK--------ASAEIDALV---INGDCTKIKTLEDAGIEDADMY 73
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKlnkgkspiYEPGLDELLakaLKAGRLRATTDYEEAIRDADVI 80


                  .
gi 21730849    74 I 74
Cdd:TIGR03026  81 I 81
PRK10537 PRK10537
voltage-gated potassium channel protein;
6-127 2.64e-05

voltage-gated potassium channel protein;


Pssm-ID: 236711 [Multi-domain]  Cd Length: 393  Bit Score: 42.32  E-value: 2.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21730849    6 YIIIAGIGRVGYTLAKSLSEKGHDIVLI---DIDKDIckkasaEIDALVINGDCTKIKTLEDAGIEDADMYIAVTGKEEV 82
Cdd:PRK10537 242 HFIICGHSPLAINTYLGLRQRGQAVTVIvplGLEHRL------PDDADLIPGDSSDSAVLKKAGAARARAILALRDNDAD 315

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 21730849   83 NLMSSLLAKSYGIN-KTIARISEIEYKDVFERLGVDVVVSPELIAA 127
Cdd:PRK10537 316 NAFVVLAAKEMSSDvKTVAAVNDSKNLEKIKRVHPDMIFSPQLLGS 361
Mdh COG0039
Malate/lactate dehydrogenase [Energy production and conversion]; Malate/lactate dehydrogenase ...
 7-78 5.08e-05

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


Pssm-ID: 439809 [Multi-domain]  Cd Length: 302  Bit Score: 41.54  E-value: 5.08e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21730849   7 IIIAGIGRVGYTLAKSLSEKG--HDIVLIDIDKDICKKASAEI-DALVINGDCTKIKTLEDAGIEDADmYIAVTG 78
Cdd:COG0039   3 VAIIGAGNVGSTLAFRLASGGlaDELVLIDINEGKAEGEALDLaDAFPLLGFDVKITAGDYEDLADAD-VVVITA 76
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 5-76 2.40e-04

Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains [General function prediction only];


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 39.41  E-value: 2.40e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21730849   5 MYIIIAGIGRVGYTLAKSLSEKGHDIV-LIDIDKDICKKASAEIDAlvingdcTKIKTLEDAgIEDADMY-IAV 76
Cdd:COG5495   4 MKIGIIGAGRVGTALAAALRAAGHEVVgVYSRSPASAERAAALLGA-------VPALDLEEL-AAEADLVlLAV 69
LDH-like_MDH cd01339
L-lactate dehydrogenase-like malate dehydrogenase proteins; Members of this subfamily have an ...
 7-101 8.40e-04

L-lactate dehydrogenase-like malate dehydrogenase proteins; Members of this subfamily have an LDH-like structure and an MDH enzymatic activity. Some members, like MJ0490 from Methanococcus jannaschii, exhibit both MDH and LDH activities. Tetrameric MDHs, including those from phototrophic bacteria, are more similar to LDHs than to other MDHs. LDH catalyzes the last step of glycolysis in which pyruvate is converted to L-lactate. MDH is one of the key enzymes in the citric acid cycle, facilitating both the conversion of malate to oxaloacetate and replenishing levels of oxalacetate by reductive carboxylation of pyruvate. The LDH-like MDHs 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: 133424 [Multi-domain]  Cd Length: 300  Bit Score: 37.84  E-value: 8.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21730849   7 IIIAGIGRVGYTLAKSLSEKG-HDIVLIDIDKDICKKASAEI-DALVINGDCTKIK-TLEDAGIEDADMYIAVTGKEEVN 83
Cdd:cd01339   1 ISIIGAGNVGATLAQLLALKElGDVVLLDIVEGLPQGKALDIsQAAPILGSDTKVTgTNDYEDIAGSDVVVITAGIPRKP 80

                        90       100
                ....*....|....*....|
gi 21730849  84 LMS--SLLAKSYGINKTIAR 101
Cdd:cd01339  81 GMSrdDLLGTNAKIVKEVAE 100
PRK03562 PRK03562
glutathione-regulated potassium-efflux system protein KefC; Provisional
 7-84 1.05e-03

glutathione-regulated potassium-efflux system protein KefC; Provisional


Pssm-ID: 235131 [Multi-domain]  Cd Length: 621  Bit Score: 37.67  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21730849    7 IIIAGIGRVGYTLAKSLSEKGHDIVLIDIDKDickkasaEIDAL------VINGDCTKIKTLEDAGIEDADMYIAVTGKE 80
Cdd:PRK03562 403 VIIAGFGRFGQIVGRLLLSSGVKMTVLDHDPD-------HIETLrkfgmkVFYGDATRMDLLESAGAAKAEVLINAIDDP 475


                 ....
gi 21730849   81 EVNL 84
Cdd:PRK03562 476 QTSL 479
NAD_binding_7 pfam13241
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
 3-95 1.34e-03

Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.


Pssm-ID: 433055 [Multi-domain]  Cd Length: 104  Bit Score: 35.91  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21730849     3 HGMYIIIAGIGRVGYTLAKSLSEKGHDIVLIdidkdiCKKASAEIDALVingDCTKIKTLEDagIEDADMYIAVTGKEEV 82
Cdd:pfam13241   6 RGKRVLVVGGGEVAARKARKLLEAGAKVTVV------SPEITPFLEGLL---DLIRREFEGD--LDGADLVIAATDDPEL 74

                          90
                  ....*....|...
gi 21730849    83 NLMSSLLAKSYGI 95
Cdd:pfam13241  75 NERIAALARARGI 87
SDH_SDR_c_like cd05322
Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate ...
 7-139 2.33e-03

Sorbitol 6-phosphate dehydrogenase (SDH), classical (c) SDRs; Sorbitol 6-phosphate dehydrogenase (SDH, aka glucitol 6-phosphate dehydrogenase) catalyzes the NAD-dependent interconversion of D-fructose 6-phosphate to D-sorbitol 6-phosphate. SDH is a member of the classical SDRs, with the characteristic catalytic tetrad, but without a complete match to the typical NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187583 [Multi-domain]  Cd Length: 257  Bit Score: 36.67  E-value: 2.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21730849   7 IIIAGIGRVGYTLAKSLSEKGHDIVLIDIDKDICKKASAEIDALVingDCTKIKTLEDAgIEDADMYIAVTGKEEVNLMS 86
Cdd:cd05322   6 VVIGGGQTLGEFLCHGLAEAGYDVAVADINSENAEKVADEINAEY---GEKAYGFGADA-TNEQSVIALSKGVDEIFKRV 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 21730849  87 SLLAKSYGINKTiARISEIEYKDvFERlGVDVVVSPELIAANYIEKLIERPGI 139
Cdd:cd05322  82 DLLVYSAGIAKS-AKITDFELGD-FDR-SLQVNLVGYFLCAREFSKLMIRDGI 131
HicDH_like cd05291
L-2-hydroxyisocapronate dehydrogenases and some bacterial L-lactate dehydrogenases; ...
 7-71 3.94e-03

L-2-hydroxyisocapronate dehydrogenases and some bacterial L-lactate dehydrogenases; L-2-hydroxyisocapronate dehydrogenase (HicDH) catalyzes the conversion of a variety of 2-oxo carboxylic acids with medium-sized aliphatic or aromatic side chains. This subfamily is composed of HicDHs and some bacterial L-lactate dehydrogenases (LDH). LDHs catalyze the last step of glycolysis in which pyruvate is converted to L-lactate. Bacterial LDHs can be non-allosteric or may be activated by an allosteric effector such as fructose-1,6-bisphosphate. Members of this subfamily with known structures such as the HicDH of Lactobacillus confusus, the non-allosteric LDH of Lactobacillus pentosus, and the allosteric LDH of Bacillus stearothermophilus, show that they exist as homotetramers. The HicDH-like subfamily is 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: 133427 [Multi-domain]  Cd Length: 306  Bit Score: 35.91  E-value: 3.94e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21730849   7 IIIAGIGRVGYTLAKSLSEKG--HDIVLIDIDKDickKASAEI----DALVINGDCTKIK--TLEDAgiEDAD 71
Cdd:cd05291   3 VVIIGAGHVGSSFAYSLVNQGiaDELVLIDINEE---KAEGEAldleDALAFLPSPVKIKagDYSDC--KDAD 70
PRK06223 PRK06223
malate dehydrogenase; Reviewed
 5-74 4.93e-03

malate dehydrogenase; Reviewed


Pssm-ID: 180477 [Multi-domain]  Cd Length: 307  Bit Score: 35.49  E-value: 4.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21730849    5 MYIIIAGIGRVGYTLAKSLSEKGH-DIVLIDIDKDICK-KASAEIDALVINGDCTKIKTLED-AGIEDADMYI 74
Cdd:PRK06223   3 KKISIIGAGNVGATLAHLLALKELgDVVLFDIVEGVPQgKALDIAEAAPVEGFDTKITGTNDyEDIAGSDVVV 75
Ugd COG1004
UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];
5-42 8.37e-03

UDP-glucose 6-dehydrogenase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440628 [Multi-domain]  Cd Length: 436  Bit Score: 35.00  E-value: 8.37e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 21730849   5 MYIIIAGIGRVGYTLAKSLSEKGHDIVLIDIDKDICKK 42
Cdd:COG1004   1 MKIAVIGTGYVGLVTAACLAELGHEVTCVDIDEEKIEA 38
 
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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