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Conserved domains on  [gi|1729883084|ref|WP_148265554|]
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NADPH-dependent F420 reductase [Pediococcus claussenii]

Protein Classification

NADPH-dependent F420 reductase( domain architecture ID 11449986)

NADPH-dependent F420 reductase may be part of a F420-dependent NADP oxidoreductase catalyzing the reduction of NADP(+) with F420H(2) via hydride transfer, as well as the reverse reaction, the reduction of F420 with NADPH

CATH:  3.40.50.720
EC:  1.-.-.-
Gene Ontology:  GO:0052851|GO:0016491|GO:0070967|GO:0016651
SCOP:  4000104

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
7-206 8.33e-60

Predicted dinucleotide-binding enzyme [General function prediction only];


:

Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 186.91  E-value: 8.33e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729883084   7 VGILGAGKVGIVLADLALRAGYEVRIsGSGSVEKIDLTIKTLVPGAIASENSDVVANSDIIILAIPLSRYKNIDPEL--- 83
Cdd:COG2085     1 IGIIGTGNIGSALARRLAAAGHEVVI-GSRDPEKAAALAAELGPGARAGTNAEAAAAADVVVLAVPYEAVPDVLESLgda 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729883084  84 LSGKLVIDAMNYWWETDGIREEVLnPESTSSEQVQDYFKNSTIVKTFNHMGYHNLQEEAHPEGDpkRKALFVTGDNKEAV 163
Cdd:COG2085    80 LAGKIVIDATNPLPERDGFILDPP-GGGSAAELVAALLPGARVVKAFNTIGAAVLADPARPAGG--RRDVFVAGDDAEAK 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1729883084 164 DEVAKFVNTMGFDQVIHYNIADGIMTEPGSPLFGASLRLNELR 206
Cdd:COG2085   157 AVVAALIEDLGFDPVDAGPLANARRLEPLTPLLINLARTAGLE 199
 
Name Accession Description Interval E-value
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
7-206 8.33e-60

Predicted dinucleotide-binding enzyme [General function prediction only];


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 186.91  E-value: 8.33e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729883084   7 VGILGAGKVGIVLADLALRAGYEVRIsGSGSVEKIDLTIKTLVPGAIASENSDVVANSDIIILAIPLSRYKNIDPEL--- 83
Cdd:COG2085     1 IGIIGTGNIGSALARRLAAAGHEVVI-GSRDPEKAAALAAELGPGARAGTNAEAAAAADVVVLAVPYEAVPDVLESLgda 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729883084  84 LSGKLVIDAMNYWWETDGIREEVLnPESTSSEQVQDYFKNSTIVKTFNHMGYHNLQEEAHPEGDpkRKALFVTGDNKEAV 163
Cdd:COG2085    80 LAGKIVIDATNPLPERDGFILDPP-GGGSAAELVAALLPGARVVKAFNTIGAAVLADPARPAGG--RRDVFVAGDDAEAK 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1729883084 164 DEVAKFVNTMGFDQVIHYNIADGIMTEPGSPLFGASLRLNELR 206
Cdd:COG2085   157 AVVAALIEDLGFDPVDAGPLANARRLEPLTPLLINLARTAGLE 199
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
8-95 6.68e-17

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 73.03  E-value: 6.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729883084   8 GILGAGKVGIVLADLALRAG-YEVRISGSGSVEKIDLTIKTLVPGAIASENSDVVANSDIIILAIPLSRYKNIDPEL--- 83
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAGpHEVVVANSRNPEKAEELAEEYGVGATAVDNEEAAEEADVVFLAVKPEDAPDVLSELsdl 80

                          90
                  ....*....|..
gi 1729883084  84 LSGKLVIDAMNY 95
Cdd:pfam03807  81 LKGKIVISIAAG 92
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
 5-92 2.70e-04

Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the D-specific 2-hydroxyacid dehydrogenase family, catalyzes the NAD-dependent formation of phosphate from phosphite (hydrogen phosphonate). PTDH has been suggested as a potential enzyme for cofactor regeneration systems. The D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD-binding domain.


Pssm-ID: 240634 [Multi-domain]  Cd Length: 318  Bit Score: 41.12  E-value: 2.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729883084   5 KRVGILGAGKVGIVLADLAlrAGYEVRISGSGSVEKIDLTIKTLvpGAIASENSDVVANSDIIILAIPLSR--YKNIDPE 82
Cdd:cd12157   145 KTVGILGMGALGRAIARRL--SGFGATLLYYDPHPLDQAEEQAL--NLRRVELDELLESSDFLVLALPLTPdtLHLINAE 220

                          90
                  ....*....|....
gi 1729883084  83 LLS----GKLVIDA 92
Cdd:cd12157   221 ALAkmkpGALLVNP 234
PRK07530 PRK07530
3-hydroxybutyryl-CoA dehydrogenase; Validated
 1-33 6.70e-04

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181018 [Multi-domain]  Cd Length: 292  Bit Score: 39.99  E-value: 6.70e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1729883084   1 MMDIKRVGILGAGKVGIVLADLALRAGYEVRIS 33
Cdd:PRK07530    1 MMAIKKVGVIGAGQMGNGIAHVCALAGYDVLLN 33
 
Name Accession Description Interval E-value
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
7-206 8.33e-60

Predicted dinucleotide-binding enzyme [General function prediction only];


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 186.91  E-value: 8.33e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729883084   7 VGILGAGKVGIVLADLALRAGYEVRIsGSGSVEKIDLTIKTLVPGAIASENSDVVANSDIIILAIPLSRYKNIDPEL--- 83
Cdd:COG2085     1 IGIIGTGNIGSALARRLAAAGHEVVI-GSRDPEKAAALAAELGPGARAGTNAEAAAAADVVVLAVPYEAVPDVLESLgda 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729883084  84 LSGKLVIDAMNYWWETDGIREEVLnPESTSSEQVQDYFKNSTIVKTFNHMGYHNLQEEAHPEGDpkRKALFVTGDNKEAV 163
Cdd:COG2085    80 LAGKIVIDATNPLPERDGFILDPP-GGGSAAELVAALLPGARVVKAFNTIGAAVLADPARPAGG--RRDVFVAGDDAEAK 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1729883084 164 DEVAKFVNTMGFDQVIHYNIADGIMTEPGSPLFGASLRLNELR 206
Cdd:COG2085   157 AVVAALIEDLGFDPVDAGPLANARRLEPLTPLLINLARTAGLE 199
F420_oxidored pfam03807
NADP oxidoreductase coenzyme F420-dependent;
8-95 6.68e-17

NADP oxidoreductase coenzyme F420-dependent;


Pssm-ID: 397743 [Multi-domain]  Cd Length: 92  Bit Score: 73.03  E-value: 6.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729883084   8 GILGAGKVGIVLADLALRAG-YEVRISGSGSVEKIDLTIKTLVPGAIASENSDVVANSDIIILAIPLSRYKNIDPEL--- 83
Cdd:pfam03807   1 GFIGAGNMGEALARGLVAAGpHEVVVANSRNPEKAEELAEEYGVGATAVDNEEAAEEADVVFLAVKPEDAPDVLSELsdl 80

                          90
                  ....*....|..
gi 1729883084  84 LSGKLVIDAMNY 95
Cdd:pfam03807  81 LKGKIVISIAAG 92
COG5495 COG5495
Predicted oxidoreductase, contains short-chain dehydrogenase (SDR) and DUF2520 domains ...
 2-72 4.59e-10

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


Pssm-ID: 444246 [Multi-domain]  Cd Length: 286  Bit Score: 57.90  E-value: 4.59e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1729883084   2 MDIKRVGILGAGKVGIVLADLALRAGYEVR-ISGSG--SVEKidltIKTLVPGAIASENSDVVANSDIIILAIP 72
Cdd:COG5495     1 MARMKIGIIGAGRVGTALAAALRAAGHEVVgVYSRSpaSAER----AAALLGAVPALDLEELAAEADLVLLAVP 70
TyrA COG0287
Prephenate dehydrogenase [Amino acid transport and metabolism]; Prephenate dehydrogenase is ...
 4-92 1.15e-04

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: 42.04  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729883084   4 IKRVGILGAGKVGIVLAdLALR-AGYEVRISGSG-SVEKIDLTIKTLVPGAIASENSDVVANSDIIILAIPLSRY----K 77
Cdd:COG0287     1 FMRIAIIGLGLIGGSLA-LALKrAGLAHEVVGVDrSPETLERALELGVIDRAATDLEEAVADADLVVLAVPVGATievlA 79

                          90
                  ....*....|....*
gi 1729883084  78 NIDPELLSGKLVIDA 92
Cdd:COG0287    80 ELAPHLKPGAIVTDV 94
PTDH cd12157
Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the ...
 5-92 2.70e-04

Thermostable Phosphite Dehydrogenase; Phosphite dehydrogenase (PTDH), a member of the D-specific 2-hydroxyacid dehydrogenase family, catalyzes the NAD-dependent formation of phosphate from phosphite (hydrogen phosphonate). PTDH has been suggested as a potential enzyme for cofactor regeneration systems. The D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD-binding domain.


Pssm-ID: 240634 [Multi-domain]  Cd Length: 318  Bit Score: 41.12  E-value: 2.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729883084   5 KRVGILGAGKVGIVLADLAlrAGYEVRISGSGSVEKIDLTIKTLvpGAIASENSDVVANSDIIILAIPLSR--YKNIDPE 82
Cdd:cd12157   145 KTVGILGMGALGRAIARRL--SGFGATLLYYDPHPLDQAEEQAL--NLRRVELDELLESSDFLVLALPLTPdtLHLINAE 220

                          90
                  ....*....|....
gi 1729883084  83 LLS----GKLVIDA 92
Cdd:cd12157   221 ALAkmkpGALLVNP 234
Rossmann-like pfam10727
Rossmann-like domain; This family of proteins contain a Rossmann-like domain.
 7-83 2.71e-04

Rossmann-like domain; This family of proteins contain a Rossmann-like domain.


Pssm-ID: 287672 [Multi-domain]  Cd Length: 127  Bit Score: 39.46  E-value: 2.71e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1729883084   7 VGILGAGKVGIVLADLALRAGYEVRISGSGSVEKIDLTiKTLVPGAIASENSDVVANSDIIILAIPlsrykniDPEL 83
Cdd:pfam10727  13 VGIISAGRVGTALGAALERAGHVVVGISAISAASRERA-ERRLPDTPVLPVPDVAARAELLLLAVP-------DAEL 81
ProC COG0345
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ...
 5-90 4.51e-04

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: 40.43  E-value: 4.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729883084   5 KRVGILGAGKVGIVLADLALRAGY---EVRISGSgSVEKIDlTIKTLVPGAIASENSDVVANSDIIILAIP-------Ls 74
Cdd:COG0345     3 MKIGFIGAGNMGSAIIKGLLKSGVppeDIIVSDR-SPERLE-ALAERYGVRVTTDNAEAAAQADVVVLAVKpqdlaevL- 79

                          90
                  ....*....|....*.
gi 1729883084  75 ryKNIDPELLSGKLVI 90
Cdd:COG0345    80 --EELAPLLDPDKLVI 93
PRK07530 PRK07530
3-hydroxybutyryl-CoA dehydrogenase; Validated
 1-33 6.70e-04

3-hydroxybutyryl-CoA dehydrogenase; Validated


Pssm-ID: 181018 [Multi-domain]  Cd Length: 292  Bit Score: 39.99  E-value: 6.70e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1729883084   1 MMDIKRVGILGAGKVGIVLADLALRAGYEVRIS 33
Cdd:PRK07530    1 MMAIKKVGVIGAGQMGNGIAHVCALAGYDVLLN 33
gpsA PRK00094
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
5-72 8.39e-04

NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;


Pssm-ID: 234629 [Multi-domain]  Cd Length: 325  Bit Score: 39.67  E-value: 8.39e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1729883084   5 KRVGILGAGKVGIVLADLALRAGYEVRISG--SGSVEKI--DLTIKTLVPGAIASEN-------SDVVANSDIIILAIP 72
Cdd:PRK00094    2 MKIAVLGAGSWGTALAIVLARNGHDVTLWArdPEQAAEInaDRENPRYLPGIKLPDNlrattdlAEALADADLILVAVP 80
PRK14619 PRK14619
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
 1-73 1.68e-03

NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional


Pssm-ID: 237771 [Multi-domain]  Cd Length: 308  Bit Score: 38.81  E-value: 1.68e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1729883084   1 MMDIKRVGILGAGKVGIVLADLALRAGYEVRI---SGSGSVEKidltiktlvpgaiasensdVVANSDIIILAIPL 73
Cdd:PRK14619    1 TTQPKTIAILGAGAWGSTLAGLASANGHRVRVwsrRSGLSLAA-------------------VLADADVIVSAVSM 57
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 5-85 3.54e-03

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240642 [Multi-domain]  Cd Length: 314  Bit Score: 37.61  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729883084   5 KRVGILGAGKVGIVLADLALRAGYEVR-ISGSGSVEKIDLTIKTLvpgaiaSENSDVVANSDIIILAIPLSRYKN--IDP 81
Cdd:cd12165   138 KTVGILGYGHIGREIARLLKAFGMRVIgVSRSPKEDEGADFVGTL------SDLDEALEQADVVVVALPLTKQTRglIGA 211


                  ....
gi 1729883084  82 ELLS 85
Cdd:cd12165   212 AELA 215
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 5-74 3.89e-03

D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family pfam00389.


Pssm-ID: 427007 [Multi-domain]  Cd Length: 178  Bit Score: 37.09  E-value: 3.89e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729883084   5 KRVGILGAGKVGIVLADLAlrAGYEVRISGSGSVEKIDLTIKTLvpGAIASENSDVVANSDIIILAIPLS 74
Cdd:pfam02826  37 KTVGIIGLGRIGRAVAKRL--KAFGMKVIAYDRYPKPEEEEEEL--GARYVSLDELLAESDVVSLHLPLT 102
PRK07688 PRK07688
thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated
 5-92 8.03e-03

thiamine/molybdopterin biosynthesis ThiF/MoeB-like protein; Validated


Pssm-ID: 181084 [Multi-domain]  Cd Length: 339  Bit Score: 36.89  E-value: 8.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729883084   5 KRVGILGAGKVGIVLADLALRAGY-EVRISGSGSVEKIDLTIKTL---------VPGAIASENSDVVANSDIIILAIPLS 74
Cdd:PRK07688   25 KHVLIIGAGALGTANAEMLVRAGVgKVTIVDRDYVEWSNLQRQQLytesdvknnLPKAVAAKKRLEEINSDVRVEAIVQD 104

                          90
                  ....*....|....*....
gi 1729883084  75 -RYKNIDPELLSGKLVIDA 92
Cdd:PRK07688  105 vTAEELEELVTGVDLIIDA 123
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 5-91 8.10e-03

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 36.63  E-value: 8.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729883084   5 KRVGILGAGKVGIVLADLALRAGYEVRISgsgsvekiDLT---IKTLVP-GAIASEN-SDVVANSDIIILAIP------- 72
Cdd:COG2084     2 MKVGFIGLGAMGAPMARNLLKAGHEVTVW--------NRTpakAEALVAaGARVAASpAEAAAAADVVITMLPddaavee 73

                          90       100
                  ....*....|....*....|
gi 1729883084  73 -LSRYKNIDPELLSGKLVID 91
Cdd:COG2084    74 vLLGEDGLLAALRPGAVVVD 93
 
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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