NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|556293694|ref|WP_023291846|]
View 

MULTISPECIES: 4-hydroxyphenylacetate 3-monooxygenase reductase subunit [Klebsiella]

Protein Classification

PNPOx family protein( domain architecture ID 1004)

PNPOx family protein similar to Escherichia coli pyridoxamine 5'-phosphate oxidase (PNPOx), a FMN flavoprotein that catalyzes the oxidation of pyridoxamine-5-P (PMP) and pyridoxine-5-P (PNP) to pyridoxal-5-P (PLP)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PNPOx/FlaRed_like super family cl00381
Pyridoxine 5'-phosphate (PNP) oxidase-like and flavin reductase-like proteins; The PNPOx-like ...
 1-170 4.99e-130

Pyridoxine 5'-phosphate (PNP) oxidase-like and flavin reductase-like proteins; The PNPOx-like superfamily is composed of pyridoxine 5'-phosphate (PNP) oxidases and other flavin mononucleotide (FMN) binding proteins, which catalyze FMN-mediated redox reactions. Flavin reductases catalyze the reduction of FMN or FAD using NAD(P)H as a cofactor. They are part of a two-component enzyme system, composed of a smaller component (flavin reductase) and a larger component (an oxidase), which uses the reduced flavin to hydroxylate substrates.


The actual alignment was detected with superfamily member PRK15486:

Pssm-ID: 469750  Cd Length: 170  Bit Score: 360.90  E-value: 4.99e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293694   1 MQLDEQRLRFRDAMASLSAAVNVVTTAGEAGRCGITATAVCSVTDTPPSVMVCINANSAMNPVFQGNGKLCINVLNHEQE 80
Cdd:PRK15486   1 MQLDEQRLRFRDAMASLSAAVNIVTTAGDAGRCGITATAVCSVTDTPPSVMVCINANSAMNPVFQGNGKLCINVLNHEQE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293694  81 IMARHFAGMTGVTMEERFALSGWQQGALGQPVLKGSLASLEGEISQVQTIGTHLVYLVEIRNITLSQQGHGLIYFKRRFH 160
Cdd:PRK15486  81 LMARHFAGMTGMAMEERFSLSCWQKGPLGQPVLKGSLASLEGEISDVQTIGTHLVYLVEIKNIILSAEGHGLIYFKRRFH 160

                        170
                 ....*....|
gi 556293694 161 PVMMEMEVAV 170
Cdd:PRK15486 161 PVMLEMEAAV 170
 
Name Accession Description Interval E-value
hpaC PRK15486
4-hydroxyphenylacetate 3-monooxygenase reductase subunit; Provisional
 1-170 4.99e-130

4-hydroxyphenylacetate 3-monooxygenase reductase subunit; Provisional


Pssm-ID: 185383  Cd Length: 170  Bit Score: 360.90  E-value: 4.99e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293694   1 MQLDEQRLRFRDAMASLSAAVNVVTTAGEAGRCGITATAVCSVTDTPPSVMVCINANSAMNPVFQGNGKLCINVLNHEQE 80
Cdd:PRK15486   1 MQLDEQRLRFRDAMASLSAAVNIVTTAGDAGRCGITATAVCSVTDTPPSVMVCINANSAMNPVFQGNGKLCINVLNHEQE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293694  81 IMARHFAGMTGVTMEERFALSGWQQGALGQPVLKGSLASLEGEISQVQTIGTHLVYLVEIRNITLSQQGHGLIYFKRRFH 160
Cdd:PRK15486  81 LMARHFAGMTGMAMEERFSLSCWQKGPLGQPVLKGSLASLEGEISDVQTIGTHLVYLVEIKNIILSAEGHGLIYFKRRFH 160

                        170
                 ....*....|
gi 556293694 161 PVMMEMEVAV 170
Cdd:PRK15486 161 PVMLEMEAAV 170
HpaC TIGR02296
4-hydroxyphenylacetate 3-monooxygenase, reductase component; This model identifies the ...
 10-163 6.22e-96

4-hydroxyphenylacetate 3-monooxygenase, reductase component; This model identifies the reductase component (HpaC) of 4-hydroxyphenylacetate 3-monooxygenase. This enzyme catalyzes the first step (hydroxylation at the 3-position) in the degradation of 4-hydroxyphenylacetate to succinate and pyruvate. 4-hydroxyphenylacetate arises from the degradation of tyrosine. These reductases catalyze the reduction of free flavins by NADPH. The flavin is then utilized by the large subunit of the monooxygenase.


Pssm-ID: 131349  Cd Length: 154  Bit Score: 274.33  E-value: 6.22e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293694   10 FRDAMASLSAAVNVVTTAGEAGRCGITATAVCSVTDTPPSVMVCINANSAMNPVFQGNGKLCINVLNHEQEIMARHFAGM 89
Cdd:TIGR02296   1 FRDAMASLAAAVNIITTNGIAGKCGITATAVCSVTDTPPTVMVCINRNSAMNPIFQENGKLCINVLAHEQQEMAEHFAGM 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556293694   90 TGVTMEERFALSGWQQGALGQPVLKGSLASLEGEISQVQTIGTHLVYLVEIRNITLSQQGHGLIYFKRRFHPVM 163
Cdd:TIGR02296  81 TGLAMEERFAWHIWHEGPDGQPVLKGALAHLEGHIVDKHEIGTHTVFLVELKEIKVNGKRHALVYFRRQFKFVD 154
Flavin_Reduct smart00903
Flavin reductase like domain; This entry represents the FMN-binding domain found in NAD(P) ...
 14-159 1.07e-47

Flavin reductase like domain; This entry represents the FMN-binding domain found in NAD(P)H-flavin oxidoreductases (flavin reductases), a class of enzymes capable of producing reduced flavin for bacterial bioluminescence and other biological processes. This domain is also found in various other oxidoreductase and monooxygenase enzymes... This domain consists of a beta-barrel with Greek key topology, and is related to the ferredoxin reductase-like FAD-binding domain. The flavin reductases have a different dimerisation mode than that found in the PNP oxidase-like family, which also carries an FMN-binding domain with a similar topology.


Pssm-ID: 214900  Cd Length: 147  Bit Score: 151.93  E-value: 1.07e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293694    14 MASLSAAVNVVTTAGEAG-RCGITATAVCSVTDTPPSVMVCINANSAMNPVFQGNGKLCINVLNHEQEIMARHFAGMTGV 92
Cdd:smart00903   1 LGRFPTGVAVVTTRDGDGgRVGLTASSFVSVSLDPPLVLVCVAKSSSTHPLIRESGRFVVNVLAEDQADLARRFAGKSGA 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556293694    93 TMEERFALSGWQQGALGQPVLKGSLASLEGEISQVQTIGTHLVYLVEIRNITLSQQGHGLIYFKRRF 159
Cdd:smart00903  81 DRFEGVAWGLTEAGVTGAPILAGALAWLECRVVQVIEVGDHTIFVGEVVAVHVRDDGEPLVYHRGGY 147
RutF COG1853
FMN reductase RutF, DIM6/NTAB family [Energy production and conversion]; FMN reductase RutF, ...
 6-160 2.42e-45

FMN reductase RutF, DIM6/NTAB family [Energy production and conversion]; FMN reductase RutF, DIM6/NTAB family is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 441458  Cd Length: 160  Bit Score: 146.13  E-value: 2.42e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293694   6 QRLRFRDAMASLSAAVNVVTTAGEAG-RCGITATAVCSVTDTPPSVMVCINANSAMNPVFQGNGKLCINVLNHEQEIMAR 84
Cdd:COG1853    1 MPDAFRDALGRLAPGVAVVTTRDADGrPNGMTASSFTSVSLDPPLVLVSVAKSSDTLENIRETGEFVVNVLSEDQAELAN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293694  85 HFAGMTGvTMEERFALSGW--QQGALGQPVLKGSLASLEGEISQVQTIGTHLVYLVEIRNITL--SQQGHGLIYFKRRFH 160
Cdd:COG1853   81 RFAGRSG-RGVDKFAGAGLttASGEVGAPLLAEAPAWLECRVVDVIELGDHTLFIGEVVAVHVdeDVDGRPLLYLGGRYR 159
Flavin_Reduct pfam01613
Flavin reductase like domain; This is a flavin reductase family consisting of enzymes known to ...
 14-162 7.31e-38

Flavin reductase like domain; This is a flavin reductase family consisting of enzymes known to be flavin reductases as well as various oxidoreductase and monooxygenase components. VlmR is a flavin reductase that functions in a two-component enzyme system to provide isobutylamine N-hydroxylase with reduced flavin and may be involved in the synthesis of valanimycin. SnaC is a flavin reductase that provides reduced flavin for the oxidation of pristinamycin IIB to pristinamycin IIA as catalyzed by SnaA, SnaB heterodimer. This flavin reductase region characterized by enzymes of the family is present in the C-terminus of potential FMN proteins from Synechocystis sp. suggesting it is a flavin reductase domain.


Pssm-ID: 460266  Cd Length: 149  Bit Score: 127.01  E-value: 7.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293694   14 MASLSAAVNVVTTAGEAGRCGITATAVCSVTDTPPSVMVCINANSAMNPVFQGNGKLCINVLNHEQEIMARHFAGMTGvt 93
Cdd:pfam01613   1 MRRFPTGVAVVTTDDGGEPNGMTVSSFTSVSLDPPLVLVSINRSSSTHDAIEASGEFVVNVLAEDQEELARRFAGRSG-- 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556293694   94 mEERFALSGWQQGALGQPVLKGSLASLEGEISQVQTIGTHLVYLVEIRNITLSQQGHG--LIYFKRRFHPV 162
Cdd:pfam01613  79 -RDKFAGITWVEGKVGAPLLKGALAALECRVVDTVDVGDHTLFIGEVVDVRVDEDADGepLLYYRRRYRSL 148
 
Name Accession Description Interval E-value
hpaC PRK15486
4-hydroxyphenylacetate 3-monooxygenase reductase subunit; Provisional
 1-170 4.99e-130

4-hydroxyphenylacetate 3-monooxygenase reductase subunit; Provisional


Pssm-ID: 185383  Cd Length: 170  Bit Score: 360.90  E-value: 4.99e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293694   1 MQLDEQRLRFRDAMASLSAAVNVVTTAGEAGRCGITATAVCSVTDTPPSVMVCINANSAMNPVFQGNGKLCINVLNHEQE 80
Cdd:PRK15486   1 MQLDEQRLRFRDAMASLSAAVNIVTTAGDAGRCGITATAVCSVTDTPPSVMVCINANSAMNPVFQGNGKLCINVLNHEQE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293694  81 IMARHFAGMTGVTMEERFALSGWQQGALGQPVLKGSLASLEGEISQVQTIGTHLVYLVEIRNITLSQQGHGLIYFKRRFH 160
Cdd:PRK15486  81 LMARHFAGMTGMAMEERFSLSCWQKGPLGQPVLKGSLASLEGEISDVQTIGTHLVYLVEIKNIILSAEGHGLIYFKRRFH 160

                        170
                 ....*....|
gi 556293694 161 PVMMEMEVAV 170
Cdd:PRK15486 161 PVMLEMEAAV 170
HpaC TIGR02296
4-hydroxyphenylacetate 3-monooxygenase, reductase component; This model identifies the ...
 10-163 6.22e-96

4-hydroxyphenylacetate 3-monooxygenase, reductase component; This model identifies the reductase component (HpaC) of 4-hydroxyphenylacetate 3-monooxygenase. This enzyme catalyzes the first step (hydroxylation at the 3-position) in the degradation of 4-hydroxyphenylacetate to succinate and pyruvate. 4-hydroxyphenylacetate arises from the degradation of tyrosine. These reductases catalyze the reduction of free flavins by NADPH. The flavin is then utilized by the large subunit of the monooxygenase.


Pssm-ID: 131349  Cd Length: 154  Bit Score: 274.33  E-value: 6.22e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293694   10 FRDAMASLSAAVNVVTTAGEAGRCGITATAVCSVTDTPPSVMVCINANSAMNPVFQGNGKLCINVLNHEQEIMARHFAGM 89
Cdd:TIGR02296   1 FRDAMASLAAAVNIITTNGIAGKCGITATAVCSVTDTPPTVMVCINRNSAMNPIFQENGKLCINVLAHEQQEMAEHFAGM 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556293694   90 TGVTMEERFALSGWQQGALGQPVLKGSLASLEGEISQVQTIGTHLVYLVEIRNITLSQQGHGLIYFKRRFHPVM 163
Cdd:TIGR02296  81 TGLAMEERFAWHIWHEGPDGQPVLKGALAHLEGHIVDKHEIGTHTVFLVELKEIKVNGKRHALVYFRRQFKFVD 154
Flavin_Reduct smart00903
Flavin reductase like domain; This entry represents the FMN-binding domain found in NAD(P) ...
 14-159 1.07e-47

Flavin reductase like domain; This entry represents the FMN-binding domain found in NAD(P)H-flavin oxidoreductases (flavin reductases), a class of enzymes capable of producing reduced flavin for bacterial bioluminescence and other biological processes. This domain is also found in various other oxidoreductase and monooxygenase enzymes... This domain consists of a beta-barrel with Greek key topology, and is related to the ferredoxin reductase-like FAD-binding domain. The flavin reductases have a different dimerisation mode than that found in the PNP oxidase-like family, which also carries an FMN-binding domain with a similar topology.


Pssm-ID: 214900  Cd Length: 147  Bit Score: 151.93  E-value: 1.07e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293694    14 MASLSAAVNVVTTAGEAG-RCGITATAVCSVTDTPPSVMVCINANSAMNPVFQGNGKLCINVLNHEQEIMARHFAGMTGV 92
Cdd:smart00903   1 LGRFPTGVAVVTTRDGDGgRVGLTASSFVSVSLDPPLVLVCVAKSSSTHPLIRESGRFVVNVLAEDQADLARRFAGKSGA 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556293694    93 TMEERFALSGWQQGALGQPVLKGSLASLEGEISQVQTIGTHLVYLVEIRNITLSQQGHGLIYFKRRF 159
Cdd:smart00903  81 DRFEGVAWGLTEAGVTGAPILAGALAWLECRVVQVIEVGDHTIFVGEVVAVHVRDDGEPLVYHRGGY 147
RutF COG1853
FMN reductase RutF, DIM6/NTAB family [Energy production and conversion]; FMN reductase RutF, ...
 6-160 2.42e-45

FMN reductase RutF, DIM6/NTAB family [Energy production and conversion]; FMN reductase RutF, DIM6/NTAB family is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 441458  Cd Length: 160  Bit Score: 146.13  E-value: 2.42e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293694   6 QRLRFRDAMASLSAAVNVVTTAGEAG-RCGITATAVCSVTDTPPSVMVCINANSAMNPVFQGNGKLCINVLNHEQEIMAR 84
Cdd:COG1853    1 MPDAFRDALGRLAPGVAVVTTRDADGrPNGMTASSFTSVSLDPPLVLVSVAKSSDTLENIRETGEFVVNVLSEDQAELAN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293694  85 HFAGMTGvTMEERFALSGW--QQGALGQPVLKGSLASLEGEISQVQTIGTHLVYLVEIRNITL--SQQGHGLIYFKRRFH 160
Cdd:COG1853   81 RFAGRSG-RGVDKFAGAGLttASGEVGAPLLAEAPAWLECRVVDVIELGDHTLFIGEVVAVHVdeDVDGRPLLYLGGRYR 159
Flavin_Reduct pfam01613
Flavin reductase like domain; This is a flavin reductase family consisting of enzymes known to ...
 14-162 7.31e-38

Flavin reductase like domain; This is a flavin reductase family consisting of enzymes known to be flavin reductases as well as various oxidoreductase and monooxygenase components. VlmR is a flavin reductase that functions in a two-component enzyme system to provide isobutylamine N-hydroxylase with reduced flavin and may be involved in the synthesis of valanimycin. SnaC is a flavin reductase that provides reduced flavin for the oxidation of pristinamycin IIB to pristinamycin IIA as catalyzed by SnaA, SnaB heterodimer. This flavin reductase region characterized by enzymes of the family is present in the C-terminus of potential FMN proteins from Synechocystis sp. suggesting it is a flavin reductase domain.


Pssm-ID: 460266  Cd Length: 149  Bit Score: 127.01  E-value: 7.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556293694   14 MASLSAAVNVVTTAGEAGRCGITATAVCSVTDTPPSVMVCINANSAMNPVFQGNGKLCINVLNHEQEIMARHFAGMTGvt 93
Cdd:pfam01613   1 MRRFPTGVAVVTTDDGGEPNGMTVSSFTSVSLDPPLVLVSINRSSSTHDAIEASGEFVVNVLAEDQEELARRFAGRSG-- 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556293694   94 mEERFALSGWQQGALGQPVLKGSLASLEGEISQVQTIGTHLVYLVEIRNITLSQQGHG--LIYFKRRFHPV 162
Cdd:pfam01613  79 -RDKFAGITWVEGKVGAPLLKGALAALECRVVDTVDVGDHTLFIGEVVDVRVDEDADGepLLYYRRRYRSL 148
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH