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Conserved domains on  [gi|1330235883|ref|WP_102394154|]
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MULTISPECIES: pyridoxamine 5'-phosphate oxidase family protein [Vibrio]

Protein Classification

pyridoxamine 5'-phosphate oxidase family protein( domain architecture ID 10583942)

pyridoxamine 5'-phosphate oxidase family protein may catalyze an FMN-mediated redox reaction, similar to Mycobacterium tuberculosis uncharacterized protein Rv0080, which is a member of the dormancy regulon and is induced in response to reduced oxygen tension, as well as low levels of nitric oxide and carbon monoxide

CATH:  2.30.110.10
EC:  1.-.-.-
Gene Ontology:  GO:0016491|GO:0010181
PubMed:  26434506|32951820
SCOP:  4002129

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Pyridox_ox_2 pfam12900
Pyridoxamine 5'-phosphate oxidase; Pyridoxamine 5'-phosphate oxidase is a FMN flavoprotein ...
20-163 6.77e-41

Pyridoxamine 5'-phosphate oxidase; Pyridoxamine 5'-phosphate oxidase is a FMN flavoprotein that catalyzes the oxidation of pyridoxamine-5-P (PMP) and pyridoxine-5-P (PNP) to pyridoxal-5-P (PLP). This entry contains several pyridoxamine 5'-phosphate oxidases, and related proteins.


:

Pssm-ID: 432864  Cd Length: 143  Bit Score: 136.39  E-value: 6.77e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330235883  20 EQEKLHQIIDESLIAHIALQGEQGPMVIPMLAWRVDDMVYIHGAKNSRLLKGLKkGEPTCLTFTLFDGWVLARSAFHHSA 99
Cdd:pfam12900   1 DREECHALLDSGPVGRLAFVDDGAPYILPVNYVVDGDTLYFHGATGSKLAAALR-GAPVCVVVFEVDGLVLARSAFHHSM 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1330235883 100 HYRSAVVLGSFSVIDDNQEKDRLLNIFIEQIAPGRTDEVRLSNEKELTATELLAIPLTEASVKI 163
Cdd:pfam12900  80 NWRSVVVRGTAELVTDPEEKAAALEALTDRIVPGRWDNLRPPTRKELAATAVLRITPDEISGRR 143
 
Name Accession Description Interval E-value
Pyridox_ox_2 pfam12900
Pyridoxamine 5'-phosphate oxidase; Pyridoxamine 5'-phosphate oxidase is a FMN flavoprotein ...
20-163 6.77e-41

Pyridoxamine 5'-phosphate oxidase; Pyridoxamine 5'-phosphate oxidase is a FMN flavoprotein that catalyzes the oxidation of pyridoxamine-5-P (PMP) and pyridoxine-5-P (PNP) to pyridoxal-5-P (PLP). This entry contains several pyridoxamine 5'-phosphate oxidases, and related proteins.


Pssm-ID: 432864  Cd Length: 143  Bit Score: 136.39  E-value: 6.77e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330235883  20 EQEKLHQIIDESLIAHIALQGEQGPMVIPMLAWRVDDMVYIHGAKNSRLLKGLKkGEPTCLTFTLFDGWVLARSAFHHSA 99
Cdd:pfam12900   1 DREECHALLDSGPVGRLAFVDDGAPYILPVNYVVDGDTLYFHGATGSKLAAALR-GAPVCVVVFEVDGLVLARSAFHHSM 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1330235883 100 HYRSAVVLGSFSVIDDNQEKDRLLNIFIEQIAPGRTDEVRLSNEKELTATELLAIPLTEASVKI 163
Cdd:pfam12900  80 NWRSVVVRGTAELVTDPEEKAAALEALTDRIVPGRWDNLRPPTRKELAATAVLRITPDEISGRR 143
NimA COG3467
Nitroimidazole reductase NimA or a related FMN-containing flavoprotein, pyridoxamine 5 ...
15-162 9.31e-31

Nitroimidazole reductase NimA or a related FMN-containing flavoprotein, pyridoxamine 5'-phosphate oxidase superfamily [Defense mechanisms];


Pssm-ID: 442690 [Multi-domain]  Cd Length: 144  Bit Score: 110.40  E-value: 9.31e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330235883  15 HKAVFEQEKLHQIIDESLIAHIALQGEQGPMVIPMLAWRVDDMVYIHGAKNSRLLKGLKKGEPTCLTFTLFDGWvlarsa 94
Cdd:COG3467     4 KDRELDREEIRALLDEARVGRLATVDDGRPYVVPVNYVYDGDTIYFHTAKEGRKLDNLRRNPRVCFEVDELDGL------ 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330235883  95 fhHSAHYRSAVVLGSFSVIDDNQEKDRLLNIFIEQIAPGRTDEVrlsNEKELTATELLAIPLTEASVK 162
Cdd:COG3467    78 --HSTNYRSVVVFGRAEEVEDPEEKARALRLLLEKYAPGRWRPF---SDKELDATAVIRIDPEEISGK 140
 
Name Accession Description Interval E-value
Pyridox_ox_2 pfam12900
Pyridoxamine 5'-phosphate oxidase; Pyridoxamine 5'-phosphate oxidase is a FMN flavoprotein ...
20-163 6.77e-41

Pyridoxamine 5'-phosphate oxidase; Pyridoxamine 5'-phosphate oxidase is a FMN flavoprotein that catalyzes the oxidation of pyridoxamine-5-P (PMP) and pyridoxine-5-P (PNP) to pyridoxal-5-P (PLP). This entry contains several pyridoxamine 5'-phosphate oxidases, and related proteins.


Pssm-ID: 432864  Cd Length: 143  Bit Score: 136.39  E-value: 6.77e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330235883  20 EQEKLHQIIDESLIAHIALQGEQGPMVIPMLAWRVDDMVYIHGAKNSRLLKGLKkGEPTCLTFTLFDGWVLARSAFHHSA 99
Cdd:pfam12900   1 DREECHALLDSGPVGRLAFVDDGAPYILPVNYVVDGDTLYFHGATGSKLAAALR-GAPVCVVVFEVDGLVLARSAFHHSM 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1330235883 100 HYRSAVVLGSFSVIDDNQEKDRLLNIFIEQIAPGRTDEVRLSNEKELTATELLAIPLTEASVKI 163
Cdd:pfam12900  80 NWRSVVVRGTAELVTDPEEKAAALEALTDRIVPGRWDNLRPPTRKELAATAVLRITPDEISGRR 143
NimA COG3467
Nitroimidazole reductase NimA or a related FMN-containing flavoprotein, pyridoxamine 5 ...
15-162 9.31e-31

Nitroimidazole reductase NimA or a related FMN-containing flavoprotein, pyridoxamine 5'-phosphate oxidase superfamily [Defense mechanisms];


Pssm-ID: 442690 [Multi-domain]  Cd Length: 144  Bit Score: 110.40  E-value: 9.31e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330235883  15 HKAVFEQEKLHQIIDESLIAHIALQGEQGPMVIPMLAWRVDDMVYIHGAKNSRLLKGLKKGEPTCLTFTLFDGWvlarsa 94
Cdd:COG3467     4 KDRELDREEIRALLDEARVGRLATVDDGRPYVVPVNYVYDGDTIYFHTAKEGRKLDNLRRNPRVCFEVDELDGL------ 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330235883  95 fhHSAHYRSAVVLGSFSVIDDNQEKDRLLNIFIEQIAPGRTDEVrlsNEKELTATELLAIPLTEASVK 162
Cdd:COG3467    78 --HSTNYRSVVVFGRAEEVEDPEEKARALRLLLEKYAPGRWRPF---SDKELDATAVIRIDPEEISGK 140
 
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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