(data stored in ACNUC1104 zone)

SWISSPROT: D7A1Y7_STAND

ID   D7A1Y7_STAND            Unreviewed;       208 AA.
AC   D7A1Y7;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   RecName: Full=Pyridoxine/pyridoxamine 5'-phosphate oxidase {ECO:0000256|HAMAP-Rule:MF_01629};
DE            EC=1.4.3.5 {ECO:0000256|HAMAP-Rule:MF_01629};
DE   AltName: Full=PNP/PMP oxidase {ECO:0000256|HAMAP-Rule:MF_01629};
DE            Short=PNPOx {ECO:0000256|HAMAP-Rule:MF_01629};
DE   AltName: Full=Pyridoxal 5'-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_01629};
GN   Name=pdxH {ECO:0000256|HAMAP-Rule:MF_01629};
GN   OrderedLocusNames=Snov_0269 {ECO:0000313|EMBL:ADH87603.1};
OS   Starkeya novella (strain ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 /
OS   NBRC 12443 / NCIB 9113).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Xanthobacteraceae; Starkeya.
OX   NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH87603.1, ECO:0000313|Proteomes:UP000006633};
RN   [1] {ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Beatson S., Kappler U.,
RA   Woyke T.;
RT   "Complete sequence of Starkeya novella DSM 506.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADH87603.1, ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RX   PubMed=23450099; DOI=10.4056/sigs.3006378;
RA   Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A.,
RA   Copeland A., Berry K.W., Glavina Del Rio T., Hammon N., Dalin E.,
RA   Tice H., Pitluck S., Richardson P., Bruce D., Goodwin L.A., Han C.,
RA   Tapia R., Detter J.C., Chang Y.J., Jeffries C.D., Land M., Hauser L.,
RA   Kyrpides N.C., Goker M., Ivanova N., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of the facultatively chemolithoautotrophic
RT   and methylotrophic alpha Proteobacterium Starkeya novella type strain
RT   (ATCC 8093(T)).";
RL   Stand. Genomic Sci. 7:44-58(2012).
CC   -!- FUNCTION: Catalyzes the oxidation of either pyridoxine 5'-
CC       phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal
CC       5'-phosphate (PLP). {ECO:0000256|HAMAP-Rule:MF_01629,
CC       ECO:0000256|SAAS:SAAS01168658}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O2 + pyridoxamine 5'-phosphate = H2O2 + NH4(+) +
CC         pyridoxal 5'-phosphate; Xref=Rhea:RHEA:15817, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58451, ChEBI:CHEBI:597326; EC=1.4.3.5;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01629,
CC         ECO:0000256|SAAS:SAAS01168662};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O2 + pyridoxine 5'-phosphate = H2O2 + pyridoxal 5'-
CC         phosphate; Xref=Rhea:RHEA:15149, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:58589, ChEBI:CHEBI:597326;
CC         EC=1.4.3.5; Evidence={ECO:0000256|HAMAP-Rule:MF_01629,
CC         ECO:0000256|SAAS:SAAS01168664};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01629, ECO:0000256|PIRSR:PIRSR000190-2};
CC       Note=Binds 1 FMN per subunit. {ECO:0000256|HAMAP-Rule:MF_01629,
CC       ECO:0000256|PIRSR:PIRSR000190-2};
CC   -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage;
CC       pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01629, ECO:0000256|SAAS:SAAS01168665}.
CC   -!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage;
CC       pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01629, ECO:0000256|SAAS:SAAS01168655}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01629,
CC       ECO:0000256|SAAS:SAAS01072423}.
CC   -!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase
CC       family. {ECO:0000256|HAMAP-Rule:MF_01629,
CC       ECO:0000256|SAAS:SAAS01071553}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01629}.
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DR   EMBL; CP002026; ADH87603.1; -; Genomic_DNA.
DR   RefSeq; WP_013165108.1; NC_014217.1.
DR   STRING; 639283.Snov_0269; -.
DR   EnsemblBacteria; ADH87603; ADH87603; Snov_0269.
DR   KEGG; sno:Snov_0269; -.
DR   eggNOG; ENOG4108S7T; Bacteria.
DR   eggNOG; COG0259; LUCA.
DR   HOGENOM; HOG000242755; -.
DR   KO; K00275; -.
DR   OMA; PEPNAMV; -.
DR   OrthoDB; 1542844at2; -.
DR   BioCyc; SNOV639283:G1GLM-271-MONOMER; -.
DR   UniPathway; UPA01068; UER00304.
DR   Proteomes; UP000006633; Chromosome.
DR   GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004733; F:pyridoxamine-phosphate oxidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.110.10; -; 1.
DR   HAMAP; MF_01629; PdxH; 1.
DR   InterPro; IPR000659; Pyridox_Oxase.
DR   InterPro; IPR019740; Pyridox_Oxase_CS.
DR   InterPro; IPR011576; Pyridox_Oxase_put.
DR   InterPro; IPR019576; Pyridoxamine_oxidase_dimer_C.
DR   InterPro; IPR012349; Split_barrel_FMN-bd.
DR   PANTHER; PTHR10851; PTHR10851; 1.
DR   Pfam; PF10590; PNP_phzG_C; 1.
DR   Pfam; PF01243; Putative_PNPOx; 1.
DR   PIRSF; PIRSF000190; Pyd_amn-ph_oxd; 1.
DR   TIGRFAMs; TIGR00558; pdxH; 1.
DR   PROSITE; PS01064; PYRIDOX_OXIDASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; D7A1Y7.
DR   SWISS-2DPAGE; D7A1Y7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006633};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01629,
KW   ECO:0000256|SAAS:SAAS01072426};
KW   FMN {ECO:0000256|HAMAP-Rule:MF_01629, ECO:0000256|PIRSR:PIRSR000190-2,
KW   ECO:0000256|SAAS:SAAS01072464};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01629,
KW   ECO:0000256|SAAS:SAAS01072441, ECO:0000313|EMBL:ADH87603.1};
KW   Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01629,
KW   ECO:0000256|SAAS:SAAS01168666};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006633}.
FT   DOMAIN       34    112       Putative_PNPOx. {ECO:0000259|Pfam:
FT                                PF01243}.
FT   DOMAIN      165    208       PNP_phzG_C. {ECO:0000259|Pfam:PF10590}.
FT   NP_BIND      69     70       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
FT   NP_BIND     133    134       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
FT   REGION      184    186       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01629}.
FT   BINDING      76     76       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
FT   BINDING      98     98       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
FT   BINDING     116    116       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01629}.
FT   BINDING     120    120       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01629}.
FT   BINDING     124    124       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01629}.
FT   BINDING     178    178       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
FT   BINDING     188    188       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
SQ   SEQUENCE   208 AA;  23740 MW;  8548E99D68BD7AD0 CRC64;
     MEASEELISG DFTAATEPFR LFEEWFAEAK EKEPRDPNAM ALATVDADGL PDVRMVLLNQ
     RDERGFVFFT NTGSAKGCEL AAVPKAAVVF HWKSMNRQIR VRGPVEVVSD EEADAYFLTR
     PRLSQIGAWA SVQSRPLEGR FALEAAVAKY TAQYALGSVP RPPHWTGFRI RPVQIEFWHD
     RPFRLHDRIV FRRDSAEATV WNKTRLYP
//

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