(data stored in SCRATCH zone)

SWISSPROT: D6ZAC8_SEGRD

ID   D6ZAC8_SEGRD            Unreviewed;       212 AA.
AC   D6ZAC8;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 60.
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=Srot_0181 {ECO:0000313|EMBL:ADG96670.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96670.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96670.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
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; CP001958; ADG96670.1; -; Genomic_DNA.
DR   STRING; 640132.Srot_0181; -.
DR   EnsemblBacteria; ADG96670; ADG96670; Srot_0181.
DR   KEGG; srt:Srot_0181; -.
DR   eggNOG; ENOG4108S7T; Bacteria.
DR   eggNOG; COG0259; LUCA.
DR   HOGENOM; HOG000242755; -.
DR   KO; K00275; -.
DR   OMA; PEPNAMV; -.
DR   UniPathway; UPA01068; UER00304.
DR   Proteomes; UP000002247; 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; D6ZAC8.
DR   SWISS-2DPAGE; D6ZAC8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
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:ADG96670.1};
KW   Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01629,
KW   ECO:0000256|SAAS:SAAS01168666};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247}.
FT   DOMAIN       35    115       Putative_PNPOx. {ECO:0000259|Pfam:
FT                                PF01243}.
FT   DOMAIN      172    212       PNP_phzG_C. {ECO:0000259|Pfam:PF10590}.
FT   NP_BIND      60     65       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
FT   NP_BIND      75     76       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
FT   NP_BIND     139    140       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
FT   REGION        5      8       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000190-1}.
FT   REGION      191    193       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01629, ECO:0000256|PIRSR:
FT                                PIRSR000190-1}.
FT   BINDING      65     65       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01629, ECO:0000256|PIRSR:PIRSR000190-
FT                                1}.
FT   BINDING      82     82       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
FT   BINDING     104    104       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
FT   BINDING     122    122       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01629, ECO:0000256|PIRSR:PIRSR000190-
FT                                1}.
FT   BINDING     126    126       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01629, ECO:0000256|PIRSR:PIRSR000190-
FT                                1}.
FT   BINDING     130    130       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01629, ECO:0000256|PIRSR:PIRSR000190-
FT                                1}.
FT   BINDING     185    185       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
FT   BINDING     195    195       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
SQ   SEQUENCE   212 AA;  23561 MW;  DC1D8DEAEC86DE5B CRC64;
     MPDLREEYTD VSPDLDVADV QAGWPELLQN WLAQAWESGL PDANALVLAT VDDAGRPHSR
     SVLCKGISAD GIDFYTHYAS AKGRQLAACP HASATFPWYG LSRQVHLRGE VRKLDHDCSI
     GYWSNRPRGS QLGAWASEQS RPIASREALV AQLRAAAERF PEGEPVPLPP GWGGYRLVPF
     EVEFWQGRAN RLHNRVLLAL ADGQWRATRL QP
//

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