(data stored in SCRATCH zone)

SWISSPROT: D4YXC9_SPHJU

ID   D4YXC9_SPHJU            Unreviewed;       191 AA.
AC   D4YXC9;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   07-JUN-2017, entry version 53.
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   ECO:0000313|EMBL:BAI95011.1};
GN   OrderedLocusNames=SJA_C1-01770 {ECO:0000313|EMBL:BAI95011.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95011.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI95011.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(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:SAAS00025342}.
CC   -!- CATALYTIC ACTIVITY: Pyridoxamine 5'-phosphate + H(2)O + O(2) =
CC       pyridoxal 5'-phosphate + NH(3) + H(2)O(2). {ECO:0000256|HAMAP-
CC       Rule:MF_01629, ECO:0000256|SAAS:SAAS00025373}.
CC   -!- CATALYTIC ACTIVITY: Pyridoxine 5'-phosphate + O(2) = pyridoxal 5'-
CC       phosphate + H(2)O(2). {ECO:0000256|HAMAP-Rule:MF_01629,
CC       ECO:0000256|SAAS:SAAS00025349}.
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:SAAS00531211}.
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:SAAS00531213}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01629,
CC       ECO:0000256|SAAS:SAAS00695030}.
CC   -!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase
CC       family. {ECO:0000256|HAMAP-Rule:MF_01629,
CC       ECO:0000256|SAAS:SAAS00695012}.
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DR   EMBL; AP010803; BAI95011.1; -; Genomic_DNA.
DR   RefSeq; WP_013038823.1; NC_014006.1.
DR   ProteinModelPortal; D4YXC9; -.
DR   STRING; 452662.SJA_C1-01770; -.
DR   EnsemblBacteria; BAI95011; BAI95011; SJA_C1-01770.
DR   GeneID; 29271883; -.
DR   KEGG; sjp:SJA_C1-01770; -.
DR   eggNOG; ENOG4108S7T; Bacteria.
DR   eggNOG; COG0259; LUCA.
DR   HOGENOM; HOG000242755; -.
DR   KO; K00275; -.
DR   OMA; PEPNAMV; -.
DR   OrthoDB; POG091H054N; -.
DR   UniPathway; UPA01068; UER00304.
DR   Proteomes; UP000007753; Chromosome 1.
DR   GO; GO:0010181; F:FMN binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004733; F:pyridoxamine-phosphate oxidase activity; IEA:UniProtKB-HAMAP.
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:SF4; PTHR10851:SF4; 1.
DR   Pfam; PF10590; PNP_phzG_C; 1.
DR   Pfam; PF01243; Putative_PNPOx; 1.
DR   PIRSF; PIRSF000190; Pyd_amn-ph_oxd; 1.
DR   SUPFAM; SSF50475; SSF50475; 1.
DR   TIGRFAMs; TIGR00558; pdxH; 1.
DR   PROSITE; PS01064; PYRIDOX_OXIDASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; D4YXC9.
DR   SWISS-2DPAGE; D4YXC9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01629,
KW   ECO:0000256|SAAS:SAAS00695028};
KW   FMN {ECO:0000256|HAMAP-Rule:MF_01629, ECO:0000256|PIRSR:PIRSR000190-2,
KW   ECO:0000256|SAAS:SAAS00695024};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01629,
KW   ECO:0000256|SAAS:SAAS00695029, ECO:0000313|EMBL:BAI95011.1};
KW   Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01629,
KW   ECO:0000256|SAAS:SAAS00025314};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753}.
FT   DOMAIN       17     97       Putative_PNPOx. {ECO:0000259|Pfam:
FT                                PF01243}.
FT   DOMAIN      151    191       PNP_phzG_C. {ECO:0000259|Pfam:PF10590}.
FT   NP_BIND      40     45       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
FT   NP_BIND      55     56       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
FT   NP_BIND     119    120       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
FT   REGION      170    172       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01629}.
FT   BINDING      45     45       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01629}.
FT   BINDING      61     61       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
FT   BINDING      62     62       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
FT   BINDING      84     84       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
FT   BINDING     102    102       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01629}.
FT   BINDING     106    106       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01629}.
FT   BINDING     110    110       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01629}.
FT   BINDING     164    164       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
FT   BINDING     174    174       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
SQ   SEQUENCE   191 AA;  22010 MW;  74284FB3CDCE83D7 CRC64;
     MTDPFLLFDA WYAEARETEI NDSNAMALAT ADARGRPSLR MVLLKGHGPD GFVFYTNFEG
     RKAQELHANP HAALLFHWKS LRRQVRIEGP VGPVDDATAD AYFATRSRDS QLGAWASDQS
     RPLESRNLFM ARYEEVSLRF EGGPVPRPPH WSGFRVAPER IEFWQDREHR LHERRLFERT
     GGGWREGLLY P
//

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