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Pyridoxine/pyridoxamine 5'-phosphate oxidase (EC 1.4.3.5) (PNP/PMP oxidase) (PNPOx) (Pyridoxal 5'-phosphate synthase)

 D1KE61_9GAMM            Unreviewed;       212 AA.
D1KE61;
19-JAN-2010, integrated into UniProtKB/TrEMBL.
19-JAN-2010, sequence version 1.
25-OCT-2017, entry version 46.
RecName: Full=Pyridoxine/pyridoxamine 5'-phosphate oxidase {ECO:0000256|HAMAP-Rule:MF_01629};
EC=1.4.3.5 {ECO:0000256|HAMAP-Rule:MF_01629};
AltName: Full=PNP/PMP oxidase {ECO:0000256|HAMAP-Rule:MF_01629};
Short=PNPOx {ECO:0000256|HAMAP-Rule:MF_01629};
AltName: Full=Pyridoxal 5'-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_01629};
Name=pdxH {ECO:0000256|HAMAP-Rule:MF_01629};
ORFNames=Sup05_0909 {ECO:0000313|EMBL:EEZ79587.1};
uncultured SUP05 cluster bacterium.
Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Thioglobus;
environmental samples.
NCBI_TaxID=655186 {ECO:0000313|EMBL:EEZ79587.1, ECO:0000313|Proteomes:UP000009383};
[1] {ECO:0000313|EMBL:EEZ79587.1, ECO:0000313|Proteomes:UP000009383}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=19900896; DOI=10.1126/science.1175309;
Walsh D.A., Zaikova E., Howes C.L., Song Y.C., Wright J.J.,
Tringe S.G., Tortell P.D., Hallam S.J.;
"Metagenome of a versatile chemolithoautotroph from expanding oceanic
dead zones.";
Science 326:578-582(2009).
-!- FUNCTION: Catalyzes the oxidation of either pyridoxine 5'-
phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal
5'-phosphate (PLP). {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|SAAS:SAAS00025342}.
-!- CATALYTIC ACTIVITY: Pyridoxamine 5'-phosphate + H(2)O + O(2) =
pyridoxal 5'-phosphate + NH(3) + H(2)O(2). {ECO:0000256|HAMAP-
Rule:MF_01629, ECO:0000256|SAAS:SAAS00025373}.
-!- CATALYTIC ACTIVITY: Pyridoxine 5'-phosphate + O(2) = pyridoxal 5'-
phosphate + H(2)O(2). {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|SAAS:SAAS00025349}.
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|PIRSR:PIRSR000190-2};
Note=Binds 1 FMN per subunit. {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|PIRSR:PIRSR000190-2};
-!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage;
pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
{ECO:0000256|HAMAP-Rule:MF_01629, ECO:0000256|SAAS:SAAS00531211}.
-!- PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage;
pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1.
{ECO:0000256|HAMAP-Rule:MF_01629, ECO:0000256|SAAS:SAAS00531213}.
-!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|SAAS:SAAS00899181}.
-!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase
family. {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|SAAS:SAAS00899054}.
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EMBL; GG730029; EEZ79587.1; -; Genomic_DNA.
ProteinModelPortal; D1KE61; -.
PATRIC; fig|655186.3.peg.75; -.
UniPathway; UPA01068; UER00304.
UniPathway; UPA01068; UER00305.
Proteomes; UP000009383; Unassembled WGS sequence.
GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
GO; GO:0004733; F:pyridoxamine-phosphate oxidase activity; IEA:UniProtKB-UniRule.
GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
Gene3D; 2.30.110.10; -; 1.
HAMAP; MF_01629; PdxH; 1.
InterPro; IPR000659; Pyridox_Oxase.
InterPro; IPR019740; Pyridox_Oxase_CS.
InterPro; IPR011576; Pyridox_Oxase_put.
InterPro; IPR019576; Pyridoxamine_oxidase_dimer_C.
InterPro; IPR012349; Split_barrel_FMN-bd.
PANTHER; PTHR10851:SF0; PTHR10851:SF0; 1.
Pfam; PF10590; PNP_phzG_C; 1.
Pfam; PF01243; Putative_PNPOx; 1.
PIRSF; PIRSF000190; Pyd_amn-ph_oxd; 1.
SUPFAM; SSF50475; SSF50475; 1.
TIGRFAMs; TIGR00558; pdxH; 1.
PROSITE; PS01064; PYRIDOX_OXIDASE; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000009383};
Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|PIRSR:PIRSR000190-2, ECO:0000256|SAAS:SAAS00899185};
FMN {ECO:0000256|HAMAP-Rule:MF_01629, ECO:0000256|PIRSR:PIRSR000190-2,
ECO:0000256|SAAS:SAAS00899185};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|SAAS:SAAS00899182};
Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|SAAS:SAAS00025314};
Reference proteome {ECO:0000313|Proteomes:UP000009383}.
DOMAIN 35 117 Putative_PNPOx.
{ECO:0000259|Pfam:PF01243}.
DOMAIN 172 212 PNP_phzG_C. {ECO:0000259|Pfam:PF10590}.
NP_BIND 61 66 FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|PIRSR:PIRSR000190-2}.
NP_BIND 76 77 FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|PIRSR:PIRSR000190-2}.
NP_BIND 140 141 FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|PIRSR:PIRSR000190-2}.
REGION 191 193 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_01629}.
BINDING 66 66 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01629}.
BINDING 82 82 FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|PIRSR:PIRSR000190-2}.
BINDING 83 83 FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|PIRSR:PIRSR000190-2}.
BINDING 105 105 FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|PIRSR:PIRSR000190-2}.
BINDING 123 123 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01629}.
BINDING 127 127 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01629}.
BINDING 131 131 Substrate. {ECO:0000256|HAMAP-
Rule:MF_01629}.
BINDING 185 185 FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|PIRSR:PIRSR000190-2}.
BINDING 195 195 FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
ECO:0000256|PIRSR:PIRSR000190-2}.
SEQUENCE 212 AA; 24433 MW; D8E09A960E8E18D9 CRC64;
MSIDLIQLRR EFTSSGLSRE ELNDNPFVQF ENWIEQATKA ELTLPNAMSL ATSDEDKISI
RTVLLKSFDE QGFVFFTNYN SKKSKQIQGN PKAALLFPWL DLERQVKISG AVEKVSALES
IKYFASRPKE SQLGAWASSQ SSVLSSRQIL LSQFESMKTK FGKGEIPLPD FWGGYRVVPR
TIEFWQGREN RLHDRFVYKK EKDKWLISRL AP


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