(data stored in ACNUC7421 zone)

SWISSPROT: C6WI17_ACTMD

ID   C6WI17_ACTMD            Unreviewed;       219 AA.
AC   C6WI17;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, 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=Amir_0501 {ECO:0000313|EMBL:ACU34468.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34468.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34468.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
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}.
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; CP001630; ACU34468.1; -; Genomic_DNA.
DR   RefSeq; WP_012783131.1; NC_013093.1.
DR   ProteinModelPortal; C6WI17; -.
DR   STRING; 446462.Amir_0501; -.
DR   EnsemblBacteria; ACU34468; ACU34468; Amir_0501.
DR   KEGG; ami:Amir_0501; -.
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; UP000002213; Chromosome.
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; C6WI17.
DR   SWISS-2DPAGE; C6WI17.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
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:ACU34468.1};
KW   Pyridoxine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01629,
KW   ECO:0000256|SAAS:SAAS00025314};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213}.
FT   DOMAIN       39    124       Putative_PNPOx. {ECO:0000259|Pfam:
FT                                PF01243}.
FT   DOMAIN      179    219       PNP_phzG_C. {ECO:0000259|Pfam:PF10590}.
FT   NP_BIND      67     72       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
FT   NP_BIND      82     83       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
FT   NP_BIND     146    147       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
FT   REGION       14     17       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR000190-1}.
FT   REGION      198    200       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01629, ECO:0000256|PIRSR:
FT                                PIRSR000190-1}.
FT   BINDING      72     72       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01629, ECO:0000256|PIRSR:PIRSR000190-
FT                                1}.
FT   BINDING      89     89       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
FT   BINDING     111    111       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
FT   BINDING     129    129       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01629, ECO:0000256|PIRSR:PIRSR000190-
FT                                1}.
FT   BINDING     133    133       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01629, ECO:0000256|PIRSR:PIRSR000190-
FT                                1}.
FT   BINDING     137    137       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01629, ECO:0000256|PIRSR:PIRSR000190-
FT                                1}.
FT   BINDING     192    192       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
FT   BINDING     202    202       FMN. {ECO:0000256|HAMAP-Rule:MF_01629,
FT                                ECO:0000256|PIRSR:PIRSR000190-2}.
SQ   SEQUENCE   219 AA;  24866 MW;  075DF50BE0B97D62 CRC64;
     MSEATTSITL PAMRVSYERS ALGEGDLAAT WHEQLQLWLD EATNAGLLEP NAMVLATADP
     SGRPSSRTVL AKGLDERGLV FFTNYTSAKS HDLMATRYAS TTFPWYGLQR QAHVRGTVEK
     VSHAETTEYW ESRPRGSQLG AWASPQSRVV TGRPTLESAL NKIERQFTDT ERVPVPPHWG
     GWRIRPEEVE FWQGRQDRMH DRLRFRLGRD GWETERVAP
//

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