FAP1_SCHPO
ID FAP1_SCHPO Reviewed; 412 AA.
AC O43029;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=L-pipecolate oxidase {ECO:0000312|EMBL:CAA17815.1};
DE EC=1.5.3.7;
DE AltName: Full=L-pipecolic acid oxidase {ECO:0000303|PubMed:16233628};
DE Flags: Precursor;
GN Name=fap1 {ECO:0000312|EMBL:CAA17815.1}; ORFNames=SPBC354.15;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000312|EMBL:CAA17815.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RX PubMed=16233628; DOI=10.1016/s1389-1723(04)70204-2;
RA Yoshida N., Akazawa S., Katsuragi T., Tani Y.;
RT "Characterization of two fructosyl-amino acid oxidase homologs of
RT Schizosaccharomyces pombe.";
RL J. Biosci. Bioeng. 97:278-280(2004).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Oxidizes L-pipecolate and L-proline (6,7% of the activity for
CC L-pipecolate). {ECO:0000269|PubMed:16233628}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-pipecolate + O2 = H(+) + H2O2 + L-1-piperideine-6-
CC carboxylate; Xref=Rhea:RHEA:11992, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:58769,
CC ChEBI:CHEBI:61185; EC=1.5.3.7;
CC Evidence={ECO:0000269|PubMed:16233628};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:16233628};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.07 mM for L-pipecolate {ECO:0000269|PubMed:16233628};
CC KM=33.5 mM for L-proline {ECO:0000269|PubMed:16233628};
CC Vmax=46.1 umol/min/mg enzyme for L-pipecolate
CC {ECO:0000269|PubMed:16233628};
CC Vmax=9.45 umol/min/mg enzyme for L-proline
CC {ECO:0000269|PubMed:16233628};
CC -!- SUBUNIT: Dimer. {ECO:0000269|PubMed:16233628}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Cytoplasm
CC {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the MSOX/MTOX family. {ECO:0000305}.
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DR EMBL; CU329671; CAA17815.1; -; Genomic_DNA.
DR PIR; T40295; T40295.
DR RefSeq; NP_595239.1; NM_001021145.2.
DR AlphaFoldDB; O43029; -.
DR SMR; O43029; -.
DR BioGRID; 277432; 6.
DR STRING; 4896.SPBC354.15.1; -.
DR MaxQB; O43029; -.
DR PaxDb; O43029; -.
DR EnsemblFungi; SPBC354.15.1; SPBC354.15.1:pep; SPBC354.15.
DR GeneID; 2540916; -.
DR KEGG; spo:SPBC354.15; -.
DR PomBase; SPBC354.15; fap1.
DR VEuPathDB; FungiDB:SPBC354.15; -.
DR eggNOG; KOG2820; Eukaryota.
DR HOGENOM; CLU_007884_0_1_1; -.
DR OMA; GYKFGAA; -.
DR PhylomeDB; O43029; -.
DR Reactome; R-SPO-71064; Lysine catabolism.
DR Reactome; R-SPO-9033241; Peroxisomal protein import.
DR SABIO-RK; O43029; -.
DR PRO; PR:O43029; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:PomBase.
DR GO; GO:0050031; F:L-pipecolate oxidase activity; IDA:PomBase.
DR GO; GO:0051699; F:proline oxidase activity; IDA:PomBase.
DR GO; GO:0008115; F:sarcosine oxidase activity; IBA:GO_Central.
DR GO; GO:0019477; P:L-lysine catabolic process; TAS:PomBase.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR045170; MTOX.
DR PANTHER; PTHR10961; PTHR10961; 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; FAD; Flavoprotein; Glycoprotein; Nucleus; Oxidoreductase;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..412
FT /note="L-pipecolate oxidase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000347274"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 412 AA; 46320 MW; BD36B86075D3F4EF CRC64;
MVKNTSVIIV GAGVFGLSAA LELTKRGGYT IKILDRAPPP VIDGSSVDAN RIIRSDYADA
VYCSMGIDAL EEWRTNPLFK EQFYGSGLMF VGRDNVEYRD MSLENLTKMG VSAAKFQTTE
ELRKLFPKWI GELNDGEAGY ANFSSGWANA EQSVKSVVNY LAHAGVSFIS GPEGTVEELI
TEENVVKGVR TTTGAYMAEK LIFATGAWTA SLLPNDHTRF LATGQPVAYI KLTPEEYIRF
LTNPVYLDFD TGFYIFPPTP DGYLKFARHG YGFTRMQNLK SGKVESVPPK KPLVSPILPK
EAELDLRRNL QRTYGEEISQ RPFYKTRICY YTDTADAEFV FDYHPDYENL FVCTGGSGHG
FKFFPILGKY SIGCMFRELE EPLLKKWRWK KENLEFAALD HSRAGPSRQE LS
