FAP2_SCHPO
ID FAP2_SCHPO Reviewed; 433 AA.
AC Q9UTM9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=L-saccharopine oxidase {ECO:0000312|EMBL:CAB59618.1};
DE EC=1.5.3.18;
DE Flags: Precursor;
GN Name=fap2 {ECO:0000312|EMBL:CAB59618.1}; ORFNames=SPAC139.04c;
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:CAB59618.1}
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 -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-saccharopine + O2 = (S)-2-amino-6-oxohexanoate + H2O2
CC + L-glutamate; Xref=Rhea:RHEA:28210, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57951, ChEBI:CHEBI:58321; EC=1.5.3.18;
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=9.02 mM for L-saccharopine {ECO:0000269|PubMed:16233628};
CC Vmax=6.72 umol/min/mg enzyme for L-pipecolate
CC {ECO:0000269|PubMed:16233628};
CC -!- SUBUNIT: Monomer. {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; CU329670; CAB59618.1; -; Genomic_DNA.
DR PIR; T37605; T37605.
DR RefSeq; NP_593171.1; NM_001018568.2.
DR AlphaFoldDB; Q9UTM9; -.
DR SMR; Q9UTM9; -.
DR BioGRID; 278260; 2.
DR STRING; 4896.SPAC139.04c.1; -.
DR MaxQB; Q9UTM9; -.
DR PaxDb; Q9UTM9; -.
DR PRIDE; Q9UTM9; -.
DR EnsemblFungi; SPAC139.04c.1; SPAC139.04c.1:pep; SPAC139.04c.
DR GeneID; 2541766; -.
DR KEGG; spo:SPAC139.04c; -.
DR PomBase; SPAC139.04c; fap2.
DR VEuPathDB; FungiDB:SPAC139.04c; -.
DR eggNOG; KOG2820; Eukaryota.
DR HOGENOM; CLU_007884_0_1_1; -.
DR InParanoid; Q9UTM9; -.
DR OMA; QFMPLED; -.
DR PhylomeDB; Q9UTM9; -.
DR BioCyc; MetaCyc:MON-16096; -.
DR BRENDA; 1.5.3.18; 5613.
DR SABIO-RK; Q9UTM9; -.
DR PRO; PR:Q9UTM9; -.
DR Proteomes; UP000002485; Chromosome I.
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:0051698; F:saccharopine 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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..433
FT /note="L-saccharopine oxidase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000347275"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 433 AA; 48974 MW; 170081BB3D48B1BE CRC64;
MSRTIVIVGC GVFGLSTAVE LAKNHSFDNI IAIDAEPVPS SMSAANDINK IVRPEYADLK
YMKLALEAME KWRNDPELSS VYFECGRLST ISKDPYRARF DEVAQRNLRK LLGDSALINL
SSSEEIRKKY PSLFSNSPLR SDMQAVVNEH AGYANSAASL KLLELKAREL GVEFVFGKAG
KFKKFVVNHS ETDIDKNDNH VSVQTEDGTI YHADTILLAV GAYLNAYLNT SHRVCAKGLP
VAHIQLTDEE FKTYKNMPII FDPDCAYAFP PYPVTKLIKL ASTGYEYVCN VETDYDENSK
VVSIPHSGPS KSSLPKYAII QMRRFLDTFL PDLADRSLIN TKMCWISDTE DANFLIDKVP
QFDNVFVANG DSGHAFKFLP NIGRYIAQRI LGDLSEEWKD AWRWREDDKA SELKWRCVRS
LIDYKDAEFT YDK
