Y9130_DICDI
ID Y9130_DICDI Reviewed; 1080 AA.
AC Q54EW2;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Putative bifunctional amine oxidase DDB_G0291301;
DE Includes:
DE RecName: Full=Putative sarcosine oxidase;
DE Short=PSO;
DE EC=1.5.3.1;
DE EC=1.5.3.7;
DE Includes:
DE RecName: Full=Putative L-amino-acid oxidase;
DE EC=1.4.3.2;
GN ORFNames=DDB_G0291301;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP PROTEIN SEQUENCE OF 40-54; 445-468 AND 1050-1060, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=AX2;
RA Bienvenut W.V., Ura S., Insall R.H.;
RL Submitted (JUL-2009) to UniProtKB.
CC -!- FUNCTION: Catalyzes an oxidative deamination of predominantly
CC hydrophobic and aromatic L-amino acids. Metabolizes sarcosine, L-
CC pipecolic acid and L-proline (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + sarcosine = formaldehyde + glycine + H2O2;
CC Xref=Rhea:RHEA:13313, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:16842, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:57433; EC=1.5.3.1;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179,
CC ChEBI:CHEBI:59869; EC=1.4.3.2;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the MSOX/MTOX family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the flavin monoamine
CC oxidase family. {ECO:0000305}.
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DR EMBL; AAFI02000177; EAL61634.1; -; Genomic_DNA.
DR RefSeq; XP_635128.1; XM_630036.1.
DR AlphaFoldDB; Q54EW2; -.
DR SMR; Q54EW2; -.
DR BioGRID; 1253077; 1.
DR STRING; 44689.DDB0235252; -.
DR PaxDb; Q54EW2; -.
DR PRIDE; Q54EW2; -.
DR EnsemblProtists; EAL61634; EAL61634; DDB_G0291301.
DR GeneID; 8628074; -.
DR KEGG; ddi:DDB_G0291301; -.
DR dictyBase; DDB_G0291301; -.
DR eggNOG; KOG2820; Eukaryota.
DR HOGENOM; CLU_286277_0_0_1; -.
DR InParanoid; Q54EW2; -.
DR OMA; LRTMYTE; -.
DR PhylomeDB; Q54EW2; -.
DR Reactome; R-DDI-8964208; Phenylalanine metabolism.
DR PRO; PR:Q54EW2; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0001716; F:L-amino-acid oxidase activity; IBA:GO_Central.
DR GO; GO:0050031; F:L-pipecolate oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0046592; F:polyamine oxidase activity; IBA:GO_Central.
DR GO; GO:0008115; F:sarcosine oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009063; P:cellular amino acid catabolic process; IBA:GO_Central.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01593; Amino_oxidase; 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; FAD; Flavoprotein; Membrane;
KW Multifunctional enzyme; Oxidoreductase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1080
FT /note="Putative bifunctional amine oxidase DDB_G0291301"
FT /id="PRO_0000388375"
FT TRANSMEM 508..528
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..?450
FT /note="Putative sarcosine oxidase"
FT REGION 445..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION ?450..1080
FT /note="Putative L-amino-acid oxidase"
FT BINDING 10..40
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT BINDING 535
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 544
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 563..564
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 886
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 978
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 987..990
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1080 AA; 120674 MW; FB0C9DA09FC71D6D CRC64;
MREFLKDDYD VIVCGGGPVG LATAYRCAKA GKKVLCLEKS VFFNGGGSSG DVVRMLRTMY
TEDYMADLAH ETLGLWKELG DDAGEGDLVW MTGLLNFGDP NYGAGGPEGT LLGPIPNLER
LGMQYKVLTA QEIMEEYPFR NIPSNHQGVF APDNGVINLP LVLRSLYKLC LQYGCKMVSH
AEVKLIKNLS TTMVEIEVEH TDVDQKNKQS FKVKSKKAAI TSNSFCNHII KPSFGWELDM
TIWEMTSSYF VAKPGPNATV FKSMWFNFQN DTDNDPTKSN LYYGFPAVPW MTDNHCRIAL
DAALRQIKDP NDRHDGVETH DVNRTRDWVR EHIPGVDDTP LFNVSALMAN VYDNMFVLDF
IPETNNNVVM FACGWAMKFI PLLGKILSQL LDEGKTQYPI DHFALNRGNG ALIIKEGQTP
KSVNSQVRAP RYTSMHCKPL TIAKSTVPTN QSSNPDGASS TAPTQSLRSL FASRLLQRSV
GMEAKFHSII AKNRSKRSTK ASQKDLTVGI IGAGMAGLYA AMILQDLGLQ YNILEANKER
VGGRIYTYRF PQNQDKYQTV ELGAMRFPKI EIMDRLLNLD KPWSLFSKLE KAGHKIPTIP
YHLTVDNNLV YYNGKRIFAN TLLNDDPLYF SDTHNGGPGT AVPDKYTYQP YGDLLDAVYK
KFSDDLENDF ESGFETLLKS DNYSTRAYLF EKGPYPQSVV NYLETMDTGT GLYDMAFSET
IMDYFDFSAG DEWLCIDGGT DIIVNSMVKT LRPGCIEQGK VVTKVSRVVG KSGDVSNLKV
DFLDGTEGRL FKHVISTGTL ASLRRVDLSD LKLSHNKRTA IRSLHYDHSV KIALSFKSRW
WEDSKFMNGK PMLGGKSSTD LPVRTIVYPS YGIGQPGVSG VLIVSYTWSL DASRIGSLVG
DRPSEEVLIK LCMANLAEVH NVPVATLQQL FVDYKCWDWY NDDYSSGAFA LYSPSQFSQL
FPSLTKPSPD GRFHLAGEAT SVHHGWVIGS LNSAYRSVDH ILQVEGLDEL RAKLRLNWGF
IDEVEDPQDD QQYVDPHHNL SGPNAKKFRS NVSQVAIQPR FKAPRNFKPR NTAASIGGLK
