ID A0A0N1IA41_LEPSE Unreviewed; 534 AA.
AC A0A0N1IA41;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Putative L-gulonolactone oxidase {ECO:0000313|EMBL:KPI89085.1};
GN ORFNames=ABL78_1821 {ECO:0000313|EMBL:KPI89085.1};
OS Leptomonas seymouri.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI89085.1, ECO:0000313|Proteomes:UP000038009};
RN [1] {ECO:0000313|EMBL:KPI89085.1, ECO:0000313|Proteomes:UP000038009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI89085.1,
RC ECO:0000313|Proteomes:UP000038009};
RX PubMed=26317207;
RA Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J., Grybchuk D.,
RA Lestinova T., Votypka J., Volf P., Opperdoes F., Flegontov P., Lukes J.,
RA Yurchenko V.;
RT "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed by
RT Genome Sequencing, Transcriptome Profiling and Co-infection with Leishmania
RT donovani.";
RL PLoS Pathog. 11:E1005127-E1005127(2015).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPI89085.1}.
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DR EMBL; LJSK01000032; KPI89085.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1IA41; -.
DR EnsemblProtists; KPI89085; KPI89085; ABL78_1821.
DR VEuPathDB; TriTrypDB:Lsey_0032_0290; -.
DR OMA; YPRFGEF; -.
DR OrthoDB; 53654at2759; -.
DR Proteomes; UP000038009; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0003885; F:D-arabinono-1,4-lactone oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2520; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR007173; ALO_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR010031; FAD_lactone_oxidase-like.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR43762; L-GULONOLACTONE OXIDASE; 1.
DR PANTHER; PTHR43762:SF1; L-GULONOLACTONE OXIDASE; 1.
DR Pfam; PF04030; ALO; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR PIRSF; PIRSF000136; LGO_GLO; 2.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 12..181
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 249..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 534 AA; 59793 MW; C34FCE747A163025 CRC64;
MSHQWTNLAQ IGFCTPAHHH YPASTMEVQQ AIAFVRACKG KCRVAGAGKS PNSSTFTSEH
LIHMNRMNRI LSIDADTCTL TCEAGALMED VMNVLDKEGL MLRCVPSYVR TTVGGCIATA
THSSGITCHS LSDYVRELKV VDGRGEVKTL GPAAGKELRL AACHLGALGV VTEIKLEVQP
RVQWRLENNP LSMADANDAA LVARKVRENE YYRWWWVPHT DGCYESYGNA HCEAAGSLAA
PKVNKKELEM KADPKARVTP KRPLPDGEPP KNGGLGAQYP DETKPGSVAV EASAAAAPVD
RSNAQSNCHN GFAVGAAPVM SALTNWISNE LIRHQLVEWS LWVACRFPSL QPHINRAYQR
MFYTTPAVLR GSALHCFTFD CLFRQWANEW AIDASRAVEA FQKIRSMIDR EQMLLHFPVE
FRFSAADDSD MSPAFGRKTC WIGVVMYRPR GQEARDTRRA YDGFNKLMEE MQGRPHWAKY
YNWGHREVSA AYGNGWDRFL ELRRKMDPDD MFLNAWLSNL MSPDRVNSTD FKGK
//
