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Database: UniProt
Entry: A0A073JST0_9BACI
LinkDB: A0A073JST0_9BACI
Original site: A0A073JST0_9BACI 
ID   A0A073JST0_9BACI        Unreviewed;       434 AA.
AC   A0A073JST0;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=FAD-binding oxidoreductase {ECO:0000313|EMBL:KEK18139.1};
GN   ORFNames=BAMA_07185 {ECO:0000313|EMBL:KEK18139.1};
OS   Bacillus manliponensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=574376 {ECO:0000313|EMBL:KEK18139.1, ECO:0000313|Proteomes:UP000027822};
RN   [1] {ECO:0000313|EMBL:KEK18139.1, ECO:0000313|Proteomes:UP000027822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 15802 {ECO:0000313|EMBL:KEK18139.1,
RC   ECO:0000313|Proteomes:UP000027822};
RA   Lai Q., Liu Y., Shao Z.;
RT   "Draft genome sequence of Bacillus manliponensis JCM 15802 (MCCC
RT   1A00708).";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005147}.
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:KEK18139.1}.
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DR   EMBL; JOTN01000017; KEK18139.1; -; Genomic_DNA.
DR   RefSeq; WP_034641785.1; NZ_JOTN01000017.1.
DR   AlphaFoldDB; A0A073JST0; -.
DR   STRING; 574376.BAMA_07185; -.
DR   eggNOG; COG0277; Bacteria.
DR   OrthoDB; 9800184at2; -.
DR   UniPathway; UPA00132; -.
DR   Proteomes; UP000027822; 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   GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IEA:UniProtKB-UniPathway.
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   InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   NCBIfam; TIGR01679; bact_FAD_ox; 1.
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; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE   4: Predicted;
KW   Ascorbate biosynthesis {ECO:0000256|ARBA:ARBA00022644};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027822}.
FT   DOMAIN          16..186
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   434 AA;  49633 MW;  C6FEDE53A1FE8DE6 CRC64;
     MLSVTGQKWK NWTGNVQGEP QYIIYPKSID DVVEVVRFAT SIGRRIRVVG SGHSFTALVQ
     TEEILVSLDE LQGIVGVDSS APVVEVWAGT KLHQLGKILA ANGYAQENLG DIDAQSIAGA
     ISTGTHGTGV LFGNLATQVV EMTVVLASGE VITCSETKHT QYWKAVQLSL GMLGIIVKVR
     LRVIPAYSLV YESKKEHLFT VLERLEEYKK NRHFEFFLFP YSDDVQVKIT NQTEEIGSTM
     RWHKLQTEVI ENMAFSLLSE SCRLFPSLSE RVSQFSAKVV PNTKIVGPSH KVFATARNVR
     FYEMEYSVPQ EHMRVVVEEI YRVIHQKNFH VHFPIECRYV KGDDLWLSPS YERDSAYIAV
     HMYKGMKYAA YFQEIERIFQ KYDGRPHWGK MHTMKYEQLE QVYPMLYSFL QVRETLDPTG
     LFLNPYLATI FSLK
//
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