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Database: UniProt
Entry: V9GAF9_9BACL
LinkDB: V9GAF9_9BACL
Original site: V9GAF9_9BACL 
ID   V9GAF9_9BACL            Unreviewed;       444 AA.
AC   V9GAF9;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Oxidoreductase, FAD-binding {ECO:0000313|EMBL:GAE06330.1};
GN   ORFNames=JCM10914_2483 {ECO:0000313|EMBL:GAE06330.1};
OS   Paenibacillus sp. JCM 10914.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1236974 {ECO:0000313|EMBL:GAE06330.1, ECO:0000313|Proteomes:UP000018028};
RN   [1] {ECO:0000313|EMBL:GAE06330.1, ECO:0000313|Proteomes:UP000018028}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10914 {ECO:0000313|EMBL:GAE06330.1,
RC   ECO:0000313|Proteomes:UP000018028};
RA   Ohkuma M., Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T.,
RA   Hattori M.;
RT   "Draft Genome Sequence of the Alkaliphilic and Xylanolytic Paenibacillus
RT   sp. Strain JCM 10914, Isolated from the Gut of a Soil-Feeding Termite.";
RL   Genome Announc. 2:e01144-13(2014).
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:GAE06330.1}.
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DR   EMBL; BAUO01000006; GAE06330.1; -; Genomic_DNA.
DR   RefSeq; WP_023960488.1; NZ_BAZR01000006.1.
DR   AlphaFoldDB; V9GAF9; -.
DR   STRING; 1236974.GCA_001315105_02413; -.
DR   OrthoDB; 9800184at2; -.
DR   UniPathway; UPA00132; -.
DR   Proteomes; UP000018028; 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:SF1; D-ARABINONO-1,4-LACTONE OXIDASE; 1.
DR   PANTHER; PTHR43762; 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:UP000018028}.
FT   DOMAIN          13..183
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   444 AA;  50524 MW;  E346E0F3EA8F0736 CRC64;
     MTQSMWSNWS GSVQARPQIV LNPASIDDVV KLVQMCRQEG RRLRVVGSGH SFTPIAASED
     CLVSLDHMQG LVHVDTQSRT AKVWAGTKLK LLGELLFQHG LAQENLGDID VQSIAGAIST
     GTHGTGRTFG NISTQVVGFT VVTGTGEVME CTAESDLKRF KALQVSLGTL GIIVQITLRL
     EPAYRLEYVS RRVTLDECLQ QQAQWAEANR HFEFYWFPYA LPCQIKTMNL TQDEPKDHPV
     KDYINEVLVE NTLFGWVSEL CRKVPQTSTL VSRFSASQVP LGRKVHHSHK LFATQRLVRF
     NEMEYNLPAE AMNAVIEEMR IELSRKPYRV HFPVECRYAK GDDIWLSPAY GRDSAYIAIH
     MYRGMPHAEY FNAMERIFLR YGGRPHWGKM HSLEAAQLQE MYPMWESFQQ VRHELDPDGI
     FLNDYVGKLF GITNPRADAN REIV
//
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