ID   Q2GL16_ANAPZ            Unreviewed;       352 AA.
AC   Q2GL16;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   SubName: Full=Oxidoreductase, FAD-binding protein {ECO:0000313|EMBL:ABD43387.1};
GN   OrderedLocusNames=APH_0325 {ECO:0000313|EMBL:ABD43387.1};
OS   Anaplasma phagocytophilum (strain HZ).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma; phagocytophilum group.
OX   NCBI_TaxID=212042 {ECO:0000313|EMBL:ABD43387.1, ECO:0000313|Proteomes:UP000001943};
RN   [1] {ECO:0000313|EMBL:ABD43387.1, ECO:0000313|Proteomes:UP000001943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HZ {ECO:0000313|EMBL:ABD43387.1,
RC   ECO:0000313|Proteomes:UP000001943};
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA   Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.,
RA   Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J., Daugherty S.C.,
RA   Davidsen T., Durkin A.S., Gwinn M., Haft D.H., Selengut J.D.,
RA   Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA   Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(2006).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the DAMOX/DASOX family.
CC       {ECO:0000256|ARBA:ARBA00006730}.
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DR   EMBL; CP000235; ABD43387.1; -; Genomic_DNA.
DR   RefSeq; WP_011450458.1; NC_007797.1.
DR   AlphaFoldDB; Q2GL16; -.
DR   STRING; 212042.APH_0325; -.
DR   PaxDb; 212042-APH_0325; -.
DR   EnsemblBacteria; ABD43387; ABD43387; APH_0325.
DR   GeneID; 56368462; -.
DR   KEGG; aph:APH_0325; -.
DR   PATRIC; fig|212042.8.peg.338; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_1_0_5; -.
DR   Proteomes; UP000001943; Chromosome.
DR   GO; GO:0003884; F:D-amino-acid oxidase activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0046416; P:D-amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR023209; DAO.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR11530; D-AMINO ACID OXIDASE; 1.
DR   PANTHER; PTHR11530:SF11; D-ASPARTATE OXIDASE; 1.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
FT   DOMAIN          7..330
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   352 AA;  38941 MW;  6E4428113F36635D CRC64;
     MVKTAGIAGA GLVGRILALV LLRDGWRVTI FDRDDTIGKA SCGYIAAGML SLYSEAENTG
     DLVIDLGYRS MELWPQILSD IGAEFCLQTS GSVMVAHAAD LSDLEMKCAI IRNRFPDVFS
     ELRITNKVYE LEEGISAPYG MYIKDEGSID SINLFKCLER ALRDYGITWY SNVNVLKVQC
     AEIVTEQGLH TFDFVFDCRG VGAKSEVAGL RGVRGEAILV KAPGVTIKRA VRMMHPRYSV
     YVVPRQENMF IVGASEIESC DYSEVSVQSA LEMLSAIYSL HRGFAEARIL DMMSACRPAF
     RDNVPRVLVE DRAIRINGLY RYGYLCVPAI VEEVLSLLNG GTLNHQALFS KN
//