ID Q9JXF8_NEIMB Unreviewed; 366 AA.
AC Q9JXF8;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE SubName: Full=Glycine oxidase ThiO {ECO:0000313|EMBL:AAF42387.1};
DE EC=1.4.3.19 {ECO:0000313|EMBL:AAF42387.1};
GN Name=thiO {ECO:0000313|EMBL:AAF42387.1};
GN OrderedLocusNames=NMB2068 {ECO:0000313|EMBL:AAF42387.1};
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586 {ECO:0000313|EMBL:AAF42387.1, ECO:0000313|Proteomes:UP000000425};
RN [1] {ECO:0000313|EMBL:AAF42387.1, ECO:0000313|Proteomes:UP000000425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58 {ECO:0000313|EMBL:AAF42387.1,
RC ECO:0000313|Proteomes:UP000000425};
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L.,
RA White O., Fleischmann R.D., Dougherty B.A., Mason T., Ciecko A.,
RA Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H., Qin H., Vamathevan J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
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; AE002098; AAF42387.1; -; Genomic_DNA.
DR PIR; H81010; H81010.
DR RefSeq; NP_275058.1; NC_003112.2.
DR RefSeq; WP_002225707.1; NC_003112.2.
DR AlphaFoldDB; Q9JXF8; -.
DR STRING; 122586.NMB2068; -.
DR PaxDb; 122586-NMB2068; -.
DR KEGG; nme:NMB2068; -.
DR PATRIC; fig|122586.8.peg.2648; -.
DR HOGENOM; CLU_007884_1_0_4; -.
DR InParanoid; Q9JXF8; -.
DR OrthoDB; 9790035at2; -.
DR Proteomes; UP000000425; 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:0043799; F:glycine oxidase activity; IEA:UniProtKB-EC.
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;
KW Oxidoreductase {ECO:0000313|EMBL:AAF42387.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000425}.
FT DOMAIN 3..338
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 366 AA; 40566 MW; E20CFFAC386CE06F CRC64;
MTRIAILGGG LSGRLTALQL AEQGYQIALF DKGCRRGEHA AAYVAAAMLA PAAEAVEATP
EVVRLGRQSI PLWRGIRCRL NTHTMMQENG SLIVWHGQDK PLSSEFVRHL KRGGVADDEI
VRWRADDIAE REPQLGGRFS DGIYLPTEGQ LDGRQILSAL ADALDELNVP CHWEHECVPE
GLQAQYDWLI DCRGYGAKTA WNQSPEHTST LRGIRGEVAR VYTPEITLNR PVRLLHPRYP
LYIAPKENHV FVIGATQIES ESQAPASVRS GLELLSALYA IHPAFGEADI LEIATGLRPT
LNHHNPEIRY NRARRLIEIN GLFRHGFMIS PAVTAAAARL AVALFDGKDA PERDKESGLA
YIRRQD
//
