ID   N8VM40_9GAMM            Unreviewed;       373 AA.
AC   N8VM40;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Glycine oxidase ThiO {ECO:0000313|EMBL:ENU85833.1};
GN   ORFNames=F973_02056 {ECO:0000313|EMBL:ENU85833.1};
OS   Acinetobacter sp. CIP 102129.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1144664 {ECO:0000313|EMBL:ENU85833.1, ECO:0000313|Proteomes:UP000023777};
RN   [1] {ECO:0000313|EMBL:ENU85833.1, ECO:0000313|Proteomes:UP000023777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 102129 {ECO:0000313|EMBL:ENU85833.1,
RC   ECO:0000313|Proteomes:UP000023777};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter sp. CIP 102129.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004948}.
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:ENU85833.1}.
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DR   EMBL; APPA01000026; ENU85833.1; -; Genomic_DNA.
DR   RefSeq; WP_004761768.1; NZ_KB849341.1.
DR   AlphaFoldDB; N8VM40; -.
DR   PATRIC; fig|1144664.3.peg.2044; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_4_5_6; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000023777; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012727; Gly_oxidase_ThiO.
DR   NCBIfam; TIGR02352; thiamin_ThiO; 1.
DR   PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR13847:SF293; TRNA 5-METHYLAMINOMETHYL-2-THIOURIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN MNMC; 1.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
FT   DOMAIN          3..347
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   373 AA;  42143 MW;  C705D7F7BDF54F66 CRC64;
     MHIAIIGAGI SGLMTALELA EQGCSVDIFD QQHAGQAASW AGGGILSPMY PWRYAPEVNQ
     LAQYGKSLYQ MWNEKLLPIT GIDFQIHDTG MLIFDREDFD IGLNYAAQFN EPMQQCDLLN
     RKQLERVNPH ISAQFQQAIY FPQLSNVRNP RLLQSLIGYL KQHSSVRFFE HCPIEQLIIQ
     NKKVQGVHTE DGRNFSADHV VMSCGAWSQH WSEQVQRKIS VHPVQGQMLL FKTPENWLPT
     MCMNRVMYLI PRQDGHIVCG SSMADCGFST TVDEQTQQDI LTACLEMVPK LEQFPIVQRW
     AGLRPSSPHG IPYIGAMPEI ENLWANFGHF RNGLCMGAGS ARLLRQLMLG QETLVSPIAY
     SPERLKKQDL ISS
//