ID   N9GFP1_ACIHA            Unreviewed;       377 AA.
AC   N9GFP1;
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:ENW18320.1};
GN   ORFNames=F927_01764 {ECO:0000313|EMBL:ENW18320.1};
OS   Acinetobacter haemolyticus CIP 64.3 = MTCC 9819.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1217659 {ECO:0000313|EMBL:ENW18320.1, ECO:0000313|Proteomes:UP000017667};
RN   [1] {ECO:0000313|EMBL:ENW18320.1, ECO:0000313|Proteomes:UP000017667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 64.3 {ECO:0000313|EMBL:ENW18320.1,
RC   ECO:0000313|Proteomes:UP000017667};
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 haemolyticus CIP 64.3.";
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:ENW18320.1}.
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DR   EMBL; APQQ01000020; ENW18320.1; -; Genomic_DNA.
DR   RefSeq; WP_005081604.1; NZ_KB849800.1.
DR   AlphaFoldDB; N9GFP1; -.
DR   PATRIC; fig|1217659.3.peg.1730; -.
DR   HOGENOM; CLU_007884_4_5_6; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000017667; 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   377 AA;  42503 MW;  B8E595CB334F712E CRC64;
     MHIAIIGAGI SGLMTALELV EQGCSVDIFD QQQAGQAASW AGGGILSPMY PWRYAPEVNQ
     LAQYGKSLYQ SWNEKLSPIT GIDFQIHNTG MLIFDQEDFQ TGLNYATQHN EPMQQCDLLN
     RIQLEAVNSH ISKQFDQAIY FPQLANVRNP RLLQSLIHYL KQHPCVRFFE HCTVEKLIIK
     NKTVHGIETE DHQQYFADQV VLTSGAWSNY WQQQVQRKIP VHPVQGQMLL FKSPENWLPT
     MCMNRVMYLI PRQDGHIVCG SSMSECGFST AVDAQTQQDI LSACLEMVPE LAQFPIVKRW
     AGLRPSSPHG IPYIGAMPEI NRLWANFGHF RNGLCMGAGS AKLLAQLMLD QKTFVDPHGY
     SPDRLACTQS AIHENLS
//