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Database: UniProt
Entry: A0A1E4HIW8_9GAMM
LinkDB: A0A1E4HIW8_9GAMM
Original site: A0A1E4HIW8_9GAMM 
ID   A0A1E4HIW8_9GAMM        Unreviewed;       328 AA.
AC   A0A1E4HIW8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Thiamine biosynthesis protein thio {ECO:0000313|EMBL:ODT96781.1};
GN   ORFNames=ABS82_03150 {ECO:0000313|EMBL:ODT96781.1};
OS   Rhodanobacter sp. SCN 67-45.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Rhodanobacter.
OX   NCBI_TaxID=1660133 {ECO:0000313|EMBL:ODT96781.1, ECO:0000313|Proteomes:UP000094158};
RN   [1] {ECO:0000313|EMBL:ODT96781.1, ECO:0000313|Proteomes:UP000094158}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA   Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA   Banfield J.F.;
RT   "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT   unravelled with genome-resolved metagenomics.";
RL   Environ. Microbiol. 17:4929-4941(2015).
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}.
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:ODT96781.1}.
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DR   EMBL; MEFB01000011; ODT96781.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E4HIW8; -.
DR   Proteomes; UP000094158; Unassembled WGS sequence.
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; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          3..314
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
SQ   SEQUENCE   328 AA;  35459 MW;  16D8B855CAFD9D88 CRC64;
     MRIGILGAGV AGLVTAVELA GRGARVEIIE RAPDHARACA WVAGGMLAPW CEQASAEPQV
     ATLGAPAVEW WQRHFDGTMQ RGTLVVAATR DAGELALFGR RTERFEPIDA ERIGALEPEL
     AGRFRQGLFF PDEAHLDPRR ALPALAAQLT AAGVAIRYGV DADAARIDAD RIVDCRGLAA
     RDTLEDLRGV RGEMIVVRSP DIQLSRPVRL LHPRFGLYVV PRGDGVFMLG GTLLESSSHD
     PMTVRSAMDV LNTAYALHPA FAEAEILELG VGVRPAFPDN LPRVLRRGRT VYLNGLYRHG
     FLLAPAMAQQ AARLIFPHTT ETPACISA
//
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