ID   F8J797_HYPSM            Unreviewed;       427 AA.
AC   F8J797;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Putative oxidoreductase {ECO:0000313|EMBL:CCB67207.1};
DE            EC=1.-.-.- {ECO:0000313|EMBL:CCB67207.1};
GN   OrderedLocusNames=HYPMC_3998 {ECO:0000313|EMBL:CCB67207.1};
OS   Hyphomicrobium sp. (strain MC1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Hyphomicrobiaceae; Hyphomicrobium.
OX   NCBI_TaxID=717785 {ECO:0000313|EMBL:CCB67207.1, ECO:0000313|Proteomes:UP000000494};
RN   [1] {ECO:0000313|Proteomes:UP000000494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC1 {ECO:0000313|Proteomes:UP000000494};
RA   Genoscope.;
RT   "The complete genome of Hyphomicrobium sp. MC1.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FQ859181; CCB67207.1; -; Genomic_DNA.
DR   RefSeq; WP_013949599.1; NC_015717.1.
DR   AlphaFoldDB; F8J797; -.
DR   STRING; 717785.HYPMC_3998; -.
DR   KEGG; hmc:HYPMC_3998; -.
DR   eggNOG; COG0665; Bacteria.
DR   HOGENOM; CLU_007884_3_3_5; -.
DR   Proteomes; UP000000494; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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   PANTHER; PTHR13847:SF295; FAD-DEPENDENT CATABOLIC D-ARGININE DEHYDROGENASE DAUA; 1.
DR   PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:CCB67207.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000494}.
FT   DOMAIN          30..378
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   427 AA;  46219 MW;  CD49AC2F2527CE6F CRC64;
     MTAFTTASAW ADTSSETLPD DPLRPDEHCD LAIVGGGILG LCSGLHAARQ GLAVRIVDAA
     RIADRASGLN GGQVIAGFKY DPDWLIEHFG DKRGSALVSF GASTPDAVFG LIERERLNVP
     RQAKGWIQAA HSETALKAAE DRAAQWIARG VPAKILSADD VTQMTGAQGY LGGWLDPRGG
     AIQPFAYTRE LARIAVAAGV RIAENTRISR LRRENSSWAL ATADGKTLHA KSVIVATNAY
     ADGLIPGLAR TLLPLHSFQI ATEPLPYEVL ANILPGGQVV SDSRRIVTYY RRGPDNRMLL
     GGRGSMAEPT SPKAWAHLEH ALKRLYPALN DVKIEKRWYG RVAVTLDYLP HVHEPERGLM
     VAAGCQGRGV GLMTALAPRL VDYLASRDPE CIPLPITPIK PIPFHTFRNI GIGAAIAWYR
     LIDMLER
//