ID   K9DAX1_9BURK            Unreviewed;       357 AA.
AC   K9DAX1;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=HMPREF9710_03183 {ECO:0000313|EMBL:EKU81343.1};
OS   Massilia timonae CCUG 45783.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=883126 {ECO:0000313|EMBL:EKU81343.1, ECO:0000313|Proteomes:UP000009874};
RN   [1] {ECO:0000313|EMBL:EKU81343.1, ECO:0000313|Proteomes:UP000009874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 45783 {ECO:0000313|EMBL:EKU81343.1,
RC   ECO:0000313|Proteomes:UP000009874};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Massilia timonae CCUG 45783.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:EKU81343.1}.
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DR   EMBL; AGZI01000041; EKU81343.1; -; Genomic_DNA.
DR   RefSeq; WP_005668039.1; NZ_JH992924.1.
DR   AlphaFoldDB; K9DAX1; -.
DR   STRING; 47229.LO55_583; -.
DR   PATRIC; fig|883126.3.peg.3208; -.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_017779_0_0_4; -.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000009874; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748:SF103; GLYCOLATE OXIDASE SUBUNIT GLCE; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000009874}.
FT   DOMAIN          1..169
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   357 AA;  37763 MW;  876499DB98CDCA02 CRC64;
     MGTIERFQER VRAAASDRQP LCIRGGGSKD WYGGAPQGAV LDTRDHAGIV DYEPTELVVT
     ARCGTPLAEI EALLARHNQM LAFEPPHFSA TATVGGTVAA GLSGPRRGSS GATRDFVLGA
     RLLDGKGDVL AFGGKVMKNV AGYDVSRMLA GSMGTLGLLL EVSLKVLPRP FAEATLRFEM
     SEIDAIRRLN EWGGQPLPLS GSAWCGGQLA LRLSGAEAAV DAAMRLLGGE AVPHPDAAAF
     WTDLREQRHA FFTGSEPLWR LSVPSTTGAL VLGGDQLIEW GGAQRWLRTG GDAATADTVR
     RTAQACGGHA TLFRGGDKGS GVFQPLAPVL ARIHARMKDA FDPAHIFNPG RLYPESA
//