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Database: UniProt
Entry: W1N1H3_9GAMM
LinkDB: W1N1H3_9GAMM
Original site: W1N1H3_9GAMM 
ID   W1N1H3_9GAMM            Unreviewed;       474 AA.
AC   W1N1H3;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=BJB45_07635 {ECO:0000313|EMBL:ERL49333.1};
OS   Halomonas huangheensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1178482 {ECO:0000313|EMBL:ERL49333.1, ECO:0000313|Proteomes:UP000019113};
RN   [1] {ECO:0000313|EMBL:ERL49333.1, ECO:0000313|Proteomes:UP000019113}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BJGMM-B45 {ECO:0000313|EMBL:ERL49333.1,
RC   ECO:0000313|Proteomes:UP000019113};
RA   Miao C., Wan Y., Jin W.;
RT   "draft genome of Halomonas huanghegensis, strain BJGMM-B45T.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC       4 family. {ECO:0000256|ARBA:ARBA00008000}.
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:ERL49333.1}.
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DR   EMBL; AVBC01000055; ERL49333.1; -; Genomic_DNA.
DR   RefSeq; WP_021821083.1; NZ_CP013106.1.
DR   AlphaFoldDB; W1N1H3; -.
DR   STRING; 1178482.AR456_08930; -.
DR   KEGG; hhu:AR456_08930; -.
DR   PATRIC; fig|1178482.3.peg.4117; -.
DR   eggNOG; COG0277; Bacteria.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000019113; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2190; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
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; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 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   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000019113}.
FT   DOMAIN          36..217
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   474 AA;  51146 MW;  8D9D7C8D14D69036 CRC64;
     MRDALITFLQ QSLGPSGVLV DGKDTERYCL DWAGARGAEP LAVARPASVD EVAQVMRYCH
     QHDIPVVPQG GGSGLVEGAL PDHHTPELVL SLERLNRIRH LDPLNFTVSV DAGCVLQMIK
     DAVQAEDCFF PLALGAQGSC QIGGNISTNA GGLNVLRYGM MRQLVLGLEV VLPDGRILSD
     MRPLHKNNTG YDLKQLFIGA EGTLGIVTGA VLKLGPRPIH SRTALIGCPD VQSVMRLYGL
     ARRSCCDLLS AFELIPRACI ELALGAAPAL KDPLDSTHPV YVLLEVGASG ELDLDAMIET
     LFSKGLDQGL LSDGVLASSE SQAAQLWQFR EAMLEGQQRR GLHLRTDIAL PISSLDAFHQ
     QAEQLVERLA HDAEVIAYGH VGDGNLHFNV LPPAALSDDD KQALLHDIEE QLFELVAEFD
     GSISAEHGIG RVKQNAFLGN LSAPQYDIMR GLKRLLDPRG NLSAGRILPR SDGR
//
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