ID E3LDH5_CAERE Unreviewed; 399 AA.
AC E3LDH5;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=FAD dependent oxidoreductase domain-containing protein {ECO:0000259|Pfam:PF01266};
GN ORFNames=CRE_00621 {ECO:0000313|EMBL:EFO82534.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) 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 MSOX/MTOX family.
CC {ECO:0000256|ARBA:ARBA00010989}.
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DR EMBL; DS268407; EFO82534.1; -; Genomic_DNA.
DR RefSeq; XP_003117936.1; XM_003117888.1.
DR AlphaFoldDB; E3LDH5; -.
DR STRING; 31234.E3LDH5; -.
DR EnsemblMetazoa; CRE00621.1; CRE00621.1; WBGene00051496.
DR eggNOG; KOG2820; Eukaryota.
DR HOGENOM; CLU_007884_2_2_1; -.
DR InParanoid; E3LDH5; -.
DR OMA; WPMLWAH; -.
DR OrthoDB; 1952715at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; 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; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR045170; MTOX.
DR PANTHER; PTHR10961; PEROXISOMAL SARCOSINE OXIDASE; 1.
DR PANTHER; PTHR10961:SF17; SARCOSINE OXIDASE; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000008281}.
FT DOMAIN 6..377
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 399 AA; 44962 MW; 96B0C94B668271FF CRC64;
MTKHYDVVVV GAGIFGSCTA YHCQRLGMRT LLLEQFNLGH SNGSSHGKSR ITRYAHTDPE
YVPLVGDSYS QIEQLEKMRG EKLWNKLGLL WAATGNQVQS ISGHLQAHNI EHEVIRGNEI
PKRYPQFKFD EKWTGLIDPM GGVIYANKWL NAFQEEFKHL GGTIQENEPL ISHDESYDSP
LELTTKNGKY TSNKIIFTVG CWITKFFPHV NFKIKVSFLL SSFFHLTYLQ PISLAVCYWK
AKEENQRHLL DEKHFPVVIA KNLEKKEYYF ALPDTDYQGA IKLVLDDGDE LNEDLSHPKK
NNKDFVDLPG KFITEHIPVV DGTKPYKVDQ CKYTNSPDHH YLIGPVSSET SNILVGGCGS
GSGFKTAPGI GRALAEMAAG KKTTVDVSFF SPSRFVTPI
//
