ID W6M6Z9_9GAMM Unreviewed; 468 AA.
AC W6M6Z9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Putative FAD/FMN-containing dehydrogenase {ECO:0000313|EMBL:CDI03681.1};
GN ORFNames=BN873_610078 {ECO:0000313|EMBL:CDI03681.1};
OS Candidatus Competibacter denitrificans Run_A_D11.
OC Bacteria; Pseudomonadota; Gammaproteobacteria;
OC Candidatus Competibacteraceae; Competibacter.
OX NCBI_TaxID=1400863 {ECO:0000313|EMBL:CDI03681.1, ECO:0000313|Proteomes:UP000035760};
RN [1] {ECO:0000313|EMBL:CDI03681.1, ECO:0000313|Proteomes:UP000035760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Run_A_D11 {ECO:0000313|EMBL:CDI03681.1,
RC ECO:0000313|Proteomes:UP000035760};
RA McIlroy S.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDI03681.1, ECO:0000313|Proteomes:UP000035760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Run_A_D11 {ECO:0000313|EMBL:CDI03681.1,
RC ECO:0000313|Proteomes:UP000035760};
RA McIlroy S.J., Albertsen M., Andresen E.K., Saunders A.M., Kristiansen R.,
RA Stokholm-Bjerregaard M., Nielsen K.L., Nielsen P.H.;
RT "Candidatus Competibacter-lineage genomes retrieved from metagenomes reveal
RT functional metabolic diversity.";
RL Submitted (FEB-2014) 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:CDI03681.1}.
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DR EMBL; CBTJ020000071; CDI03681.1; -; Genomic_DNA.
DR AlphaFoldDB; W6M6Z9; -.
DR STRING; 1400863.BN873_610078; -.
DR Proteomes; UP000035760; 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 InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
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:UP000035760}.
FT DOMAIN 43..222
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 468 AA; 51542 MW; F5B96433EF48955B CRC64;
MTMHSSSETT ALLDGIRAFI EPASLRTDAD SALLYGRDWT RLYQPNPLAV VLPGTIEQVR
QLVCYANDHR LALVPSGGRT GLSGAAVASH GELVVSLERM NRILDFDAVD RSVTCQAGTV
TEALQNFARE QGLSYPVDFA SRGSSHIGGN IATNAGGIKV VRYGLTRDWV TGLKVVTGRG
DLLDLNRGLI KNASGYDLRH LFIGSEGTLG IIVEATLKLT RPLHEPNVMV LGVPDLNGLM
AIYGVLRGAL ELSAFEFFSE LALRHVLKKG LHRPFETATP YYVLTEFENP AGRFTDQALQ
LFEHCTEQGW LVDGVISQSE QQAKELWRLR EDISESIAEH QPYKNDISVR ISRVPALLEE
IDHLLAREYP NFEVLWYGHI GDGNLHINIL KPAEMATATF AENCGAVSEH LFATLQRHGG
SISAEHGVGL TKKPYLHYTR DATEVGYLRA LKQVFDPNGI MNPGKIFD
//
