ID L0F8I0_DESDL Unreviewed; 472 AA.
AC L0F8I0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=FAD/FMN-dependent dehydrogenase {ECO:0000313|EMBL:AGA69258.1};
GN OrderedLocusNames=Desdi_1808 {ECO:0000313|EMBL:AGA69258.1};
OS Desulfitobacterium dichloroeliminans (strain LMG P-21439 / DCA1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=871963 {ECO:0000313|EMBL:AGA69258.1, ECO:0000313|Proteomes:UP000010797};
RN [1] {ECO:0000313|Proteomes:UP000010797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG P-21439 / DCA1 {ECO:0000313|Proteomes:UP000010797};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Kruse T.,
RA de Vos W.M., Boon N., Smidt H., Woyke T.;
RT "Complete sequence of Desulfitobacterium dichloroeliminans LMG P-21439.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP003344; AGA69258.1; -; Genomic_DNA.
DR RefSeq; WP_015262248.1; NC_019903.1.
DR AlphaFoldDB; L0F8I0; -.
DR STRING; 871963.Desdi_1808; -.
DR KEGG; ddl:Desdi_1808; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_9_2_9; -.
DR OrthoDB; 9767256at2; -.
DR Proteomes; UP000010797; Chromosome.
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 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; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11748:SF103; GLYCOLATE OXIDASE SUBUNIT GLCE; 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 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000010797}.
FT DOMAIN 41..223
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 472 AA; 51325 MW; 759D80CA214FA159 CRC64;
MVSKNQLIQD LEGMFKPERV FKSELQRYCY TYDSSFVSQQ TEYYPDVVVC LDSTEDVSRL
MKYAWDNEVP VTPRGGGSGQ TGGSVAIKGG IVVDLSGWDD IVEIDDANMQ VVVRPGIVHS
DLNDKLSPYC LFFPPDPGSS KMATVGGMVA NNASGLRAVK YGATFQYVLG LEVVLPNGDV
MKTGGLKSKA LKSVSGIDLT RIYCGSEGTL GIITEIRLKV LPKPQSRGIM LALFEKLEDS
ALTVLDVFKA GLIPSGIEIL DDGGIRCANI FKPDLNIPEV EAAIFFEING SKPAVAEEGA
QVRAIAEKRA SSVEWATDAD RMAKLWQGRA VIGAASARFM EGKTRIFAGE DVCFPISKVP
EALRNIRSIG AKYNIPVVIY GHIGDGNMHT APIMDPLNPD EVERTHKVAE AIHRLALEMG
GSTTGEHGVG FARVPYMEEE HGKALDVMWA IKKAIDPKLL MNPGKIWKLG RE
//
