ID A0A0R1W4Q8_9LACO Unreviewed; 455 AA.
AC A0A0R1W4Q8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=FAD FMN-containing dehydrogenase {ECO:0000313|EMBL:KRM12800.1};
GN ORFNames=FD16_GL001978 {ECO:0000313|EMBL:KRM12800.1};
OS Paucilactobacillus suebicus DSM 5007 = KCTC 3549.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Paucilactobacillus.
OX NCBI_TaxID=1423807 {ECO:0000313|EMBL:KRM12800.1, ECO:0000313|Proteomes:UP000051820};
RN [1] {ECO:0000313|EMBL:KRM12800.1, ECO:0000313|Proteomes:UP000051820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5007 {ECO:0000313|EMBL:KRM12800.1,
RC ECO:0000313|Proteomes:UP000051820};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM12800.1}.
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DR EMBL; AZGF01000005; KRM12800.1; -; Genomic_DNA.
DR RefSeq; WP_010621937.1; NZ_BACO01000036.1.
DR AlphaFoldDB; A0A0R1W4Q8; -.
DR STRING; 1423807.FD16_GL001978; -.
DR PATRIC; fig|1423807.3.peg.2030; -.
DR eggNOG; COG0277; Bacteria.
DR Proteomes; UP000051820; 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 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; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR PANTHER; PTHR42934:SF2; GLYCOLATE OXIDASE SUBUNIT GLCD; 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}.
FT DOMAIN 35..214
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 455 AA; 48205 MW; 7C0346192566EF05 CRC64;
MADISELSLT NGQVITDPDV LKKFGKNDST QEVVKVYQPL AVVEAQSIKD VQDTMKFANA
HKIPVTTWGA GSSIVNSSAG LDDGIVLNLS KMNKILEINI PNQYAIVEAG VINADLDKEV
RKQGYFFAPD PGSKPISSVG GNIATNAGGM SSLKYGTTKQ SVIGLQIVLA DGTLIDTGGK
TFKNNVGYDL TDLLVGSEGT LAVIVSATVK LLPIPFGKPV TGLATFANMA ELSVGVQKIS
ASGLYPSMLE ALNDTSIEAL DRLEGSDLGN GGTAKALLIF KLEGAPAGAV DALKKILDEA
KAIHVSVTDD QEYSDNIIKI RQDYYKAEAA YGRLIVEDIA VPLSKLPELA AFVADLKFTT
NVTAFLGGHA GDGNFHPNIA IPRDSDSVPA DVREAINKIF TYAQSVGGTI SAEHGIGEIK
KQWVLPQLGQ DLVDLQKKVK LAFDPNNILN PGRKI
//
