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Database: UniProt
Entry: C7N5W3_SLAHD
LinkDB: C7N5W3_SLAHD
Original site: C7N5W3_SLAHD 
ID   C7N5W3_SLAHD            Unreviewed;       470 AA.
AC   C7N5W3;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=FAD/FMN-dependent dehydrogenase {ECO:0000313|EMBL:ACV22298.1};
GN   OrderedLocusNames=Shel_12710 {ECO:0000313|EMBL:ACV22298.1};
OS   Slackia heliotrinireducens (strain ATCC 29202 / DSM 20476 / NCTC 11029 /
OS   RHS 1) (Peptococcus heliotrinreducens).
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Slackia.
OX   NCBI_TaxID=471855 {ECO:0000313|EMBL:ACV22298.1, ECO:0000313|Proteomes:UP000002026};
RN   [1] {ECO:0000313|EMBL:ACV22298.1, ECO:0000313|Proteomes:UP000002026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29202 / DSM 20476 / NCTC 11029 / RHS 1
RC   {ECO:0000313|Proteomes:UP000002026};
RX   PubMed=21304663; DOI=10.4056/sigs.37633;
RA   Pukall R., Lapidus A., Nolan M., Copeland A., Glavina Del Rio T., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L., Kuske C.,
RA   Brettin T., Detter J.C., Han C., Pitluck S., Pati A., Mavrommatis K.,
RA   Ivanova N., Ovchinnikova G., Chen A., Palaniappan K., Schneider S.,
RA   Rohde M., Chain P., D'haeseleer P., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Kyrpides N.C., Klenk H.P., Hugenholtz P.;
RT   "Complete genome sequence of Slackia heliotrinireducens type strain (RHS
RT   1).";
RL   Stand. Genomic Sci. 1:234-241(2009).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP001684; ACV22298.1; -; Genomic_DNA.
DR   RefSeq; WP_012798401.1; NC_013165.1.
DR   AlphaFoldDB; C7N5W3; -.
DR   STRING; 471855.Shel_12710; -.
DR   KEGG; shi:Shel_12710; -.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_017779_9_2_11; -.
DR   Proteomes; UP000002026; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000002026}.
FT   DOMAIN          42..221
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   470 AA;  50921 MW;  FB0176A0E759E4F3 CRC64;
     MSQFNEVTQD LIQQIESIVG EDYCYVGERI NSDFARDEMP IYGAHMPDVV CEPANTEEVS
     VVMRACYEAN VPVTVRGAGT GLVSGSVAVE GGVMLCTMRM DKILEYDMNN LFVRVQPGVR
     LCDLAADALE HDLMYPPDPG EKTASVGGNV STNAGGMRAV KYGTTRDYVL AMTVVLADGE
     ILQIGRPVTK TSTGYSLLHL MIGSEGTLGV ITELTLRLIP NPKENASFLL PFVDIHAAMA
     SVPKIKLSGL DPQSIEFMER DIVDSSAAHT DNYIIPTEVQ GQEAGAYILV TFDGNDIDEI
     FQRAETLAEL ADEAGAFDTL VLEGSEKRAV WELRGAFLTA IEAEEKLIDE MDVVVPVDSI
     TEFLEFVHSE GEKVGLRIRS FGHAGDGNLH IYCCSQTLDE EEFLIRNKKV MDASYAKCAE
     LNGQVSGEHG IGAAKATYLA QSVGDTQMRL MAGIKAAFDP KGILNPGKVV
//
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