ID   A0A1M3G5K0_9SPHI        Unreviewed;       974 AA.
AC   A0A1M3G5K0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=FAD-binding oxidoreductase {ECO:0000313|EMBL:OJW35339.1};
GN   ORFNames=BGO54_03880 {ECO:0000313|EMBL:OJW35339.1};
OS   Sphingobacteriales bacterium 46-32.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=1895839 {ECO:0000313|EMBL:OJW35339.1, ECO:0000313|Proteomes:UP000184358};
RN   [1] {ECO:0000313|EMBL:OJW35339.1, ECO:0000313|Proteomes:UP000184358}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=46-32 {ECO:0000313|EMBL:OJW35339.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:OJW35339.1}.
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DR   EMBL; MKTY01000014; OJW35339.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3G5K0; -.
DR   STRING; 1895839.BGO54_03880; -.
DR   Proteomes; UP000184358; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   PANTHER; PTHR11748:SF119; D-2-HYDROXYGLUTARATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   Pfam; PF13534; Fer4_17; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          34..273
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   974 AA;  108577 MW;  664775351D871BAF CRC64;
     MNDELLRQLA QTLEGELHTD TVMRTLYATD ASAYREMPLA VAIPLHQEDL RQLILFAGKH
     KLSLIPRTAG TSLAGQVVGP GIVVDLSRHF TRILELNKEA HWVRVQPGVI RDELNYFLKP
     HGLFFGPETS TANRAMIGGM VGNNSCGSNS IVYRSTREHL LEVTALLSDG SEAVFGALSL
     DDFHAKCEGD TLEAAIYKRT RQLLGSYDTQ EEIRRQFPKK TVERRNTGYA VDLLIDMAPF
     HAGGPDFNFC SLIAGSEGTL AMITEIKLNV VPLPPREIGL LCVHFHSVDE ALRANLVAVR
     HRISASELID HYILDCTKQN IEQQKNRFFV QGEPGAILVI EFARDTREEI QEEAARCEAA
     MKAQGLGYHF PLLFGADSKK IWTLRKAGLG LLSNLPGDEK AVPVIEDTAV DVNDLPAYIR
     DFNEILKKHG LYSVHYAHAG SGELHLRPII NLKTPEGNLL FRRIAEDIAT LVKKYDGSLS
     GEHGDGRLRG EFIPQMIGPK NYELLREIKK TWDPQHIFNP NKIVDTPSMN SMLRYEPGQQ
     TPAFKTVFRF HDQDVLQHAE QCNGSGDCRK THLSGGTMCP SYMATRNEKD STRARANILR
     EFLTHSTKAN RFDHKEIYEV MDLCLSCKGC KSECPSNVDV AKLKAEFLQH YHDEHGVPLR
     SRLIAGFARS SRLGSLVPGL YNFFMTNKVT SNLIKSTIGF ARDRSMPTLQ KTTLHKWFTR
     RGPGPKKGHS GRKVYLFCDE FTNYNDTHIG IKAVELLEKL GYTVEIPAHI ESGRAHLSKG
     LLREAKKIAE RNVSMLAPLI SADSPLIGVE PSAILTFRDE YPDLVSDEQL PAARQLAKHV
     LLIDEFIAGE ISKGNIQASQ FTRNKKSIKL HGHCQQKAMS SVEHSVKILS LPENYTVEVI
     PSGCCGMAGS FGYEKEHYDL SMKVGELVLL PAVRAAAADQ LIAAPGTSCR HQIKDGTGRK
     AQHPVEILWE ALEH
//