ID   I4BZP5_DESTA            Unreviewed;       863 AA.
AC   I4BZP5;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=FAD/FMN-dependent dehydrogenase {ECO:0000313|EMBL:AFM22786.1};
GN   OrderedLocusNames=Desti_0036 {ECO:0000313|EMBL:AFM22786.1};
OS   Desulfomonile tiedjei (strain ATCC 49306 / DSM 6799 / DCB-1).
OC   Bacteria; Thermodesulfobacteriota; Desulfomonilia; Desulfomonilales;
OC   Desulfomonilaceae; Desulfomonile.
OX   NCBI_TaxID=706587 {ECO:0000313|EMBL:AFM22786.1, ECO:0000313|Proteomes:UP000006055};
RN   [1] {ECO:0000313|Proteomes:UP000006055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49306 / DSM 6799 / DCB-1
RC   {ECO:0000313|Proteomes:UP000006055};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Zeytun A.,
RA   Lu M., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "Complete sequence of chromosome of Desulfomonile tiedjei DSM 6799.";
RL   Submitted (JUN-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; CP003360; AFM22786.1; -; Genomic_DNA.
DR   RefSeq; WP_014807945.1; NC_018025.1.
DR   AlphaFoldDB; I4BZP5; -.
DR   STRING; 706587.Desti_0036; -.
DR   KEGG; dti:Desti_0036; -.
DR   PATRIC; fig|706587.4.peg.40; -.
DR   eggNOG; COG0247; Bacteria.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_331702_0_0_7; -.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000006055; Chromosome.
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   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004017; Cys_rich_dom.
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; IPR009051; Helical_ferredxn.
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; PF02754; CCG; 2.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   Pfam; PF13183; Fer4_8; 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; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006055}.
FT   DOMAIN          33..211
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          482..515
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   863 AA;  92918 MW;  D2A49C49DDF317DD CRC64;
     MDFVQRLTGL VGAENITASP VDCLAYSRDM SIHVGVPHAI VFAKSTEQVS EILQFANSEK
     IPVTARGTGS SVTGAVLAPK GGIILDFTRM NAVLEINKAD GYAVIEPGVI CNALNAKLAP
     SHFFPPDPGS AAIATIGGMI ATNASGVRAA KYGTTKDYVK TLTVVLADGR ILETGDMAPK
     SSAGYDLTHL FSSSEGTLGI ITRAVVKILP MPEYEAFAKA SFPDVDTAGL AVEKIFTSGL
     ELATCEILDN ICLQVCRDAL KMDIPREVNC QLFMGIDGPK TAVQEQIKKI DEICKSVGGI
     ENIWSDNPVE KAKLFAARGG LVPAMSRLKP GYRLVPLVED FGVPISKIPQ TIAEIQQIGA
     KYGFPVATFG HIGDGNLHAT FIMNPTIPEE WEKVKGIALE FIDMTLKHSG TVSAEHGVGM
     AKSPYINRQL GESLEIMKDI KKTLDPNNVL NPGKMGFDDS IKDILDENSF QKFLKAPEEV
     FHFPEGVDNE IMACIQCGFC RAGCPTFGET TLESLNAKGR VTLAYNMLMG NIEASPELAK
     RLYQCMLCLN CKSVCPAQVK VSTIVRSARE KLVNKGYLPE IFKPALAAMI DAANPLLADP
     AKRCDSYPSE YKKAIPGNTD AILHLGCVTS FQDIKIIPAL MQVLDKAGVN YGALGEDESC
     CGYLAYLVGD MQTFKQAMAK YSGKLETYHP SQLITSCAGC LKTFRDIYPS YGGLQNGLSV
     VHAVELMEKL IADGKLTFKT DVPPIKVVYH DPCDMGRHMG VYEPPRNVLK AIPGVDLLEF
     PLNRNLAKCC GGGGGMKGFD NEMAGDIGYK RLLSAVDLGA EMIVSACPSC KGSFNQAAAR
     ARKEKKAKIK VMDITELVAS RLA
//