ID   A0A136MTU6_9BACT        Unreviewed;       967 AA.
AC   A0A136MTU6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=FAD-binding protein {ECO:0000313|EMBL:KXK37297.1};
GN   ORFNames=UZ09_BCD002002069 {ECO:0000313|EMBL:KXK37297.1};
OS   Bacteroidetes bacterium OLB9.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1617420 {ECO:0000313|EMBL:KXK37297.1, ECO:0000313|Proteomes:UP000070267};
RN   [1] {ECO:0000313|EMBL:KXK37297.1, ECO:0000313|Proteomes:UP000070267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB9 {ECO:0000313|EMBL:KXK37297.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (NOV-2015) 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:KXK37297.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LNBW01000066; KXK37297.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136MTU6; -.
DR   STRING; 1617420.UZ09_BCD002002069; -.
DR   PATRIC; fig|1617420.3.peg.2193; -.
DR   Proteomes; UP000070267; 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   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; 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; PF02754; CCG; 1.
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; 1.
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}.
FT   DOMAIN          41..269
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          609..642
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   967 AA;  109536 MW;  32895423312469DF CRC64;
     MHSSKSQKIQ QFLKEVQAIS PNTVKADIQT LGLYATDASL YQVFPLAVAI PRDEKELIDI
     IRLANQYEVP VLPRGSATSL AGQTVNKSLV IDFTRYFSKI LEINVEERYA IVQPGVVRDW
     LNDALKPHRL HFAPDPATTS RATFGGMIAN NSSGTRSIKY GKTIDHLLEL KVLLMDGTIL
     RMGALTPDAY DEKCRQKDRE GAIYRKFRSI IHDNKGAIKE AYPTVLRRVQ GYPLDEFIGT
     DQWNFAKILS GSEGSLGIIL EAKVHLEPLP NFRAAYNVHY NDRMKAIREV QKIVDFHPIA
     VEMLDYNVFR QSIRNNVTKE LHKMLIEGKP EATLFVEFYA DTQQKLNEQI TAFGNWLKEN
     SSGYAFPLYR EEKTINAAIE LRKKGLGLIM GDPTGRKPIP FIEDQAIPLE HLADYIQAVL
     YICDKYDVKT VLYAHASVGV LHVRPELDMT KQEDIEIMKK ISSEVFKLVK QYKGSWSGEH
     GDGRNRGPKL REYFGEEVYQ CLREVKEAFD PKYLLNPGII IDVPPMDEHL RYGTEYKEKK
     YDFVYQYRKD RSFENIVHNC SGLGVCRNHY GGGMCPSFRA TLDEKSSTRG RANALRLGIS
     GQFGFSSLTD PKVLDTLDLC LSCKACKSEC PSNVDMAKLK SEVLQLKHDE SKISLKEKAI
     RENASMSAKI AGWKAPIFNF FLKNSLFKRM AEKWMGIDRR RQLPLYATTS LEEWYHKHYK
     PKGYDRKVVL FADTYINYHE IKVGKAAIRL LNDCGYEVLL AAVGCCQRPR ISNGFLKEAK
     AAGTAVVEQL IPYMEQGLKI VVCEPSCTSA FLDDIPDLLE NDAWADQLQN HVQAIDVFLS
     EALESGALKG KFVATSDHIL LHGHCHQKSL FGTAGMHHIY DSIEGLQYYE PDSGCCGMAG
     SFGYEKEHYD VSKKVADLVL IPEINKTADQ TLIVTSGFSC RHQINDFTDR TPVHWVESIR
     FVQDTAK
//