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Database: UniProt
Entry: R5UZF7_9BACT
LinkDB: R5UZF7_9BACT
Original site: R5UZF7_9BACT 
ID   R5UZF7_9BACT            Unreviewed;      1076 AA.
AC   R5UZF7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=FAD dependent oxidoreductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BN709_00559 {ECO:0000313|EMBL:CCZ81194.1};
OS   Odoribacter laneus CAG:561.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Odoribacteraceae;
OC   Odoribacter.
OX   NCBI_TaxID=1263089 {ECO:0000313|EMBL:CCZ81194.1, ECO:0000313|Proteomes:UP000017974};
RN   [1] {ECO:0000313|EMBL:CCZ81194.1, ECO:0000313|Proteomes:UP000017974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:561 {ECO:0000313|Proteomes:UP000017974};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CCZ81194.1}.
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DR   EMBL; CBAQ010000059; CCZ81194.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5UZF7; -.
DR   Proteomes; UP000017974; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd00207; fer2; 1.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 3.10.20.440; 2Fe-2S iron-sulphur cluster binding domain, sarcosine oxidase, alpha subunit, N-terminal domain; 1.
DR   Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 4.
DR   InterPro; IPR042204; 2Fe-2S-bd_N.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42949; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT B; 1.
DR   PANTHER; PTHR42949:SF2; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT B; 1.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF13510; Fer2_4; 1.
DR   Pfam; PF04324; Fer2_BFD; 1.
DR   Pfam; PF00037; Fer4; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017974}.
FT   DOMAIN          16..96
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          486..516
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   1076 AA;  118945 MW;  2AFBC322ED2D2232 CRC64;
     MSKIENHPIL DVPVRDKVVF LYNGKKIEAE SGYTIAAALH RAGYPVHSHS LDGRERSLEC
     GIGKCGACEM LVDGKIRRIC ITKVDGIKEV EEISEKCMPK EKSSVVPEKK QILRTRVVII
     GAGPAGLAVR EEFNKHGVDN IVIDSNDKIG GQFTMQTHQF FFFEKEKRFG GMRGFDIAKT
     LAGENADGIY LNCVVWDLLE GKRVAVKNIS TEEVFFVDAD YLVVATGAVP FMPAFENDDL
     PGVYTAAVVQ KMMNNEMTLL GKNVLTVGAG NIGYLTSYQL MQAGAKVKAI IEAMPREGGF
     PVQANRVRRL AIPVMTSYIL LKAIPNKTRD GIVGAVIARC ENFKPVPGTE KIIEGIDVIN
     ICTGLIPDNQ LLTKGKEVFG GKCFAAGDAI RIGEGTSAVL KGRHTAMQIM MELGVNINYD
     DYLLLSKEYI DSQQHPEKIL DEPNLPDPER MLARGFVQAD CLYGFACNPC SFACPHGAIT
     KSSTSAVPTV HYDKCIGCME CVYQCPGLAI FGYHIKKDML FLPVEYEAQE GQEVYLVNNN
     GEKLGEGVLE KILRKPNKTN VARVRALTIH GEELTLVRGF IVKSNYPEPL DLKPLLRDEK
     GETYICHCDD VKLEEVLQVI GDRSFISIDE IKHTTHLGMG PCRGKRCIPR LRQALRSRGI
     ELTGDATPRA PLSNQLSLGE LHPAKKGDVY RVANRDGFKK IEVGALIAGG GMAGSSLFRY
     MAEAGMNPVL VNADRGSSWR NIGGGRTAFS LPELAEIAAR NHSIFKELQY LSNIDYRPIK
     YVNFAHDEET YKALEASKAW SKAEMVAPKQ FREEISPYFN SKSKKYLAAL ISDECWQATP
     GKVVDLIRNI GIAAGGTVME DCRVIEAVRD GKYTSVLVST HDKQYIEYRT EHFVNALGSG
     AGKLCDSMGI DAGLYPVRHQ AFITRRLPML GKNGANLDML IDRQDYKGFS AVYGQQIAYT
     GQIIGCASPK LDAMRIDKNL KLNTKAFLEI VSEMFVEWIP DLAGVGIQAV WAGYYTEPRY
     IVDPELGLFV GMRGHGFMLS QYIAKMYVDK LMGRPVPEYF DKLKLNGPGL SEKAFK
//
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