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Database: UniProt
Entry: R6AF91_9PROT
LinkDB: R6AF91_9PROT
Original site: R6AF91_9PROT 
ID   R6AF91_9PROT            Unreviewed;       513 AA.
AC   R6AF91;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=FAD binding domain protein {ECO:0000313|EMBL:CDA45226.1};
GN   ORFNames=BN492_00441 {ECO:0000313|EMBL:CDA45226.1};
OS   Proteobacteria bacterium CAG:139.
OC   Bacteria; Pseudomonadota.
OX   NCBI_TaxID=1262986 {ECO:0000313|EMBL:CDA45226.1, ECO:0000313|Proteomes:UP000018405};
RN   [1] {ECO:0000313|EMBL:CDA45226.1, ECO:0000313|Proteomes:UP000018405}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:139 {ECO:0000313|Proteomes:UP000018405};
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   -!- 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:CDA45226.1}.
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DR   EMBL; CBBV010000190; CDA45226.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6AF91; -.
DR   Proteomes; UP000018405; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR43400:SF7; FAD_BINDING_2 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   4: Predicted;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018405};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..513
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004400119"
FT   DOMAIN          44..491
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
SQ   SEQUENCE   513 AA;  55232 MW;  E827A9323F19E147 CRC64;
     MTSVSRRTFL GTAAAASVSA VAAPAMAAST SGNNLPAKWD DTVDVVVLGC GGAGMMAACQ
     AHDAGGKVAV YDAGQSPFHT ATNLCGGLFT AWGSKMQNAD PEGRKDSWQQ FAEDIMAYGN
     YMSLKEPVYC FAKNSGKAFD FLEDAGLAKH HLEPYAGHSR LRAHRQDSFK GRDYIEVLVK
     QLDKRGIKIN HGMGVTKFYY DPATNTVVGV QVGEGDKAKN VKANKGVIMA TGGITGTPQS
     LDRWVPSVAG KGVAIGGPKN DGTAMMVAVR DVGVPLSHMQ YIASYPCGIV VNGRNGPYCR
     WWFITNNGGI LVNKNGQRFI TEKEGICHVT PSLASQPDGC HYVLVDQAGW ERTLDKIKLG
     ALIGLPSWPA ERVEAEFKAG KNLWKCDTLE ELCQKSGMNL DGLKKQIATW NEAAKNHNDL
     QFGRSDKDMY PLGKGPYYMI RMEPWNNLSC GGVRVNEDLQ VLGWDMKPVN HFYAAGETVA
     GVHGAFYCGG NACGFAHTSG WVAGQKVMGK QIG
//
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