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Database: UniProt
Entry: B9Y301_9FIRM
LinkDB: B9Y301_9FIRM
Original site: B9Y301_9FIRM 
ID   B9Y301_9FIRM            Unreviewed;       740 AA.
AC   B9Y301;
DT   14-APR-2009, integrated into UniProtKB/TrEMBL.
DT   14-APR-2009, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=FAD binding domain protein {ECO:0000313|EMBL:EEF69649.1};
GN   ORFNames=HOLDEFILI_00176 {ECO:0000313|EMBL:EEF69649.1};
OS   Holdemania filiformis DSM 12042.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Holdemania.
OX   NCBI_TaxID=545696 {ECO:0000313|EMBL:EEF69649.1, ECO:0000313|Proteomes:UP000005950};
RN   [1] {ECO:0000313|EMBL:EEF69649.1, ECO:0000313|Proteomes:UP000005950}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12042 {ECO:0000313|EMBL:EEF69649.1,
RC   ECO:0000313|Proteomes:UP000005950};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEF69649.1, ECO:0000313|Proteomes:UP000005950}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12042 {ECO:0000313|EMBL:EEF69649.1,
RC   ECO:0000313|Proteomes:UP000005950};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Holdemania filiformis DSM 12042.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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:EEF69649.1}.
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DR   EMBL; ACCF01000008; EEF69649.1; -; Genomic_DNA.
DR   RefSeq; WP_006057393.1; NZ_GG657551.1.
DR   AlphaFoldDB; B9Y301; -.
DR   STRING; 545696.HOLDEFILI_00176; -.
DR   eggNOG; COG1053; Bacteria.
DR   eggNOG; COG3976; Bacteria.
DR   HOGENOM; CLU_011398_4_0_9; -.
DR   OrthoDB; 9806724at2; -.
DR   Proteomes; UP000005950; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1010.20; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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; IPR007329; FMN-bd.
DR   InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR   PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR   Pfam; PF00890; FAD_binding_2; 2.
DR   Pfam; PF04205; FMN_bind; 1.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SMART; SM00900; FMN_bind; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..740
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002893492"
FT   DOMAIN          45..119
FT                   /note="FMN-binding"
FT                   /evidence="ECO:0000259|SMART:SM00900"
SQ   SEQUENCE   740 AA;  79398 MW;  DAFA98AA1CAA3FE4 CRC64;
     MKRLGLVLVS LFMVLSCVAC GQTKEETKKS ELKFTPGSYT ASAQGYNGEV SIEATFSETA
     ITDIQVKEQK ETAHVGDVAY PILIEDILAA NGTGVDVVSG ATFTSIGLKN AVNAAAEAAS
     ASDLDAFKKN TVEHTAQEEI TGTWDVVIVG AGGAGMMAAA QAAQNGDTVL VLEKNAEMGG
     NTLVSGGAYQ STFDAVVWDP ANPDATTGEY NGETYEKVKN DAGRIDTLKT ILNWSEEPFD
     GTIDDEHPFV AGDIALNAVR GVHEEYLPTL KALKEEIQAY LDWAQPQLDA GVHETKLTLF
     STINLHIFQT YYGGLRPNRE NTEWIYGDEK LVRQFVEGGQ EIKDWLEAQG ASIDQSRAFT
     LIGCLWQREN AVNGGTVDGE FYDGKWGAYF AVPANTVLKA NEANKIMTRT TANELITDES
     GRVTGVKATQ FDGTPVTVMA NKGVILATGG YGANIEMVQK TNDYWKDEYI ANNIGTTNRS
     SLKGDGTTMG QAVGAATIGE GWTQMMPLGW VDNGNLAGGA GENVIYVNPE TGKRYVDESA
     ERDVLSEGGF ENGMSEAKAK ELGLKYVPGI YVEISNVGTT AGTGGFNNVP EDVEGRMIFR
     TVEETAKLIG CDAETLRQTI VDYDNYVMGV ADTLDVEKLS YRGTVGQVEM DDDGNYLPDT
     YNLDMIRVRF MAPSTHHTMG GLLVDTERRV LNESGEAIKG LYAAGEVTGG FHSGNRLGGN
     AITEIIVSGR IAGNSASNEK
//
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