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Database: UniProt
Entry: A0A1Y4GD20_9ACTN
LinkDB: A0A1Y4GD20_9ACTN
Original site: A0A1Y4GD20_9ACTN 
ID   A0A1Y4GD20_9ACTN        Unreviewed;       642 AA.
AC   A0A1Y4GD20;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=FAD-dependent oxidoreductase 2 FAD binding domain-containing protein {ECO:0000259|Pfam:PF00890};
GN   ORFNames=B5F40_07920 {ECO:0000313|EMBL:OUO90151.1};
OS   Gordonibacter sp. An230.
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Gordonibacter.
OX   NCBI_TaxID=1965592 {ECO:0000313|EMBL:OUO90151.1, ECO:0000313|Proteomes:UP000196177};
RN   [1] {ECO:0000313|Proteomes:UP000196177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An230 {ECO:0000313|Proteomes:UP000196177};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) 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:OUO90151.1}.
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DR   EMBL; NFJP01000012; OUO90151.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4GD20; -.
DR   OrthoDB; 9813348at2; -.
DR   Proteomes; UP000196177; Unassembled WGS sequence.
DR   GO; GO:0033765; F:steroid dehydrogenase activity, acting on the CH-CH group of donors; IEA:UniProt.
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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..642
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding domain-
FT                   containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038916726"
FT   DOMAIN          80..545
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   REGION          594..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   642 AA;  68050 MW;  2D1882D4CA6415E2 CRC64;
     MGSFEMNRRA FLGLGATAAV AAGMGLAGCS PRAASEEAAS GAAVEAVELP VGAPKGTPTT
     AAWCAVPEAI ADISEEKSFD VVVVGAGIAG LSAAATAAEL GASVAVIETL STYQTRGQDI
     GTVNSSFQKA NGLEASEEDI NQMCLALQRY AGNRTDQRIY RVWGQRSGAD FDWWYNTMLE
     PKGYGIEIPR WPMEVEYDPV DGEWFPQFCN QQEFTAPEGE EAGMNGGFPG AIGELEAYAK
     DHGAEFFYEH RGRQLVRGGQ PNGTEGRVTG VIAETSDGSH IQFNATKGVI LATGDYGHNV
     DMMQAWCPSQ LELSQENNVY PSTGNVGDGH LMGLWVGGMM QAIPHAYMAH GTPGMLGSDP
     FLIVDMNGRR FTNEDIPGQS FSDLAEEQPG VVFWQIADAK YPEQMKWSSP THGAQMSFTG
     DIDAWNAAME TGDKDAIESM LTEQGVNLQH AWTVEELAEG IHVDAATLQE TLDRYNGFCH
     DGYDADFGKQ AKRLWPVENP PYFYSTSGQW AFMLTMGGLK GTEKAEAIDQ WGNPIPGLWM
     AGNVQGMRFA IDYPTIVCGL SHSLCLTFGR VAAEQAVAAD PDVTEHESVY REWKEANPDA
     DAAGGAAGAG GAPAGGGAPA GGEAAGGTPA DGEAPVAGGS TE
//
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