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Database: UniProt
Entry: A0A2T3N1D6_9GAMM
LinkDB: A0A2T3N1D6_9GAMM
Original site: A0A2T3N1D6_9GAMM 
ID   A0A2T3N1D6_9GAMM        Unreviewed;       437 AA.
AC   A0A2T3N1D6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Oxidoreductase {ECO:0000313|EMBL:PSW06035.1};
GN   ORFNames=C9I89_05835 {ECO:0000313|EMBL:PSW06035.1};
OS   Photobacterium lipolyticum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=266810 {ECO:0000313|EMBL:PSW06035.1, ECO:0000313|Proteomes:UP000240904};
RN   [1] {ECO:0000313|EMBL:PSW06035.1, ECO:0000313|Proteomes:UP000240904}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16190 {ECO:0000313|EMBL:PSW06035.1,
RC   ECO:0000313|Proteomes:UP000240904};
RA   Butler K.;
RT   "Whole genome sequencing of Histamine producing bacteria.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:PSW06035.1}.
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DR   EMBL; PYMC01000003; PSW06035.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T3N1D6; -.
DR   OrthoDB; 9796486at2; -.
DR   Proteomes; UP000240904; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd06198; FNR_like_3; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR013112; FAD-bd_8.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR47354:SF8; 1,2-PHENYLACETYL-COA EPOXIDASE, SUBUNIT E; 1.
DR   PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR   Pfam; PF08022; FAD_binding_8; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240904};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        75..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        127..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        155..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          206..308
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   437 AA;  49149 MW;  C979D7381AD40B0B CRC64;
     MLKFTLILVL LWSPALLMGY DEMGNFFFWR HQLTMLSGII GLGYMSFAVL IAARLSWVES
     RLNGLDKGYA LHKKLGIGAT VALVLHWLCV QSAKWFVQAG LLARPTISRP AIEGINWHHV
     ASEIGEFTFY VFVLFSLISL VQAISYKKFK FTHKIGGLLV IAGVLHSVLL LDWNSQSIPM
     NIAIAGISLI GIWCSFISLT GKIGASYKSA GEVVRVEPLK VNTESNIAIR IGIKLDSAIR
     YKEGQFVYLN FHDGEAPHPF SILNYDAERK LIEFGIKGLG DYTNKMVNQL TAGQRVTVEG
     GYGYFQIPEQ ETQVWVGAGI GIVPFMSRLY WLERKAHKED LEFKKIHLFY CVNTRNEAFF
     EKEILSILQR LDFIELEILD AAKGEFLSAE QILSTTDSKE FDVSFCGPEE FGKILSTHLA
     AAGLGSDRFH KEIFKMR
//
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