ID A0A0F4YRA4_TALEM Unreviewed; 534 AA.
AC A0A0F4YRA4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Salicylate hydroxylase {ECO:0000313|EMBL:KKA20386.1};
GN ORFNames=T310_5594 {ECO:0000313|EMBL:KKA20386.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA20386.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA20386.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA20386.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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:KKA20386.1}.
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DR EMBL; LASV01000264; KKA20386.1; -; Genomic_DNA.
DR RefSeq; XP_013326998.1; XM_013471544.1.
DR AlphaFoldDB; A0A0F4YRA4; -.
DR STRING; 1408163.A0A0F4YRA4; -.
DR GeneID; 25317938; -.
DR OrthoDB; 1113861at2759; -.
DR Proteomes; UP000053958; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR13789:SF215; FAD-BINDING DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR13789; MONOOXYGENASE; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053958};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 36..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..333
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT COILED 425..458
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 534 AA; 59271 MW; 7ECC78996AF4AC45 CRC64;
MPLDVIIVGA GIGGLCAAIA LRRAGHSVRI FEKSRFASEI GAAVAISPNG ALVLAALGFS
FDRARACVLP SWESVDGISL SPLTALDLSN AEAKYGAPMM AIHRVDLHSE LRRLALEGDD
NPAELVLATA AEGIDDEGRL LLSDGSTHRA DLIIGADGVH SVVRRAVVGE EADLAAETDM
SAFRFLIPTS RLQGDPALEK LLQWKSPGAT IFADTLDKAH ERHLVWYPCQ GGDVQNVVGI
HPTRPNAAET DFKASLLDEF RYFNPDVVKL LELAEDVKCW KLARYEPFPR WTRKDIVLVG
DAAHPMLPFG AQAANQAIED GAALGQLLRG VDDAAEIPHR LQLFEDIRRR RTAIIQILSS
ARIGREGTVT DKLREFVADG ESVPTTFAER TEHAYRFALL FLSPYGCNSG VRLIDPFEKS
SFDVLKECEK ALQQEEKKET ATEELNEKEK ENLAVLSNNN AKGEDLQDPN NYNYDKGCAR
LLLAYSVRLF KPFKPFLRMI YITLIIRVYY TKEEERNKGR NIRSIPRYYS HSWL
//
