ID A0A1R4HN70_9MICO Unreviewed; 634 AA.
AC A0A1R4HN70;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Salicylate hydroxylase {ECO:0000313|EMBL:SJN08980.1};
DE EC=1.14.13.1 {ECO:0000313|EMBL:SJN08980.1};
GN ORFNames=FM113_04945 {ECO:0000313|EMBL:SJN08980.1};
OS Leucobacter sp. 7(1).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1255613 {ECO:0000313|EMBL:SJN08980.1, ECO:0000313|Proteomes:UP000195513};
RN [1] {ECO:0000313|EMBL:SJN08980.1, ECO:0000313|Proteomes:UP000195513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7(1) {ECO:0000313|Proteomes:UP000195513};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007801}.
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DR EMBL; FUID01000022; SJN08980.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4HN70; -.
DR OrthoDB; 4246007at2; -.
DR Proteomes; UP000195513; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0018658; F:salicylate 1-monooxygenase activity; IEA:UniProtKB-EC.
DR CDD; cd02979; PHOX_C; 1.
DR Gene3D; 3.40.30.20; -; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
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 InterPro; IPR012941; Phe_hydrox_C_dim_dom.
DR InterPro; IPR038220; PHOX_C_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43004:SF6; FAD_NAD(P)-BINDING OXIDOREDUCTASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR43004; TRK SYSTEM POTASSIUM UPTAKE PROTEIN; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR Pfam; PF07976; Phe_hydrox_dim; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:SJN08980.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000195513}.
FT DOMAIN 32..413
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 444..599
FT /note="Phenol hydroxylase C-terminal dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07976"
SQ SEQUENCE 634 AA; 69936 MW; 8059757EA24F52B7 CRC64;
MQFHHHGYVS TDPRVQLAAG VGIDRPDDLP SEIDVLIVGS GPAGIVAAAQ LAQFPNVVTR
VVERRDSRLV LGQADGIQAR SVETFQAFGF AQQIIQEAYQ ITETSFWTPD PANPKNIVRS
SVTPDDPQGI SEFPHLIVNQ ARVIDYFAEY ARRAPARGDI DYGYEFVSLE VGEGEYPVAV
TLRKVSGQTG AGINAAAEAN AEQGETVVVH TKYVIGADGA RSKVRRAIGG SLSGDQAFHA
WGVMDVLSVT DFPDIRKKCI IHSEAGSILH IPREGNHLAR IYVDLGEVDE QDGGKVRDTP
LEDVIAQANA IMHPYTLDVR NVAWHSVYEV AHRLTDRFDD AETSPDGKQR VFLMGDACHT
HSAKAGQGMN VSMQDGWNLG WKLGYVIEGR SPESLLQTYS DERRVTAKNL IDFDKEWSTL
MAKKPEEFDS PGQLEEFYVQ TAEFPAGFMT EYTESMLTGS AEHQALAPGF PLGKRFKSVM
TTRVSDAVDV HLGHHHRADG RFRVYAFADA SGEQLNAWAE WLLSNTDSPL QRFTPLGGDL
DAIFDVKAVY QQEHHGVDIM QASKLFLPLT GPFQLVDYEK IYAAKPGEDI FEERGISRDG
AVVIVRPDHY VSAVLPLTDP EAVARFFEPI FLTP
//
