ID A0A095AMT7_9SPHN Unreviewed; 486 AA.
AC A0A095AMT7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Flavoprotein subunit p-cresol methylhydroxylase {ECO:0000313|EMBL:KGB52070.1};
GN Name=pchFb {ECO:0000313|EMBL:KGB52070.1};
GN ORFNames=FG95_03680 {ECO:0000313|EMBL:KGB52070.1};
OS Sphingopyxis sp. LC363.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1120705 {ECO:0000313|EMBL:KGB52070.1, ECO:0000313|Proteomes:UP000029625};
RN [1] {ECO:0000313|EMBL:KGB52070.1, ECO:0000313|Proteomes:UP000029625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC363 {ECO:0000313|EMBL:KGB52070.1,
RC ECO:0000313|Proteomes:UP000029625};
RA Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT isolate.";
RL Submitted (MAY-2014) 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:KGB52070.1}.
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DR EMBL; JNFC01000067; KGB52070.1; -; Genomic_DNA.
DR RefSeq; WP_037557721.1; NZ_JNFC01000067.1.
DR AlphaFoldDB; A0A095AMT7; -.
DR STRING; 1120705.FG95_03680; -.
DR PATRIC; fig|1120705.3.peg.3679; -.
DR eggNOG; COG0277; Bacteria.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000029625; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.10; FAD-linked oxidases, C-terminal domain; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR016170; Cytok_DH_C_sf.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR PANTHER; PTHR11748:SF114; ARYL-ALCOHOL OXIDASE VANILLYL-ALCOHOL OXIDASE (AFU_ORTHOLOGUE AFUA_3G09500)-RELATED; 1.
DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Reference proteome {ECO:0000313|Proteomes:UP000029625}.
FT DOMAIN 35..218
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 486 AA; 51573 MW; 3F3F6D2943115505 CRC64;
MDANRQAAAL DALEALVGAD GVTRDPAALA PFHSGVALPL GIIAPRDTEQ LAKVLAVASE
AGAALQPVCR AVAGQEVAAR DKIILLDLGR MNEILEINEN LAYCLVEPGV TFRQLSEQIG
ERGLKLWVDC PGEPDESVAS AFLKRRVGYT PYADHYLMQC GLELMLADGR SVRTGMGAMP
KSTCWQLFKF GYGPWIDGLF TQSDLGVVTK LGLWLMPQPP AAQSFAVTVP DEDDLGKLLD
VLGPLKTNMV VPNGVAVANA LHEAARSGKV RRDFGGTGPM SAGEVRKAGE SIGLGYWTLY
GSLYGLPDNV RIAWSMVQDA FASIKGSRVL AAPAAGMEGL WAWRKGMMLG SVGNALGRPS
AWAGGSSLDI GPISPVDGKE GLRLYDLSRD ISGRHGFDFV GETNAVWRSA QHRQYLCFDG
SPAGSKRARD CAIELIDAQA GAGFGQTHVE PALAASARAT YESGAITQLH ARVKRALDPA
NLFLSA
//
