ID   A0A1I0FP91_9BACI        Unreviewed;       486 AA.
AC   A0A1I0FP91;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=4-hydroxyphenylacetate 3-monooxygenase {ECO:0000313|EMBL:SET59981.1};
GN   ORFNames=SAMN05216389_11665 {ECO:0000313|EMBL:SET59981.1};
OS   Oceanobacillus limi.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=930131 {ECO:0000313|EMBL:SET59981.1, ECO:0000313|Proteomes:UP000198618};
RN   [1] {ECO:0000313|EMBL:SET59981.1, ECO:0000313|Proteomes:UP000198618}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBRC-M 10780 {ECO:0000313|EMBL:SET59981.1,
RC   ECO:0000313|Proteomes:UP000198618};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOHE01000016; SET59981.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0FP91; -.
DR   STRING; 930131.SAMN05216389_11665; -.
DR   OrthoDB; 9785230at2; -.
DR   Proteomes; UP000198618; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   GO; GO:0010124; P:phenylacetate catabolic process; IEA:InterPro.
DR   Gene3D; 1.10.3140.10; 4-hydroxybutyryl-coa dehydratase, domain 1; 1.
DR   Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   InterPro; IPR004925; HpaB/PvcC/4-BUDH.
DR   InterPro; IPR024719; HpaB/PvcC/4-BUDH_C.
DR   InterPro; IPR024674; HpaB/PvcC/4-BUDH_N.
DR   InterPro; IPR012687; HpaB_Deino-type.
DR   NCBIfam; TIGR02309; HpaB-1; 1.
DR   PANTHER; PTHR36117; 4-HYDROXYPHENYLACETATE 3-MONOOXYGENASE-RELATED; 1.
DR   PANTHER; PTHR36117:SF3; 4-HYDROXYPHENYLACETATE 3-MONOOXYGENASE-RELATED; 1.
DR   Pfam; PF03241; HpaB; 1.
DR   Pfam; PF11794; HpaB_N; 1.
DR   PIRSF; PIRSF000331; HpaA_HpaB; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|PIRSR:PIRSR000331-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Monooxygenase {ECO:0000313|EMBL:SET59981.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198618}.
FT   DOMAIN          5..272
FT                   /note="HpaB/PvcC/4-BUDH N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11794"
FT   DOMAIN          279..478
FT                   /note="HpaB/PvcC/4-BUDH C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03241"
FT   BINDING         101..105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000331-1"
FT   BINDING         147..149
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000331-1"
FT   BINDING         153..156
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
FT   BINDING         190
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
FT   BINDING         203..204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000331-1"
SQ   SEQUENCE   486 AA;  55308 MW;  EDD22E5A296A8FD0 CRC64;
     MPAKTGKEYI SRLKEAKNNV YIHGERVEDV TEHPAFKNVI KSMANLYDLQ HEKQDKMLYT
     SPTTGEKVGM TFLQPKTVED LIARREAITE WARTSGGMMG RSPDYLNAEV MAMGVNNRLF
     AEADPRFAEN ARNYYEYARE NDISLTHTLI HPQVNRAKMQ HQQKDANVAL HLVEERDDGI
     IVDGIRLLAT QGGITDEILV FPSTVKKAGE LDDPYSLAFA IPNNTPGLKY ISRESFDYGK
     NDWDHPLSAR FEEGDAIVSF ENVFVPWERV FVCGNSSVCN RTFRETNAVV HMAHQVVSKN
     IVKTEFVLGV ALSIMDAIGI DQFQHVKDKG TEIMLTLEAM RSHLYRAEHN AKLDSSGTMT
     PDYAALDAAR NWYPRIYPRL SEIVRIIGAS GLMGIPTEAD FNHDEIGPLI HRGLQGKNLE
     GYERVQLFRL AWDMTMSAFG SRQTHYEYYF FGDPVKMGMT YFDNYDKDTY KDYVDNFLKK
     SSSVQV
//