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Database: UniProt
Entry: A0A1S2QSY0_9BACI
LinkDB: A0A1S2QSY0_9BACI
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ID   A0A1S2QSY0_9BACI        Unreviewed;       479 AA.
AC   A0A1S2QSY0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=4-hydroxyphenylacetate 3-monooxygenase, oxygenase component {ECO:0000313|EMBL:OIK09259.1};
GN   ORFNames=BIV59_17530 {ECO:0000313|EMBL:OIK09259.1};
OS   Bacillus sp. MUM 13.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1678001 {ECO:0000313|EMBL:OIK09259.1, ECO:0000313|Proteomes:UP000180199};
RN   [1] {ECO:0000313|EMBL:OIK09259.1, ECO:0000313|Proteomes:UP000180199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUM 13 {ECO:0000313|EMBL:OIK09259.1,
RC   ECO:0000313|Proteomes:UP000180199};
RA   Lee L.-H., Ser H.-L.;
RT   "Genome sequence of Bacillus sp. MUM 13.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OIK09259.1}.
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DR   EMBL; MLYQ01000083; OIK09259.1; -; Genomic_DNA.
DR   RefSeq; WP_071352746.1; NZ_MLYQ01000083.1.
DR   AlphaFoldDB; A0A1S2QSY0; -.
DR   Proteomes; UP000180199; 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:OIK09259.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000180199}.
FT   DOMAIN          6..270
FT                   /note="HpaB/PvcC/4-BUDH N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11794"
FT   DOMAIN          279..476
FT                   /note="HpaB/PvcC/4-BUDH C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03241"
FT   BINDING         156..159
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
FT   BINDING         193
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
FT   BINDING         451..454
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
SQ   SEQUENCE   479 AA;  55250 MW;  F7BD6BE3EFE0ECA9 CRC64;
     MGIINGKDFI DRLNKLENEI WFDGEKIKVK ISEHPAFKGI LKAKAALYDL QNDPILKDEM
     TFFLPDIEEP IGLSYMQPKT KEDLKRRRKM MEQWARFTHG LMGRSPDYMN TAVMSFASSS
     VILNGKENCF PENIQSLYGR AMEHDLSFTH TFITPQVNRS EFYLEMAKNP ISAKVIERNE
     KGLIIKGARL LATQGGLTDE VLVISAPRLF DRDEAFAFSI PSNTKGIKFI CRESFVGGES
     SFNHPLSSRY EEMDSIVVFD NVLVPWDRVF FYNNVEAATD FMNRSSFYTF AYHQVVNRQI
     VKAEFMLGVA QLIVETINVG EYQHIQEKLS EIIIGLETMK ALLEKSENDA VLDEWGCMRP
     SMIPLQVASN VFPRIYPRFC EIIQLIGASG MVSLPTERDF DSEIRVELDQ YLQAYGMSAE
     ERVKLFRLAW DLTMSSFGTR QTQYERYFFG DPIRLSSSLY RNYLKDQHVD DISKFLNQM
//
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