ID A0A1S2R8V9_9BACI Unreviewed; 489 AA.
AC A0A1S2R8V9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=4-hydroxyphenylacetate 3-monooxygenase, oxygenase component {ECO:0000313|EMBL:OIK14900.1};
GN ORFNames=BIV59_01595 {ECO:0000313|EMBL:OIK14900.1};
OS Bacillus sp. MUM 13.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1678001 {ECO:0000313|EMBL:OIK14900.1, ECO:0000313|Proteomes:UP000180199};
RN [1] {ECO:0000313|EMBL:OIK14900.1, ECO:0000313|Proteomes:UP000180199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUM 13 {ECO:0000313|EMBL:OIK14900.1,
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:OIK14900.1}.
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DR EMBL; MLYQ01000003; OIK14900.1; -; Genomic_DNA.
DR RefSeq; WP_071349683.1; NZ_MLYQ01000003.1.
DR AlphaFoldDB; A0A1S2R8V9; -.
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:OIK14900.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000180199}.
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"
FT BINDING 453..456
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
SQ SEQUENCE 489 AA; 55348 MW; DA88194863880A7D CRC64;
MPAKTGKEYL DRLKKANNNI YLHGKRVDDV TGYPGLKGVV KSMAKLYDLQ YEKPEIMLFN
SPTSGEKIGI TFMQPKTIDE IIQRRQAIQE WAITSCGLMG RSPDYLNAEV MAMGASSSFF
AEGDPMFAEN AKLYYEYARE NDISLTHTLI HPQVNRSKAQ HEQEDANVAL CLTEKRSDGI
IVNGIRLLAT QGGITDEILV FPSTVKKAGE KDDAYSLAFA IPNNTAGLKF ISRESFDCGK
NEWDHPLSSR FEEGDAIVSF ENVFVPWDRV FVCGNSSICN RTFRETNAVV HMSHQVVSKN
IIKTEFLLGV ALSIMDAIGI DQFQHVKEKG TEIMLTLEAM KSHLYRAEHN AKLDKWGTMT
PEYAALDAAR NWYPKMYPRL AEIIRILGAS GLMGIPTKED FDSEEIGPLI QRGLQGKSLD
GYEKVQLFRL AWDLTLSSFG SRQTHYEYYF FGDPIRMGMT YFDNYEKDYV KQRVQDFLKS
ATKHDISAI
//
