ID A0A150KKZ7_9BACI Unreviewed; 513 AA.
AC A0A150KKZ7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=4-hydroxyphenylacetate 3-monooxygenase {ECO:0000313|EMBL:KYC92507.1};
DE EC=1.14.14.9 {ECO:0000313|EMBL:KYC92507.1};
GN ORFNames=B4102_3726 {ECO:0000313|EMBL:KYC92507.1};
OS Heyndrickxia sporothermodurans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX NCBI_TaxID=46224 {ECO:0000313|EMBL:KYC92507.1, ECO:0000313|Proteomes:UP000075666};
RN [1] {ECO:0000313|EMBL:KYC92507.1, ECO:0000313|Proteomes:UP000075666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4102 {ECO:0000313|EMBL:KYC92507.1,
RC ECO:0000313|Proteomes:UP000075666};
RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA Eijlander R.T., Kuipers O.P.;
RT "Genome Sequences of Twelve Sporeforming Bacillus Species Isolated from
RT Foods.";
RL Submitted (JAN-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:KYC92507.1}.
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DR EMBL; LQYN01000110; KYC92507.1; -; Genomic_DNA.
DR RefSeq; WP_066235263.1; NZ_LQYN01000110.1.
DR AlphaFoldDB; A0A150KKZ7; -.
DR STRING; 46224.B4102_3726; -.
DR PATRIC; fig|46224.3.peg.563; -.
DR OrthoDB; 9785230at2; -.
DR Proteomes; UP000075666; Unassembled WGS sequence.
DR GO; GO:0052881; F:4-hydroxyphenylacetate 3-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; 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:KYC92507.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KYC92507.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000075666}.
FT DOMAIN 5..294
FT /note="HpaB/PvcC/4-BUDH N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11794"
FT DOMAIN 301..501
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 169..171
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000331-1"
FT BINDING 175..178
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
FT BINDING 212
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
FT BINDING 225..226
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000331-1"
FT BINDING 475..478
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000331-2"
SQ SEQUENCE 513 AA; 58134 MW; A3EFF65BD26248CF CRC64;
MPAKTGKEYI ERLKQANNNI YIHGERVNDV TEHAAFKNVI QSMAKLYDLQ YEKEDKLLYK
SPTTGDKVGM TFLQPKTIDD LIARRMAMTE WAKVSGGMMG RSPDYLNAEV MAMGVAYDFF
SEGDPTLALI GGIIGTRGYD FFSEGDPTLA ENAKNYYEYA RENDISLTHT LIHPQVNRAK
AQHEQKDANV ALHLVEKNKD GIIVDGIRLL ATQGGITDEI LVFPSTVKKA GELDDPYSLA
FAIPNNTPGL KFISRESFDY GKNQWDHPLS SRFEEGDAIV SFENVFVPWN RVFVCGNSSI
CNRTFRETNA VVHMAHQVVA KNIVKTEFLL GLALSVMDAI GIDQFQHVQD KGTEIMLALE
TMRSHLYRAE HNAKLDKWGT MTPDYAALDA ARNWYPRVYP RLVEILRILG ASGLMGIPTQ
ADFQNEDIGA LIDRGLQGKN LEGYERVQLF RLAWDMTMSA FGSRQMHYEY YFFGDPIRMG
MTYFEGYEKE PYKEIIRDFL GQVKSDKSSF LNV
//
