YOAI_BACSU
ID YOAI_BACSU Reviewed; 483 AA.
AC C0SPC0; O34710; Q796F7;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Probable 4-hydroxyphenylacetate 3-monooxygenase;
DE EC=1.14.14.9;
DE AltName: Full=4-hydroxyphenylacetate 3-hydroxylase;
DE Short=4-HPA 3-hydroxylase;
GN Name=yoaI; OrderedLocusNames=BSU18620;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lapidus A., Galleron N., Sorokin A., Ehrlich D.;
RT "Sequence analysis of the Bacillus subtilis chromosome region between the
RT terC and odhAB loci cloned in a yeast artificial chromosome.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO N-TERMINUS.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
CC -!- FUNCTION: Catalyzes the hydroxylation of 4-hydroxyphenylacetic acid
CC (4HPA), leading to the production of 3,4-dihydroxyphenylacetic acid
CC (DHPA). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxyphenylacetate + FADH2 + O2 = 3,4-
CC dihydroxyphenylacetate + FAD + H(+) + H2O; Xref=Rhea:RHEA:30595,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17612, ChEBI:CHEBI:48999, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307; EC=1.14.14.9;
CC -!- PATHWAY: Aromatic compound metabolism; 4-hydroxyphenylacetate
CC degradation; pyruvate and succinate semialdehyde from 4-
CC hydroxyphenylacetate: step 1/7.
CC -!- SIMILARITY: Belongs to the FADH(2)-utilizing monooxygenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB84421.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF027868; AAB84421.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB13754.2; -; Genomic_DNA.
DR PIR; C69896; C69896.
DR RefSeq; NP_389743.2; NC_000964.3.
DR RefSeq; WP_003231423.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; C0SPC0; -.
DR SMR; C0SPC0; -.
DR STRING; 224308.BSU18620; -.
DR PRIDE; C0SPC0; -.
DR EnsemblBacteria; CAB13754; CAB13754; BSU_18620.
DR GeneID; 940107; -.
DR KEGG; bsu:BSU18620; -.
DR PATRIC; fig|224308.179.peg.2030; -.
DR eggNOG; COG2368; Bacteria.
DR InParanoid; C0SPC0; -.
DR OMA; GWDALNT; -.
DR PhylomeDB; C0SPC0; -.
DR BioCyc; BSUB:BSU18620-MON; -.
DR UniPathway; UPA00208; UER00416.
DR Proteomes; UP000001570; Chromosome.
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; 2.40.110.10; -; 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.
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 PANTHER; PTHR36117; PTHR36117; 1.
DR Pfam; PF03241; HpaB; 1.
DR Pfam; PF11794; HpaB_N; 1.
DR PIRSF; PIRSF000331; HpaA_HpaB; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
DR TIGRFAMs; TIGR02309; HpaB-1; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; FAD; Flavoprotein; Monooxygenase;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..483
FT /note="Probable 4-hydroxyphenylacetate 3-monooxygenase"
FT /id="PRO_0000387996"
FT BINDING 104..108
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 150..152
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 156..159
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 206..207
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 452..455
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 483 AA; 55850 MW; 86B510ADA4029008 CRC64;
MGIINGKEFI DRLNKLENEI WYDGEKIKGN ISEHPAFKGI IKTKSSLYEL QTKDELIHEM
TYCLPGDHNR IGLSYLQPKT KNDLKKRRTM IEHWARHTHG MMGRSPDYMN TVMMSFASSA
ELLKDKENCF PEHILDMYEQ AAKHDLSFTH TFITPQVNRS QSYFGLSEKP ISAKVIDRTE
KGLMIHGARL LATQGGLTDE ILVFSAPKFF FETDEAYAFS IPSNTKGVKF ITRESFVLSD
SSFNHPLSSR YEEMDSIVVF DHVLVPWNRV FFYDNVEAAK DFMTKSSFHA FTFHQVVIRQ
MIKIEFLLGV AQLLVDTINV SEYQHIQEKL SEIIVGLETI KALIDKSEND AQLDEFGYMR
PCLIPLQVIS TIIPKLYPRF TEIIQLIGAS GMVTLPTENA FDSEIREDLD QYLQATNTNA
EERVKIFRLA WDLTMSSFGT RQTHYERYFF GDPIRISSRL YTSYPKQEQL NMIKTFLHAD
TEH
