HPAB_PSEAE
ID HPAB_PSEAE Reviewed; 520 AA.
AC Q9HWT7;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=4-hydroxyphenylacetate 3-monooxygenase oxygenase component {ECO:0000305|PubMed:20000468};
DE Short=HPA 3-monooxygenase oxygenase component {ECO:0000305|PubMed:20000468};
DE EC=1.14.14.9 {ECO:0000269|PubMed:20000468, ECO:0000269|PubMed:23666444};
DE AltName: Full=p-hydroxyphenylacetate 3-hydroxylase large component {ECO:0000305|PubMed:20000468};
DE Short=HPAH large component {ECO:0000305|PubMed:20000468};
GN Name=hpaB {ECO:0000303|PubMed:23666444};
GN Synonyms=hpaA {ECO:0000303|PubMed:20000468, ECO:0000312|EMBL:AAG07478.1};
GN OrderedLocusNames=PA4091 {ECO:0000312|EMBL:AAG07478.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND REACTION MECHANISM.
RX PubMed=20000468; DOI=10.1021/bi901454u;
RA Chakraborty S., Ortiz-Maldonado M., Entsch B., Ballou D.P.;
RT "Studies on the mechanism of p-hydroxyphenylacetate 3-hydroxylase from
RT Pseudomonas aeruginosa: a system composed of a small flavin reductase and a
RT large flavin-dependent oxygenase.";
RL Biochemistry 49:372-385(2010).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, SUBUNIT, AND
RP BIOTECHNOLOGY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=23666444; DOI=10.1007/s00253-013-4958-y;
RA Furuya T., Kino K.;
RT "Catalytic activity of the two-component flavin-dependent monooxygenase
RT from Pseudomonas aeruginosa toward cinnamic acid derivatives.";
RL Appl. Microbiol. Biotechnol. 98:1145-1154(2014).
CC -!- FUNCTION: Oxygenase component of the 4-hydroxyphenylacetate (HPA) 3-
CC hydroxylase. Catalyzes the hydroxylation of 4-hydroxyphenylacetate to
CC form 3,4-dihydroxyphenylacetate, using FADH(-) provided by the
CC reductase component HpaC to activate oxygen. To a lesser extent, can
CC also use reduced FMN (PubMed:20000468). In vitro, has hydroxylation
CC activity toward tyrosol and various cinnamic acid derivatives,
CC catalyzing the hydroxylation of p-coumaric acid, caffeic acid, ferulic
CC acid, and coniferaldehyde (PubMed:23666444).
CC {ECO:0000269|PubMed:20000468, ECO:0000269|PubMed:23666444}.
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 Evidence={ECO:0000269|PubMed:20000468, ECO:0000269|PubMed:23666444};
CC -!- PATHWAY: Aromatic compound metabolism; 4-hydroxyphenylacetate
CC degradation; pyruvate and succinate semialdehyde from 4-
CC hydroxyphenylacetate: step 1/7. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. HPA 3-hydroxylase consists of a reductase component
CC HpaC and an oxygenase component HpaB. Some form of interactions between
CC the reductase and the oxygenase facilitate the transfer of FADH(-) to
CC the oxygenase in P.aeruginosa, although interactions are not required
CC in other species. {ECO:0000269|PubMed:20000468,
CC ECO:0000305|PubMed:23666444}.
CC -!- BIOTECHNOLOGY: HpaBC can provide a biocatalytic synthetic approach to
CC the production of hydroxycinnamic acids that is an alternative to, or
CC complementary to, conventional methods such as chemical synthesis and
CC extraction from plant sources. {ECO:0000269|PubMed:23666444}.
CC -!- SIMILARITY: Belongs to the FADH(2)-utilizing monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG07478.1; -; Genomic_DNA.
DR PIR; H83134; H83134.
DR RefSeq; NP_252780.1; NC_002516.2.
DR RefSeq; WP_003104533.1; NZ_QZGE01000013.1.
DR AlphaFoldDB; Q9HWT7; -.
DR SMR; Q9HWT7; -.
DR STRING; 287.DR97_3776; -.
DR PaxDb; Q9HWT7; -.
DR PRIDE; Q9HWT7; -.
DR EnsemblBacteria; AAG07478; AAG07478; PA4091.
DR GeneID; 878727; -.
DR KEGG; pae:PA4091; -.
DR PATRIC; fig|208964.12.peg.4284; -.
DR PseudoCAP; PA4091; -.
DR HOGENOM; CLU_023920_2_1_6; -.
DR InParanoid; Q9HWT7; -.
DR OMA; GWDALNT; -.
DR PhylomeDB; Q9HWT7; -.
DR BioCyc; PAER208964:G1FZ6-4163-MON; -.
DR BRENDA; 1.14.14.9; 5087.
DR UniPathway; UPA00208; UER00416.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0052881; F:4-hydroxyphenylacetate 3-monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
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; IPR024677; HpaB/PvcC.
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; IPR012688; HpaB_gammaproteobact.
DR PANTHER; PTHR36117; PTHR36117; 1.
DR Pfam; PF03241; HpaB; 1.
DR Pfam; PF11794; HpaB_N; 1.
DR PIRSF; PIRSF500125; 4_HPA_large; 1.
DR PIRSF; PIRSF000331; HpaA_HpaB; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
DR TIGRFAMs; TIGR02310; HpaB-2; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; FAD; Flavoprotein; Monooxygenase;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..520
FT /note="4-hydroxyphenylacetate 3-monooxygenase oxygenase
FT component"
FT /id="PRO_0000437538"
FT BINDING 155..157
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|PIRSR:PIRSR000331-2"
FT BINDING 196
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|PIRSR:PIRSR000331-2"
SQ SEQUENCE 520 AA; 58464 MW; D2C52E302EC63A10 CRC64;
MKPEDFRASA TRPFTGEEYL ASLRDDREIY IYGDRVKDVT SHPAFRNAAA SMARLYDALH
DPQSKEKLCW ETDTGNGGYT HKFFRYARSA DELRQQRDAI AEWSRLTYGW MGRTPDYKAA
FGSALGANPG FYGRFEDNAK TWYKRIQEAC LYLNHAIVNP PIDRDKPVDQ VKDVFISVDE
EVDGGIVVSG AKVVATNSAL THYNFVGQGS AQLLGDNTDF ALMFIAPMNT PGMKLICRPS
YELVAGIAGS PFDYPLSSRF DENDAILVMD KVFIPWENVL IYRDFERCKQ WFPQGGFGRL
FPMQGCTRLA VKLDFITGAL YKALQCTGSL EFRGVQAQVG EVVAWRNLFW SLTDAMYGNA
SEWHGGAFLP SAEALQAYRV LAPQAYPEIK KTIEQVVASG LIYLPSGVRD LHNPQLDKYL
STYCRGSGGM GHRERIKILK LLWDAIGSEF GGRHELYEIN YAGSQDEIRM QALRQAIGSG
AMKGMLGMVE QCMGDYDENG WTVPHLHNPD DINVLDRIRQ
