HPAC_PSEAE
ID HPAC_PSEAE Reviewed; 170 AA.
AC Q9HWT6;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=4-hydroxyphenylacetate 3-monooxygenase reductase component {ECO:0000305|PubMed:20000468};
DE Short=HPA 3-monooxygenase reductase component {ECO:0000305|PubMed:20000468};
DE EC=1.5.1.37 {ECO:0000269|PubMed:20000468};
DE AltName: Full=FAD reductase (NADH) {ECO:0000305};
DE AltName: Full=p-hydroxyphenylacetate 3-hydroxylase small component {ECO:0000305|PubMed:20000468};
DE Short=HPAH small component {ECO:0000305|PubMed:20000468};
GN Name=hpaC {ECO:0000303|PubMed:20000468, ECO:0000303|PubMed:23666444,
GN ECO:0000312|EMBL:AAG07479.1};
GN OrderedLocusNames=PA4092 {ECO:0000312|EMBL:AAG07479.1};
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, SUBSTRATE SPECIFICITY, AND ACTIVITY
RP REGULATION.
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 SUBUNIT, AND 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: Reductase component of the 4-hydroxyphenylacetate (HPA) 3-
CC hydroxylase. Catalyzes the reduction of FAD by NADH. The reduced flavin
CC is then transferred to the oxygenase component HpaB. Is also able to
CC reduce FMN and riboflavin, but preferentially binds FAD. Has no
CC activity with NADPH as the reductant. {ECO:0000269|PubMed:20000468}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=FADH2 + NAD(+) = FAD + 2 H(+) + NADH; Xref=Rhea:RHEA:30147,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58307; EC=1.5.1.37;
CC Evidence={ECO:0000269|PubMed:20000468};
CC -!- ACTIVITY REGULATION: The rate of FAD reduction is independent of the
CC presence of HPA, demonstrating that, in contrast to HPAH from
CC A.baumannii, the activity of the HPAH reductase is not allosterically
CC regulated by the substrate. {ECO:0000269|PubMed:20000468}.
CC -!- PATHWAY: Aromatic compound metabolism; 4-hydroxyphenylacetate
CC degradation; pyruvate and succinate semialdehyde from 4-
CC hydroxyphenylacetate: step 1/7. {ECO:0000305}.
CC -!- SUBUNIT: Monomer. 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 non-flavoprotein flavin reductase family.
CC HpaC subfamily. {ECO:0000305}.
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DR EMBL; AE004091; AAG07479.1; -; Genomic_DNA.
DR PIR; A83135; A83135.
DR RefSeq; NP_252781.1; NC_002516.2.
DR RefSeq; WP_003104531.1; NZ_QZGE01000013.1.
DR AlphaFoldDB; Q9HWT6; -.
DR SMR; Q9HWT6; -.
DR STRING; 287.DR97_3775; -.
DR PaxDb; Q9HWT6; -.
DR DNASU; 878735; -.
DR EnsemblBacteria; AAG07479; AAG07479; PA4092.
DR GeneID; 878735; -.
DR KEGG; pae:PA4092; -.
DR PATRIC; fig|208964.12.peg.4285; -.
DR PseudoCAP; PA4092; -.
DR HOGENOM; CLU_059021_2_2_6; -.
DR InParanoid; Q9HWT6; -.
DR OMA; CINVLPA; -.
DR PhylomeDB; Q9HWT6; -.
DR BioCyc; PAER208964:G1FZ6-4164-MON; -.
DR BRENDA; 1.14.14.9; 5087.
DR UniPathway; UPA00208; UER00416.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0036382; F:flavin reductase (NADH) activity; IDA:UniProtKB.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR GO; GO:0042602; F:riboflavin reductase (NADPH) activity; IBA:GO_Central.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042537; P:benzene-containing compound metabolic process; IEA:InterPro.
DR GO; GO:0006208; P:pyrimidine nucleobase catabolic process; IBA:GO_Central.
DR Gene3D; 2.30.110.10; -; 1.
DR InterPro; IPR002563; Flavin_Rdtase-like_dom.
DR InterPro; IPR011982; HPA_mOase_red.
DR InterPro; IPR012349; Split_barrel_FMN-bd.
DR Pfam; PF01613; Flavin_Reduct; 1.
DR SMART; SM00903; Flavin_Reduct; 1.
DR TIGRFAMs; TIGR02296; HpaC; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; FAD; Flavoprotein; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..170
FT /note="4-hydroxyphenylacetate 3-monooxygenase reductase
FT component"
FT /id="PRO_0000437539"
SQ SEQUENCE 170 AA; 18616 MW; AB8FCCF4BBD61519 CRC64;
MSQLEPRQQA FRNAMAHLSA AVNVITSNGP AGRCGITATA VCSVTDSPPT LMLCINRNSE
MNTVFKANGR LCVNVLSGEH EEVARHFAGM TEVPMERRFA LHDWREGLAG LPVLHGALAN
LQGRIAEVQE IGTHSVLLLE LEDIQVLEQG DGLVYFSRSF HRLQCPRRAA
