HPAC_THET8
ID HPAC_THET8 Reviewed; 149 AA.
AC Q5SJP7;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=4-hydroxyphenylacetate 3-monooxygenase, reductase component {ECO:0000303|PubMed:17729270};
DE EC=1.5.1.36 {ECO:0000269|PubMed:17729270};
DE AltName: Full=4-HPA 3-monooxygenase small component;
DE AltName: Full=Flavin:NADH reductase;
GN OrderedLocusNames=TTHA0961;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH FAD AND NAD,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
RP SUBUNIT, AND SUBSTRATE SPECIFICITY.
RX PubMed=17729270; DOI=10.1002/prot.21534;
RA Kim S.-H., Hisano T., Iwasaki W., Ebihara A., Miki K.;
RT "Crystal structure of the flavin reductase component (hpaC) of 4-
RT hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8:
RT Structural basis for the flavin affinity.";
RL Proteins 70:718-730(2008).
CC -!- FUNCTION: Catalyzes the reduction of free flavins (FMN, FAD and
CC riboflavin) by NADH. Subsequently, the reduced flavins diffuse to the
CC large HpaB component. It utilizes NADH, but not NADPH as an electron
CC donor, and both FAD and FMN as electron acceptors.
CC {ECO:0000269|PubMed:17729270}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a reduced flavin + NAD(+) = an oxidized flavin + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:31303, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:60531, ChEBI:CHEBI:62787; EC=1.5.1.36;
CC Evidence={ECO:0000269|PubMed:17729270};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.9 uM for FAD (at 30 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:17729270};
CC KM=36.8 uM for FMN (at 30 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:17729270};
CC -!- PATHWAY: Aromatic compound metabolism; 4-hydroxyphenylacetate
CC degradation; pyruvate and succinate semialdehyde from 4-
CC hydroxyphenylacetate: step 1/7. {ECO:0000305|PubMed:17729270}.
CC -!- SUBUNIT: Homodimer. 4-HPA 3-monooxygenase consists of a reductase
CC component HpaC and an oxygenase component HpaB.
CC {ECO:0000269|PubMed:17729270}.
CC -!- SIMILARITY: Belongs to the non-flavoprotein flavin reductase family.
CC HpaC subfamily. {ECO:0000305}.
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DR EMBL; AP008226; BAD70784.1; -; Genomic_DNA.
DR RefSeq; WP_011228329.1; NC_006461.1.
DR RefSeq; YP_144227.1; NC_006461.1.
DR PDB; 2ECR; X-ray; 1.60 A; A/B=1-149.
DR PDB; 2ECU; X-ray; 1.30 A; A/B=1-149.
DR PDB; 2ED4; X-ray; 1.85 A; A/B=1-149.
DR PDBsum; 2ECR; -.
DR PDBsum; 2ECU; -.
DR PDBsum; 2ED4; -.
DR AlphaFoldDB; Q5SJP7; -.
DR SMR; Q5SJP7; -.
DR STRING; 300852.55772343; -.
DR EnsemblBacteria; BAD70784; BAD70784; BAD70784.
DR GeneID; 3170068; -.
DR KEGG; ttj:TTHA0961; -.
DR PATRIC; fig|300852.9.peg.943; -.
DR eggNOG; COG1853; Bacteria.
DR HOGENOM; CLU_059021_1_4_0; -.
DR OMA; WFDRGYH; -.
DR PhylomeDB; Q5SJP7; -.
DR SABIO-RK; Q5SJP7; -.
DR UniPathway; UPA00208; UER00416.
DR EvolutionaryTrace; Q5SJP7; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0036382; F:flavin reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.30.110.10; -; 1.
DR InterPro; IPR002563; Flavin_Rdtase-like_dom.
DR InterPro; IPR012349; Split_barrel_FMN-bd.
DR Pfam; PF01613; Flavin_Reduct; 1.
DR SMART; SM00903; Flavin_Reduct; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; FAD; Flavoprotein; FMN;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..149
FT /note="4-hydroxyphenylacetate 3-monooxygenase, reductase
FT component"
FT /id="PRO_0000387997"
FT BINDING 27..34
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17729270,
FT ECO:0007744|PDB:2ED4"
FT BINDING 37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:17729270,
FT ECO:0007744|PDB:2ED4"
FT BINDING 48..50
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17729270,
FT ECO:0007744|PDB:2ED4"
FT BINDING 54..55
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17729270,
FT ECO:0007744|PDB:2ED4"
FT BINDING 80
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17729270,
FT ECO:0007744|PDB:2ED4"
FT BINDING 116
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:17729270,
FT ECO:0007744|PDB:2ED4"
FT BINDING 137..140
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:17729270,
FT ECO:0007744|PDB:2ED4"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:2ECU"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:2ECU"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:2ECU"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:2ECU"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:2ECU"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:2ECU"
FT HELIX 55..62
FT /evidence="ECO:0007829|PDB:2ECU"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:2ECU"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:2ECU"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:2ECU"
FT STRAND 100..113
FT /evidence="ECO:0007829|PDB:2ECU"
FT STRAND 116..128
FT /evidence="ECO:0007829|PDB:2ECU"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:2ECU"
SQ SEQUENCE 149 AA; 16111 MW; CD963ADB68B1D66A CRC64;
MKEAFKEALA RFASGVTVVA ARLGEEERGM TATAFMSLSL EPPLVALAVS ERAKLLPVLE
GAGAFTVSLL REGQEAVSEH FAGRPKEGIA LEEGRVKGAL AVLRCRLHAL YPGGDHRIVV
GLVEEVELGE EGPPLVYFQR GYRRLVWPS
