HPAB_THET8
ID HPAB_THET8 Reviewed; 481 AA.
AC Q5SJP8;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=4-hydroxyphenylacetate 3-monooxygenase oxygenase component;
DE EC=1.14.14.9;
DE AltName: Full=4-HPA 3-hydroxylase;
DE AltName: Full=4-HPA 3-monooxygenase large component;
GN OrderedLocusNames=TTHA0960;
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 (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND FAD,
RP FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, AND SUBUNIT.
RX PubMed=17804419; DOI=10.1074/jbc.m703440200;
RA Kim S.-H., Hisano T., Takeda K., Iwasaki W., Ebihara A., Miki K.;
RT "Crystal structure of the oxygenase component (hpaB) of the 4-
RT hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8.";
RL J. Biol. Chem. 282:33107-33117(2007).
CC -!- FUNCTION: Utilizes FADH(2) supplied by HpaC, to catalyze the
CC hydroxylation of 4-hydroxyphenylacetic acid, leading to the production
CC of 3,4-dihydroxyphenylacetic acid (DHPA).
CC {ECO:0000269|PubMed:17804419}.
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:17804419};
CC -!- PATHWAY: Aromatic compound metabolism; 4-hydroxyphenylacetate
CC degradation; pyruvate and succinate semialdehyde from 4-
CC hydroxyphenylacetate: step 1/7.
CC -!- SUBUNIT: Homotetramer consisting of a dimer of dimers. 4-HPA 3-
CC monooxygenase consists of a reductase component HpaC and an oxygenase
CC component HpaB. {ECO:0000269|PubMed:17804419}.
CC -!- SIMILARITY: Belongs to the FADH(2)-utilizing monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; AP008226; BAD70783.1; -; Genomic_DNA.
DR RefSeq; WP_011228328.1; NC_006461.1.
DR RefSeq; YP_144226.1; NC_006461.1.
DR PDB; 2YYG; X-ray; 2.00 A; A=1-481.
DR PDB; 2YYI; X-ray; 1.66 A; A=1-481.
DR PDB; 2YYJ; X-ray; 1.66 A; A=1-481.
DR PDB; 2YYK; X-ray; 1.60 A; A=1-481.
DR PDB; 2YYL; X-ray; 1.75 A; A=1-481.
DR PDB; 2YYM; X-ray; 1.70 A; A=1-481.
DR PDBsum; 2YYG; -.
DR PDBsum; 2YYI; -.
DR PDBsum; 2YYJ; -.
DR PDBsum; 2YYK; -.
DR PDBsum; 2YYL; -.
DR PDBsum; 2YYM; -.
DR AlphaFoldDB; Q5SJP8; -.
DR SMR; Q5SJP8; -.
DR STRING; 300852.55772342; -.
DR EnsemblBacteria; BAD70783; BAD70783; BAD70783.
DR GeneID; 3170066; -.
DR KEGG; ttj:TTHA0960; -.
DR PATRIC; fig|300852.9.peg.942; -.
DR eggNOG; COG2368; Bacteria.
DR HOGENOM; CLU_023920_2_1_0; -.
DR OMA; NPQVNRA; -.
DR PhylomeDB; Q5SJP8; -.
DR BRENDA; 1.14.14.9; 2305.
DR UniPathway; UPA00208; UER00416.
DR EvolutionaryTrace; Q5SJP8; -.
DR Proteomes; UP000000532; 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 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; FAD; Flavoprotein;
KW Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..481
FT /note="4-hydroxyphenylacetate 3-monooxygenase oxygenase
FT component"
FT /id="PRO_0000387994"
FT BINDING 100..104
FT /ligand="substrate"
FT BINDING 142..144
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17804419"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17804419"
FT BINDING 148..151
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17804419"
FT BINDING 185
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17804419"
FT BINDING 197..198
FT /ligand="substrate"
FT BINDING 444..447
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17804419"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:2YYK"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:2YYK"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:2YYK"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:2YYK"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:2YYK"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:2YYK"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:2YYK"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:2YYK"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:2YYK"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:2YYK"
FT HELIX 77..93
FT /evidence="ECO:0007829|PDB:2YYK"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:2YYK"
FT HELIX 103..114
FT /evidence="ECO:0007829|PDB:2YYK"
FT HELIX 116..122
FT /evidence="ECO:0007829|PDB:2YYK"
FT HELIX 123..136
FT /evidence="ECO:0007829|PDB:2YYK"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:2YYK"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:2YYI"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:2YYI"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:2YYK"
FT STRAND 172..185
FT /evidence="ECO:0007829|PDB:2YYK"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:2YYK"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:2YYJ"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:2YYK"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:2YYK"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:2YYK"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:2YYK"
FT TURN 238..242
FT /evidence="ECO:0007829|PDB:2YYK"
FT STRAND 247..258
FT /evidence="ECO:0007829|PDB:2YYK"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:2YYK"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:2YYK"
FT HELIX 268..278
FT /evidence="ECO:0007829|PDB:2YYK"
FT HELIX 280..309
FT /evidence="ECO:0007829|PDB:2YYK"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:2YYK"
FT HELIX 316..341
FT /evidence="ECO:0007829|PDB:2YYK"
FT HELIX 355..380
FT /evidence="ECO:0007829|PDB:2YYK"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:2YYK"
FT HELIX 390..394
FT /evidence="ECO:0007829|PDB:2YYK"
FT HELIX 398..404
FT /evidence="ECO:0007829|PDB:2YYK"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:2YYJ"
FT HELIX 412..424
FT /evidence="ECO:0007829|PDB:2YYK"
FT TURN 425..427
FT /evidence="ECO:0007829|PDB:2YYK"
FT HELIX 429..440
FT /evidence="ECO:0007829|PDB:2YYK"
FT HELIX 445..455
FT /evidence="ECO:0007829|PDB:2YYK"
FT HELIX 459..468
FT /evidence="ECO:0007829|PDB:2YYK"
FT HELIX 470..473
FT /evidence="ECO:0007829|PDB:2YYK"
FT HELIX 474..476
FT /evidence="ECO:0007829|PDB:2YYK"
SQ SEQUENCE 481 AA; 54303 MW; 29ED75B3C034FBC0 CRC64;
MARTGAEYIE ALKTRPPNLW YKGEKVEDPT THPVFRGIVR TMAALYDLQH DPRYREVLTY
EEEGKRHGMS FLIPKTKEDL KRRGQAYKLW ADQNLGMMGR SPDYLNAVVM AYAASADYFG
EFAENVRNYY RYLRDQDLAT THALTNPQVN RARPPSGQPD PYIPVGVVKQ TEKGIVVRGA
RMTATFPLAD EVLIFPSTLL QAGSEKYALA FALPTSTPGL HFVCREALVG GDSPFDHPLS
SRVEEMDCLV IFDDVLVPWE RVFILGNVEL CNNAYAATGA LNHMAHQVVA LKTAKTEAFL
GVAALMAEGI GADVYGHVQE KIAEIIVYLE AMRAFWTRAE EEAKENAYGL LVPDRGALDG
ARNLYPRLYP RIREILEQIG ASGLITLPSE KDFKGPLGPF LEKFLQGAAL EAKERVALFR
LAWDMTLSGF GARQELYERF FFGDPVRMYQ TLYNVYNKEP YKERIRAFLK ESLKVFEEVQ
A
