HPAB_ECOLX
ID HPAB_ECOLX Reviewed; 520 AA.
AC Q57160;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 97.
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 Name=hpaB;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-20.
RC STRAIN=W / ATCC 11105 / DSM 1900 / 113-3;
RX PubMed=8077235; DOI=10.1016/s0021-9258(17)31719-2;
RA Prieto M.A., Garcia J.L.;
RT "Molecular characterization of 4-hydroxyphenylacetate 3-hydroxylase of
RT Escherichia coli. A two-protein component enzyme.";
RL J. Biol. Chem. 269:22823-22829(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=W / ATCC 11105 / DSM 1900 / 113-3;
RX PubMed=8550403; DOI=10.1128/jb.178.1.111-120.1996;
RA Prieto M.A., Diaz E., Garcia J.L.;
RT "Molecular characterization of the 4-hydroxyphenylacetate catabolic pathway
RT of Escherichia coli W: engineering a mobile aromatic degradative cluster.";
RL J. Bacteriol. 178:111-120(1996).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10653707; DOI=10.1128/aem.66.2.481-486.2000;
RA Xun L., Sandvik E.R.;
RT "Characterization of 4-hydroxyphenylacetate 3-hydroxylase (HpaB) of
RT Escherichia coli as a reduced flavin adenine dinucleotide-utilizing
RT monooxygenase.";
RL Appl. Environ. Microbiol. 66:481-486(2000).
CC -!- FUNCTION: Utilizes FADH(2) supplied by HpaC or by another flavin
CC reductase, to catalyze the hydroxylation of 4-hydroxyphenylacetic acid,
CC leading to the production of 3,4-DHPA. Can also oxidize phenol to
CC catechol, and hydroxylate other phenol derivatives.
CC {ECO:0000269|PubMed:10653707}.
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:10653707};
CC -!- PATHWAY: Aromatic compound metabolism; 4-hydroxyphenylacetate
CC degradation; pyruvate and succinate semialdehyde from 4-
CC hydroxyphenylacetate: step 1/7.
CC -!- SUBUNIT: 4-HPA 3-monooxygenase consists of a reductase component HpaC
CC and an oxygenase component HpaB.
CC -!- INDUCTION: By 4-hydroxyphenylacetic acid.
CC -!- MISCELLANEOUS: E.coli K12 lacks the oxygenase component HpaB.
CC -!- SIMILARITY: Belongs to the FADH(2)-utilizing monooxygenase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z37980; CAA86048.1; -; Genomic_DNA.
DR EMBL; Z29081; CAA82321.1; -; Genomic_DNA.
DR PIR; B55349; B55349.
DR PDB; 6QYH; X-ray; 1.94 A; A/B=1-520.
DR PDB; 6QYI; X-ray; 1.80 A; A/B=1-520.
DR PDBsum; 6QYH; -.
DR PDBsum; 6QYI; -.
DR AlphaFoldDB; Q57160; -.
DR SMR; Q57160; -.
DR STRING; 585034.ECIAI1_4567; -.
DR eggNOG; COG2368; Bacteria.
DR BioCyc; MetaCyc:MON-2841; -.
DR BRENDA; 1.14.14.9; 2026.
DR UniPathway; UPA00208; UER00416.
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; 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 3D-structure; Aromatic hydrocarbons catabolism; Direct protein sequencing;
KW FAD; Flavoprotein; Monooxygenase; Oxidoreductase.
FT CHAIN 1..520
FT /note="4-hydroxyphenylacetate 3-monooxygenase oxygenase
FT component"
FT /id="PRO_0000084032"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:6QYI"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:6QYI"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:6QYI"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:6QYI"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 46..58
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:6QYI"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:6QYI"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:6QYI"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 90..105
FT /evidence="ECO:0007829|PDB:6QYI"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 116..127
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 129..135
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 136..149
FT /evidence="ECO:0007829|PDB:6QYI"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:6QYI"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:6QYI"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:6QYI"
FT STRAND 183..196
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:6QYI"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:6QYI"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:6QYI"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 241..248
FT /evidence="ECO:0007829|PDB:6QYI"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:6QYI"
FT STRAND 264..275
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:6QYI"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 285..294
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 301..327
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 333..358
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 372..397
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 398..401
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 408..411
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 414..423
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 432..446
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 449..460
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 465..479
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 481..494
FT /evidence="ECO:0007829|PDB:6QYI"
FT STRAND 500..503
FT /evidence="ECO:0007829|PDB:6QYI"
FT TURN 510..512
FT /evidence="ECO:0007829|PDB:6QYI"
FT HELIX 515..518
FT /evidence="ECO:0007829|PDB:6QYI"
SQ SEQUENCE 520 AA; 58848 MW; 1E93BBCC29BBB55C CRC64;
MKPEDFRAST QRPFTGEEYL KSLQDGREIY IYGERVKDVT THPAFRNAAA SVAQLYDALH
KPEMQDSLCW NTDTGSGGYT HKFFRVAKSA DDLRHERDAI AEWSRLSYGW MGRTPDYKAA
FGCALGGTPG FYGQFEQNAR NWYTRIQETG LYFNHAIVNP PIDRHLPTDK VKDVYIKLEK
ETDAGIIVSG AKVVATNSAL THYNMIGFGS AQVMGENPDF ALMFVAPMDA DGVKLISRAS
YEMVAGATGS PYDYPLSSRF DENDAILVMD NVLIPWENVL LYRDFDRCRR WTMEGGFARM
YPLQACVRLA VKLDFITALL KKSLECTGTL EFRGVQADLG EVVAWRNTFW ALSDSMCSEA
TPWVNGAYLP DHAALQTYRV LAPMAYAKIK NIIERNVTSG LIYLPSSARD LNNPQIDQYL
AKYVRGSNGM DHVQRIKILK LMWDAIGSEF GGRHELYEIN YSGSQDEIRL QCLRQAQSSG
NMDKMMAMVD RCLSEYDQNG WTVPHLHNND DINMLDKLLK
