PRAI_PAESP
ID PRAI_PAESP Reviewed; 394 AA.
AC C4TP09;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=4-hydroxybenzoate 3-monooxygenase (NAD(P)H) {ECO:0000303|PubMed:19717587};
DE EC=1.14.13.33 {ECO:0000269|PubMed:19717587};
DE AltName: Full=4-hydroxybenzoate 3-hydroxylase {ECO:0000303|PubMed:19717587};
DE Short=4HB 3-hydroxylase {ECO:0000303|PubMed:19717587};
GN Name=praI;
OS Paenibacillus sp.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=58172;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBSTRATE SPECIFICITY.
RC STRAIN=JJ-1b;
RX PubMed=19717587; DOI=10.1128/jb.00840-09;
RA Kasai D., Fujinami T., Abe T., Mase K., Katayama Y., Fukuda M., Masai E.;
RT "Uncovering the protocatechuate 2,3-cleavage pathway genes.";
RL J. Bacteriol. 191:6758-6768(2009).
CC -!- FUNCTION: Involved in the degradation of 4-hydroxybenzoate (4HB) via
CC the protocatechuate (PCA) 2,3-cleavage pathway. Catalyzes the
CC conversion of 4HB into 2-hydroxypenta-2,4-dienoate (HPD). It is highly
CC specific for 4-hydroxybenzoate, and is able to utilize both NADH and
CC NADPH as electron donors at approximately equal rates.
CC {ECO:0000269|PubMed:19717587}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybenzoate + H(+) + NADH + O2 = 3,4-dihydroxybenzoate +
CC H2O + NAD(+); Xref=Rhea:RHEA:19473, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17879,
CC ChEBI:CHEBI:36241, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC EC=1.14.13.33; Evidence={ECO:0000269|PubMed:19717587};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-hydroxybenzoate + H(+) + NADPH + O2 = 3,4-dihydroxybenzoate
CC + H2O + NADP(+); Xref=Rhea:RHEA:19477, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17879,
CC ChEBI:CHEBI:36241, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.14.13.33; Evidence={ECO:0000269|PubMed:19717587};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000305|PubMed:19717587};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P20586};
CC -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family.
CC {ECO:0000305}.
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DR EMBL; AB505864; BAH79107.1; -; Genomic_DNA.
DR PDB; 7ON9; X-ray; 1.63 A; A/B/C/D=1-394.
DR PDBsum; 7ON9; -.
DR AlphaFoldDB; C4TP09; -.
DR SMR; C4TP09; -.
DR GO; GO:0018671; F:4-hydroxybenzoate 3-monooxygenase [NAD(P)H] activity; IDA:UniProtKB.
DR GO; GO:0106355; F:4-hydroxybenzoate 3-monooxygenase [NADH] activity; IEA:RHEA.
DR GO; GO:0106356; F:4-hydroxybenzoate 3-monooxygenase [NADPH] activity; IEA:RHEA.
DR GO; GO:0018659; F:4-hydroxybenzoate 3-monooxygenase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0043639; P:benzoate catabolic process; IEA:InterPro.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012733; HB_mOase.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR02360; pbenz_hydroxyl; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; FAD; Flavoprotein;
KW Monooxygenase; NAD; NADP; Oxidoreductase.
FT CHAIN 1..394
FT /note="4-hydroxybenzoate 3-monooxygenase (NAD(P)H)"
FT /id="PRO_0000435797"
FT BINDING 32
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P20586"
FT BINDING 42..47
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P20586"
FT BINDING 102
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P20586"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20586"
FT BINDING 214..216
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20586"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20586"
FT BINDING 288
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P20586"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20586"
FT BINDING 301..302
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P20586"
FT SITE 203
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P20586"
FT SITE 387
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P20586"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:7ON9"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:7ON9"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:7ON9"
FT HELIX 36..40
FT /evidence="ECO:0007829|PDB:7ON9"
FT HELIX 50..58
FT /evidence="ECO:0007829|PDB:7ON9"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:7ON9"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:7ON9"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:7ON9"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:7ON9"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:7ON9"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:7ON9"
FT HELIX 102..115
FT /evidence="ECO:0007829|PDB:7ON9"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:7ON9"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:7ON9"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:7ON9"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:7ON9"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:7ON9"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:7ON9"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:7ON9"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:7ON9"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:7ON9"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:7ON9"
FT STRAND 184..194
FT /evidence="ECO:0007829|PDB:7ON9"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:7ON9"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:7ON9"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:7ON9"
FT STRAND 220..228
FT /evidence="ECO:0007829|PDB:7ON9"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:7ON9"
FT HELIX 238..249
FT /evidence="ECO:0007829|PDB:7ON9"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:7ON9"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:7ON9"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:7ON9"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:7ON9"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:7ON9"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:7ON9"
FT HELIX 300..321
FT /evidence="ECO:0007829|PDB:7ON9"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:7ON9"
FT HELIX 330..352
FT /evidence="ECO:0007829|PDB:7ON9"
FT HELIX 360..373
FT /evidence="ECO:0007829|PDB:7ON9"
FT HELIX 377..388
FT /evidence="ECO:0007829|PDB:7ON9"
SQ SEQUENCE 394 AA; 44265 MW; 81B7D8E5656D1E9A CRC64;
MRTQVGIIGA GPAGLLLSHL LYLQGIESII IENRTREEIE GTIRAGVLEQ GTVDLMNQMG
VGARMMKEGH FHEGFELRFN GRGHRINVHE LTGGKYVTVY AQHEVIKDLV AARLQTGGQI
HFNVGDVSLH DVDTSSPKIR FRPNKDGELQ EIECDFIAGC DGFRGPSRPA IPQSVRKEYQ
KVYPFSWLGI LVEAPPSAHE LIYANHERGF ALVSTRSPQI QRLYLQVDAQ DHIDNWSDDR
IWSELHARLE TRDGFKLLEG PIFQKGIVSM RSFVCDPMQH GRLFLAGDAA HIVPPTGAKG
LNLAAADVQV LARGLEAYYK AGKMEILNRC TEICLRRIWK AERFSWFMTT MLHRDQGHTP
FERGIQLAEL DYVTSSRAAS TSLAENYIGL PMEF
