PHHA_EMENI
ID PHHA_EMENI Reviewed; 636 AA.
AC C8VBV0;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=p-hydroxybenzoate-m-hydroxylase {ECO:0000303|PubMed:25479309};
DE EC=1.14.13.33 {ECO:0000305|PubMed:25479309};
DE AltName: Full=4-hydroxybenzoate-3-monooxygenase phhA {ECO:0000303|PubMed:25479309};
DE AltName: Full=FAD-dependent monooxygenase phhA {ECO:0000305};
GN ORFNames=ANIA_10952;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP FUNCTION, AND INDUCTION.
RX PubMed=25479309; DOI=10.1016/j.fgb.2014.11.002;
RA Martins T.M., Hartmann D.O., Planchon S., Martins I., Renaut J.,
RA Silva Pereira C.;
RT "The old 3-oxoadipate pathway revisited: new insights in the catabolism of
RT aromatics in the saprophytic fungus Aspergillus nidulans.";
RL Fungal Genet. Biol. 74:32-44(2015).
CC -!- FUNCTION: FAD-dependent monooxygenase; part of the benzoic acid
CC degradation pathway also known as the protocatechuic acid pathway
CC (PubMed:25479309). Benzoic acid debradation begins with the conversion
CC of benzoic acid into 4-hydroxybenzoic acid through hydroxylation by the
CC benzoate-4-monooxygenase bphA, and its partner NADPH-cytochrome P450
CC reductase cprA which act as a mediator in electron donation from NADPH
CC (By similarity). 4-Hydroxybenzoic acid is then converted into 3,4-
CC dihydroxybenzoic acid (also called protocatechuic acid) by the p-
CC hydroxybenzoate-m-hydroxylase phhA (Probable). Protocatechuic acid is
CC converted into 3-carboxy-cis,cis-muconic acid by the intradiol ring-
CC cleavage dioxygenase prcA, which is further metabolized through the 3-
CC oxoadipate pathway to finally enter the tricarboxylic acid cycle (TCA)
CC (Probable). {ECO:0000250|UniProtKB:A2QTW5, ECO:0000269|PubMed:25479309,
CC ECO:0000305|PubMed:25479309}.
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:0000305|PubMed:25479309};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19474;
CC Evidence={ECO:0000305|PubMed:25479309};
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:0000305|PubMed:25479309};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19478;
CC Evidence={ECO:0000305|PubMed:25479309};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q6SSJ6};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:Q6SSJ6};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is largely up-regulated in the presence of
CC benzoate. {ECO:0000269|PubMed:25479309}.
CC -!- SIMILARITY: Belongs to the PheA/TfdB FAD monooxygenase family.
CC {ECO:0000305}.
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DR EMBL; BN001304; CBF79728.1; -; Genomic_DNA.
DR SMR; C8VBV0; -.
DR STRING; 162425.CADANIAP00000719; -.
DR EnsemblFungi; CBF79728; CBF79728; ANIA_10952.
DR eggNOG; KOG3855; Eukaryota.
DR HOGENOM; CLU_009665_9_3_1; -.
DR InParanoid; C8VBV0; -.
DR OMA; WKIHHVE; -.
DR OrthoDB; 366744at2759; -.
DR Proteomes; UP000000560; Chromosome IV.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 3.40.30.20; -; 1.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012941; Phe_hydrox_C_dim_dom.
DR InterPro; IPR038220; PHOX_C_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR Pfam; PF07976; Phe_hydrox_dim; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Glycoprotein; Membrane; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..636
FT /note="p-hydroxybenzoate-m-hydroxylase"
FT /id="PRO_0000453617"
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 11..40
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q6SSJ6"
FT BINDING 242..244
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q6SSJ6"
FT BINDING 290
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q6SSJ6"
FT BINDING 311
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q6SSJ6"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 636 AA; 71277 MW; 8DC5BBBB49DB809C CRC64;
MTTDSYPKKY DIVIVGAGPV GILLSLCMSR WGYKVKHIDN RPVPTATGRA DGIQPRSTEI
LRNLGLKRKI MAYDPAKVYD VSFWDPRPDG SGIMRTGNWP SCPRFIDTRY PFTTLVHQGK
IETVFLDEIK KAGTTVERPW TIIGFKNDGL DATYPVQVQL KCLDTNVVET VRAKYLFSGE
GARSFVREQL GIQIRHKDPI SYVWGVMDGV VRTDFPDIQT KCTIHSDAGS IMVIPREDDM
VRLYVQIASS SDPDFNPRKT ATAEEVQNVA KKILKPYYIE WDRVEWYSVY PIGQGISEKY
TLDERVFMGG DACHTHSPKA GQGMNTAFHD ALNMAWKLHA VESGLAQRSI LSTYETERKN
IAETLLDFDN KYAALFSKRR PNAGEVGEAA TAETGRSAEE DPFVKTFKDS CEFTSGYGVA
YLPNIFNWDP SHPAKSPLFD VPGINLVTGK AFTPSTVTRL ADSNFVHLEQ EIPANGAFRI
FIFAGRQSRS KKAIADFAAN LEKERSFLSA YRRSDIGEIS FFERHNPHSK LFTLCLIYAE
KKNDIDMDSI PQILRDYRYH IYSDDIPDVR VPNATYAAHE KLGFDPEKGG VVVTRPDSHI
ACTVQLAEGS GTVDALNAYF GSFSTKPLGQ EQASRL
