UniProtKB - A2QGH7 (PHHA_ASPNC)
p-hydroxybenzoate-m-hydroxylase A
phhA
Functioni
FAD-dependent monooxygenase; part of the benzoic acid degradation pathway also known as the protocatechuic acid pathway (Ref. 2). Benzoic acid debradation begins with the conversion of benzoic acid into 4-hydroxybenzoic acid through hydroxylation by the benzoate-4-monooxygenase bphA, and its partner NADPH-cytochrome P450 reductase cprA which act as a mediator in electron donation from NADPH (By similarity).
4-Hydroxybenzoic acid is then converted into 3,4-dihydroxybenzoic acid (also called protocatechuic acid) by the p-hydroxybenzoate-m-hydroxylase phhA (Ref. 2). Protocatechuic acid is converted into 3-carboxy-cis,cis-muconic acid by the intradiol ring-cleavage dioxygenase prcA, which is further metabolized through the 3-oxoadipate pathway to finally enter the tricarboxylic acid cycle (TCA) (Ref. 2).
By similarity1 PublicationCatalytic activityi
- EC:1.14.13.331 PublicationThis reaction proceeds in the forward1 Publication direction.
- EC:1.14.13.331 PublicationThis reaction proceeds in the forward1 Publication direction.
Cofactori
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 289 | FADBy similarity | 1 | |
Binding sitei | 310 | FADBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 10 – 39 | FADBy similarityAdd BLAST | 30 | |
Nucleotide bindingi | 241 – 243 | FADBy similarity | 3 |
GO - Molecular functioni
- 4-hydroxybenzoate 3-monooxygenase [NADH] activity Source: RHEA
- 4-hydroxybenzoate 3-monooxygenase [NADPH] activity Source: RHEA
- FAD binding Source: InterPro
- phenol 2-monooxygenase activity Source: UniProtKB-EC
Keywordsi
Molecular function | Oxidoreductase |
Ligand | FAD, Flavoprotein |
Names & Taxonomyi
Protein namesi | Recommended name: p-hydroxybenzoate-m-hydroxylase A1 Publication (EC:1.14.13.331 Publication)Alternative name(s): 4-hydroxybenzoate-3-monooxygenase phhA1 Publication FAD-dependent monooxygenase phhACurated |
Gene namesi | Name:phhA1 Publication ORF Names:An03g03330 |
Organismi | Aspergillus niger (strain CBS 513.88 / FGSC A1513) |
Taxonomic identifieri | 425011 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Aspergillaceae › Aspergillus › Aspergillus subgen. Circumdati › |
Proteomesi |
|
Organism-specific databases
VEuPathDBi | FungiDB:An03g03330 |
Subcellular locationi
Other locations
- Membrane Sequence analysis; Single-pass membrane protein Sequence analysis
Other locations
- integral component of membrane Source: UniProtKB-KW
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transmembranei | 11 – 28 | HelicalSequence analysisAdd BLAST | 18 |
Keywords - Cellular componenti
MembranePathology & Biotechi
Disruption phenotypei
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000453616 | 1 – 636 | p-hydroxybenzoate-m-hydroxylase AAdd BLAST | 636 |
Proteomic databases
PaxDbi | A2QGH7 |
Expressioni
Inductioni
Structurei
Family & Domainsi
Sequence similaritiesi
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
HOGENOMi | CLU_009665_9_3_1 |
Family and domain databases
Gene3Di | 3.40.30.20, 1 hit 3.50.50.60, 1 hit |
InterProi | View protein in InterPro IPR002938, FAD-bd IPR036188, FAD/NAD-bd_sf IPR012941, Phe_hydrox_C_dim_dom IPR038220, PHOX_C_sf IPR036249, Thioredoxin-like_sf |
Pfami | View protein in Pfam PF01494, FAD_binding_3, 1 hit PF07976, Phe_hydrox_dim, 1 hit |
SUPFAMi | SSF51905, SSF51905, 1 hit SSF52833, SSF52833, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MAPSQQEKYD IVIVGAGPVG IVLSLCMSRW GYKVKHIDNR PVPTATGRAD
60 70 80 90 100
GIQPRSTEIL RNLGLKRQIM AFKPAKVYDV AFWDPLPGGQ GIHRTGSWPS
110 120 130 140 150
CPRFIDTRYP FTTLVHQGKI ERVFLDEIQK AGTTVERPWT IVGFKNDGLD
160 170 180 190 200
ETYPVEVQLK SIDTNVIETV RTKYLFSGEG ARSFIRQQLG IQIQYKDPIS
210 220 230 240 250
YVWGVMDGVV RTNFPDIETK CTIHSDAGSI MVIPREDNMV RLYVQIASSD
260 270 280 290 300
DPDFDPRKTA TAEDVQATAR KILQPYWVEW DRVEWYSVYP IGQGISEKYT
310 320 330 340 350
LDERVFMGGD ACHTHSPKAG QGMNTAFHDA LNMAWKLHAV ESGLAKRSIL
360 370 380 390 400
STYETERKDI AETLLSFDNK YAALFSKRRP TAGEVGEASH TTAAAGGEED
410 420 430 440 450
EFVKTFKSSC EFTSGYGVAY KPNVFTWDAT HPAQSPLFDV PGVRLTPGRA
460 470 480 490 500
FTPTTVTRLA DSNHVHLEQE IPANGAFRIF IFAGKQDKTS KAITDLAANL
510 520 530 540 550
EKERSFLSVY RRADIADVSF FENHLPHSKL FSICLVYAGE KNQIDVDSIP
560 570 580 590 600
KILRDYHHHL YADNIPDVRV PQATYAAHEK LGFDVEKGGV VVTRPDSHVA
610 620 630
CTVQLSEGSG TVDALNAFFG SFATKPLGQD SQQSRL
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AM270053 Genomic DNA Translation: CAK47774.1 |
RefSeqi | XP_001390216.1, XM_001390179.1 |
Genome annotation databases
EnsemblFungii | CAK47774; CAK47774; An03g03330 |
GeneIDi | 4980323 |
KEGGi | ang:ANI_1_382034 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AM270053 Genomic DNA Translation: CAK47774.1 |
RefSeqi | XP_001390216.1, XM_001390179.1 |
3D structure databases
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Proteomic databases
PaxDbi | A2QGH7 |
Genome annotation databases
EnsemblFungii | CAK47774; CAK47774; An03g03330 |
GeneIDi | 4980323 |
KEGGi | ang:ANI_1_382034 |
Organism-specific databases
VEuPathDBi | FungiDB:An03g03330 |
Phylogenomic databases
HOGENOMi | CLU_009665_9_3_1 |
Family and domain databases
Gene3Di | 3.40.30.20, 1 hit 3.50.50.60, 1 hit |
InterProi | View protein in InterPro IPR002938, FAD-bd IPR036188, FAD/NAD-bd_sf IPR012941, Phe_hydrox_C_dim_dom IPR038220, PHOX_C_sf IPR036249, Thioredoxin-like_sf |
Pfami | View protein in Pfam PF01494, FAD_binding_3, 1 hit PF07976, Phe_hydrox_dim, 1 hit |
SUPFAMi | SSF51905, SSF51905, 1 hit SSF52833, SSF52833, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | PHHA_ASPNC | |
Accessioni | A2QGH7Primary (citable) accession number: A2QGH7 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | September 29, 2021 |
Last sequence update: | March 6, 2007 | |
Last modified: | February 23, 2022 | |
This is version 71 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families