VANA_PSES9
ID VANA_PSES9 Reviewed; 329 AA.
AC P12609;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Vanillate O-demethylase oxygenase subunit;
DE EC=1.14.13.82;
DE AltName: Full=4-hydroxy-3-methoxybenzoate demethylase;
GN Name=vanA;
OS Pseudomonas sp. (strain ATCC 19151).
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=315;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3170489; DOI=10.1128/jb.170.10.4924-4930.1988;
RA Brunel F., Davison J.;
RT "Cloning and sequencing of Pseudomonas genes encoding vanillate
RT demethylase.";
RL J. Bacteriol. 170:4924-4930(1988).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADH + O2 + vanillate = 3,4-dihydroxybenzoate +
CC formaldehyde + H2O + NAD(+); Xref=Rhea:RHEA:13021, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16632,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:36241, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.14.13.82;
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000305};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000305};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000305};
CC Note=Binds 1 Fe cation. {ECO:0000305};
CC -!- PATHWAY: Xenobiotic degradation; vanillyl-alcohol degradation.
CC -!- SUBUNIT: This demethylase system consists of two proteins: an oxygenase
CC and an oxygenase reductase.
CC -!- SIMILARITY: Belongs to the bacterial ring-hydroxylating dioxygenase
CC alpha subunit family. {ECO:0000305}.
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DR EMBL; M22077; AAA26019.1; -; Genomic_DNA.
DR AlphaFoldDB; P12609; -.
DR SMR; P12609; -.
DR PRIDE; P12609; -.
DR KEGG; ag:AAA26019; -.
DR UniPathway; UPA00217; -.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0018489; F:vanillate monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR InterPro; IPR044043; VanA_C_cat.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF19112; VanA_C; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
DR PROSITE; PS00570; RING_HYDROXYL_ALPHA; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Aromatic hydrocarbons catabolism; Iron; Iron-sulfur;
KW Lignin degradation; Metal-binding; Monooxygenase; NAD; Oxidoreductase.
FT CHAIN 1..329
FT /note="Vanillate O-demethylase oxygenase subunit"
FT /id="PRO_0000085058"
FT DOMAIN 1..84
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 24
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 26
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 43
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 46
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
SQ SEQUENCE 329 AA; 36579 MW; BAEA8D469E92BF43 CRC64;
MICNERMVIY RGAGQRVAAL EDFCPHRGAP LSLGSIQDGK LVCGYHGLVM DCDGRTASMP
AQRVQAFPCI RAFPAQERHG FIWVWPGDAA LADPALIPHL EWAENPAWAY GGGLYHIACD
YRLMIDNLMD LTHETYVHAS SIGQKEIDEA PVSTRVEGDR LITGRFMEGI LAPPFWRAAL
RGNGLADDVP VDRWQICRFT PPSHVLIEVG VAHAGRGGYD APADCKASSI VVDFITPETD
TSIWYFWGMA RSFRPEDNEL TARIREGQGT IFAEDLEMLE QQQRNLLAWP ERPLLKLNID
AGGVQSRRII ERLVSAERAA EAQLIGRQA
