DH4C_PSEPU
ID DH4C_PSEPU Reviewed; 521 AA.
AC P09788; Q59705; Q59706;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=4-cresol dehydrogenase [hydroxylating] flavoprotein subunit;
DE EC=1.17.9.1 {ECO:0000269|PubMed:3790500};
DE AltName: Full=P-cresol methylhydroxylase;
DE Short=PCMH;
GN Name=pchF;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OG Plasmid pRA4000, and Plasmid pRA500.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCIMB 9866, and NCIMB 9869; PLASMID=pRA4000, and pRA500;
RX PubMed=7929007; DOI=10.1128/jb.176.20.6349-6361.1994;
RA Kim J.-H., Fuller J.H., Cecchini G., McIntire W.S.;
RT "Cloning, sequencing, and expression of the structural genes for the
RT cytochrome and flavoprotein subunits of p-cresol methylhydroxylase from two
RT strains of Pseudomonas putida.";
RL J. Bacteriol. 176:6349-6361(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCIMB 9866, and NCIMB 9869; PLASMID=pRA4000, and pRA500;
RX PubMed=10565539; DOI=10.3109/10425179909033930;
RA Cronin C.N., Kim J.-H., Fuller J.H., Zhang X.-P., McIntire W.S.;
RT "Organization and sequences of p-hydroxybenzaldehyde dehydrogenase and
RT other plasmid-encoded genes for early enzymes of the p-cresol degradative
RT pathway in Pseudomonas putida NCIMB 9866 and 9869.";
RL DNA Seq. 10:7-17(1999).
RN [3]
RP PROTEIN SEQUENCE OF 2-57, SUBUNIT, AND CHARACTERIZATION.
RC STRAIN=NCIMB 9869; PLASMID=pRA500;
RX PubMed=3790500; DOI=10.1021/bi00368a021;
RA McIntire W.S., Singer T.P., Smith A.J., Mathews F.S.;
RT "Amino acid and sequence analysis of the cytochrome and flavoprotein
RT subunits of p-cresol methylhydroxylase.";
RL Biochemistry 25:5975-5981(1986).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=588247; DOI=10.1042/bj1670155;
RA Hopper D.J., Taylor D.G.;
RT "The purification and properties of p-cresol-(acceptor) oxidoreductase
RT (hydroxylating), a flavocytochrome from Pseudomonas putida.";
RL Biochem. J. 167:155-162(1977).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RC STRAIN=NCIMB 9869; PLASMID=pRA500;
RX PubMed=1846290; DOI=10.1021/bi00215a034;
RA Mathews F.S., Chen Z.-W., Bellamy H.D., McIntire W.S.;
RT "Three-dimensional structure of p-cresol methylhydroxylase (flavocytochrome
RT c) from Pseudomonas putida at 3.0-A resolution.";
RL Biochemistry 30:238-247(1991).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RC STRAIN=NCIMB 9869; PLASMID=pRA500;
RX PubMed=10623531; DOI=10.1006/jmbi.1999.3290;
RA Cunane L.M., Chen Z.-W., Shamala N., Mathews F.S., Cronin C.N.,
RA McIntire W.S.;
RT "Structures of the flavocytochrome p-cresol methylhydroxylase and its
RT enzyme-substrate complex: gated substrate entry and proton relays support
RT the proposed catalytic mechanism.";
RL J. Mol. Biol. 295:357-374(2000).
CC -!- FUNCTION: Catalyzes the azurin dependent hydroxylation of the methyl
CC group of 4-methylphenol to form 4-hydroxybenzaldehyde.
CC {ECO:0000269|PubMed:588247}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methylphenol + H2O + 4 oxidized [azurin] = 4-
CC hydroxybenzaldehyde + 4 H(+) + 4 reduced [azurin];
CC Xref=Rhea:RHEA:15141, Rhea:RHEA-COMP:11034, Rhea:RHEA-COMP:11035,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17597,
CC ChEBI:CHEBI:17847, ChEBI:CHEBI:29036, ChEBI:CHEBI:49552; EC=1.17.9.1;
CC Evidence={ECO:0000269|PubMed:3790500};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD covalently per subunit.;
CC -!- PATHWAY: Aromatic compound metabolism; p-cresol degradation.
CC -!- SUBUNIT: Tetramer of two cytochrome subunits and two flavoprotein
CC subunits. {ECO:0000269|PubMed:3790500}.
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DR EMBL; U96338; AAA80318.2; -; Genomic_DNA.
DR EMBL; U96339; AAA80463.2; -; Genomic_DNA.
DR PIR; T46687; T46687.
DR PDB; 1DII; X-ray; 2.50 A; A/B=1-521.
DR PDB; 1DIQ; X-ray; 2.75 A; A/B=1-521.
DR PDB; 1WVE; X-ray; 1.85 A; A/B=2-521.
DR PDB; 1WVF; X-ray; 1.30 A; A=2-521.
DR PDBsum; 1DII; -.
DR PDBsum; 1DIQ; -.
DR PDBsum; 1WVE; -.
DR PDBsum; 1WVF; -.
DR AlphaFoldDB; P09788; -.
DR SMR; P09788; -.
DR IntAct; P09788; 1.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR BioCyc; MetaCyc:MON-19460; -.
DR BRENDA; 1.17.9.1; 5092.
DR UniPathway; UPA00708; -.
DR EvolutionaryTrace; P09788; -.
DR GO; GO:0018695; F:4-cresol dehydrogenase (hydroxylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 1.10.45.10; -; 1.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.10; -; 1.
DR InterPro; IPR016170; Cytok_DH_C_sf.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR004113; FAD-linked_oxidase_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF55103; SSF55103; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase;
KW Plasmid.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3790500"
FT CHAIN 2..521
FT /note="4-cresol dehydrogenase [hydroxylating] flavoprotein
FT subunit"
FT /id="PRO_0000079883"
FT DOMAIN 54..268
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT MOD_RES 384
FT /note="O-8alpha-FAD tyrosine"
FT CONFLICT 47
FT /note="I -> K (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="E -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 56..57
FT /note="HA -> MG (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 15..29
FT /evidence="ECO:0007829|PDB:1WVF"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:1WVF"
FT HELIX 38..45
FT /evidence="ECO:0007829|PDB:1WVF"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:1WVF"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:1WVF"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:1WVF"
FT HELIX 67..80
FT /evidence="ECO:0007829|PDB:1WVF"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:1WVF"
FT TURN 93..98
FT /evidence="ECO:0007829|PDB:1WVF"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:1WVF"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:1WVF"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:1WVF"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:1WVF"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:1WVF"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:1WVF"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:1WVE"
FT HELIX 161..166
FT /evidence="ECO:0007829|PDB:1WVF"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:1WVF"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:1WVF"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:1WVF"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:1WVF"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:1WVF"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:1WVE"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:1WVF"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:1WVF"
FT STRAND 230..237
FT /evidence="ECO:0007829|PDB:1WVF"
FT STRAND 243..252
FT /evidence="ECO:0007829|PDB:1WVF"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:1WVF"
FT HELIX 258..270
FT /evidence="ECO:0007829|PDB:1WVF"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:1WVF"
FT HELIX 283..289
FT /evidence="ECO:0007829|PDB:1WVF"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:1WVF"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:1WVF"
FT HELIX 306..316
FT /evidence="ECO:0007829|PDB:1WVF"
FT STRAND 320..330
FT /evidence="ECO:0007829|PDB:1WVF"
FT HELIX 331..348
FT /evidence="ECO:0007829|PDB:1WVF"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:1WVF"
FT HELIX 356..359
FT /evidence="ECO:0007829|PDB:1WVF"
FT HELIX 365..372
FT /evidence="ECO:0007829|PDB:1WVF"
FT HELIX 379..385
FT /evidence="ECO:0007829|PDB:1WVF"
FT STRAND 390..395
FT /evidence="ECO:0007829|PDB:1WVF"
FT STRAND 397..401
FT /evidence="ECO:0007829|PDB:1WVF"
FT HELIX 403..419
FT /evidence="ECO:0007829|PDB:1WVF"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:1WVF"
FT STRAND 432..444
FT /evidence="ECO:0007829|PDB:1WVF"
FT HELIX 448..467
FT /evidence="ECO:0007829|PDB:1WVF"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:1DII"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:1WVF"
FT HELIX 480..486
FT /evidence="ECO:0007829|PDB:1WVF"
FT HELIX 489..502
FT /evidence="ECO:0007829|PDB:1WVF"
FT HELIX 512..514
FT /evidence="ECO:0007829|PDB:1WVF"
SQ SEQUENCE 521 AA; 57945 MW; CFF28ACD77FDC2DE CRC64;
MSEQNNAVLP KGVTQGEFNK AVQKFRALLG DDNVLVESDQ LVPYNKIMMP VENAAHAPSA
AVTATTVEQV QGVVKICNEH KIPIWTISTG RNFGYGSAAP VQRGQVILDL KKMNKIIKID
PEMCYALVEP GVTFGQMYDY IQENNLPVML SFSAPSAIAG PVGNTMDRGV GYTPYGEHFM
MQCGMEVVLA NGDVYRTGMG GVPGSNTWQI FKWGYGPTLD GMFTQANYGI CTKMGFWLMP
KPPVFKPFEV IFEDEADIVE IVDALRPLRM SNTIPNSVVI ASTLWEAGSA HLTRAQYTTE
PGHTPDSVIK QMQKDTGMGA WNLYAALYGT QEQVDVNWKI VTDVFKKLGK GRIVTQEEAG
DTQPFKYRAQ LMSGVPNLQE FGLYNWRGGG GSMWFAPVSE ARGSECKKQA AMAKRVLHKY
GLDYVAEFIV APRDMHHVID VLYDRTNPEE TKRADACFNE LLDEFEKEGY AVYRVNTRFQ
DRVAQSYGPV KRKLEHAIKR AVDPNNILAP GRSGIDLNND F
