CY4C_PSEPU
ID CY4C_PSEPU Reviewed; 113 AA.
AC P09787; Q59698; Q59707;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=4-cresol dehydrogenase [hydroxylating] cytochrome c subunit;
DE AltName: Full=Flavocytochrome c;
DE AltName: Full=P-cresol methylhydroxylase cytochrome subunit;
DE Flags: Precursor;
GN Name=pchC;
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 34-113, 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 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 [5]
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: This is the heme-containing component of the p-cresol
CC methylhydroxylase. It accepts electrons from the flavoprotein subunit.
CC -!- PATHWAY: Aromatic compound metabolism; p-cresol degradation.
CC -!- SUBUNIT: Tetramer of two cytochrome subunits and two flavoprotein
CC subunits.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U96339; AAA80317.2; -; Genomic_DNA.
DR EMBL; U96338; AAA80319.2; -; Genomic_DNA.
DR PIR; T46685; T46685.
DR PDB; 1DII; X-ray; 2.50 A; C/D=34-113.
DR PDB; 1DIQ; X-ray; 2.75 A; C/D=34-113.
DR PDB; 1WVE; X-ray; 1.85 A; C/D=34-113.
DR PDBsum; 1DII; -.
DR PDBsum; 1DIQ; -.
DR PDBsum; 1WVE; -.
DR AlphaFoldDB; P09787; -.
DR SMR; P09787; -.
DR IntAct; P09787; 1.
DR BioCyc; MetaCyc:MON-19459; -.
DR UniPathway; UPA00708; -.
DR EvolutionaryTrace; P09787; -.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.760.10; -; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR Pfam; PF13442; Cytochrome_CBB3; 1.
DR SUPFAM; SSF46626; SSF46626; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW Metal-binding; Plasmid; Signal; Transport.
FT SIGNAL 1..33
FT /evidence="ECO:0000269|PubMed:3790500"
FT CHAIN 34..113
FT /note="4-cresol dehydrogenase [hydroxylating] cytochrome c
FT subunit"
FT /id="PRO_0000006567"
FT BINDING 48
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 51
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 52
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 83
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT VARIANT 74
FT /note="D -> A (in strain: NCIMB 9866)"
FT CONFLICT 111
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1WVE"
FT HELIX 40..46
FT /evidence="ECO:0007829|PDB:1WVE"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:1WVE"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:1WVE"
FT HELIX 69..78
FT /evidence="ECO:0007829|PDB:1WVE"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:1WVE"
FT HELIX 93..105
FT /evidence="ECO:0007829|PDB:1WVE"
SQ SEQUENCE 113 AA; 11934 MW; 568ED7438521C1E1 CRC64;
MTFPFSGAAV KRMLVTGVVL PFGLLVAAGQ AQADSQWGSG KNLYDKVCGH CHKPEVGVGP
VLEGRGLPEA YIKDIVRNGF RAMPAFPASY VDDESLTQVA EYLSSLPAPA AQP
