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Protein

4-cresol dehydrogenase [hydroxylating] flavoprotein subunit

Gene

pchF

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

4-methylphenol + 2 acceptor + H2O = 4-hydroxybenzaldehyde + 2 reduced acceptor.

Cofactori

FADNote: Binds 1 FAD covalently per subunit.

Pathwayi: p-cresol degradation

This protein is involved in the pathway p-cresol degradation, which is part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the pathway p-cresol degradation and in Aromatic compound metabolism.

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.17.99.1. 5092.
UniPathwayiUPA00708.

Names & Taxonomyi

Protein namesi
Recommended name:
4-cresol dehydrogenase [hydroxylating] flavoprotein subunit (EC:1.17.99.1)
Alternative name(s):
P-cresol methylhydroxylase
Short name:
PCMH
Gene namesi
Name:pchF
Encoded oniPlasmid pRA40002 Publications
Plasmid pRA5005 Publications
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Pathology & Biotechi

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 5215204-cresol dehydrogenase [hydroxylating] flavoprotein subunitPRO_0000079883Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei384 – 3841O-8alpha-FAD tyrosine

Interactioni

Subunit structurei

Tetramer of two cytochrome subunits and two flavoprotein subunits.

Protein-protein interaction databases

IntActiP09788. 1 interaction.

Structurei

Secondary structure

1
521
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 2915Combined sources
Helixi31 – 333Combined sources
Helixi38 – 458Combined sources
Beta strandi49 – 513Combined sources
Helixi53 – 564Combined sources
Beta strandi59 – 635Combined sources
Helixi67 – 8014Combined sources
Beta strandi84 – 896Combined sources
Turni93 – 986Combined sources
Beta strandi106 – 1094Combined sources
Beta strandi116 – 1205Combined sources
Turni121 – 1244Combined sources
Beta strandi125 – 1284Combined sources
Helixi134 – 14310Combined sources
Beta strandi147 – 1493Combined sources
Helixi156 – 1583Combined sources
Helixi161 – 1666Combined sources
Helixi178 – 1814Combined sources
Beta strandi182 – 1887Combined sources
Beta strandi194 – 1963Combined sources
Helixi198 – 2014Combined sources
Turni208 – 2103Combined sources
Beta strandi215 – 2173Combined sources
Helixi220 – 2234Combined sources
Beta strandi226 – 2283Combined sources
Beta strandi230 – 2378Combined sources
Beta strandi243 – 25210Combined sources
Helixi255 – 2573Combined sources
Helixi258 – 27013Combined sources
Beta strandi278 – 2825Combined sources
Helixi283 – 2897Combined sources
Helixi294 – 2963Combined sources
Beta strandi301 – 3033Combined sources
Helixi306 – 31611Combined sources
Beta strandi320 – 33011Combined sources
Helixi331 – 34818Combined sources
Beta strandi352 – 3554Combined sources
Helixi356 – 3594Combined sources
Helixi365 – 3728Combined sources
Helixi379 – 3857Combined sources
Beta strandi390 – 3956Combined sources
Beta strandi397 – 4015Combined sources
Helixi403 – 41917Combined sources
Beta strandi426 – 4305Combined sources
Beta strandi432 – 44413Combined sources
Helixi448 – 46720Combined sources
Beta strandi472 – 4743Combined sources
Helixi477 – 4793Combined sources
Helixi480 – 4867Combined sources
Helixi489 – 50214Combined sources
Helixi512 – 5143Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DIIX-ray2.50A/B1-521[»]
1DIQX-ray2.75A/B1-521[»]
1WVEX-ray1.85A/B2-521[»]
1WVFX-ray1.30A2-521[»]
ProteinModelPortaliP09788.
SMRiP09788. Positions 7-521.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09788.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 268215FAD-binding PCMH-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

Family and domain databases

Gene3Di1.10.45.10. 1 hit.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.40.462.10. 1 hit.
InterProiIPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR016164. FAD-linked_Oxase-like_C.
IPR004113. FAD-linked_oxidase_C.
IPR006094. Oxid_FAD_bind_N.
IPR016170. V_Alc_oxidase/Cytok_DH_C_dom.
IPR016171. Vanillyl_alc_oxidase_C-sub2.
[Graphical view]
PfamiPF02913. FAD-oxidase_C. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMiSSF55103. SSF55103. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09788-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEQNNAVLP KGVTQGEFNK AVQKFRALLG DDNVLVESDQ LVPYNKIMMP
60 70 80 90 100
VENAAHAPSA AVTATTVEQV QGVVKICNEH KIPIWTISTG RNFGYGSAAP
110 120 130 140 150
VQRGQVILDL KKMNKIIKID PEMCYALVEP GVTFGQMYDY IQENNLPVML
160 170 180 190 200
SFSAPSAIAG PVGNTMDRGV GYTPYGEHFM MQCGMEVVLA NGDVYRTGMG
210 220 230 240 250
GVPGSNTWQI FKWGYGPTLD GMFTQANYGI CTKMGFWLMP KPPVFKPFEV
260 270 280 290 300
IFEDEADIVE IVDALRPLRM SNTIPNSVVI ASTLWEAGSA HLTRAQYTTE
310 320 330 340 350
PGHTPDSVIK QMQKDTGMGA WNLYAALYGT QEQVDVNWKI VTDVFKKLGK
360 370 380 390 400
GRIVTQEEAG DTQPFKYRAQ LMSGVPNLQE FGLYNWRGGG GSMWFAPVSE
410 420 430 440 450
ARGSECKKQA AMAKRVLHKY GLDYVAEFIV APRDMHHVID VLYDRTNPEE
460 470 480 490 500
TKRADACFNE LLDEFEKEGY AVYRVNTRFQ DRVAQSYGPV KRKLEHAIKR
510 520
AVDPNNILAP GRSGIDLNND F
Length:521
Mass (Da):57,945
Last modified:January 23, 2007 - v3
Checksum:iCFF28ACD77FDC2DE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 471I → K AA sequence (PubMed:3790500).Curated
Sequence conflicti52 – 521E → G AA sequence (PubMed:3790500).Curated
Sequence conflicti56 – 572HA → MG AA sequence (PubMed:3790500).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U96338 Genomic DNA. Translation: AAA80318.2.
U96339 Genomic DNA. Translation: AAA80463.2.
PIRiT46687.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U96338 Genomic DNA. Translation: AAA80318.2.
U96339 Genomic DNA. Translation: AAA80463.2.
PIRiT46687.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DIIX-ray2.50A/B1-521[»]
1DIQX-ray2.75A/B1-521[»]
1WVEX-ray1.85A/B2-521[»]
1WVFX-ray1.30A2-521[»]
ProteinModelPortaliP09788.
SMRiP09788. Positions 7-521.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP09788. 1 interaction.

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00708.
BRENDAi1.17.99.1. 5092.

Miscellaneous databases

EvolutionaryTraceiP09788.

Family and domain databases

Gene3Di1.10.45.10. 1 hit.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.40.462.10. 1 hit.
InterProiIPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR016164. FAD-linked_Oxase-like_C.
IPR004113. FAD-linked_oxidase_C.
IPR006094. Oxid_FAD_bind_N.
IPR016170. V_Alc_oxidase/Cytok_DH_C_dom.
IPR016171. Vanillyl_alc_oxidase_C-sub2.
[Graphical view]
PfamiPF02913. FAD-oxidase_C. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMiSSF55103. SSF55103. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning, sequencing, and expression of the structural genes for the cytochrome and flavoprotein subunits of p-cresol methylhydroxylase from two strains of Pseudomonas putida."
    Kim J.-H., Fuller J.H., Cecchini G., McIntire W.S.
    J. Bacteriol. 176:6349-6361(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: NCIMB 9866 and NCIMB 9869.
    Plasmid: pRA4000 pRA500
  2. "Organization and sequences of p-hydroxybenzaldehyde dehydrogenase and other plasmid-encoded genes for early enzymes of the p-cresol degradative pathway in Pseudomonas putida NCIMB 9866 and 9869."
    Cronin C.N., Kim J.-H., Fuller J.H., Zhang X.-P., McIntire W.S.
    DNA Seq. 10:7-17(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: NCIMB 9866 and NCIMB 9869.
    Plasmid: pRA4000 pRA500
  3. "Amino acid and sequence analysis of the cytochrome and flavoprotein subunits of p-cresol methylhydroxylase."
    McIntire W.S., Singer T.P., Smith A.J., Mathews F.S.
    Biochemistry 25:5975-5981(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-57, CHARACTERIZATION.
    Strain: NCIMB 9869.
    Plasmid: pRA500
  4. "Three-dimensional structure of p-cresol methylhydroxylase (flavocytochrome c) from Pseudomonas putida at 3.0-A resolution."
    Mathews F.S., Chen Z.-W., Bellamy H.D., McIntire W.S.
    Biochemistry 30:238-247(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    Strain: NCIMB 9869.
    Plasmid: pRA500
  5. "Structures of the flavocytochrome p-cresol methylhydroxylase and its enzyme-substrate complex: gated substrate entry and proton relays support the proposed catalytic mechanism."
    Cunane L.M., Chen Z.-W., Shamala N., Mathews F.S., Cronin C.N., McIntire W.S.
    J. Mol. Biol. 295:357-374(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    Strain: NCIMB 9869.
    Plasmid: pRA500

Entry informationi

Entry nameiDH4C_PSEPU
AccessioniPrimary (citable) accession number: P09788
Secondary accession number(s): Q59705, Q59706
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 96 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Plasmid

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.