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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

BioCyciMetaCyc:MONOMER-19460.
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 databases

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000798832 – 5214-cresol dehydrogenase [hydroxylating] flavoprotein subunitAdd BLAST520

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei384O-8alpha-FAD tyrosine1

Interactioni

Subunit structurei

Tetramer of two cytochrome subunits and two flavoprotein subunits.

Protein-protein interaction databases

IntActiP09788. 1 interactor.

Structurei

Secondary structure

1521
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi15 – 29Combined sources15
Helixi31 – 33Combined sources3
Helixi38 – 45Combined sources8
Beta strandi49 – 51Combined sources3
Helixi53 – 56Combined sources4
Beta strandi59 – 63Combined sources5
Helixi67 – 80Combined sources14
Beta strandi84 – 89Combined sources6
Turni93 – 98Combined sources6
Beta strandi106 – 109Combined sources4
Beta strandi116 – 120Combined sources5
Turni121 – 124Combined sources4
Beta strandi125 – 128Combined sources4
Helixi134 – 143Combined sources10
Beta strandi147 – 149Combined sources3
Helixi156 – 158Combined sources3
Helixi161 – 166Combined sources6
Helixi178 – 181Combined sources4
Beta strandi182 – 188Combined sources7
Beta strandi194 – 196Combined sources3
Helixi198 – 201Combined sources4
Turni208 – 210Combined sources3
Beta strandi215 – 217Combined sources3
Helixi220 – 223Combined sources4
Beta strandi226 – 228Combined sources3
Beta strandi230 – 237Combined sources8
Beta strandi243 – 252Combined sources10
Helixi255 – 257Combined sources3
Helixi258 – 270Combined sources13
Beta strandi278 – 282Combined sources5
Helixi283 – 289Combined sources7
Helixi294 – 296Combined sources3
Beta strandi301 – 303Combined sources3
Helixi306 – 316Combined sources11
Beta strandi320 – 330Combined sources11
Helixi331 – 348Combined sources18
Beta strandi352 – 355Combined sources4
Helixi356 – 359Combined sources4
Helixi365 – 372Combined sources8
Helixi379 – 385Combined sources7
Beta strandi390 – 395Combined sources6
Beta strandi397 – 401Combined sources5
Helixi403 – 419Combined sources17
Beta strandi426 – 430Combined sources5
Beta strandi432 – 444Combined sources13
Helixi448 – 467Combined sources20
Beta strandi472 – 474Combined sources3
Helixi477 – 479Combined sources3
Helixi480 – 486Combined sources7
Helixi489 – 502Combined sources14
Helixi512 – 514Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP09788.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini54 – 268FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST215

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)DescriptionActionsGraphical viewLength
Sequence conflicti47I → K AA sequence (PubMed:3790500).Curated1
Sequence conflicti52E → G AA sequence (PubMed:3790500).Curated1
Sequence conflicti56 – 57HA → MG AA sequence (PubMed:3790500).Curated2

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DIIX-ray2.50A/B1-521[»]
1DIQX-ray2.75A/B1-521[»]
1WVEX-ray1.85A/B2-521[»]
1WVFX-ray1.30A2-521[»]
ProteinModelPortaliP09788.
SMRiP09788.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP09788. 1 interactor.

Chemistry databases

DrugBankiDB03147. Flavin adenine dinucleotide.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00708.
BioCyciMetaCyc:MONOMER-19460.
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...

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: November 2, 2016
This is version 98 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.