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Protein

1,8-cineole 2-endo-monooxygenase

Gene

cinA

Organism
Citrobacter braakii
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the degradation of cineol (eucalyptol). Catalyzes the initial hydroxylation of cineole exclusively at the pro-R carbon to give the (S)-6beta-hydroxycineole. Cineole is the natural substrate of CinA.1 Publication

Catalytic activityi

1,8-cineole + NADPH + O2 = 2-endo-hydroxy-1,8-cineole + NADP+ + H2O.1 Publication

Cofactori

heme1 Publication

Pathwayi: 1,8-cineol degradation

This protein is involved in the pathway 1,8-cineol degradation, which is part of Terpene metabolism.
View all proteins of this organism that are known to be involved in the pathway 1,8-cineol degradation and in Terpene metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei73 – 731Heme3 Publications
Binding sitei98 – 981Heme3 Publications
Binding sitei102 – 1021Heme3 Publications
Binding sitei242 – 2421Substrate1 Publication
Sitei242 – 2421Controls regioselective substrate oxidation
Binding sitei289 – 2891Heme3 Publications
Binding sitei345 – 3451Heme3 Publications
Metal bindingi347 – 3471Iron (heme axial ligand)

GO - Molecular functioni

GO - Biological processi

  • carbazole catabolic process Source: UniProtKB-UniPathway
  • oxidation-reduction process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17202.
BRENDAi1.14.13.156. 6880.
UniPathwayiUPA01032.

Names & Taxonomyi

Protein namesi
Recommended name:
1,8-cineole 2-endo-monooxygenase (EC:1.14.13.156)
Alternative name(s):
cytochrome P450
Short name:
CYP176A1
Short name:
P450cin
Gene namesi
Name:cinA
OrganismiCitrobacter braakii
Taxonomic identifieri57706 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCitrobacterCitrobacter freundii complex

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi242 – 2421N → A: Has only a modest effect on monooxygenase activity. The substrate is free to adopt an alternate conformation which places the ethereal oxygen in an optimal position for polar interactions with solvent. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4044041,8-cineole 2-endo-monooxygenasePRO_0000422738Add
BLAST

Interactioni

Subunit structurei

Homodimer.3 Publications

Structurei

Secondary structure

1
404
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni10 – 134Combined sources
Beta strandi16 – 183Combined sources
Beta strandi25 – 273Combined sources
Helixi28 – 3811Combined sources
Beta strandi42 – 465Combined sources
Helixi48 – 503Combined sources
Beta strandi52 – 554Combined sources
Helixi58 – 658Combined sources
Beta strandi69 – 724Combined sources
Helixi73 – 753Combined sources
Beta strandi77 – 793Combined sources
Turni89 – 924Combined sources
Helixi97 – 10610Combined sources
Turni107 – 1093Combined sources
Helixi111 – 1155Combined sources
Helixi118 – 13013Combined sources
Turni131 – 1355Combined sources
Beta strandi136 – 1394Combined sources
Helixi140 – 1434Combined sources
Turni144 – 1474Combined sources
Helixi148 – 1569Combined sources
Helixi161 – 1633Combined sources
Helixi164 – 17613Combined sources
Helixi180 – 20324Combined sources
Helixi209 – 2157Combined sources
Helixi225 – 25632Combined sources
Helixi258 – 2669Combined sources
Helixi268 – 2703Combined sources
Helixi271 – 28212Combined sources
Beta strandi287 – 2915Combined sources
Beta strandi295 – 2973Combined sources
Beta strandi300 – 3023Combined sources
Beta strandi307 – 3104Combined sources
Helixi312 – 3154Combined sources
Turni319 – 3213Combined sources
Beta strandi322 – 3243Combined sources
Helixi343 – 3453Combined sources
Helixi350 – 36718Combined sources
Beta strandi380 – 3823Combined sources
Beta strandi384 – 3863Combined sources
Beta strandi388 – 3914Combined sources
Beta strandi393 – 3953Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T2BX-ray1.70A/B8-404[»]
3BDZX-ray2.00A/B8-404[»]
3BE0X-ray3.05A/B8-404[»]
4FB2X-ray1.37A/B/C/D8-404[»]
4FMXX-ray1.55A/B8-404[»]
4FYZX-ray2.32A/B8-404[»]
4L6GX-ray1.37A/B8-404[»]
4L77X-ray1.38A/B8-404[»]
4LHTX-ray2.14A/B8-404[»]
ProteinModelPortaliQ8VQF6.
SMRiQ8VQF6. Positions 8-404.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8VQF6.

Family & Domainsi

Sequence similaritiesi

Belongs to the cytochrome P450 family.Curated

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR002397. Cyt_P450_B.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00359. BP450.
SUPFAMiSSF48264. SSF48264. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8VQF6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTATVASTSL FTTADHYHTP LGPDGTPHAF FEALRDEAET TPIGWSEAYG
60 70 80 90 100
GHWVVAGYKE IQAVIQNTKA FSNKGVTFPR YETGEFELMM AGQDDPVHKK
110 120 130 140 150
YRQLVAKPFS PEATDLFTEQ LRQSTNDLID ARIELGEGDA ATWLANEIPA
160 170 180 190 200
RLTAILLGLP PEDGDTYRRW VWAITHVENP EEGAEIFAEL VAHARTLIAE
210 220 230 240 250
RRTNPGNDIM SRVIMSKIDG ESLSEDDLIG FFTILLLGGI DNTARFLSSV
260 270 280 290 300
FWRLAWDIEL RRRLIAHPEL IPNAVDELLR FYGPAMVGRL VTQEVTVGDI
310 320 330 340 350
TMKPGQTAML WFPIASRDRS AFDSPDNIVI ERTPNRHLSL GHGIHRCLGA
360 370 380 390 400
HLIRVEARVA ITEFLKRIPE FSLDPNKECE WLMGQVAGML HVPIIFPKGK

RLSE
Length:404
Mass (Da):45,266
Last modified:March 1, 2002 - v1
Checksum:i1EA334C5CF1B8243
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF456128 Genomic DNA. Translation: AAL57614.1.

Genome annotation databases

KEGGiag:AAL57614.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF456128 Genomic DNA. Translation: AAL57614.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T2BX-ray1.70A/B8-404[»]
3BDZX-ray2.00A/B8-404[»]
3BE0X-ray3.05A/B8-404[»]
4FB2X-ray1.37A/B/C/D8-404[»]
4FMXX-ray1.55A/B8-404[»]
4FYZX-ray2.32A/B8-404[»]
4L6GX-ray1.37A/B8-404[»]
4L77X-ray1.38A/B8-404[»]
4LHTX-ray2.14A/B8-404[»]
ProteinModelPortaliQ8VQF6.
SMRiQ8VQF6. Positions 8-404.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAL57614.

Enzyme and pathway databases

UniPathwayiUPA01032.
BioCyciMetaCyc:MONOMER-17202.
BRENDAi1.14.13.156. 6880.

Miscellaneous databases

EvolutionaryTraceiQ8VQF6.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
InterProiIPR001128. Cyt_P450.
IPR002397. Cyt_P450_B.
[Graphical view]
PfamiPF00067. p450. 1 hit.
[Graphical view]
PRINTSiPR00359. BP450.
SUPFAMiSSF48264. SSF48264. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cytochrome P450(cin) (CYP176A), isolation, expression, and characterization."
    Hawkes D.B., Adams G.W., Burlingame A.L., Ortiz de Montellano P.R., De Voss J.J.
    J. Biol. Chem. 277:27725-27732(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 171-195, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
  2. "Crystal structure of P450cin in a complex with its substrate, 1,8-cineole, a close structural homologue to D-camphor, the substrate for P450cam."
    Meharenna Y.T., Li H., Hawkes D.B., Pearson A.G., De Voss J., Poulos T.L.
    Biochemistry 43:9487-9494(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 8-404 IN COMPLEX WITH HEME AND SUBSTRATE, COFACTOR, SUBUNIT.
  3. "The critical role of substrate-protein hydrogen bonding in the control of regioselective hydroxylation in p450cin."
    Meharenna Y.T., Slessor K.E., Cavaignac S.M., Poulos T.L., De Voss J.J.
    J. Biol. Chem. 283:10804-10812(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 8-404 OF MUTANT ALA-242 IN COMPLEX WITH HEME AND SUSBTRATE, SUBSTRATE SPECIFICITY, MUTAGENESIS OF ASN-242, SUBUNIT.
  4. "Crystal structures of substrate-free and nitrosyl cytochrome P450cin: implications for O(2) activation."
    Madrona Y., Tripathi S., Li H., Poulos T.L.
    Biochemistry 51:6623-6631(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.37 ANGSTROMS) OF 8-404 IN COMPLEX WITH HEME AND SUSBTRATE, SUBUNIT.

Entry informationi

Entry nameiCINA_CITBR
AccessioniPrimary (citable) accession number: Q8VQF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2013
Last sequence update: March 1, 2002
Last modified: May 11, 2016
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

It lacks the conserved threonine believed to be involved in dioxygen activation and instead contains an asparagine at position 242. It is the first isolated P450 using the flavoprotein cindoxin (CinC) as its natural redox partner (PubMed:12016226).1 Publication

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.