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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)DescriptionActionsGraphical viewLength
Binding sitei73Heme3 Publications1
Binding sitei98Heme3 Publications1
Binding sitei102Heme3 Publications1
Binding sitei242Substrate1 Publication1
Sitei242Controls regioselective substrate oxidation1
Binding sitei289Heme3 Publications1
Binding sitei345Heme3 Publications1
Metal bindingi347Iron (heme axial ligand)1

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeCitrobacterCitrobacter freundii complex

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi242N → 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 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004227381 – 4041,8-cineole 2-endo-monooxygenaseAdd BLAST404

Interactioni

Subunit structurei

Homodimer.3 Publications

Structurei

Secondary structure

1404
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni10 – 13Combined sources4
Beta strandi16 – 18Combined sources3
Beta strandi25 – 27Combined sources3
Helixi28 – 38Combined sources11
Beta strandi42 – 46Combined sources5
Helixi48 – 50Combined sources3
Beta strandi52 – 55Combined sources4
Helixi58 – 65Combined sources8
Beta strandi69 – 72Combined sources4
Helixi73 – 75Combined sources3
Beta strandi77 – 79Combined sources3
Turni89 – 92Combined sources4
Helixi97 – 106Combined sources10
Turni107 – 109Combined sources3
Helixi111 – 115Combined sources5
Helixi118 – 130Combined sources13
Turni131 – 135Combined sources5
Beta strandi136 – 139Combined sources4
Helixi140 – 143Combined sources4
Turni144 – 147Combined sources4
Helixi148 – 156Combined sources9
Helixi161 – 163Combined sources3
Helixi164 – 176Combined sources13
Helixi180 – 203Combined sources24
Helixi209 – 215Combined sources7
Helixi225 – 256Combined sources32
Helixi258 – 266Combined sources9
Helixi268 – 270Combined sources3
Helixi271 – 282Combined sources12
Beta strandi287 – 291Combined sources5
Beta strandi295 – 297Combined sources3
Beta strandi300 – 302Combined sources3
Beta strandi307 – 310Combined sources4
Helixi312 – 315Combined sources4
Turni319 – 321Combined sources3
Beta strandi322 – 324Combined sources3
Helixi343 – 345Combined sources3
Helixi350 – 367Combined sources18
Beta strandi380 – 382Combined sources3
Beta strandi384 – 386Combined sources3
Beta strandi388 – 391Combined sources4
Beta strandi393 – 395Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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
PDB 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.
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...

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: November 2, 2016
This is version 76 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.