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P30621 (MOXR_METEA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein MoxR
Alternative name(s):
Protein MxaR
Gene names
Name:moxR
Synonyms:mxaR
Ordered Locus Names:MexAM1_META1p4534
OrganismMethylobacterium extorquens (strain ATCC 14718 / DSM 1338 / AM1) [Complete proteome] [HAMAP]
Taxonomic identifier272630 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium

Protein attributes

Sequence length343 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

May be involved in the regulation of formation of active methanol dehydrogenase.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the MoxR family.

Ontologies

Keywords
   Biological processMethanol utilization
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processmethanol metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 343343Protein MoxR
PRO_0000096543

Regions

Nucleotide binding53 – 608ATP Potential

Experimental info

Sequence conflict1921Missing in CAA69191. Ref.1
Sequence conflict255 – 26511GPAGIRLPGIA → APPHPLARHR in CAA69191. Ref.1
Sequence conflict3271Q → E in CAA69191. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P30621 [UniParc].

Last modified September 22, 2009. Version 3.
Checksum: 7019BABA2856D94F

FASTA34338,614
        10         20         30         40         50         60 
MNTLRPGDAM LTDWRDAAAR FEREIAKAVV GQDRAIRLLT IAIFARGHVM LEGDVGVGKT 

        70         80         90        100        110        120 
TLLRAVARGL GGAYERVEGT VDMMPTDLIY HTYLGEDGRP RVEPGPVLRR AEDLSVFFFN 

       130        140        150        160        170        180 
EINRARPQVH ALLLRIMAER SVSAFNREYR FPNLQVFADR NRVEREETFE LPAAARDRFL 

       190        200        210        220        230        240 
MEIGMEAPRD ARARRDLVFD PRFHDTDRLT EEVEAGVLDF ERIGTIASAI QHAISAEPAI 

       250        260        270        280        290        300 
EAYVVGLWEA LVRPGPAGIR LPGIAMDRLV QGGASPRGVA FLVRAARVRA WLEGRDWLVP 

       310        320        330        340 
EDIRAVFPEV MAHRVFLEPV YEMRRAQIVP DLIRAVFETV PAP 

« Hide

References

« Hide 'large scale' references
[1]"The methanol oxidation genes mxaFJGIR (S) ACKLD in Methylobacterium extorquens."
Amaratunga K., Goodwin P.M., O'Connor C.D., Anthony C.
FEMS Microbiol. Lett. 146:31-38(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Erratum
Amaratunga K., Goodwin P.M., O'Connor C.D., Anthony C.
FEMS Microbiol. Lett. 150:175-177(1997) [PubMed] [Europe PMC] [Abstract]
[3]"Methylobacterium genome sequences: a reference blueprint to investigate microbial metabolism of C1 compounds from natural and industrial sources."
Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y., Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W., Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E. expand/collapse author list , Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D., Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J., Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C., Lidstrom M.E.
PLoS ONE 4:E5584-E5584(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14718 / DSM 1338 / AM1.
[4]"The second subunit of methanol dehydrogenase of Methylobacterium extorquens AM1."
Nunn D.N., Day D., Anthony C.
Biochem. J. 260:857-862(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y07864 Genomic DNA. Translation: CAA69191.1.
CP001510 Genomic DNA. Translation: ACS42165.1.
X15792 Genomic DNA. No translation available.
RefSeqYP_002965442.1. NC_012808.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP30621.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS42165; ACS42165; MexAM1_META1p4534.
GeneID7994320.
KEGGmea:Mex_1p4534.
PATRIC22514711. VBIMetExt101010_4410.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0714.
HOGENOMHOG000236943.
OMAMAHRVFL.
OrthoDBEOG65J4ZT.

Enzyme and pathway databases

BioCycMEXT272630:GBY6-4279-MONOMER.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR011703. ATPase_AAA-3.
IPR016366. ATPase_chaperone_AAA_MoxR_prd.
IPR001270. ClpA/B.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF07726. AAA_3. 1 hit.
[Graphical view]
PIRSFPIRSF002849. AAA_ATPase_chaperone_MoxR_prd. 1 hit.
PRINTSPR00300. CLPPROTEASEA.
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
ProtoNetSearch...

Entry information

Entry nameMOXR_METEA
AccessionPrimary (citable) accession number: P30621
Secondary accession number(s): C5AQA5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: September 22, 2009
Last modified: June 11, 2014
This is version 70 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families