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P21795 (LA2M_MYCSM) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 68. 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:
Lactate 2-monooxygenase

EC=1.13.12.4
Alternative name(s):
Lactate oxidase
OrganismMycobacterium smegmatis
Taxonomic identifier1772 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

(S)-lactate + O2 = acetate + CO2 + H2O.

Cofactor

FMN.

Sequence similarities

Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family.

Contains 1 FMN hydroxy acid dehydrogenase domain.

Ontologies

Keywords
   LigandFlavoprotein
FMN
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Molecular_functionFMN binding

Inferred from electronic annotation. Source: InterPro

lactate 2-monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 394393Lactate 2-monooxygenase
PRO_0000206326

Regions

Domain19 – 394376FMN hydroxy acid dehydrogenase
Nucleotide binding321 – 34525FMN By similarity

Sites

Active site2911Proton acceptor By similarity
Binding site451Substrate Potential
Binding site1291FMN By similarity
Binding site1511FMN By similarity
Binding site1531Substrate By similarity
Binding site1791FMN By similarity
Binding site1881Substrate By similarity
Binding site2671FMN By similarity
Binding site2941Substrate Potential

Sequences

Sequence LengthMass (Da)Tools
P21795 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: D535A910E7F7232A

FASTA39442,747
        10         20         30         40         50         60 
MSNWGDYENE IYGQGLVGVA PTLPMSYADW EAHAQQALPP GVLSYVAGGS GDEHTQRANV 

        70         80         90        100        110        120 
EAFKHWGLMP RMLMAATERD LSVELWGKTW AAPMFFAPIG VIALCAQDGH GDAASAQASA 

       130        140        150        160        170        180 
RTGVPYITST LAVSSLEDIR KHAGDTPAYF QLYYPEDRDL AESFIRRAEE AGYDGLVITL 

       190        200        210        220        230        240 
DTWIFGWRPR DLTISNFPFL RGLCLTNYVT DPVFQKKFKA HSGVEAEGLR DNPRLAADFW 

       250        260        270        280        290        300 
HGLFGHSVTW EDIDWVRSIT KMPVILKGIQ HPDDARRAVD SGVDGIYCSN HGGRQANGGL 

       310        320        330        340        350        360 
PALDCLPEVV KASGDTPVLF DSGIRTGADV VKALAMGASA VGIGRPYAWG AALGGSKGIE 

       370        380        390 
HVARSLLAEA DLIMAVDGYR NLKELTIDAL RPTR 

« Hide

References

[1]"L-lactate 2-monooxygenase from Mycobacterium smegmatis. Cloning, nucleotide sequence, and primary structure homology within an enzyme family."
Giegel D.A., Williams C.H. Jr., Massey V.
J. Biol. Chem. 265:6626-6632(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"L-lactate-2-monooxygenase. Sequence of peptides containing residues modified by 1-fluoro-2,4-dinitrobenzene."
Giegel D.A., Massey V., Williams C.H. Jr.
J. Biol. Chem. 262:5705-5710(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05402 Genomic DNA. Translation: AAA60429.1.
PIRA35745.

3D structure databases

ProteinModelPortalP21795.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR012133. Alpha-hydoxy_acid_DH_FMN.
IPR000262. FMN-dep_DH.
IPR008259. FMN_hydac_DH_AS.
[Graphical view]
PfamPF01070. FMN_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000138. Al-hdrx_acd_dh. 1 hit.
PROSITEPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLA2M_MYCSM
AccessionPrimary (citable) accession number: P21795
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 68 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