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P21795

- LA2M_MYCSM

UniProt

P21795 - LA2M_MYCSM

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Protein
Lactate 2-monooxygenase
Gene
N/A
Organism
Mycobacterium smegmatis
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

FMN.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei45 – 451Substrate Reviewed prediction
Binding sitei129 – 1291FMN By similarity
Binding sitei151 – 1511FMN By similarity
Binding sitei153 – 1531Substrate By similarity
Binding sitei179 – 1791FMN By similarity
Binding sitei188 – 1881Substrate By similarity
Binding sitei267 – 2671FMN By similarity
Active sitei291 – 2911Proton acceptor By similarity
Binding sitei294 – 2941Substrate Reviewed prediction

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi321 – 34525FMN By similarity
Add
BLAST

GO - Molecular functioni

  1. FMN binding Source: InterPro
  2. lactate 2-monooxygenase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Ligandi

    Flavoprotein, FMN

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lactate 2-monooxygenase (EC:1.13.12.4)
    Alternative name(s):
    Lactate oxidase
    OrganismiMycobacterium smegmatis
    Taxonomic identifieri1772 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 394393Lactate 2-monooxygenase
    PRO_0000206326Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP21795.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini19 – 394376FMN hydroxy acid dehydrogenase
    Add
    BLAST

    Sequence similaritiesi

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR012133. Alpha-hydoxy_acid_DH_FMN.
    IPR000262. FMN-dep_DH.
    IPR008259. FMN_hydac_DH_AS.
    [Graphical view]
    PfamiPF01070. FMN_dh. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000138. Al-hdrx_acd_dh. 1 hit.
    PROSITEiPS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
    PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P21795-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNWGDYENE IYGQGLVGVA PTLPMSYADW EAHAQQALPP GVLSYVAGGS    50
    GDEHTQRANV EAFKHWGLMP RMLMAATERD LSVELWGKTW AAPMFFAPIG 100
    VIALCAQDGH GDAASAQASA RTGVPYITST LAVSSLEDIR KHAGDTPAYF 150
    QLYYPEDRDL AESFIRRAEE AGYDGLVITL DTWIFGWRPR DLTISNFPFL 200
    RGLCLTNYVT DPVFQKKFKA HSGVEAEGLR DNPRLAADFW HGLFGHSVTW 250
    EDIDWVRSIT KMPVILKGIQ HPDDARRAVD SGVDGIYCSN HGGRQANGGL 300
    PALDCLPEVV KASGDTPVLF DSGIRTGADV VKALAMGASA VGIGRPYAWG 350
    AALGGSKGIE HVARSLLAEA DLIMAVDGYR NLKELTIDAL RPTR 394
    Length:394
    Mass (Da):42,747
    Last modified:January 23, 2007 - v3
    Checksum:iD535A910E7F7232A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05402 Genomic DNA. Translation: AAA60429.1.
    PIRiA35745.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05402 Genomic DNA. Translation: AAA60429.1 .
    PIRi A35745.

    3D structure databases

    ProteinModelPortali P21795.
    ModBasei Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR012133. Alpha-hydoxy_acid_DH_FMN.
    IPR000262. FMN-dep_DH.
    IPR008259. FMN_hydac_DH_AS.
    [Graphical view ]
    Pfami PF01070. FMN_dh. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000138. Al-hdrx_acd_dh. 1 hit.
    PROSITEi PS00557. FMN_HYDROXY_ACID_DH_1. 1 hit.
    PS51349. FMN_HYDROXY_ACID_DH_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiLA2M_MYCSM
    AccessioniPrimary (citable) accession number: P21795
    Entry historyi
    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 statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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