ID   LA2M_MYCSM              Reviewed;         394 AA.
AC   P21795;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 55.
DE   RecName: Full=Lactate 2-monooxygenase;
DE            EC=1.13.12.4;
DE   AltName: Full=Lactate oxidase;
OS   Mycobacterium smegmatis.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=1772;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=90216683; PubMed=2324094;
RA   Giegel D.A., Williams C.H. Jr., Massey V.;
RT   "L-lactate 2-monooxygenase from Mycobacterium smegmatis. Cloning,
RT   nucleotide sequence, and primary structure homology within an enzyme
RT   family.";
RL   J. Biol. Chem. 265:6626-6632(1990).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=87194765; PubMed=3571231;
RA   Giegel D.A., Massey V., Williams C.H. Jr.;
RT   "L-lactate-2-monooxygenase. Sequence of peptides containing residues
RT   modified by 1-fluoro-2,4-dinitrobenzene.";
RL   J. Biol. Chem. 262:5705-5710(1987).
CC   -!- CATALYTIC ACTIVITY: (S)-lactate + O(2) = acetate + CO(2) + H(2)O.
CC   -!- COFACTOR: FMN.
CC   -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC       dehydrogenase family.
CC   -!- SIMILARITY: Contains 1 FMN hydroxy acid dehydrogenase domain.
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DR   EMBL; J05402; AAA60429.1; -; Genomic_DNA.
DR   PIR; A35745; A35745.
DR   HSSP; P05414; 1GOX.
DR   BRENDA; 1.13.12.4; 259.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0050040; F:lactate 2-monooxygenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR012133; a-Hydoxy_acid_DH_FMN.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000262; FMN-dep_DH.
DR   InterPro; IPR017934; FMN-dep_OHA_DH.
DR   InterPro; IPR008259; FMN_hydac_DH_AS.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   Pfam; PF01070; FMN_dh; 1.
DR   PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1.
DR   PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1.
DR   PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Flavoprotein; FMN; Monooxygenase;
KW   Oxidoreductase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    394       Lactate 2-monooxygenase.
FT                                /FTId=PRO_0000206326.
FT   DOMAIN       19    394       FMN hydroxy acid dehydrogenase.
FT   NP_BIND     321    345       FMN (By similarity).
FT   ACT_SITE    291    291       Proton acceptor (By similarity).
FT   BINDING      45     45       Substrate (Potential).
FT   BINDING     129    129       FMN (By similarity).
FT   BINDING     151    151       FMN (By similarity).
FT   BINDING     153    153       Substrate (By similarity).
FT   BINDING     179    179       FMN (By similarity).
FT   BINDING     188    188       Substrate (By similarity).
FT   BINDING     267    267       FMN (By similarity).
FT   BINDING     294    294       Substrate (Potential).
SQ   SEQUENCE   394 AA;  42747 MW;  D535A910E7F7232A CRC64;
     MSNWGDYENE IYGQGLVGVA PTLPMSYADW EAHAQQALPP GVLSYVAGGS GDEHTQRANV
     EAFKHWGLMP RMLMAATERD LSVELWGKTW AAPMFFAPIG VIALCAQDGH GDAASAQASA
     RTGVPYITST LAVSSLEDIR KHAGDTPAYF QLYYPEDRDL AESFIRRAEE AGYDGLVITL
     DTWIFGWRPR DLTISNFPFL RGLCLTNYVT DPVFQKKFKA HSGVEAEGLR DNPRLAADFW
     HGLFGHSVTW EDIDWVRSIT KMPVILKGIQ HPDDARRAVD SGVDGIYCSN HGGRQANGGL
     PALDCLPEVV KASGDTPVLF DSGIRTGADV VKALAMGASA VGIGRPYAWG AALGGSKGIE
     HVARSLLAEA DLIMAVDGYR NLKELTIDAL RPTR
//