ID   LLDD_ALCFA              Reviewed;         379 AA.
AC   Q6WB83;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-NOV-2008, entry version 28.
DE   RecName: Full=L-lactate dehydrogenase [cytochrome];
DE            EC=1.1.2.3;
GN   Name=lldD;
OS   Alcaligenes faecalis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Alcaligenes.
OX   NCBI_TaxID=511;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CCUG 2071 / LMG 3368 / NCIB 8687;
RA   Silver S., Phung L.T., Malo B.J.;
RT   "Genes for arsenite oxidation from Alcaligenes faecalis.";
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: (S)-lactate + 2 ferricytochrome c = pyruvate +
CC       2 ferrocytochrome c + 2 H(+).
CC   -!- COFACTOR: FMN (By similarity).
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; AY297781; AAQ19817.1; -; Genomic_DNA.
DR   HSSP; P05414; 1AL8.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0004460; F:L-lactate dehydrogenase (cytochrome) activity; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01559; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR012133; Alpha_OHA_DHase_FMN.
DR   InterPro; IPR008259; FMN_hydac_DHase_AS.
DR   InterPro; IPR000262; FMN_OHA_DHase.
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   3: Inferred from homology;
KW   Flavoprotein; FMN; Oxidoreductase.
FT   CHAIN         1    379       L-lactate dehydrogenase [cytochrome].
FT                                /FTId=PRO_0000206330.
FT   DOMAIN        1    379       FMN hydroxy acid dehydrogenase.
FT   NP_BIND     306    330       FMN (By similarity).
FT   ACT_SITE    275    275       Proton acceptor (By similarity).
FT   BINDING      24     24       Substrate (Potential).
FT   BINDING     106    106       FMN (By similarity).
FT   BINDING     127    127       FMN (By similarity).
FT   BINDING     129    129       Substrate (By similarity).
FT   BINDING     155    155       FMN (By similarity).
FT   BINDING     164    164       Substrate (By similarity).
FT   BINDING     251    251       FMN (By similarity).
FT   BINDING     278    278       Substrate (Potential).
SQ   SEQUENCE   379 AA;  41414 MW;  9975D092C4DDF2F9 CRC64;
     MIISSSTDYR RAAQKRLPPF LFHYIDGGAY AEHTLRRNVD DLAEVALRQR VLKDMSQLDT
     SIDLFGEKLS MPVALSPVGL TGMYARRGEV QAARAADARG IPFTMSSVSV CPIEEVAPRL
     SRPMWFQLYV LKDRGFMRNA LERAQAAGCS TLVFTVDMPV PGARYRDAHS GMSGPNAALR
     RYAQAVMHPR WAWDVGLLGR PHDLGNISRY LGKPTGLEDY MGYLGANFDP SISWKDLEWI
     REFWKGPMLI KGILDPDDAR DAVRFGADGI IVSNHGGRQL DGVLSSARAL PAIADAVKGQ
     IKILADSGIR SGLDVVRMIA LGADAAMLGR AYIYALAAAG QSGVDHLLGL IEKEIRVAMT
     LTSVSSISQI TSELLVREP
//