ID   LLDD_CHRSD              Reviewed;         392 AA.
AC   Q1R0J2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=L-lactate dehydrogenase [cytochrome];
DE            EC=1.1.2.3;
GN   Name=lldD; OrderedLocusNames=Csal_0404;
OS   Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB
OS   13768).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Chromohalobacter.
OX   NCBI_TaxID=290398;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N.,
RA   O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R.,
RA   Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D.,
RA   Canovas D., Richardson P.;
RT   "Complete sequence of Chromohalobacter salexigens DSM 3043.";
RL   Submitted (MAR-2006) 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; CP000285; ABE57766.1; -; Genomic_DNA.
DR   RefSeq; YP_572465.1; -.
DR   GeneID; 4025998; -.
DR   GenomeReviews; CP000285_GR; Csal_0404.
DR   KEGG; csa:Csal_0404; -.
DR   NMPDR; fig|290398.4.peg.512; -.
DR   HOGENOM; Q1R0J2; -.
DR   OMA; Q1R0J2; NFDPSIG.
DR   BioCyc; CSAL290398:CSAL_0404-MON; -.
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; 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   3: Inferred from homology;
KW   Complete proteome; Flavoprotein; FMN; Oxidoreductase.
FT   CHAIN         1    392       L-lactate dehydrogenase [cytochrome].
FT                                /FTId=PRO_1000068977.
FT   DOMAIN        1    380       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   392 AA;  42414 MW;  631A171A271F1091 CRC64;
     MIISASTDYR HAAKRRLPPF LFHYADGGAY AEHTLRRNVE DLAGIALRQR VLKDMSHLSL
     ETELFGEPLA MPVALAPVGL AGMYARRGEV QAARAAASKG IPFTLSTVSV CPIAEVASAI
     ERPLWFQLYV LRDRGFMKHV LERAKAAGVK TLVFTVDMPV PGARYRDAHS GMSGKHGGLR
     RMLQAVTHPS WAWDVGLHGR PHDLGNVSDY RGQPTELEDY IAWLGNNFDP SISWKDLEWI
     REFWDGPMII KGILDPEDAR DAVRFGADGI VVSNHGGRQL DGVPSTARAL PAIADAVKGD
     LAILADSGVR NGLDVVRMIA MGADTILLGR AYIYALATAG EAGVAHLLEL FEKEMRVAMT
     LTGARSIAEL GSDSLVTGSA AASIERTLSP SL
//