ID   LLDD_VIBCH              Reviewed;         378 AA.
AC   Q9KKW6;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   16-JUN-2009, entry version 46.
DE   RecName: Full=L-lactate dehydrogenase [cytochrome];
DE            EC=1.1.2.3;
GN   Name=lldD; OrderedLocusNames=VC_A0984;
OS   Vibrio cholerae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961 / Serotype O1;
RX   MEDLINE=20406833; PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A.,
RA   Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L.,
RA   Ermolaeva M.D., Vamathevan J.J., Bass S., Qin H., Dragoi I.,
RA   Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D.,
RA   Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R.,
RA   Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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; AE003853; AAF96880.1; -; Genomic_DNA.
DR   PIR; B82392; B82392.
DR   RefSeq; NP_233368.1; -.
DR   HSSP; P00175; 1LTD.
DR   GeneID; 2612817; -.
DR   GenomeReviews; AE003853_GR; VC_A0984.
DR   KEGG; vch:VCA0984; -.
DR   TIGR; VC_A0984; -.
DR   HOGENOM; Q9KKW6; -.
DR   OMA; Q9KKW6; ARYRDMH.
DR   BRENDA; 1.1.2.3; 19019.
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    378       L-lactate dehydrogenase [cytochrome].
FT                                /FTId=PRO_0000206352.
FT   DOMAIN        1    378       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   378 AA;  41291 MW;  8310DF5B3F217ADC CRC64;
     MIISASTDYR AAAKAKLPPF LFHYIDGGSY GEHTLRRNTD DLADIALRQR VLSDMSELSL
     ETELFGEKMA LPIALSPVGL TGMYARRGEV QAAQAAEAKG IPFTLSTVSV CPIEEVAPSI
     HRPIWFQLYV LKDRGFMKNV LERAKAAGVK NLVFTVDMPV PGARYRDMHS GMSGPNAAMR
     RVLQAMAHPS WAWDVGLLGK PHDLGNISKY RGSPTKLEDY IGWLGANFDP SISWKDLEWI
     RDFWDGPMII KGILDTEDAK DAVRFGADGI VVSNHGGRQL DGVLSTVQAL PAIADAVKGD
     LKILVDSGIR TGLDVVRMLA LGADCTMLGR SFIYALAAQG RAGVENLLDL YEKEMRVAMT
     LTGAKSIAEL SRDSLVKR
//