ID   LLDD_SALPA              Reviewed;         396 AA.
AC   Q5PLQ7;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   16-JUN-2009, entry version 33.
DE   RecName: Full=L-lactate dehydrogenase [cytochrome];
DE            EC=1.1.2.3;
GN   Name=lldD; Synonyms=lctD; OrderedLocusNames=SPA3546;
OS   Salmonella paratyphi A.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=54388;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P.,
RA   Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M.,
RA   Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G.,
RA   Kohlberg S., Strong C., Du F., Carter J., Kremizki C., Layman D.,
RA   Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P.,
RA   Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L.,
RA   Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV79347.1; -; Genomic_DNA.
DR   RefSeq; YP_152659.1; -.
DR   GeneID; 3175919; -.
DR   GenomeReviews; CP000026_GR; SPA3546.
DR   KEGG; spt:SPA3546; -.
DR   NMPDR; fig|295319.3.peg.2695; -.
DR   HOGENOM; Q5PLQ7; -.
DR   OMA; Q5PLQ7; ARYRDMH.
DR   BioCyc; SENT295319:SPA3546-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    396       L-lactate dehydrogenase [cytochrome].
FT                                /FTId=PRO_0000206345.
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   396 AA;  42700 MW;  1CFC8958AEB781CA CRC64;
     MIISAASDYR AAAQRTLPPF LFHYIDGGAY AEYTLRRNVE DLSQVALRQR VLKNMSDLSL
     ETTLFNETLS MPVALAPVGL CGMYARRGEV QAAAAADAKG IPFTLSTVSV CPIEEVAPTI
     QRPMWFQLYV LRDRGFMRNA LERAKAAGCS TLVFTVDMPT PGARYRDAHS GMSGPNAAMR
     RYWQAVMHPK WAWDVGLNGR PHDLGNISAY LGKPTGLEDY IGWLANNFDP SISWKDLEWI
     REFWDGPMVI KGILDPEDAR DAVRFGADGI VVSNHGGRQL DGVLSSARAL PAIADAVKGD
     IAILADSGIR NGLDVVRMIA LGADTVLLGR AYLYALATAG KAGVANLLDL VEKEMKVAMT
     LTGAKSISEI SGDSLVQELG KSLPAALAPM SKGDAA
//