ID   LLDD_BARQU              Reviewed;         383 AA.
AC   Q6G0J2;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-NOV-2008, entry version 32.
DE   RecName: Full=L-lactate dehydrogenase [cytochrome];
DE            EC=1.1.2.3;
GN   Name=lldD; OrderedLocusNames=BQ02590;
OS   Bartonella quintana (Rochalimaea quintana).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=803;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Toulouse;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic
RT   derivative of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(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; BX897700; CAF25762.1; -; Genomic_DNA.
DR   RefSeq; YP_031962.1; -.
DR   GeneID; 2867178; -.
DR   GenomeReviews; BX897700_GR; BQ02590.
DR   KEGG; bqu:BQ02590; -.
DR   NMPDR; fig|283165.1.peg.232; -.
DR   HOGENOM; Q6G0J2; -.
DR   BioCyc; BQUI283165:BQ02590-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; 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   Complete proteome; Flavoprotein; FMN; Oxidoreductase.
FT   CHAIN         1    383       L-lactate dehydrogenase [cytochrome].
FT                                /FTId=PRO_0000206332.
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   383 AA;  42094 MW;  53E7E179EED53120 CRC64;
     MIISSTFDYR KAAKRRLPPF LFHYIDGGAY AEETMRRNYA DLQALALRQR ILRQVGEVDL
     SIKLFDQRLN LPIVLAPVGL TGMYARRGEV KAARAAVAKG IPFTLSSVSV CSLAEVHAEV
     GSGFWFQLYV LKDRGFMRDV LERSWLAGVR TLVFTVDMPV PGARYRDAHS GMSGPYAGLR
     RILQAVVHPH WAWNVGIMGR PHDLGNVSTY LQKKITLEDY VGWLGANFDP SIGWSDLQWI
     RDFWKGKMIL KGILDPQDAR EAVQFGADGI VVSNHGGRQL DGVLSTARAL PAIAEVVTGD
     LTILADSGVR SGLDVVRMIA QGADAVMIGR AFIYALAAAG EKGVMHLLDL FANEMRVAMT
     LTGVRAVKEI THESLASTDA LNQ
//