ID   LLDD_XANCP              Reviewed;         386 AA.
AC   Q8PE75;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 41.
DE   RecName: Full=L-lactate dehydrogenase [cytochrome];
DE            EC=1.1.2.3;
GN   Name=lldD; OrderedLocusNames=XCC0106;
OS   Xanthomonas campestris pv. campestris.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=340;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / NCPPB 528 / LMG 568;
RX   MEDLINE=22022145; PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A.,
RA   Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
RA   Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
RA   Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
RA   El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
RA   Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
RA   Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F.,
RA   Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
RA   Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
RA   Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
RA   Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
RA   Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
RA   Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
RA   Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing
RT   host specificities.";
RL   Nature 417:459-463(2002).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE012105; AAM39425.1; -; Genomic_DNA.
DR   RefSeq; NP_635501.1; -.
DR   HSSP; P05414; 1GOX.
DR   GeneID; 1002315; -.
DR   GenomeReviews; AE008922_GR; XCC0106.
DR   KEGG; xcc:XCC0106; -.
DR   HOGENOM; Q8PE75; -.
DR   OMA; Q8PE75; ARYRDMH.
DR   BioCyc; XCAM190485:XCC0106-MON; -.
DR   BRENDA; 1.1.2.3; 281360.
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    386       L-lactate dehydrogenase [cytochrome].
FT                                /FTId=PRO_0000206355.
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   386 AA;  41622 MW;  5B3E3BD0B59E46C8 CRC64;
     MIISAASDYR AAAEARLPPF LFHYIDGGAY AEHTLRRNVS DLADIALRQR VLRNMSDLSL
     STELFGETLA MPVALAPVGL TGMYARRGEV QAARAAAARG IPFTLSTVSV CPIEEVAPAI
     DRPMWFQLYV LKDRGFMRNA LERAKTAGVT TLVFTVDMPT PGARYRDAHS GMSGPNASLR
     RMLQAMTHPR WAWDVGLLGK PHDLGNISTY RGSPTGLQDY IGWLAANFDP SISWKDLEWI
     REFWTGPMVI KGILDPEDAR DAVRFGADGI VVSNHGGRQL DGVLSSARAL PAIADAVKGE
     LKILADSGIR SGLDVVRMLA LGADAVLLGR AFVYALAAGG QAGVENLLTL IEREMRVAMI
     LTGTHSVAEI SGDALSRVTR EAAVVP
//