ID LLDD_ECOUT Reviewed; 396 AA. AC Q1R4Z0; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 16-JUN-2009, entry version 26. DE RecName: Full=L-lactate dehydrogenase [cytochrome]; DE EC=1.1.2.3; GN Name=lldD; OrderedLocusNames=UTI89_C4146; OS Escherichia coli (strain UTI89 / UPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=364106; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16585510; DOI=10.1073/pnas.0600938103; RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., RA Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., RA Hultgren S.J., Gordon J.I.; RT "Identification of genes subject to positive selection in RT uropathogenic strains of Escherichia coli: a comparative genomics RT approach."; RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006). 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; CP000243; ABE09574.1; -; Genomic_DNA. DR RefSeq; YP_543105.1; -. DR GeneID; 3989607; -. DR GenomeReviews; CP000243_GR; UTI89_C4146. DR KEGG; eci:UTI89_C4146; -. DR HOGENOM; Q1R4Z0; -. DR OMA; Q1R4Z0; ARYRDMH. DR BioCyc; ECOL364106:UTI89_C4146-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_1000068983. 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; 42770 MW; A4367FA59716513F CRC64; MIISAASDYR AAAQRILPPF LFHYMDGGAY SEYTLRRNVE DLSEVALRQR ILKNMSDLSL ETTLFNEKLS MPVALGPVGL CGMYARRGEV QAAKAADAHG IPFTLSTVSV CPIEEVAPAI KRPMWFQLYV LRDRGFMRNA LERAKAAGCS TLVFTVDMPT PGARYRDAHS GMSGPNAAMR RYLQAVTHPQ WAWDVGLNGR PHDLGNISAY LGKPTGLEDY IGWLANNFDP SISWKDLEWI RDFWDGPMVI KGILDPEDAR DAVRFGADGI VVSNHGGRQL DGVLSSARAL PAIADAVKGD IAILADSGIR NGLDVVRMIA LGADTVLLGR AFLYALATAG QAGVANLLNL IEKEMKVAMT LTGAKSISEI TQDSLVQVLG KELPAALAPM AKGNAA //