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Database: UniProt/TrEMBL
Entry: B1Y6Z9_LEPCP
LinkDB: B1Y6Z9_LEPCP
Original site: B1Y6Z9_LEPCP 
ID   B1Y6Z9_LEPCP            Unreviewed;       473 AA.
AC   B1Y6Z9;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   29-OCT-2014, entry version 37.
DE   SubName: Full=D-lactate dehydrogenase (Cytochrome) {ECO:0000313|EMBL:ACB32477.1};
DE            EC=1.1.2.4 {ECO:0000313|EMBL:ACB32477.1};
GN   OrderedLocusNames=Lcho_0202 {ECO:0000313|EMBL:ACB32477.1};
OS   Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS   discophora (strain SP-6)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Leptothrix.
OX   NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB32477.1, ECO:0000313|Proteomes:UP000001693};
RN   [1] {ECO:0000313|EMBL:ACB32477.1, ECO:0000313|Proteomes:UP000001693}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51168 / LMG 8142 / SP-6
RC   {ECO:0000313|Proteomes:UP000001693};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT   "Complete sequence of Leptothrix cholodnii SP-6.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains FAD-binding PCMH-type domain.
CC       {ECO:0000256|SAAS:SAAS00083646}.
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DR   EMBL; CP001013; ACB32477.1; -; Genomic_DNA.
DR   RefSeq; WP_012345239.1; NC_010524.1.
DR   RefSeq; YP_001789242.1; NC_010524.1.
DR   ProteinModelPortal; B1Y6Z9; -.
DR   STRING; 395495.Lcho_0202; -.
DR   EnsemblBacteria; ACB32477; ACB32477; Lcho_0202.
DR   GeneID; 6161411; -.
DR   KEGG; lch:Lcho_0202; -.
DR   PATRIC; 22390673; VBILepCho83238_0206.
DR   eggNOG; COG0277; -.
DR   HOGENOM; HOG000230995; -.
DR   KO; K00102; -.
DR   OMA; GQGFEWA; -.
DR   OrthoDB; EOG6RZB40; -.
DR   BioCyc; LCHO395495:GHYL-202-MONOMER; -.
DR   GO; GO:0004458; F:D-lactate dehydrogenase (cytochrome) activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:InterPro.
DR   Gene3D; 1.10.45.10; -; 1.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
DR   InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2.
DR   InterPro; IPR016166; FAD-bd_2.
DR   InterPro; IPR016167; FAD-bd_2_sub1.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR004113; FAD-linked_oxidase_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF55103; SSF55103; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001693};
KW   Oxidoreductase {ECO:0000313|EMBL:ACB32477.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001693}.
SQ   SEQUENCE   473 AA;  50940 MW;  B9A9851474E9546B CRC64;
     MNAPHSHDWQ PAIRPRPMPA AMREQLQQRF GSRLSTAQAV RDQHGRDESP YDTAAPEAVL
     FCESNEDVAA AVAIAHEHAV PVIPFGVGSS LEGHLLAVQG GLSLDLSRMN RILSLNPEDL
     TVTVQAGVTR MQLNNEIRHS GLFFPIDPGA DATLGGMSAT RASGTNAVRY GTMRENVLAL
     TVVTASGELV HTGTRARKSS AGYDLTRLFV GSEGTLGVMT EITLKLYPLP EAVLAAICHF
     PSIAAAVDTT IGLIQMGVPI ARCELIDART VGMVNRHNKL DLREQDMLLM EFHGSPASVR
     EQAETVQALA AENGGESFEW AETPEERTRL WTARHHAYFA AVQSRPGCRA ISTDTCVPIS
     RLAECIVDTV ADVDACGLPY FLVGHVGDGN FHIGFLIDPD SPDEGRIAEQ VNRTLVARAL
     QMAGTCTGEH GIGLHKMGFL LDEAGPGAVA LMRQIKHALD PKNIMNPGKI FAW
//
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