ID B6JB59_OLICO Unreviewed; 469 AA.
AC B6JB59;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 01-MAY-2013, entry version 33.
DE SubName: Full=D-lactate dehydrogenase;
DE EC=1.1.2.4;
GN Name=dld; OrderedLocusNames=OCA5_c27030, OCAR_5269;
OS Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Bradyrhizobiaceae; Oligotropha.
OX NCBI_TaxID=504832;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49405 / DSM 1227 / OM5 [Mississippi], and OM5;
RX PubMed=18539730; DOI=10.1128/JB.00614-08;
RA Paul D., Bridges S., Burgess S.C., Dandass Y., Lawrence M.L.;
RT "Genome sequence of the chemolithoautotrophic bacterium Oligotropha
RT carboxidovorans OM5T.";
RL J. Bacteriol. 190:5531-5532(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49405 / DSM 1227 / OM5, and OM5;
RX PubMed=21742883; DOI=10.1128/JB.05619-11;
RA Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G.,
RA Meyer O.;
RT "Complete Genome Sequences of the Chemolithoautotrophic Oligotropha
RT carboxidovorans Strains OM4 and OM5.";
RL J. Bacteriol. 193:5043-5043(2011).
CC -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain.
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DR EMBL; CP001196; ACI92401.1; -; Genomic_DNA.
DR EMBL; CP002826; AEI07397.1; -; Genomic_DNA.
DR RefSeq; YP_002288265.1; NC_011386.1.
DR RefSeq; YP_004633638.1; NC_015684.1.
DR STRING; 504832.OCAR_5269; -.
DR EnsemblBacteria; ACI92401; ACI92401; OCAR_5269.
DR EnsemblBacteria; AEI07397; AEI07397; OCA5_c27030.
DR GeneID; 10847835; -.
DR GeneID; 6991255; -.
DR KEGG; oca:OCAR_5269; -.
DR KEGG; ocg:OCA5_c27030; -.
DR PATRIC; 22804465; VBIOliCar134280_1203.
DR eggNOG; COG0277; -.
DR HOGENOM; HOG000230995; -.
DR KO; K00102; -.
DR OMA; HDAYWSV; -.
DR ProtClustDB; CLSK820212; -.
DR BioCyc; OCAR504832:GJPZ-2703-MONOMER; -.
DR GO; GO:0004458; F:D-lactate dehydrogenase (cytochrome) activity; IEA: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; FAD-binding_2; 1.
DR SUPFAM; SSF56176; FAD-binding_2; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW Complete proteome; Oxidoreductase.
SQ SEQUENCE 469 AA; 50575 MW; D457B21230CB2444 CRC64;
MTTTTAPRVS PQTLSNAFET LATRFQRDFF TSQSQREQHS HTTTWIAPQL PDAVVLVRSV
ADIQDAVRIC ARHRLPIVPF GAGTSLEGQV NAPFGGISLD LREMNRVLAV HSEDLDCVIE
PGITRKTLNE NLRDQGLFFP IDPGADATLG GMASTRASGT NAVRYGTVRD NVLALKVVRG
DGEIITTGTR AKKSSAGYDL THLFIGAEGT LGIICEMTMR LRGIPQSIAA ASCSFGSVKG
ACDATILAIQ SGIPLARIEL LNAAQVAACN AYSKLTLPLT PLLLLEFHGS EAEVAEQSSA
FAEIAKDCGG GAFEWTTRAE DRTRLWQARH DAYWAAAAIR PGSRPMSTDV CVPISRLADC
VSETEHDIER FKLIAPIVGH VGDGNFHCLM LCDVNDPDEV ARGHEFVHRL AERAHRMDGT
CTGEHGIGQG KQDYLVPELG PEAIEAMRAI KKALDPNGIF NPGKIFPLP
//