(data stored in SCRATCH zone)

SWISSPROT: Q145G8_PARXL

ID   Q145G8_PARXL            Unreviewed;       497 AA.
AC   Q145G8;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 85.
DE   SubName: Full=D-lactate dehydrogenase (Cytochrome) {ECO:0000313|EMBL:ABE29021.1};
DE            EC=1.1.3.15 {ECO:0000313|EMBL:ABE29021.1};
GN   ORFNames=Bxe_A3978 {ECO:0000313|EMBL:ABE29021.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE29021.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE29021.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE29021.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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DR   EMBL; CP000270; ABE29021.1; -; Genomic_DNA.
DR   RefSeq; WP_011486844.1; NZ_CP008760.1.
DR   STRING; 266265.Bxe_A3978; -.
DR   EnsemblBacteria; ABE29021; ABE29021; Bxe_A3978.
DR   GeneID; 4004615; -.
DR   KEGG; bxb:DR64_1654; -.
DR   KEGG; bxe:Bxe_A3978; -.
DR   PATRIC; fig|266265.5.peg.511; -.
DR   eggNOG; ENOG4105CQB; Bacteria.
DR   eggNOG; COG0277; LUCA.
DR   HOGENOM; HOG000230998; -.
DR   KO; K00104; -.
DR   OMA; EFMDKPA; -.
DR   OrthoDB; 1188552at2; -.
DR   BioCyc; BXEN266265:BXE_RS02420-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 1.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0052853; F:long-chain-(S)-2-hydroxy-long-chain-acid oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052854; F:medium-chain-(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052852; F:very-long-chain-(S)-2-hydroxy-acid oxidase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR004113; FAD-linked_oxidase_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
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;
DR   PRODOM; Q145G8.
DR   SWISS-2DPAGE; Q145G8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Oxidoreductase {ECO:0000313|EMBL:ABE29021.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN       50    228       FAD-binding PCMH-type.
FT                                {ECO:0000259|PROSITE:PS51387}.
SQ   SEQUENCE   497 AA;  53682 MW;  E28742D309361F3D CRC64;
     MNAPAELTAE VLAQRQREVV QALMAVLPTH CLLYREEDTV AYECDGLAAY RRLPLAVALP
     ETESQVQRIV QICHRLDVPI VPRGAGTGLS GGAMPIRHGV VVSLARLRKI VEVDSYARTA
     TVQPGVRNLS ISEAAAPYGL YYAPDPSSQI ACTIGGNVSE NSGGVHCLKY GLTVHNVLRV
     RAVTMEGEIV EFGSLAPDAP GLDLLAVLIG SEGMFAIVTE VTVKLIPKPQ TAQVIMASFD
     DVVKGGDAVA GIIAAGIIPA GLEMMDKPAT RAVEEFVNAG YDLDAAAILL CESDGTPDEV
     ADEIVRMTAV LREHGATRIQ ISRSENERLR FWSGRKNAFP AAGRISPDYY CMDGTVPRRS
     IGPLLTRIEA MEKIYNLRCI NVFHAGDGNM HPLILFNGND RDEWHRAEAF GCDILEACVE
     LGGTVTGEHG VGIEKINSMC VQFSPEERDA FHAVKRAFDA PGLLNPDKGI PTRARCAEYG
     KMHVRGGLLP HPDLPRF
//

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