(data stored in ACNUC29543 zone)

SWISSPROT: B2JRL0_PARP8

ID   B2JRL0_PARP8            Unreviewed;       399 AA.
AC   B2JRL0;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   SubName: Full=L-lactate dehydrogenase (Cytochrome) {ECO:0000313|EMBL:ACC72337.1};
DE            EC=1.1.2.3 {ECO:0000313|EMBL:ACC72337.1};
GN   OrderedLocusNames=Bphy_3174 {ECO:0000313|EMBL:ACC72337.1};
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC72337.1, ECO:0000313|Proteomes:UP000001192};
RN   [1] {ECO:0000313|Proteomes:UP000001192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC   {ECO:0000313|Proteomes:UP000001192};
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A.,
RA   Melkonian R., James E.K., Young J.P., Bena G., Hauser L., Land M.,
RA   Kyrpides N., Bruce D., Chain P., Copeland A., Pitluck S., Woyke T.,
RA   Lizotte-Waniewski M., Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad
RT   host range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000138-2, ECO:0000256|PROSITE-
CC         ProRule:PRU00683};
CC   -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid
CC       dehydrogenase family. {ECO:0000256|PROSITE-ProRule:PRU00683}.
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DR   EMBL; CP001044; ACC72337.1; -; Genomic_DNA.
DR   RefSeq; WP_012402510.1; NC_010623.1.
DR   STRING; 391038.Bphy_3174; -.
DR   EnsemblBacteria; ACC72337; ACC72337; Bphy_3174.
DR   GeneID; 27742866; -.
DR   KEGG; bph:Bphy_3174; -.
DR   eggNOG; ENOG4105DMF; Bacteria.
DR   eggNOG; COG1304; LUCA.
DR   HOGENOM; HOG000217464; -.
DR   KO; K00101; -.
DR   OMA; WHGRAWS; -.
DR   OrthoDB; 1186741at2; -.
DR   BioCyc; BPHY391038:G1GBS-3271-MONOMER; -.
DR   Proteomes; UP000001192; Chromosome 2.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0004460; F:L-lactate dehydrogenase (cytochrome) activity; IEA:UniProtKB-EC.
DR   CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN.
DR   InterPro; IPR000262; FMN-dep_DH.
DR   InterPro; IPR037396; FMN_HAD.
DR   InterPro; IPR008259; FMN_hydac_DH_AS.
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;
DR   PRODOM; B2JRL0.
DR   SWISS-2DPAGE; B2JRL0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001192};
KW   Flavoprotein {ECO:0000256|PROSITE-ProRule:PRU00683};
KW   FMN {ECO:0000256|PIRSR:PIRSR000138-2, ECO:0000256|PROSITE-
KW   ProRule:PRU00683}; Oxidoreductase {ECO:0000313|EMBL:ACC72337.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001192}.
FT   DOMAIN        8    391       FMN hydroxy acid dehydrogenase.
FT                                {ECO:0000259|PROSITE:PS51349}.
FT   NP_BIND     317    341       FMN. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00683}.
FT   NP_BIND     317    321       FMN. {ECO:0000256|PIRSR:PIRSR000138-2}.
FT   ACT_SITE    286    286       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000138-1, ECO:0000256|PROSITE-
FT                                ProRule:PRU00683}.
FT   BINDING      34     34       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000138-2, ECO:0000256|PROSITE-
FT                                ProRule:PRU00683}.
FT   BINDING     116    116       FMN. {ECO:0000256|PIRSR:PIRSR000138-2,
FT                                ECO:0000256|PROSITE-ProRule:PRU00683}.
FT   BINDING     137    137       FMN. {ECO:0000256|PIRSR:PIRSR000138-2,
FT                                ECO:0000256|PROSITE-ProRule:PRU00683}.
FT   BINDING     139    139       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000138-2, ECO:0000256|PROSITE-
FT                                ProRule:PRU00683}.
FT   BINDING     165    165       FMN. {ECO:0000256|PIRSR:PIRSR000138-2,
FT                                ECO:0000256|PROSITE-ProRule:PRU00683}.
FT   BINDING     174    174       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000138-2, ECO:0000256|PROSITE-
FT                                ProRule:PRU00683}.
FT   BINDING     262    262       FMN. {ECO:0000256|PIRSR:PIRSR000138-2,
FT                                ECO:0000256|PROSITE-ProRule:PRU00683}.
FT   BINDING     284    284       FMN. {ECO:0000256|PIRSR:PIRSR000138-2}.
FT   BINDING     289    289       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000138-2, ECO:0000256|PROSITE-
FT                                ProRule:PRU00683}.
FT   BINDING     341    341       FMN. {ECO:0000256|PIRSR:PIRSR000138-2}.
SQ   SEQUENCE   399 AA;  43267 MW;  CF4B54796F8421C6 CRC64;
     MANGAINRRL TGALSIGDLR KLAQRALPRV LFDYVEGGPD DEHGIVHNRE VFNRWALVPR
     YMQDVSDRST ATSILETRHS APFGVSPTGF AGLLRPRADL MLARAANEAG LPFVLSGVSN
     ATLESVAAEI GEALWFQLYP SRDRQISDDM VRRAGSAGVT HLVVTVDLPV TSNRERDARN
     GFGFPPALKP SGYLEAMTHP AWCLRYLTSG GAPLFANWTE YASENPSTSD VARLIKSNSP
     AMFTWSDVRR LRDSWPHKLI VKGILHPDDA LNAQRHGVDA VIISNHGGRQ LDRAIASINA
     LPLIRREVGD DFPLMIDGGV RRGSDIAIAL CLGANFVFVG RPTLYGVAAA GEAGASRAIQ
     ILRTEFDRVM GQLGATRPEI LDTSFLADSY CAAGSLRNA
//

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