(data stored in SCRATCH zone)

SWISSPROT: B2JS94_PARP8

ID   B2JS94_PARP8            Unreviewed;       310 AA.
AC   B2JS94;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   08-MAY-2019, entry version 60.
DE   SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding {ECO:0000313|EMBL:ACC72471.1};
GN   OrderedLocusNames=Bphy_3315 {ECO:0000313|EMBL:ACC72471.1};
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:ACC72471.1, 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   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; CP001044; ACC72471.1; -; Genomic_DNA.
DR   RefSeq; WP_012402644.1; NC_010623.1.
DR   STRING; 391038.Bphy_3315; -.
DR   EnsemblBacteria; ACC72471; ACC72471; Bphy_3315.
DR   GeneID; 27743001; -.
DR   KEGG; bph:Bphy_3315; -.
DR   eggNOG; ENOG4106IH4; Bacteria.
DR   eggNOG; COG1052; LUCA.
DR   HOGENOM; HOG000136700; -.
DR   OMA; HVAGWSP; -.
DR   OrthoDB; 1638924at2; -.
DR   BioCyc; BPHY391038:G1GBS-3411-MONOMER; -.
DR   Proteomes; UP000001192; Chromosome 2.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; B2JS94.
DR   SWISS-2DPAGE; B2JS94.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001192};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001192}.
FT   DOMAIN       24    307       2-Hacid_dh. {ECO:0000259|Pfam:PF00389}.
FT   DOMAIN      108    279       2-Hacid_dh_C. {ECO:0000259|Pfam:PF02826}.
SQ   SEQUENCE   310 AA;  32822 MW;  6329AF7BD364DA10 CRC64;
     MKPSLLVLIP LGDDSRARIA ASFDLHYAPT HEARTAAVGT HGAAIRAVLT NGTTGLTSAE
     IDAMPALEFV SALGAGYENI AVDHARARGI VLANGAGTND DCVADHAMAL LLAVVRDVPQ
     RDRATREGIW RDALPMRPSV SGKRLGVIGL GNIGRKVARR AEGFDIEIGY HNRNARDGVA
     WRYFDDVREI ARWSDYLVVA TPGGPSTHHL IDRDVLEALG RQGFLVNVSR GSVVDTDALA
     HALGNGVIAG AGLDVYEGEP RPPQALLHLP NVVLTPHVAG TSPEAIGASV DNFITNATRH
     FAGEDVLTPI
//

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