(data stored in ACNUC7421 zone)

SWISSPROT: Q13EN2_RHOPS

ID   Q13EN2_RHOPS            Unreviewed;       333 AA.
AC   Q13EN2;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 75.
DE   SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding {ECO:0000313|EMBL:ABE37457.1};
GN   OrderedLocusNames=RPD_0217 {ECO:0000313|EMBL:ABE37457.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37457.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37457.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37457.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000283; ABE37457.1; -; Genomic_DNA.
DR   RefSeq; WP_011500647.1; NC_007958.1.
DR   STRING; 316057.RPD_0217; -.
DR   EnsemblBacteria; ABE37457; ABE37457; RPD_0217.
DR   KEGG; rpd:RPD_0217; -.
DR   eggNOG; ENOG4105C5I; Bacteria.
DR   eggNOG; COG1052; LUCA.
DR   HOGENOM; HOG000136700; -.
DR   KO; K00015; -.
DR   OMA; YGAGVDH; -.
DR   OrthoDB; 1638924at2; -.
DR   BioCyc; RPAL316057:RPD_RS01100-MONOMER; -.
DR   Proteomes; UP000001818; Chromosome.
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; Q13EN2.
DR   SWISS-2DPAGE; Q13EN2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719}.
FT   DOMAIN       18    328       2-Hacid_dh. {ECO:0000259|Pfam:PF00389}.
FT   DOMAIN      114    297       2-Hacid_dh_C. {ECO:0000259|Pfam:PF02826}.
SQ   SEQUENCE   333 AA;  36552 MW;  F307D65833931397 CRC64;
     MSVKKKPLVV VTRKLPDSIE TRMRELFDAR LNLDDVPMSA DQLAEAARTA DVLVPTVTDT
     ITSAMLNQPD CTLRLIAHFG NGIDNLDVAA AHARGITVTN TPKVLTEDTA DMTMALILAV
     PRRLIEGAAL LTDGGEWPGW SPTWMLGRRL GGKRLGIIGM GRIGQAVARR ARAFGLQIHY
     HNRKPVAPRI ADELGATYWD SLDQMLARMD IISVNCPHTP ATFHLLSARR LKLIRKDAFI
     VNTARGEVID EETLTRLIET GDIAGAGLDV YEHEPVVNPK LVRLAKAGKV VLLPHMGSAT
     IEGRVEMGEK VIINIRTFLD NHKPPDRVLP AML
//

If you have problems or comments...

PBIL Back to PBIL home page