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Database: UniProt
Entry: A9CLC8_AGRFC
LinkDB: A9CLC8_AGRFC
Original site: A9CLC8_AGRFC 
ID   A9CLC8_AGRFC            Unreviewed;       349 AA.
AC   A9CLC8;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   28-MAR-2018, entry version 55.
DE   SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding {ECO:0000313|EMBL:AAK90702.2};
GN   OrderedLocusNames=Atu5328 {ECO:0000313|EMBL:AAK90702.2};
OS   Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium
OS   tumefaciens (strain C58)).
OG   Plasmid At {ECO:0000313|EMBL:AAK90702.2,
OG   ECO:0000313|Proteomes:UP000000813}.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=176299 {ECO:0000313|EMBL:AAK90702.2, ECO:0000313|Proteomes:UP000000813};
RN   [1] {ECO:0000313|EMBL:AAK90702.2, ECO:0000313|Proteomes:UP000000813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970 {ECO:0000313|Proteomes:UP000000813};
RC   PLASMID=Plasmid At {ECO:0000313|Proteomes:UP000000813};
RX   PubMed=11743194; DOI=10.1126/science.1066803;
RA   Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M.,
RA   Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L.,
RA   Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F.,
RA   Wollam C., Allinger M., Doughty D., Scott C., Lappas C., Markelz B.,
RA   Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G.,
RA   Cielo C., Slater S.;
RT   "Genome sequence of the plant pathogen and biotechnology agent
RT   Agrobacterium tumefaciens C58.";
RL   Science 294:2323-2328(2001).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; AE007872; AAK90702.2; -; Genomic_DNA.
DR   RefSeq; NP_396261.2; NC_003064.2.
DR   RefSeq; WP_010974582.1; NC_003064.2.
DR   ProteinModelPortal; A9CLC8; -.
DR   EnsemblBacteria; AAK90702; AAK90702; Atu5328.
DR   GeneID; 1137101; -.
DR   KEGG; atu:Atu5328; -.
DR   PATRIC; fig|176299.10.peg.5001; -.
DR   HOGENOM; HOG000136700; -.
DR   OMA; WRESDAI; -.
DR   Proteomes; UP000000813; Plasmid At.
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; IPR029753; D-isomer_DH_CS.
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; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000813};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Plasmid {ECO:0000313|EMBL:AAK90702.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000813}.
FT   DOMAIN       25    332       2-Hacid_dh. {ECO:0000259|Pfam:PF00389}.
FT   DOMAIN      130    306       2-Hacid_dh_C. {ECO:0000259|Pfam:PF02826}.
SQ   SEQUENCE   349 AA;  37260 MW;  AA0A345D5C7B408F CRC64;
     MPKRCNGSAA SSRIQFEVRM GSRNILVTGP AINEQAVKLI TDNGYQVSYV PPYTSEADLV
     RIVTELDPVG VVVRMGRFSE AAIKAAPSLR VLSKHGVGVD NIDVDAASRR EIPVVVAAGA
     NALSVAEHAI TLLFAVVKRI VPLDSGIRAG RWEKAGYSGK ELAGMIIGLV GFGAIARQTA
     VFARGFGLKV QAYDPFTDET AFVEAGVHRV ADVDDLISSS DILSLHCPLT PDTRNLLDDR
     RLGMMKPGSF IINTARGGLI DEDALLRAVE SGHIAGAGLD TFQIEPPAAN HPFWQNQKIV
     VTPHIGGVTQ EANVRVGVDA VEGIFAIVEG RHLGRERIVN HRALAKTPA
//
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