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Database: UniProt
Entry: A0A0C1JNY3_9RHOB
LinkDB: A0A0C1JNY3_9RHOB
Original site: A0A0C1JNY3_9RHOB 
ID   A0A0C1JNY3_9RHOB        Unreviewed;       323 AA.
AC   A0A0C1JNY3;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:KIC45593.1};
GN   ORFNames=RA28_07625 {ECO:0000313|EMBL:KIC45593.1};
OS   Ruegeria sp. ANG-S4.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=1577904 {ECO:0000313|EMBL:KIC45593.1, ECO:0000313|Proteomes:UP000031326};
RN   [1] {ECO:0000313|Proteomes:UP000031326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANG-S4 {ECO:0000313|Proteomes:UP000031326};
RX   PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA   Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT   "Comparative genomics of Roseobacter clade bacteria isolated from the
RT   accessory nidamental gland of Euprymna scolopes.";
RL   Front. Microbiol. 6:123-123(2015).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC       ECO:0000256|RuleBase:RU003719}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KIC45593.1}.
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DR   EMBL; JWLK01000002; KIC45593.1; -; Genomic_DNA.
DR   RefSeq; WP_039526294.1; NZ_JWLK01000002.1.
DR   AlphaFoldDB; A0A0C1JNY3; -.
DR   STRING; 1577904.RA28_07625; -.
DR   OrthoDB; 9793626at2; -.
DR   Proteomes; UP000031326; Unassembled WGS sequence.
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   CDD; cd05301; GDH; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR   PANTHER; PTHR10996:SF178; GLYOXYLATE REDUCTASE 1; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 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   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031326}.
FT   DOMAIN          7..322
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          111..291
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   323 AA;  35135 MW;  64FA5B1629E01753 CRC64;
     MAKPSVLVTR RWPAAVEAQL AENYNVSLNT GDKPMSPAEI RQALKSHDAV LPTVTDTLSA
     EAMDVPDAQA KILANYGVGY SHICAPSARG MGLMVTNTPD VLSECTADLA MTLLLMVARR
     AGEGERELRA GNWTGWRPTH LVGTKVSGKT LGIIGYGRIG QEMARRAHHG FGMNVIVYNR
     RPVDRDLLAT CNATQVNSVD ALLPLCDFVS LHCPGGAANR HLINAQRLNL MKPDAFLINT
     ARGEVVDEWA LIQALMFDMI GGAALDVFDG EPRVSPDLLQ CDNLVMLPHL GSATREAREA
     MGFRVLDNLS DFFQGHEPRD RVI
//
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