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Database: UniProt
Entry: A0A081PCF0_9SPHI
LinkDB: A0A081PCF0_9SPHI
Original site: A0A081PCF0_9SPHI 
ID   A0A081PCF0_9SPHI        Unreviewed;       328 AA.
AC   A0A081PCF0;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:KEQ28373.1};
GN   ORFNames=N180_01695 {ECO:0000313|EMBL:KEQ28373.1};
OS   Pedobacter antarcticus 4BY.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1358423 {ECO:0000313|EMBL:KEQ28373.1, ECO:0000313|Proteomes:UP000028007};
RN   [1] {ECO:0000313|EMBL:KEQ28373.1, ECO:0000313|Proteomes:UP000028007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4BY {ECO:0000313|EMBL:KEQ28373.1,
RC   ECO:0000313|Proteomes:UP000028007};
RA   Shivaji S., Ray M.K., Rao N.S., Saiserr L., Jagannadham M.V., Kumar G.S.,
RA   Reddy G., Bhargava P.M.;
RT   "Sphingobacterium antarcticus sp. nov. a Psychrotrophic Bacterium from the
RT   Soils of Schirmacher Oasis, Antarctica.";
RL   Int. J. Syst. Bacteriol. 42:102-106(1992).
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:KEQ28373.1}.
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DR   EMBL; JNFF01000116; KEQ28373.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A081PCF0; -.
DR   eggNOG; COG1052; Bacteria.
DR   OrthoDB; 1522997at2; -.
DR   Proteomes; UP000028007; 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; cd12183; LDH_like_2; 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; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43026; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR   PANTHER; PTHR43026:SF1; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 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.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028007}.
FT   DOMAIN          3..326
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          108..295
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   328 AA;  36262 MW;  A8E443EEA8933672 CRC64;
     MKVAVFSTNQ YDQDFLTQYN TGHEVKFLKV SLSEETAAVA FGYEAVCVFV NDKLNKAVLD
     LLAVAGLKLI VLRCAGFNNV DLPYAEELNI PVLRVPAYSP EAVAEHAMAL ILTLNRKTHK
     AYNRVREGNF SLEKLMGVNL FQRTVAVIGT GNIGQAFCRI LKGFGCTVKA YDPYPSSDMQ
     DLGVIYGTLE DTLRDADIIS LHCPLNSSTQ YLINENQLKQ LKRGAMLINT SRGGLIHTHA
     VIKALKSGII GSLGLDVYEQ ESEFFFHDFS EDVIQDDQLT QLISFPNVLI TGHQGFLTAE
     ALSEIAKVTF GNIDAWYSGS ELVNRVRP
//
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