ID A0A1G3JK02_9SPHN Unreviewed; 309 AA.
AC A0A1G3JK02;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:OHC93647.1};
GN ORFNames=A3H25_12115 {ECO:0000313|EMBL:OHC93647.1};
OS Sphingomonadales bacterium RIFCSPLOWO2_12_FULL_63_15.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales.
OX NCBI_TaxID=1802170 {ECO:0000313|EMBL:OHC93647.1, ECO:0000313|Proteomes:UP000176465};
RN [1] {ECO:0000313|EMBL:OHC93647.1, ECO:0000313|Proteomes:UP000176465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {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:OHC93647.1}.
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DR EMBL; MIAK01000070; OHC93647.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G3JK02; -.
DR Proteomes; UP000176465; 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; cd12156; HPPR; 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; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..309
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009594596"
FT DOMAIN 18..307
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 104..276
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 309 AA; 32989 MW; 6C188406BFD5D484 CRC64;
MTRPILLVGQ ALLAPVVPLL AQDYDVMALW EEPDAAALAR VDAVIWAGEF VLERALVEAM
PRLSLIACFT VGYDGVDLAL ARERGIAVTH AGDANAQDVA DHAIGLMIAH RRWIVGGDRH
VRSGQWTMAA KTRTRSMGGA KLGIIGMGSI GVAVAERTQA MRMQVRWWGP REKPALPWPR
TVSLDALARE SDILLVAARA DESNRGMISA DIMDALGPEG LLVNVARGQL VDEAALIAAL
ISGRLGGAAI DVYDPEPTDP KRWADVPNVV LTPHTGGATH EAVAHMAQML LANLTAHFAD
KPLISPVRG
//
