ID A0A1F7W5M8_9BACT Unreviewed; 326 AA.
AC A0A1F7W5M8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=D-glycerate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2304_03380 {ECO:0000313|EMBL:OGL98101.1};
OS Candidatus Uhrbacteria bacterium RIFOXYB2_FULL_57_15.
OC Bacteria; Candidatus Uhrbacteria.
OX NCBI_TaxID=1802422 {ECO:0000313|EMBL:OGL98101.1, ECO:0000313|Proteomes:UP000176501};
RN [1] {ECO:0000313|EMBL:OGL98101.1, ECO:0000313|Proteomes:UP000176501}
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|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:OGL98101.1}.
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; MGFE01000023; OGL98101.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7W5M8; -.
DR Proteomes; UP000176501; 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; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 6..323
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 113..291
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 326 AA; 36011 MW; B4E1FA55F189F8C0 CRC64;
MKPRIFVTRI IPDEGLKLLR RDKRVTVDVY EHDKIIPRTE LLRRVKGATA ILPILTDKID
AQLFDAAGPS LRMVANYAVG FDNVDLTEAA KRGIVVTNTP GLEIAETVAE HTIAFIFALA
HRLVETDQFA RDGKYHGWGP QMLLGTDVIG KTLGIIGTGK IGEGVVKRMY EGFGVKIVYN
DVRRNETIEK EELATFMTLE GVLKTADFIS LHVPLLPSTR HLIGAKQLKL MKKTAFLINT
SRGPVIDEKA LIAALQKKQI AGAGIDVYEH EPDIPLALRK LQNVVITPHT ASATIETRQV
MSRRAAENIL AFLDGKTPPN AVKTQK
//
