ID A0A1F5ZZD9_9BACT Unreviewed; 310 AA.
AC A0A1F5ZZD9;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2721_00540 {ECO:0000313|EMBL:OGG17715.1};
OS Candidatus Gottesmanbacteria bacterium RIFCSPHIGHO2_01_FULL_47_48.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1798381 {ECO:0000313|EMBL:OGG17715.1, ECO:0000313|Proteomes:UP000177871};
RN [1] {ECO:0000313|EMBL:OGG17715.1, ECO:0000313|Proteomes:UP000177871}
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:OGG17715.1}.
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DR EMBL; MFJK01000017; OGG17715.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5ZZD9; -.
DR STRING; 1798381.A2721_00540; -.
DR Proteomes; UP000177871; 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 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; 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.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 13..309
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 116..266
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 310 AA; 34846 MW; 5835FAE9AEE64FD9 CRC64;
MKLVILNARN RFREQDLKRL DKYKPVFYEE KDKNLESIKE FKSNEGVVFA VQPGWIKGSW
EGLPWEIIKD LKNLKGLCLS TTAYGWVPFK ELGKIGIPVT NVPGKSTDAV AEYYVFLMIA
LLRKLPGVIK NNWKFTYGPD VLGTDAKGLT AGIVGLGKIG SKIAKICQGY EMNITYWSRS
KKKTTYQRLE LDDLCRTADV VFLTTLADNS TKGLITRDKI DLMKSTAIIL SPIEKTVYDQ
KYVLEKIANG QLGGLGFESE DKTPLSYEGN VFPAPEIGYY TKQTLDNESR IMTDSIVSIF
EGKPVNVVNL
//