ID A0A0X8JVQ4_9FUSO Unreviewed; 344 AA.
AC A0A0X8JVQ4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:AMD95768.1};
GN ORFNames=AXF11_09400 {ECO:0000313|EMBL:AMD95768.1};
OS Leptotrichia sp. oral taxon 847.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Leptotrichia.
OX NCBI_TaxID=1785996 {ECO:0000313|EMBL:AMD95768.1, ECO:0000313|Proteomes:UP000065271};
RN [1] {ECO:0000313|Proteomes:UP000065271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0260 {ECO:0000313|Proteomes:UP000065271};
RA Holder M.E., Ajami N.J., Petrosino J.F.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP014231; AMD95768.1; -; Genomic_DNA.
DR RefSeq; WP_068157553.1; NZ_CP014231.1.
DR AlphaFoldDB; A0A0X8JVQ4; -.
DR STRING; 1785996.AXF11_09400; -.
DR KEGG; lot:AXF11_09400; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000065271; Chromosome.
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; IPR029753; D-isomer_DH_CS.
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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 3..329
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 110..298
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 344 AA; 38484 MW; 0D5506E27E115FED CRC64;
MKIVVFDAKP YDIEFFDKWN KKFGAQITYF EEKLSLKNVM LTKYQDVVCT FVNDDLNEKV
LNILSKNGVR VIAARCAGYN NINLKAAREN RITVLRVPAY SPYAVAEHSL ALLMSVNRKT
HKAYNRTREG NFSLAGLTGM DLNGKTAGII GTGRIARIFI KILNGLGMKV IGYDKFPNEQ
AAKEGNFTYV TLDELFAKSD VISLHCPLFP ETRHTINKET IAKMKDGVII INAARGGLID
TEALVEGLKD KKIGGAGLDV YENESSYFFE DESASVLEDD LLARLLSFNN VVLTSHQAFL
TKEALDNIAE ATFNNILSYV KEEPLVNEVW YNEETGKVVE GLRK
//
