ID   A0A1Y4SIW6_9FIRM        Unreviewed;       430 AA.
AC   A0A1Y4SIW6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:OUQ28793.1};
GN   ORFNames=B5E77_00010 {ECO:0000313|EMBL:OUQ28793.1};
OS   Lachnoclostridium sp. An131.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1965555 {ECO:0000313|EMBL:OUQ28793.1, ECO:0000313|Proteomes:UP000199743};
RN   [1] {ECO:0000313|Proteomes:UP000199743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An131 {ECO:0000313|Proteomes:UP000199743};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) 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}.
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:OUQ28793.1}.
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DR   EMBL; NFLI01000001; OUQ28793.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4SIW6; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000199743; 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   CDD; cd00367; PTS-HPr_like; 1.
DR   Gene3D; 3.30.1340.10; HPr-like; 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; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR000032; HPr-like.
DR   InterPro; IPR035895; HPr-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01003; PTS_HPr_family; 1.
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   Pfam; PF00381; PTS-HPr; 1.
DR   PRINTS; PR00107; PHOSPHOCPHPR.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF55594; HPr-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
DR   PROSITE; PS51350; PTS_HPR_DOM; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199743}.
FT   DOMAIN          1..88
FT                   /note="HPr"
FT                   /evidence="ECO:0000259|PROSITE:PS51350"
SQ   SEQUENCE   430 AA;  47526 MW;  3D12032319A2BED7 CRC64;
     MKEIKYVVSN PNGVHARPCA LLAQCCMNFK SQITVSVEEE TASAQNVLEL MALHAKKGDT
     LEIRIEGADE EQAYVAVQQV LDHSFNEKRA GQILKIAFFG TKDYDRIFFS ELSRDKGEGT
     YNCEIKYFSS NLGPETAGMS KGYDAVCVFV NDNVSRPVVE QLHDNGVRLI LLRCAGFNNV
     DLEAAKEYGI TVLRVPAYSP YAVAEHAMAI LQEANRRLHK AYNKVRDNNF ALSGLLGMDL
     HNKVAGIVGT GKIGICMAKI CKGYGMTVLG WDAYPNKALE EEGLLTYVEK EELFRRADLI
     SLHAPLFPST HHIINETSIA LMKNSAMLVN TARGGLVDTE ALIAALKQGK FHAVALDVYE
     GEDDNVYTDR SDQAIAEDVT ARLMMFPQVV MTSHQAFFTR EAMQAIAVVT MENARNFNEG
     NDYGDAEVKA
//