ID A0A1S8T0I3_9CLOT Unreviewed; 289 AA.
AC A0A1S8T0I3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=D-specific alpha-keto acid dehydrogenase {ECO:0000313|EMBL:OOM71131.1};
DE EC=1.1.1.- {ECO:0000313|EMBL:OOM71131.1};
GN Name=vanH {ECO:0000313|EMBL:OOM71131.1};
GN ORFNames=CLPUN_51230 {ECO:0000313|EMBL:OOM71131.1};
OS Clostridium puniceum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=29367 {ECO:0000313|EMBL:OOM71131.1, ECO:0000313|Proteomes:UP000190890};
RN [1] {ECO:0000313|EMBL:OOM71131.1, ECO:0000313|Proteomes:UP000190890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2619 {ECO:0000313|EMBL:OOM71131.1,
RC ECO:0000313|Proteomes:UP000190890};
RA Poehlein A., Montoya Solano J.D., Flitsch S., Krabben P., Duerre P.,
RA Daniel R.;
RT "Microbial solvent formation.";
RL Submitted (MAY-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}.
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:OOM71131.1}.
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DR EMBL; LZZM01000234; OOM71131.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S8T0I3; -.
DR STRING; 29367.CLPUN_51230; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000190890; 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; cd00448; YjgF_YER057c_UK114_family; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR Gene3D; 3.30.1330.40; RutC-like; 1.
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 InterPro; IPR035959; RutC-like_sf.
DR InterPro; IPR006175; YjgF/YER057c/UK114.
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; PF01042; Ribonuc_L-PSP; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF55298; YjgF-like; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000190890}.
FT DOMAIN 2..226
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 41..186
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 289 AA; 31726 MW; 39B25F98B6A77477 CRC64;
MKYVATRSIG YDHIDIEHAK RIGMKVSKVN YAPDSVAEYT LMLMMMGCRR ICHVLDRAKV
QDFSLKGKLG KNLCDCTVGV IGTGQIGVAV IKYLKAFGCR ILANDSHQKQ ELSELLEYTD
LNILLKESDI ITLHVPAHKE NNYLLDKEAF EIMKHGVMIV NTARGTLIDT DALIDAIEEG
KIGHVAGHFL FTSGQGGLNP FDGSVVEGGI EAQAEQTMKN LSELFQAAGT NFTKTVKTTC
FLADMSDFAA FNQVYGKYFT GKPARSCVAE KTLPLGILCE VEAIVYLGE
//
