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Database: UniProt
Entry: A0A143X466_9FIRM
LinkDB: A0A143X466_9FIRM
Original site: A0A143X466_9FIRM 
ID   A0A143X466_9FIRM        Unreviewed;       300 AA.
AC   A0A143X466;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=(S)-sulfolactate dehydrogenase {ECO:0000313|EMBL:CVH77418.1};
DE            EC=1.1.1.310 {ECO:0000313|EMBL:CVH77418.1};
GN   Name=slcC {ECO:0000313|EMBL:CVH77418.1};
GN   ORFNames=BN3662_02178 {ECO:0000313|EMBL:CVH77418.1};
OS   Clostridiales bacterium CHKCI006.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales.
OX   NCBI_TaxID=1780379 {ECO:0000313|EMBL:CVH77418.1, ECO:0000313|Proteomes:UP000198633};
RN   [1] {ECO:0000313|EMBL:CVH77418.1, ECO:0000313|Proteomes:UP000198633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHKC6 {ECO:0000313|EMBL:CVH77418.1};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; FCNA01000112; CVH77418.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A143X466; -.
DR   STRING; 1780379.BN3662_02178; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000198633; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0102155; F:S-sulfolactate dehydrogenase activity; IEA:UniProtKB-EC.
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; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 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.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198633}.
FT   DOMAIN          12..298
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          105..276
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   300 AA;  34014 MW;  4DEF74CCF54B8168 CRC64;
     MNLLVTGSFS WEKDEINILK DLGHEIIFMQ QETDDLPCAP EWVEGIIGNG ILLKHPIQQF
     TSLQYIQLTS AGYDRVPMEY IKNNKIRIFN AMGVYSVPMA EFAVMSVLQL LKHSKFFLEN
     QKEHKWIKNR NIIELSEKIV CIVGCGNVGT ECAKRFSSFC CKVIGVDSSP YQSEYFETIL
     HMNDFEQALS ISDVVILTLP LTEDTRGMMD AKRFSVMKDG AILVNIARGP IVKTDDLISA
     LNNKLGGAVL DVFEEEPLSK KSILWDLKSV IITPHNSFVG DGNHKRMFKI IFNNLRSWSI
//
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