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Database: UniProt
Entry: A0A1G6V213_9MICO
LinkDB: A0A1G6V213_9MICO
Original site: A0A1G6V213_9MICO 
ID   A0A1G6V213_9MICO        Unreviewed;       339 AA.
AC   A0A1G6V213;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Lactate dehydrogenase {ECO:0000313|EMBL:SDD47588.1};
GN   ORFNames=SAMN05216410_3384 {ECO:0000313|EMBL:SDD47588.1};
OS   Sanguibacter gelidistatuariae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Sanguibacteraceae;
OC   Sanguibacter.
OX   NCBI_TaxID=1814289 {ECO:0000313|EMBL:SDD47588.1, ECO:0000313|Proteomes:UP000199039};
RN   [1] {ECO:0000313|EMBL:SDD47588.1, ECO:0000313|Proteomes:UP000199039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISLP-3 {ECO:0000313|EMBL:SDD47588.1,
RC   ECO:0000313|Proteomes:UP000199039};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-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; FMYH01000007; SDD47588.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6V213; -.
DR   STRING; 1814289.SAMN05216410_3384; -.
DR   OrthoDB; 4324715at2; -.
DR   Proteomes; UP000199039; 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; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
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; 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:UP000199039}.
FT   DOMAIN          58..339
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          128..305
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   339 AA;  35539 MW;  3A170D1CBDABF2F2 CRC64;
     MAHRQHAPAS GDEYVVGLSS DVTAPDGSTI FGDVGLDRLT DAGLRWEVMA PIAGHAPTAT
     ELAPYDAVLS FGHWGYSRDV AAATPRLKHV ARFGAGFDGI DLAGLADEGV VVTNTPDGVR
     RPLALAAMTL LLALSHRLLD NQRAVAEGRW RDRGSYRGLG LAGRTVGIIG FGSVGADLAE
     LIAPLGVRII TVDRPSVRAR QQAGELAGVE LLSLDELAAR SDYVILTASL TPSSHHMVDA
     DFLARMPSTS YVINVGRGPL IDQVALTEAL RTGSIAGAGL DVLESEPPTA DEPLLAMDSV
     IVTPHALCWT ADFVQDVAGS VMEALIDVAN GRPPSHPLN
//
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