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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//