ID A0A0K8PAL4_9CHLR Unreviewed; 322 AA.
AC A0A0K8PAL4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Lactate dehydrogenase {ECO:0000313|EMBL:GAP39693.1};
GN ORFNames=ATC1_12227 {ECO:0000313|EMBL:GAP39693.1};
OS Flexilinea flocculi.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Flexilinea.
OX NCBI_TaxID=1678840 {ECO:0000313|EMBL:GAP39693.1};
RN [1] {ECO:0000313|EMBL:GAP39693.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC1 {ECO:0000313|EMBL:GAP39693.1};
RA Matsuura N., Tourlousse D.M., Sun L., Toyonaga M., Kuroda K., Ohashi A.,
RA Cruz R., Yamaguchi T., Sekiguchi Y.;
RT "Draft Genome Sequence of Anaerolineae Strain TC1, a Novel Isolate from a
RT Methanogenic Wastewater Treatment System.";
RL Genome Announc. 3:e01104-15(2015).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; DF968180; GAP39693.1; -; Genomic_DNA.
DR RefSeq; WP_062278353.1; NZ_DF968180.1.
DR AlphaFoldDB; A0A0K8PAL4; -.
DR STRING; 1678840.ATC1_12227; -.
DR PATRIC; fig|1678840.3.peg.778; -.
DR OrthoDB; 9792971at2; -.
DR Proteomes; UP000053370; 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; cd12162; 2-Hacid_dh_4; 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; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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; PS00065; D_2_HYDROXYACID_DH_1; 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:UP000053370}.
FT DOMAIN 22..321
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..290
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 322 AA; 34712 MW; 5B9B18E6E35E2F6C CRC64;
MAKIVVLDGY AENPGDLSWD ELAKLGELQV YDRTSCTDDD EIISRIGDAA YVYTNKTPIR
KAVLDACPGI RFISMLATGY NVVDVAAAKE KGIPVCNIPT YGTAAVAQFA IALLLEICHN
IGHHSNAVHN GKWANSADWC FWDYPLIELE GKTMGIIGLG RIGQRTAAIA KALGMKVIAY
DEHPSDAGKA VADYVDLDTL LKTSDVIALH CPLFPSTEGI INKDSISKMK DGVIILNNSR
GPLIVEKDLA DALNSGKVAA AGLDVVSSEP IKNDNPLLQA KNCFITPHIS WAPKESRQRL
MDAAVDNLRQ FLAGTPVNVV NQ
//
