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Database: UniProt
Entry: A0A0R1M9W8_9LACO
LinkDB: A0A0R1M9W8_9LACO
Original site: A0A0R1M9W8_9LACO 
ID   A0A0R1M9W8_9LACO        Unreviewed;       304 AA.
AC   A0A0R1M9W8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=L-2-hydroxyisocaproate dehydrogenase {ECO:0000313|EMBL:KRL00296.1};
GN   ORFNames=FC81_GL000073 {ECO:0000313|EMBL:KRL00296.1};
OS   Liquorilactobacillus capillatus DSM 19910.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Liquorilactobacillus.
OX   NCBI_TaxID=1423731 {ECO:0000313|EMBL:KRL00296.1, ECO:0000313|Proteomes:UP000051621};
RN   [1] {ECO:0000313|EMBL:KRL00296.1, ECO:0000313|Proteomes:UP000051621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19910 {ECO:0000313|EMBL:KRL00296.1,
RC   ECO:0000313|Proteomes:UP000051621};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
CC       {ECO:0000256|ARBA:ARBA00006054}.
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:KRL00296.1}.
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DR   EMBL; AZEF01000053; KRL00296.1; -; Genomic_DNA.
DR   RefSeq; WP_057746367.1; NZ_AZEF01000053.1.
DR   AlphaFoldDB; A0A0R1M9W8; -.
DR   STRING; 1423731.FC81_GL000073; -.
DR   PATRIC; fig|1423731.3.peg.76; -.
DR   OrthoDB; 9802969at2; -.
DR   Proteomes; UP000051621; Unassembled WGS sequence.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   CDD; cd05291; HicDH_like; 1.
DR   Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR022383; Lactate/malate_DH_C.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR   PANTHER; PTHR43128:SF34; L-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   PRINTS; PR00086; LLDHDRGNASE.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051621}.
FT   DOMAIN          3..143
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          146..297
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        176
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         8..13
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         33
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         96
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         119..121
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ   SEQUENCE   304 AA;  33100 MW;  3D0C269D50C3C506 CRC64;
     MRKIGVIGLG HVGATIAYTL VTKGIADELV LIDSKKDKAV AEEYDLRDTL SRLDTFTKII
     PQNYAALADA DIIITAFGDI SAIQLDGDRF GELKHNITAV TEIAQKIKQT GFNGVLINIS
     NPCDVITQLL QQKTGLSTNQ VFGTGTFLDT ARMQRAVGQA LNEDPKNISG YVLGEHGESQ
     FTAWSSVRVK GHPIQDIASA RGLDLNDLDQ RARRGGWLVF SGKHYTCYAI ATCAIKLALA
     VLSDAHLACP TSVYLESYQH YIGYPSVIGR QGIIEVNKIE LTLDEQNRLD SSAKIISTKL
     ASFN
//
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