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Database: UniProt
Entry: A0A0R1MJF1_9LACO
LinkDB: A0A0R1MJF1_9LACO
Original site: A0A0R1MJF1_9LACO 
ID   A0A0R1MJF1_9LACO        Unreviewed;       302 AA.
AC   A0A0R1MJF1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=L-2-hydroxyisocaproate dehydrogenase {ECO:0000313|EMBL:KRL08173.1};
GN   ORFNames=FC92_GL000688 {ECO:0000313|EMBL:KRL08173.1};
OS   Liquorilactobacillus hordei DSM 19519.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Liquorilactobacillus.
OX   NCBI_TaxID=1423759 {ECO:0000313|EMBL:KRL08173.1, ECO:0000313|Proteomes:UP000051448};
RN   [1] {ECO:0000313|EMBL:KRL08173.1, ECO:0000313|Proteomes:UP000051448}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19519 {ECO:0000313|EMBL:KRL08173.1,
RC   ECO:0000313|Proteomes:UP000051448};
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:KRL08173.1}.
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DR   EMBL; AZDX01000002; KRL08173.1; -; Genomic_DNA.
DR   RefSeq; WP_057868672.1; NZ_CP049303.1.
DR   AlphaFoldDB; A0A0R1MJF1; -.
DR   STRING; 1423759.FC92_GL000688; -.
DR   PATRIC; fig|1423759.3.peg.728; -.
DR   OrthoDB; 9802969at2; -.
DR   Proteomes; UP000051448; 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}.
FT   DOMAIN          3..143
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          146..302
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   302 AA;  33001 MW;  E02DE2E057B60467 CRC64;
     MRKIGIIGLG HVGATIAYTL VTKGIADELV IIDTNDEKTT AEEYDLRDTL ARLDTFTKII
     PQDYDSLSNA DVVITAFGNI DSIKMDGDRF GELNFNAEAV EEVAANLRTS GFNGVLINIS
     NPCDVITTLL QQQTGLSKNQ VFGTGTFLDT ARMQRAVGQA LHEDPKNISG YVLGEHGESQ
     YTAWSTVEVK GHPIIKLAEE KGLDLTSLDQ QARRGGWLVF SGKHYTCYAI ATCAIKLTQA
     VLSDAHLACP TSVYLEEYDH YIGYPAVIGR KGIVEVNSIT LSIEEKAQLD NSAKIIKEKL
     NK
//
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